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Conserved domains on  [gi|569026720|ref|NP_001275634|]
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macrophage colony-stimulating factor 1 receptor isoform a precursor [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PTKc_CSF-1R cd05106
Catalytic domain of the Protein Tyrosine Kinase, Colony-Stimulating Factor-1 Receptor; PTKs ...
543-914 0e+00

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: 776.33  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 543 KPKYQVRWKIIESYEGNSYTFIDPTQLPYNEKWEFPRNNLQFGKTLGAGAFGKVVEATAFGLGKEDAVLKVAVKMLKSTA 622
Cdd:cd05106    1 KPKYEIRWKIIEAAEGNNYTFIDPTQLPYNEKWEFPRDNLQFGKTLGAGAFGKVVEATAFGLGKEDNVLRVAVKMLKASA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 623 HADEKEALMSELKIMSHLGQHENIVNLLGACTHGGPVLVITEYCCYGDLLNFLRRKAEAMLGPSLSPGQDPEGGVDYKNI 702
Cdd:cd05106   81 HTDEREALMSELKILSHLGQHKNIVNLLGACTHGGPVLVITEYCCYGDLLNFLRKKAETFLNFVMALPEISETSSDYKNI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 703 HLEKKYVRRDSGFSSQGVDTYVEMRPVSTSSNDSF-SEQDLDKEDGRPLELRDLLHFSSQVAQGMAFLASKNCIHRDVAA 781
Cdd:cd05106  161 TLEKKYIRSDSGFSSQGSDTYVEMRPVSSSSSQSSdSKDEEDTEDSWPLDLDDLLRFSSQVAQGMDFLASKNCIHRDVAA 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 782 RNVLLTNGHVAKIGDFGLARDIMNDSNYIVKGNARLPVKWMAPESIFDCVYTVQSDVWSYGILLWEIFSLGLNPYPGILV 861
Cdd:cd05106  241 RNVLLTDGRVAKICDFGLARDIMNDSNYVVKGNARLPVKWMAPESIFDCVYTVQSDVWSYGILLWEIFSLGKSPYPGILV 320
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 569026720 862 NSKFYKLVKDGYQMAQPAFAPKNIYSIMQACWALEPTHRPTFQQICSFLQEQA 914
Cdd:cd05106  321 NSKFYKMVKRGYQMSRPDFAPPEIYSIMKMCWNLEPTERPTFSQISQLIQRQL 373
IgI_3_CSF-1R cd20936
Third immunoglobulin domain of the hematopoietic colony-stimulating factor 1 receptor (CSF-1R), ...
203-295 1.64e-59

Third immunoglobulin domain of the hematopoietic colony-stimulating factor 1 receptor (CSF-1R), and similar domains; member of the I-set of IgSF domains; The members here are composed of the third immunoglobulin domain of the hematopoietic colony-stimulating factor 1 receptor (CSF-1R) and similar proteins. CSF-1R, a class III receptor tyrosine kinase (RTKIII), is critical to the survival, proliferation, and differentiation of mononuclear phagocytic cells such as monocytes, tissue macrophages, muscularis macrophages, microglia, osteoclasts, Paneth cells, and myeloid dendritic cells. Human colony-stimulating factor 1 receptor (hCSF-1R) is unique among the hematopoietic receptors because it is activated by two distinct cytokines, CSF-1 and interleukin-34 (IL-34). The Ig superfamily (IgSF) 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, such as, T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, such as, 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. 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 I-set of IgSF domains.


:

Pssm-ID: 409530  Cd Length: 93  Bit Score: 197.87  E-value: 1.64e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 203 PALTLVPAELVRIRGEAAQIVCSASSVDVNFDVFLQHNNTKLAIPQQSDFHNNRYQKVLTLNLDQVDFQHAGNYSCVASN 282
Cdd:cd20936    1 PALTLEPAELVRIRGEAAQIVCSASNVDVNFDVFLQHGDTKLAIPQQSDFHDNRYQKVLTLNLDQVDFQDAGNYSCVASN 80
                         90
                 ....*....|...
gi 569026720 283 VQGKHSTSMFFRV 295
Cdd:cd20936   81 VQGKHSASMFFRV 93
IgI_4_SCFR_like cd04975
Fourth immunoglobulin (Ig)-like domain of stem cell factor receptor (SCFR), and similar ...
299-400 3.89e-54

Fourth immunoglobulin (Ig)-like domain of stem cell factor receptor (SCFR), and similar domains; member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain of stem cell factor receptor (SCFR). In addition to SCFR, this group also includes the fourth Ig domain of macrophage colony stimulating factor receptor (M-CSF-R). SCFR, also called receptor tyrosine kinase KIT or proto-oncogene c-Kit, contains an extracellular component having five Ig-like domains, a transmembrane segment, and a cytoplasmic portion having protein tyrosine kinase activity. SCFR and its ligand SCF are critical for normal hematopoiesis, mast cell development, melanocytes, and gametogenesis. SCF binds to the second and third Ig-like domains of SCFR, this fourth Ig-like domain participates in SCFR dimerization, which follows ligand binding. Deletion of this fourth SCFR Ig-like domain abolishes the ligand-induced dimerization of SCFR and completely inhibits signal transduction. M-CSF-R, also called proto-oncogene c-Fms, acts as cell-surface receptor for CSF1 and IL34 and plays an essential role in the regulation of survival, proliferation and differentiation of hematopoietic precursor cells, such as macrophages and monocytes. 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: 409364  Cd Length: 101  Bit Score: 183.19  E-value: 3.89e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 299 AYLNLSSEQNLIQEVTVGEGLNLKVMVEAYPGLQGFNWTYLGPFSDhQPEPKLANATTKDTYRHTFTLSLPRLKPSEAGR 378
Cdd:cd04975    1 GYINLSSEQNLTVEVNVGENLDLIVEVEAYPKPEHQNWTYMGPFFT-DKWEDLPNSENESTYRYVSTLHLTRLKGSEAGT 79
                         90       100
                 ....*....|....*....|..
gi 569026720 379 YSFLARNPGGWRALTFELTLRY 400
Cdd:cd04975   80 YTFLASNSDVNAALAFEVYLNY 101
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
21-85 6.77e-08

Immunoglobulin domain; This family contains immunoglobulin-like domains.


:

Pssm-ID: 433584 [Multi-domain]  Cd Length: 75  Bit Score: 50.66  E-value: 6.77e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 569026720   21 PVIEPSVPELVVKPGATVTLRCVGNGS----VEW--DGPPSPHWTLYSDGSSSILSTNNATFQNTGTYRCT 85
Cdd:pfam13927   2 PVITVSPSSVVVVEGETVTLTCEASGSppptITWykNGGKLSSGRTSLVGGNGTLTISNVTREDSGTYTCT 72
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
401-489 6.68e-06

Immunoglobulin domain; This family contains immunoglobulin-like domains.


:

Pssm-ID: 433584 [Multi-domain]  Cd Length: 75  Bit Score: 44.88  E-value: 6.68e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720  401 PPEVSV----IWTFINGSGTLLCAASGYPQPNVTWLQCSghtdrcdeaqvlqvwddpypEVLSQEPFHKVTVQSLLTVE- 475
Cdd:pfam13927   1 KPVITVspssVVVVEGETVTLTCEASGSPPPTITWYKNG--------------------GKLSSGRTSLVGGNGTLTISn 60
                          90
                  ....*....|....*
gi 569026720  476 -TLEHNQTYECRAHN 489
Cdd:pfam13927  61 vTREDSGTYTCTASN 75
 
Name Accession Description Interval E-value
PTKc_CSF-1R cd05106
Catalytic domain of the Protein Tyrosine Kinase, Colony-Stimulating Factor-1 Receptor; PTKs ...
543-914 0e+00

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: 776.33  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 543 KPKYQVRWKIIESYEGNSYTFIDPTQLPYNEKWEFPRNNLQFGKTLGAGAFGKVVEATAFGLGKEDAVLKVAVKMLKSTA 622
Cdd:cd05106    1 KPKYEIRWKIIEAAEGNNYTFIDPTQLPYNEKWEFPRDNLQFGKTLGAGAFGKVVEATAFGLGKEDNVLRVAVKMLKASA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 623 HADEKEALMSELKIMSHLGQHENIVNLLGACTHGGPVLVITEYCCYGDLLNFLRRKAEAMLGPSLSPGQDPEGGVDYKNI 702
Cdd:cd05106   81 HTDEREALMSELKILSHLGQHKNIVNLLGACTHGGPVLVITEYCCYGDLLNFLRKKAETFLNFVMALPEISETSSDYKNI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 703 HLEKKYVRRDSGFSSQGVDTYVEMRPVSTSSNDSF-SEQDLDKEDGRPLELRDLLHFSSQVAQGMAFLASKNCIHRDVAA 781
Cdd:cd05106  161 TLEKKYIRSDSGFSSQGSDTYVEMRPVSSSSSQSSdSKDEEDTEDSWPLDLDDLLRFSSQVAQGMDFLASKNCIHRDVAA 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 782 RNVLLTNGHVAKIGDFGLARDIMNDSNYIVKGNARLPVKWMAPESIFDCVYTVQSDVWSYGILLWEIFSLGLNPYPGILV 861
Cdd:cd05106  241 RNVLLTDGRVAKICDFGLARDIMNDSNYVVKGNARLPVKWMAPESIFDCVYTVQSDVWSYGILLWEIFSLGKSPYPGILV 320
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 569026720 862 NSKFYKLVKDGYQMAQPAFAPKNIYSIMQACWALEPTHRPTFQQICSFLQEQA 914
Cdd:cd05106  321 NSKFYKMVKRGYQMSRPDFAPPEIYSIMKMCWNLEPTERPTFSQISQLIQRQL 373
Pkinase_Tyr pfam07714
Protein tyrosine kinase;
582-910 3.52e-129

Protein tyrosine kinase;


Pssm-ID: 429616 [Multi-domain]  Cd Length: 258  Bit Score: 390.32  E-value: 3.52e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720  582 LQFGKTLGAGAFGKVVEATAFGLGKEDAVlKVAVKMLKSTAHADEKEALMSELKIMSHLgQHENIVNLLGACTHGGPVLV 661
Cdd:pfam07714   1 LTLGEKLGEGAFGEVYKGTLKGEGENTKI-KVAVKTLKEGADEEEREDFLEEASIMKKL-DHPNIVKLLGVCTQGEPLYI 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720  662 ITEYCCYGDLLNFLRRKaeamlgpslspgqdpeggvdyknihlekkyvrrdsgfssqgvdtyvemrpvstssndsfseqd 741
Cdd:pfam07714  79 VTEYMPGGDLLDFLRKH--------------------------------------------------------------- 95
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720  742 ldkedGRPLELRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDIMNDSNYIVKGNARLPVKW 821
Cdd:pfam07714  96 -----KRKLTLKDLLSMALQIAKGMEYLESKNFVHRDLAARNCLVSENLVVKISDFGLSRDIYDDDYYRKRGGGKLPIKW 170
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720  822 MAPESIFDCVYTVQSDVWSYGILLWEIFSLGLNPYPGIlVNSKFYKLVKDGYQMAQPAFAPKNIYSIMQACWALEPTHRP 901
Cdd:pfam07714 171 MAPESLKDGKFTSKSDVWSFGVLLWEIFTLGEQPYPGM-SNEEVLEYLEDGYRLPQPENCPDELYDLMKQCWAYDPEDRP 249

                  ....*....
gi 569026720  902 TFQQICSFL 910
Cdd:pfam07714 250 TFSELVEDL 258
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
582-910 2.89e-115

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: 354.16  E-value: 2.89e-115
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720   582 LQFGKTLGAGAFGKVVEATAFGLGKEdAVLKVAVKMLKSTAHADEKEALMSELKIMSHLgQHENIVNLLGACTHGGPVLV 661
Cdd:smart00221   1 LTLGKKLGEGAFGEVYKGTLKGKGDG-KEVEVAVKTLKEDASEQQIEEFLREARIMRKL-DHPNIVKLLGVCTEEEPLMI 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720   662 ITEYCCYGDLLNFLRrkaeamlgpslspgqdpeggvdyknihlekkyvrrdsgfssqgvdtyvemrpvstssndsfseqd 741
Cdd:smart00221  79 VMEYMPGGDLLDYLR----------------------------------------------------------------- 93
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720   742 ldKEDGRPLELRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDImNDSNYIVKGNARLPVKW 821
Cdd:smart00221  94 --KNRPKELSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGENLVVKISDFGLSRDL-YDDDYYKVKGGKLPIRW 170
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720   822 MAPESIFDCVYTVQSDVWSYGILLWEIFSLGLNPYPGIlVNSKFYKLVKDGYQMAQPAFAPKNIYSIMQACWALEPTHRP 901
Cdd:smart00221 171 MAPESLKEGKFTSKSDVWSFGVLLWEIFTLGEEPYPGM-SNAEVLEYLKKGYRLPKPPNCPPELYKLMLQCWAEDPEDRP 249

                   ....*....
gi 569026720   902 TFQQICSFL 910
Cdd:smart00221 250 TFSELVEIL 258
IgI_3_CSF-1R cd20936
Third immunoglobulin domain of the hematopoietic colony-stimulating factor 1 receptor (CSF-1R), ...
203-295 1.64e-59

Third immunoglobulin domain of the hematopoietic colony-stimulating factor 1 receptor (CSF-1R), and similar domains; member of the I-set of IgSF domains; The members here are composed of the third immunoglobulin domain of the hematopoietic colony-stimulating factor 1 receptor (CSF-1R) and similar proteins. CSF-1R, a class III receptor tyrosine kinase (RTKIII), is critical to the survival, proliferation, and differentiation of mononuclear phagocytic cells such as monocytes, tissue macrophages, muscularis macrophages, microglia, osteoclasts, Paneth cells, and myeloid dendritic cells. Human colony-stimulating factor 1 receptor (hCSF-1R) is unique among the hematopoietic receptors because it is activated by two distinct cytokines, CSF-1 and interleukin-34 (IL-34). The Ig superfamily (IgSF) 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, such as, T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, such as, 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. 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 I-set of IgSF domains.


Pssm-ID: 409530  Cd Length: 93  Bit Score: 197.87  E-value: 1.64e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 203 PALTLVPAELVRIRGEAAQIVCSASSVDVNFDVFLQHNNTKLAIPQQSDFHNNRYQKVLTLNLDQVDFQHAGNYSCVASN 282
Cdd:cd20936    1 PALTLEPAELVRIRGEAAQIVCSASNVDVNFDVFLQHGDTKLAIPQQSDFHDNRYQKVLTLNLDQVDFQDAGNYSCVASN 80
                         90
                 ....*....|...
gi 569026720 283 VQGKHSTSMFFRV 295
Cdd:cd20936   81 VQGKHSASMFFRV 93
IgI_4_SCFR_like cd04975
Fourth immunoglobulin (Ig)-like domain of stem cell factor receptor (SCFR), and similar ...
299-400 3.89e-54

Fourth immunoglobulin (Ig)-like domain of stem cell factor receptor (SCFR), and similar domains; member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain of stem cell factor receptor (SCFR). In addition to SCFR, this group also includes the fourth Ig domain of macrophage colony stimulating factor receptor (M-CSF-R). SCFR, also called receptor tyrosine kinase KIT or proto-oncogene c-Kit, contains an extracellular component having five Ig-like domains, a transmembrane segment, and a cytoplasmic portion having protein tyrosine kinase activity. SCFR and its ligand SCF are critical for normal hematopoiesis, mast cell development, melanocytes, and gametogenesis. SCF binds to the second and third Ig-like domains of SCFR, this fourth Ig-like domain participates in SCFR dimerization, which follows ligand binding. Deletion of this fourth SCFR Ig-like domain abolishes the ligand-induced dimerization of SCFR and completely inhibits signal transduction. M-CSF-R, also called proto-oncogene c-Fms, acts as cell-surface receptor for CSF1 and IL34 and plays an essential role in the regulation of survival, proliferation and differentiation of hematopoietic precursor cells, such as macrophages and monocytes. 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: 409364  Cd Length: 101  Bit Score: 183.19  E-value: 3.89e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 299 AYLNLSSEQNLIQEVTVGEGLNLKVMVEAYPGLQGFNWTYLGPFSDhQPEPKLANATTKDTYRHTFTLSLPRLKPSEAGR 378
Cdd:cd04975    1 GYINLSSEQNLTVEVNVGENLDLIVEVEAYPKPEHQNWTYMGPFFT-DKWEDLPNSENESTYRYVSTLHLTRLKGSEAGT 79
                         90       100
                 ....*....|....*....|..
gi 569026720 379 YSFLARNPGGWRALTFELTLRY 400
Cdd:cd04975   80 YTFLASNSDVNAALAFEVYLNY 101
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
581-888 4.39e-23

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 223589 [Multi-domain]  Cd Length: 384  Bit Score: 102.51  E-value: 4.39e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 581 NLQFGKTLGAGAFGKVVEATAfglgkedaVLKVAVKMLKSTAHADEKEA--LMSELKIMSHLGQHENIVNLLGACTHGGP 658
Cdd:COG0515    1 SYRILRKLGEGSFGEVYLARD--------RKLVALKVLAKKLESKSKEVerFLREIQILASLNHPPNIVKLYDFFQDEGS 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 659 VLVITEYCCYGDLLNFLRRKaeamlgpslspgqdpeggvdyknihlekkyvrrdsgfssqgvdtyvemrpvstssndsfs 738
Cdd:COG0515   73 LYLVMEYVDGGSLEDLLKKI------------------------------------------------------------ 92
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 739 eqdldkEDGRPLELRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLT-NGHVAKIGDFGLARdIMNDSNYIVKGNARL 817
Cdd:COG0515   93 ------GRKGPLSESEALFILAQILSALEYLHSKGIIHRDIKPENILLDrDGRVVKLIDFGLAK-LLPDPGSTSSIPALP 165
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 569026720 818 PVK-----WMAPESIFDCV---YTVQSDVWSYGILLWEIFsLGLNPYPGILVNSKFYKLVKDGYQMAQPAFAPKNIYSI 888
Cdd:COG0515  166 STSvgtpgYMAPEVLLGLSlayASSSSDIWSLGITLYELL-TGLPPFEGEKNSSATSQTLKIILELPTPSLASPLSPSN 243
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
207-293 8.68e-13

Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of proteins of different functions. Examples include antibodies, the giant muscle kinase titin and receptor tyrosine kinases. Immunoglobulin-like domains may be involved in protein-protein and protein-ligand interactions.


Pssm-ID: 395002  Cd Length: 86  Bit Score: 64.91  E-value: 8.68e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720  207 LVPAELVRIRGEAAQIVCSASSVDVNFDVFLQHNNTKLAIPQQsDFHNNRYQKVLTLNLDQVDFQHAGNYSCVASNVQGK 286
Cdd:pfam00047   1 SAPPTVTVLEGDSATLTCSASTGSPGPDVTWSKEGGTLIESLK-VKHDNGRTTQSSLLISNVTKEDAGTYTCVVNNPGGS 79

                  ....*..
gi 569026720  287 HSTSMFF 293
Cdd:pfam00047  80 ATLSTSL 86
PHA03209 PHA03209
serine/threonine kinase US3; Provisional
742-860 1.24e-10

serine/threonine kinase US3; Provisional


Pssm-ID: 177557 [Multi-domain]  Cd Length: 357  Bit Score: 64.13  E-value: 1.24e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 742 LDKEDgRPLELRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDIMNDSNYI-VKGNarlpVK 820
Cdd:PHA03209 147 LTKRS-RPLPIDQALIIEKQILEGLRYLHAQRIIHRDVKTENIFINDVDQVCIGDLGAAQFPVVAPAFLgLAGT----VE 221
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 569026720 821 WMAPESIFDCVYTVQSDVWSYGILLWEIFSlglnpYPGIL 860
Cdd:PHA03209 222 TNAPEVLARDKYNSKADIWSAGIVLFEMLA-----YPSTI 256
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
745-847 6.09e-08

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 411126 [Multi-domain]  Cd Length: 563  Bit Score: 56.34  E-value: 6.09e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 745 EDGRPLELRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDImnDSNYIVKGNARL-PVKWMA 823
Cdd:NF033483  99 REHGPLSPEEAVEIMIQILSALEHAHRNGIVHRDIKPQNILITKDGRVKVTDFGIARAL--SSTTMTQTNSVLgTVHYLS 176
                         90       100
                 ....*....|....*....|....
gi 569026720 824 PESIFDCVYTVQSDVWSYGILLWE 847
Cdd:NF033483 177 PEQARGGTVDARSDIYSLGIVLYE 200
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
21-85 6.77e-08

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 433584 [Multi-domain]  Cd Length: 75  Bit Score: 50.66  E-value: 6.77e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 569026720   21 PVIEPSVPELVVKPGATVTLRCVGNGS----VEW--DGPPSPHWTLYSDGSSSILSTNNATFQNTGTYRCT 85
Cdd:pfam13927   2 PVITVSPSSVVVVEGETVTLTCEASGSppptITWykNGGKLSSGRTSLVGGNGTLTISNVTREDSGTYTCT 72
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
28-85 1.12e-07

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: 50.20  E-value: 1.12e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 569026720    28 PELVVKPGATVTLRCVGNGS----VEW--DGP----PSPHWTLYSDGSSSILSTNNATFQNTGTYRCT 85
Cdd:smart00410   2 PSVTVKEGESVTLSCEASGSpppeVTWykQGGkllaESGRFSVSRSGSTSTLTISNVTPEDSGTYTCA 69
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
209-290 2.73e-06

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: 46.34  E-value: 2.73e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720   209 PAELVRIRGEAAQIVCSASSvDVNFDVFLQHNNTKLaIPQQSDFHNNRYQKVLTLNLDQVDFQHAGNYSCVASNVQGKHS 288
Cdd:smart00410   1 PPSVTVKEGESVTLSCEASG-SPPPEVTWYKQGGKL-LAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSAS 78

                   ..
gi 569026720   289 TS 290
Cdd:smart00410  79 SG 80
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
401-489 6.68e-06

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 433584 [Multi-domain]  Cd Length: 75  Bit Score: 44.88  E-value: 6.68e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720  401 PPEVSV----IWTFINGSGTLLCAASGYPQPNVTWLQCSghtdrcdeaqvlqvwddpypEVLSQEPFHKVTVQSLLTVE- 475
Cdd:pfam13927   1 KPVITVspssVVVVEGETVTLTCEASGSPPPTITWYKNG--------------------GKLSSGRTSLVGGNGTLTISn 60
                          90
                  ....*....|....*
gi 569026720  476 -TLEHNQTYECRAHN 489
Cdd:pfam13927  61 vTREDSGTYTCTASN 75
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
416-492 9.37e-06

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: 44.24  E-value: 9.37e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 569026720 416 TLLCAASGYPQPNVTWLqcsghtdrcdeaqvlqvWDDPYPEVLSQEPFHKVTVQSLLTVE--TLEHNQTYECRAHNSVG 492
Cdd:cd00096    2 TLTCSASGNPPPTITWY-----------------KNGKPLPPSSRDSRRSELGNGTLTISnvTLEDSGTYTCVASNSAG 63
Ig1_FcgammaR_like cd05752
First immunoglobulin (Ig)-like domain of Fcgamma-receptors (FcgammaRs), and similar domains; ...
35-101 3.30e-05

First immunoglobulin (Ig)-like domain of Fcgamma-receptors (FcgammaRs), and similar domains; The members here are composed of the first immunoglobulin (Ig)-like domain of Fcgamma-receptors (FcgammaRs). Interactions between IgG and FcgammaR are important to the initiation of cellular and humoral response. IgG binding to FcgammaR leads to a cascade of signals and ultimately to functions such as antibody-dependent-cellular-cytotoxicity (ADCC), endocytosis, phagocytosis, release of inflammatory mediators, etc. FcgammaR has two Ig-like domains. This group also contains FcepsilonRI which binds IgE with high affinity.


Pssm-ID: 409410 [Multi-domain]  Cd Length: 79  Bit Score: 43.12  E-value: 3.30e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 569026720  35 GATVTLRCVGNGSVEwdgPPSPHW----TLYSDGSSSIlSTNNATFQNTGTYRCTEPGDPLggSAAIHLYV 101
Cdd:cd05752   15 GEKVTLTCQGFYSPE---QNSTQWyhngTLISSTSSSY-RIVAATVNDSGEYRCQTQGSSL--SDPVHLEV 79
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
401-495 1.12e-03

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: 38.64  E-value: 1.12e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720   401 PPEVSViwtFINGSGTLLCAASGYPQPNVTWLQcsghtdrcdeaqvlqvwddPYPEVLSQEPFHKVTVQSL---LTVE-- 475
Cdd:smart00410   1 PPSVTV---KEGESVTLSCEASGSPPPEVTWYK-------------------QGGKLLAESGRFSVSRSGStstLTISnv 58
                           90       100
                   ....*....|....*....|
gi 569026720   476 TLEHNQTYECRAHNSVGSGS 495
Cdd:smart00410  59 TPEDSGTYTCAATNSSGSAS 78
 
Name Accession Description Interval E-value
PTKc_CSF-1R cd05106
Catalytic domain of the Protein Tyrosine Kinase, Colony-Stimulating Factor-1 Receptor; PTKs ...
543-914 0e+00

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: 776.33  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 543 KPKYQVRWKIIESYEGNSYTFIDPTQLPYNEKWEFPRNNLQFGKTLGAGAFGKVVEATAFGLGKEDAVLKVAVKMLKSTA 622
Cdd:cd05106    1 KPKYEIRWKIIEAAEGNNYTFIDPTQLPYNEKWEFPRDNLQFGKTLGAGAFGKVVEATAFGLGKEDNVLRVAVKMLKASA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 623 HADEKEALMSELKIMSHLGQHENIVNLLGACTHGGPVLVITEYCCYGDLLNFLRRKAEAMLGPSLSPGQDPEGGVDYKNI 702
Cdd:cd05106   81 HTDEREALMSELKILSHLGQHKNIVNLLGACTHGGPVLVITEYCCYGDLLNFLRKKAETFLNFVMALPEISETSSDYKNI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 703 HLEKKYVRRDSGFSSQGVDTYVEMRPVSTSSNDSF-SEQDLDKEDGRPLELRDLLHFSSQVAQGMAFLASKNCIHRDVAA 781
Cdd:cd05106  161 TLEKKYIRSDSGFSSQGSDTYVEMRPVSSSSSQSSdSKDEEDTEDSWPLDLDDLLRFSSQVAQGMDFLASKNCIHRDVAA 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 782 RNVLLTNGHVAKIGDFGLARDIMNDSNYIVKGNARLPVKWMAPESIFDCVYTVQSDVWSYGILLWEIFSLGLNPYPGILV 861
Cdd:cd05106  241 RNVLLTDGRVAKICDFGLARDIMNDSNYVVKGNARLPVKWMAPESIFDCVYTVQSDVWSYGILLWEIFSLGKSPYPGILV 320
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 569026720 862 NSKFYKLVKDGYQMAQPAFAPKNIYSIMQACWALEPTHRPTFQQICSFLQEQA 914
Cdd:cd05106  321 NSKFYKMVKRGYQMSRPDFAPPEIYSIMKMCWNLEPTERPTFSQISQLIQRQL 373
PTKc_PDGFR cd05055
Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; ...
546-914 0e+00

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: 624.89  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 546 YQVRWKIIESYEGNSYTFIDPTQLPYNEKWEFPRNNLQFGKTLGAGAFGKVVEATAFGLGKEDAVLKVAVKMLKSTAHAD 625
Cdd:cd05055    1 YEVRWKVIESINGNEYVYIDPTQLPYDLKWEFPRNNLSFGKTLGAGAFGKVVEATAYGLSKSDAVMKVAVKMLKPTAHSS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 626 EKEALMSELKIMSHLGQHENIVNLLGACTHGGPVLVITEYCCYGDLLNFLRRKAEAMLgpslspgqdpeggvdyknihle 705
Cdd:cd05055   81 EREALMSELKIMSHLGNHENIVNLLGACTIGGPILVITEYCCYGDLLNFLRRKRESFL---------------------- 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 706 kkyvrrdsgfssqgvdtyvemrpvstssndsfseqdldkedgrplELRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVL 785
Cdd:cd05055  139 ---------------------------------------------TLEDLLSFSYQVAKGMAFLASKNCIHRDLAARNVL 173
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 786 LTNGHVAKIGDFGLARDIMNDSNYIVKGNARLPVKWMAPESIFDCVYTVQSDVWSYGILLWEIFSLGLNPYPGILVNSKF 865
Cdd:cd05055  174 LTHGKIVKICDFGLARDIMNDSNYVVKGNARLPVKWMAPESIFNCVYTFESDVWSYGILLWEIFSLGSNPYPGMPVDSKF 253
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 569026720 866 YKLVKDGYQMAQPAFAPKNIYSIMQACWALEPTHRPTFQQICSFLQEQA 914
Cdd:cd05055  254 YKLIKEGYRMAQPEHAPAEIYDIMKTCWDADPLKRPTFKQIVQLIGKQL 302
PTKc_Kit cd05104
Catalytic domain of the Protein Tyrosine Kinase, Kit; PTKs catalyze the transfer of the ...
546-913 0e+00

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: 548.74  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 546 YQVRWKIIESYEGNSYTFIDPTQLPYNEKWEFPRNNLQFGKTLGAGAFGKVVEATAFGLGKEDAVLKVAVKMLKSTAHAD 625
Cdd:cd05104    1 YEIQWKVVEEINGNNYVYIDPTQLPYDHKWEFPRDRLRFGKTLGAGAFGKVVEATAYGLAKADSAMTVAVKMLKPSAHST 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 626 EKEALMSELKIMSHLGQHENIVNLLGACTHGGPVLVITEYCCYGDLLNFLRRKAEAMLGPSLspgQDPEGGVDYKNIHLE 705
Cdd:cd05104   81 EREALMSELKVLSYLGNHINIVNLLGACTVGGPTLVITEYCCYGDLLNFLRRKRDSFICPKF---EDLAEAALYRNLLHQ 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 706 KKyvrrdsgFSSQGVDTYVEMRP----VSTSSND--------SFSEQDLD----KEDGRPLELRDLLHFSSQVAQGMAFL 769
Cdd:cd05104  158 RE-------MACDSLNEYMDMKPsvsyVVPTKADkrrgvrsgSYVDQDVTseilEEDELALDTEDLLSFSYQVAKGMEFL 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 770 ASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDIMNDSNYIVKGNARLPVKWMAPESIFDCVYTVQSDVWSYGILLWEIF 849
Cdd:cd05104  231 ASKNCIHRDLAARNILLTHGRITKICDFGLARDIRNDSNYVVKGNARLPVKWMAPESIFECVYTFESDVWSYGILLWEIF 310
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 569026720 850 SLGLNPYPGILVNSKFYKLVKDGYQMAQPAFAPKNIYSIMQACWALEPTHRPTFQQICSFLQEQ 913
Cdd:cd05104  311 SLGSSPYPGMPVDSKFYKMIKEGYRMDSPEFAPSEMYDIMRSCWDADPLKRPTFKQIVQLIEQQ 374
PTKc_PDGFR_alpha cd05105
Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor alpha; ...
546-906 3.66e-147

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: 442.54  E-value: 3.66e-147
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 546 YQVRWKIIESY--EGNSYTFIDPTQLPYNEKWEFPRNNLQFGKTLGAGAFGKVVEATAFGLGKEDAVLKVAVKMLKSTAH 623
Cdd:cd05105    1 YEIRWRVIESIspDGHEYIYVDPMQLPYDSRWEFPRDGLVLGRILGSGAFGKVVEGTAYGLSRSQPVMKVAVKMLKPTAR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 624 ADEKEALMSELKIMSHLGQHENIVNLLGACTHGGPVLVITEYCCYGDLLNFLRRKAEAMLGP------------SLSPGQ 691
Cdd:cd05105   81 SSEKQALMSELKIMTHLGPHLNIVNLLGACTKSGPIYIITEYCFYGDLVNYLHKNRDNFLSRhpekpkkdldifGINPAD 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 692 DP---------EGGVDYKNIH----------LEKKYVRRDSGFSSQGVDtyvemRPVS-TSSNDSFSEQDLDKEDGRPLE 751
Cdd:cd05105  161 EStrsyvilsfENKGDYMDMKqadttqyvpmLEIKEASKYSDIQRSNYD-----RPASyKGSNDSEVKNLLSDDGSEGLT 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 752 LRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDIMNDSNYIVKGNARLPVKWMAPESIFDCV 831
Cdd:cd05105  236 TLDLLSFTYQVARGMEFLASKNCVHRDLAARNVLLAQGKIVKICDFGLARDIMHDSNYVSKGSTFLPVKWMAPESIFDNL 315
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 569026720 832 YTVQSDVWSYGILLWEIFSLGLNPYPGILVNSKFYKLVKDGYQMAQPAFAPKNIYSIMQACWALEPTHRPTFQQI 906
Cdd:cd05105  316 YTTLSDVWSYGILLWEIFSLGGTPYPGMIVDSTFYNKIKSGYRMAKPDHATQEVYDIMVKCWNSEPEKRPSFLHL 390
PTKc_PDGFR_beta cd05107
Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor beta; ...
546-906 2.57e-145

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: 437.91  E-value: 2.57e-145
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 546 YQVRWKIIESY--EGNSYTFIDPTQLPYNEKWEFPRNNLQFGKTLGAGAFGKVVEATAFGLGKEDAVLKVAVKMLKSTAH 623
Cdd:cd05107    1 YEIRWKVIESVssDGHEYIYVDPMQLPYDSAWEMPRDNLVLGRTLGSGAFGRVVEATAHGLSHSQSTMKVAVKMLKSTAR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 624 ADEKEALMSELKIMSHLGQHENIVNLLGACTHGGPVLVITEYCCYGDLLNFLRRKAEAMLGPSLSPGQDPEG---GVDYK 700
Cdd:cd05107   81 SSEKQALMSELKIMSHLGPHLNIVNLLGACTKGGPIYIITEYCRYGDLVDYLHRNKHTFLQYYLDKNRDDGSlisGGSTP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 701 NIHLeKKYV----RRDSGFSSQGVD---TYVEMRP---------VSTSSNDSFSEQDLDKEDGRP-----------LELR 753
Cdd:cd05107  161 LSQR-KSHVslgsESDGGYMDMSKDesaDYVPMQDmkgtvkyadIESSNYESPYDQYLPSAPERTrrdtlinespaLSYM 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 754 DLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDIMNDSNYIVKGNARLPVKWMAPESIFDCVYT 833
Cdd:cd05107  240 DLVGFSYQVANGMEFLASKNCVHRDLAARNVLICEGKLVKICDFGLARDIMRDSNYISKGSTFLPLKWMAPESIFNNLYT 319
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 569026720 834 VQSDVWSYGILLWEIFSLGLNPYPGILVNSKFYKLVKDGYQMAQPAFAPKNIYSIMQACWALEPTHRPTFQQI 906
Cdd:cd05107  320 TLSDVWSFGILLWEIFTLGGTPYPELPMNEQFYNAIKRGYRMAKPAHASDEIYEIMQKCWEEKFEIRPDFSQL 392
PTKc_VEGFR cd05054
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
574-913 9.80e-130

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: 393.39  E-value: 9.80e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 574 KWEFPRNNLQFGKTLGAGAFGKVVEATAFGLGKEDAVLKVAVKMLKSTAHADEKEALMSELKIMSHLGQHENIVNLLGAC 653
Cdd:cd05054    1 KWEFPRDRLKLGKPLGRGAFGKVIQASAFGIDKSATCRTVAVKMLKEGATASEHKALMTELKILIHIGHHLNVVNLLGAC 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 654 TH-GGPVLVITEYCCYGDLLNFLRRKAEAMLGpslspgqdpeggvdYKNihlekkyvrrdsgfssqgvdtyvemrpvsTS 732
Cdd:cd05054   81 TKpGGPLMVIVEFCKFGNLSNYLRSKREEFVP--------------YRD-----------------------------KG 117
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 733 SNDSFSEQDLDKEDGRPLELRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDIMNDSNYIVK 812
Cdd:cd05054  118 ARDVEEEEDDDELYKEPLTLEDLICYSFQVARGMEFLASRKCIHRDLAARNILLSENNVVKICDFGLARDIYKDPDYVRK 197
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 813 GNARLPVKWMAPESIFDCVYTVQSDVWSYGILLWEIFSLGLNPYPGILVNSKFYKLVKDGYQMAQPAFAPKNIYSIMQAC 892
Cdd:cd05054  198 GDARLPLKWMAPESIFDKVYTTQSDVWSFGVLLWEIFSLGASPYPGVQMDEEFCRRLKEGTRMRAPEYTTPEIYQIMLDC 277
                        330       340
                 ....*....|....*....|.
gi 569026720 893 WALEPTHRPTFQQICSFLQEQ 913
Cdd:cd05054  278 WHGEPKERPTFSELVEKLGDL 298
Pkinase_Tyr pfam07714
Protein tyrosine kinase;
582-910 3.52e-129

Protein tyrosine kinase;


Pssm-ID: 429616 [Multi-domain]  Cd Length: 258  Bit Score: 390.32  E-value: 3.52e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720  582 LQFGKTLGAGAFGKVVEATAFGLGKEDAVlKVAVKMLKSTAHADEKEALMSELKIMSHLgQHENIVNLLGACTHGGPVLV 661
Cdd:pfam07714   1 LTLGEKLGEGAFGEVYKGTLKGEGENTKI-KVAVKTLKEGADEEEREDFLEEASIMKKL-DHPNIVKLLGVCTQGEPLYI 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720  662 ITEYCCYGDLLNFLRRKaeamlgpslspgqdpeggvdyknihlekkyvrrdsgfssqgvdtyvemrpvstssndsfseqd 741
Cdd:pfam07714  79 VTEYMPGGDLLDFLRKH--------------------------------------------------------------- 95
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720  742 ldkedGRPLELRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDIMNDSNYIVKGNARLPVKW 821
Cdd:pfam07714  96 -----KRKLTLKDLLSMALQIAKGMEYLESKNFVHRDLAARNCLVSENLVVKISDFGLSRDIYDDDYYRKRGGGKLPIKW 170
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720  822 MAPESIFDCVYTVQSDVWSYGILLWEIFSLGLNPYPGIlVNSKFYKLVKDGYQMAQPAFAPKNIYSIMQACWALEPTHRP 901
Cdd:pfam07714 171 MAPESLKDGKFTSKSDVWSFGVLLWEIFTLGEQPYPGM-SNEEVLEYLEDGYRLPQPENCPDELYDLMKQCWAYDPEDRP 249

                  ....*....
gi 569026720  902 TFQQICSFL 910
Cdd:pfam07714 250 TFSELVEDL 258
PTKc_VEGFR3 cd05102
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 3; ...
574-917 1.90e-124

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: 381.25  E-value: 1.90e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 574 KWEFPRNNLQFGKTLGAGAFGKVVEATAFGLGKEDAVLKVAVKMLKSTAHADEKEALMSELKIMSHLGQHENIVNLLGAC 653
Cdd:cd05102    1 QWEFPRDRLRLGKVLGHGAFGKVVEASAFGIDKSSSCETVAVKMLKEGATASEHKALMSELKILIHIGNHLNVVNLLGAC 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 654 TH-GGPVLVITEYCCYGDLLNFLRRKAEAmlgpsLSPGQD--PEGGVDYKNIHLEKKYVRRDSGFSSQGvdtyveMRPVS 730
Cdd:cd05102   81 TKpNGPLMVIVEFCKYGNLSNFLRAKREG-----FSPYRErsPRTRSQVRSMVEAVRADRRSRQGSDRV------ASFTE 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 731 TSSNDSFSEQDLDKEDGRPLELRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDIMNDSNYI 810
Cdd:cd05102  150 STSSTNQPRQEVDDLWQSPLTMEDLICYSFQVARGMEFLASRKCIHRDLAARNILLSENNVVKICDFGLARDIYKDPDYV 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 811 VKGNARLPVKWMAPESIFDCVYTVQSDVWSYGILLWEIFSLGLNPYPGILVNSKFYKLVKDGYQMAQPAFAPKNIYSIMQ 890
Cdd:cd05102  230 RKGSARLPLKWMAPESIFDKVYTTQSDVWSFGVLLWEIFSLGASPYPGVQINEEFCQRLKDGTRMRAPEYATPEIYRIML 309
                        330       340
                 ....*....|....*....|....*..
gi 569026720 891 ACWALEPTHRPTFQQICSFLQEQAQED 917
Cdd:cd05102  310 SCWHGDPKERPTFSDLVEILGDLLQEN 336
PTKc_VEGFR2 cd05103
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 2; ...
574-910 1.63e-122

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: 376.24  E-value: 1.63e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 574 KWEFPRNNLQFGKTLGAGAFGKVVEATAFGLGKEDAVLKVAVKMLKSTAHADEKEALMSELKIMSHLGQHENIVNLLGAC 653
Cdd:cd05103    1 KWEFPRDRLKLGKPLGRGAFGQVIEADAFGIDKTATCRTVAVKMLKEGATHSEHRALMSELKILIHIGHHLNVVNLLGAC 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 654 TH-GGPVLVITEYCCYGDLLNFLRRKAEAMLGPSLSPGQDPEGGVDYKNIHLEKKYvRRDSGFSSQGVDT--YVEMRPVS 730
Cdd:cd05103   81 TKpGGPLMVIVEFCKFGNLSAYLRSKRSEFVPYKTKGARFRQGKDYVGDISVDLKR-RLDSITSSQSSASsgFVEEKSLS 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 731 TSSNDSFSEQDLDKEdgrPLELRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDIMNDSNYI 810
Cdd:cd05103  160 DVEEEEAGQEDLYKD---FLTLEDLICYSFQVAKGMEFLASRKCIHRDLAARNILLSENNVVKICDFGLARDIYKDPDYV 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 811 VKGNARLPVKWMAPESIFDCVYTVQSDVWSYGILLWEIFSLGLNPYPGILVNSKFYKLVKDGYQMAQPAFAPKNIYSIMQ 890
Cdd:cd05103  237 RKGDARLPLKWMAPETIFDRVYTIQSDVWSFGVLLWEIFSLGASPYPGVKIDEEFCRRLKEGTRMRAPDYTTPEMYQTML 316
                        330       340
                 ....*....|....*....|
gi 569026720 891 ACWALEPTHRPTFQQICSFL 910
Cdd:cd05103  317 DCWHGEPSQRPTFSELVEHL 336
PTKc_VEGFR1 cd14207
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
574-906 5.23e-121

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: 372.41  E-value: 5.23e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 574 KWEFPRNNLQFGKTLGAGAFGKVVEATAFGLGKEDAVLKVAVKMLKSTAHADEKEALMSELKIMSHLGQHENIVNLLGAC 653
Cdd:cd14207    1 KWEFARERLKLGKSLGRGAFGKVVQASAFGIKKSPTCRVVAVKMLKEGATASEYKALMTELKILIHIGHHLNVVNLLGAC 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 654 T-HGGPVLVITEYCCYGDLLNFLRRKAEaMLGPSLSPGQDPEGGVDYKNIHLEK-KYVRRDSGFSSQGVDT--YVEMRPV 729
Cdd:cd14207   81 TkSGGPLMVIVEYCKYGNLSNYLKSKRD-FFVTNKDTSLQEELIKEKKEAEPTGgKKKRLESVTSSESFASsgFQEDKSL 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 730 STSSNDsfsEQDLDKEDGRPLELRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDIMNDSNY 809
Cdd:cd14207  160 SDVEEE---EEDSGDFYKRPLTMEDLISYSFQVARGMEFLSSRKCIHRDLAARNILLSENNVVKICDFGLARDIYKNPDY 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 810 IVKGNARLPVKWMAPESIFDCVYTVQSDVWSYGILLWEIFSLGLNPYPGILVNSKFYKLVKDGYQMAQPAFAPKNIYSIM 889
Cdd:cd14207  237 VRKGDARLPLKWMAPESIFDKIYSTKSDVWSYGVLLWEIFSLGASPYPGVQIDEDFCSKLKEGIRMRAPEFATSEIYQIM 316
                        330
                 ....*....|....*..
gi 569026720 890 QACWALEPTHRPTFQQI 906
Cdd:cd14207  317 LDCWQGDPNERPRFSEL 333
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
586-911 9.21e-119

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: 363.40  E-value: 9.21e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 586 KTLGAGAFGKVVEATAFGLGKEdaVLKVAVKMLKSTAHADEKEALMSELKIMSHLGqHENIVNLLGACTHGGPVLVITEY 665
Cdd:cd00192    1 KKLGEGAFGEVYKGKLKGGDGK--TVDVAVKTLKEDASESERKDFLKEARVMKKLG-HPNVVRLLGVCTEEEPLYLVMEY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 666 CCYGDLLNFLRRKaeamlgpslspgqdpeggvdyknihlekkyvrrdsgfssqgvdtyvemRPVSTSSNDSfseqdldke 745
Cdd:cd00192   78 MEGGDLLDFLRKS------------------------------------------------RPVFPSPEPS--------- 100
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 746 dgrPLELRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDIMNDSNYIVKGNARLPVKWMAPE 825
Cdd:cd00192  101 ---TLSLKDLLSFAIQIAKGMEYLASKKFVHRDLAARNCLVGEDLVVKISDFGLSRDIYDDDYYRKKTGGKLPIRWMAPE 177
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 826 SIFDCVYTVQSDVWSYGILLWEIFSLGLNPYPGIlVNSKFYKLVKDGYQMAQPAFAPKNIYSIMQACWALEPTHRPTFQQ 905
Cdd:cd00192  178 SLKDGIFTSKSDVWSFGVLLWEIFTLGATPYPGL-SNEEVLEYLRKGYRLPKPENCPDELYELMLSCWQLDPEDRPTFSE 256

                 ....*.
gi 569026720 906 ICSFLQ 911
Cdd:cd00192  257 LVERLE 262
PTKc_FGFR cd05053
Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs ...
569-906 1.14e-115

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: 356.73  E-value: 1.14e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 569 LPYNEKWEFPRNNLQFGKTLGAGAFGKVVEATAFGLGKE-DAVLKVAVKMLKSTAHADEKEALMSELKIMSHLGQHENIV 647
Cdd:cd05053    1 LPLDPEWELPRDRLTLGKPLGEGAFGQVVKAEAVGLDNKpNEVVTVAVKMLKDDATEKDLSDLVSEMEMMKMIGKHKNII 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 648 NLLGACTHGGPVLVITEYCCYGDLLNFLRRKaeamlgpslspgqdpeggvdyknihlekkyvrrdsgfssqgvdtyvemR 727
Cdd:cd05053   81 NLLGACTQDGPLYVVVEYASKGNLREFLRAR------------------------------------------------R 112
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 728 PVSTSSNdsfseQDLDKEDGRPLELRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDIMNDS 807
Cdd:cd05053  113 PPGEEAS-----PDDPRVPEEQLTQKDLVSFAYQVARGMEYLASKKCIHRDLAARNVLVTEDNVMKIADFGLARDIHHID 187
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 808 NYIVKGNARLPVKWMAPESIFDCVYTVQSDVWSYGILLWEIFSLGLNPYPGILVnSKFYKLVKDGYQMAQPAFAPKNIYS 887
Cdd:cd05053  188 YYRKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTLGGSPYPGIPV-EELFKLLKEGHRMEKPQNCTQELYM 266
                        330
                 ....*....|....*....
gi 569026720 888 IMQACWALEPTHRPTFQQI 906
Cdd:cd05053  267 LMRDCWHEVPSQRPTFKQL 285
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
582-910 2.89e-115

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: 354.16  E-value: 2.89e-115
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720   582 LQFGKTLGAGAFGKVVEATAFGLGKEdAVLKVAVKMLKSTAHADEKEALMSELKIMSHLgQHENIVNLLGACTHGGPVLV 661
Cdd:smart00221   1 LTLGKKLGEGAFGEVYKGTLKGKGDG-KEVEVAVKTLKEDASEQQIEEFLREARIMRKL-DHPNIVKLLGVCTEEEPLMI 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720   662 ITEYCCYGDLLNFLRrkaeamlgpslspgqdpeggvdyknihlekkyvrrdsgfssqgvdtyvemrpvstssndsfseqd 741
Cdd:smart00221  79 VMEYMPGGDLLDYLR----------------------------------------------------------------- 93
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720   742 ldKEDGRPLELRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDImNDSNYIVKGNARLPVKW 821
Cdd:smart00221  94 --KNRPKELSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGENLVVKISDFGLSRDL-YDDDYYKVKGGKLPIRW 170
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720   822 MAPESIFDCVYTVQSDVWSYGILLWEIFSLGLNPYPGIlVNSKFYKLVKDGYQMAQPAFAPKNIYSIMQACWALEPTHRP 901
Cdd:smart00221 171 MAPESLKEGKFTSKSDVWSFGVLLWEIFTLGEEPYPGM-SNAEVLEYLKKGYRLPKPPNCPPELYKLMLQCWAEDPEDRP 249

                   ....*....
gi 569026720   902 TFQQICSFL 910
Cdd:smart00221 250 TFSELVEIL 258
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
582-910 1.07e-114

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


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 352.60  E-value: 1.07e-114
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720   582 LQFGKTLGAGAFGKVVEATAFGLGKeDAVLKVAVKMLKSTAHADEKEALMSELKIMSHLgQHENIVNLLGACTHGGPVLV 661
Cdd:smart00219   1 LTLGKKLGEGAFGEVYKGKLKGKGG-KKKVEVAVKTLKEDASEQQIEEFLREARIMRKL-DHPNVVKLLGVCTEEEPLYI 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720   662 ITEYCCYGDLLNFLRRKAEAmlgpslspgqdpeggvdyknihlekkyvrrdsgfssqgvdtyvemrpvstssndsfseqd 741
Cdd:smart00219  79 VMEYMEGGDLLSYLRKNRPK------------------------------------------------------------ 98
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720   742 ldkedgrpLELRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDIMNDSnYIVKGNARLPVKW 821
Cdd:smart00219  99 --------LSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGENLVVKISDFGLSRDLYDDD-YYRKRGGKLPIRW 169
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720   822 MAPESIFDCVYTVQSDVWSYGILLWEIFSLGLNPYPGIlVNSKFYKLVKDGYQMAQPAFAPKNIYSIMQACWALEPTHRP 901
Cdd:smart00219 170 MAPESLKEGKFTSKSDVWSFGVLLWEIFTLGEQPYPGM-SNEEVLEYLKNGYRLPQPPNCPPELYDLMLQCWAEDPEDRP 248

                   ....*....
gi 569026720   902 TFQQICSFL 910
Cdd:smart00219 249 TFSELVEIL 257
PTKc_FGFR4 cd05099
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4; PTKs ...
569-906 1.53e-98

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: 312.28  E-value: 1.53e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 569 LPYNEKWEFPRNNLQFGKTLGAGAFGKVVEATAFGLGKE--DAVLKVAVKMLKSTAHADEKEALMSELKIMSHLGQHENI 646
Cdd:cd05099    1 LPLDPKWEFPRDRLVLGKPLGEGCFGQVVRAEAYGIDKSrpDQTVTVAVKMLKDNATDKDLADLISEMELMKLIGKHKNI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 647 VNLLGACTHGGPVLVITEYCCYGDLLNFLRrkAEAMLGPSLSPgqdpeggvdyknihlekkyvrrdsgfssqgvdtyvem 726
Cdd:cd05099   81 INLLGVCTQEGPLYVIVEYAAKGNLREFLR--ARRPPGPDYTF------------------------------------- 121
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 727 rpvstssndsfseqDLDKEDGRPLELRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDIMND 806
Cdd:cd05099  122 --------------DITKVPEEQLSFKDLVSCAYQVARGMEYLESRRCIHRDLAARNVLVTEDNVMKIADFGLARGVHDI 187
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 807 SNYIVKGNARLPVKWMAPESIFDCVYTVQSDVWSYGILLWEIFSLGLNPYPGILVnSKFYKLVKDGYQMAQPAFAPKNIY 886
Cdd:cd05099  188 DYYKKTSNGRLPVKWMAPEALFDRVYTHQSDVWSFGILMWEIFTLGGSPYPGIPV-EELFKLLREGHRMDKPSNCTHELY 266
                        330       340
                 ....*....|....*....|
gi 569026720 887 SIMQACWALEPTHRPTFQQI 906
Cdd:cd05099  267 MLMRECWHAVPTQRPTFKQL 286
PTKc_FGFR2 cd05101
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs ...
568-906 4.37e-94

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: 300.39  E-value: 4.37e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 568 QLPYNEKWEFPRNNLQFGKTLGAGAFGKVVEATAFGLGKE--DAVLKVAVKMLKSTAHADEKEALMSELKIMSHLGQHEN 645
Cdd:cd05101   12 ELPEDPKWEFPRDKLTLGKPLGEGCFGQVVMAEAVGIDKDkpKEAVTVAVKMLKDDATEKDLSDLVSEMEMMKMIGKHKN 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 646 IVNLLGACTHGGPVLVITEYCCYGDLLNFLRrkaeamlgpslspGQDPEGgvdyknihLEKKYvrrdsgfssqgvdtyve 725
Cdd:cd05101   92 IINLLGACTQDGPLYVIVEYASKGNLREYLR-------------ARRPPG--------MEYSY----------------- 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 726 mrpvstssndsfseqDLDKEDGRPLELRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDIMN 805
Cdd:cd05101  134 ---------------DINRVPEEQMTFKDLVSCTYQLARGMEYLASQKCIHRDLAARNVLVTENNVMKIADFGLARDINN 198
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 806 DSNYIVKGNARLPVKWMAPESIFDCVYTVQSDVWSYGILLWEIFSLGLNPYPGILVnSKFYKLVKDGYQMAQPAFAPKNI 885
Cdd:cd05101  199 IDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLMWEIFTLGGSPYPGIPV-EELFKLLKEGHRMDKPANCTNEL 277
                        330       340
                 ....*....|....*....|.
gi 569026720 886 YSIMQACWALEPTHRPTFQQI 906
Cdd:cd05101  278 YMMMRDCWHAVPSQRPTFKQL 298
PTKc_FGFR1 cd05098
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 1; PTKs ...
568-906 1.83e-93

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: 298.46  E-value: 1.83e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 568 QLPYNEKWEFPRNNLQFGKTLGAGAFGKVVEATAFGLGKE--DAVLKVAVKMLKSTAHADEKEALMSELKIMSHLGQHEN 645
Cdd:cd05098    1 ELPEDPRWELPRDRLVLGKPLGEGCFGQVVLAEAIGLDKDkpNRVTKVAVKMLKSDATEKDLSDLISEMEMMKMIGKHKN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 646 IVNLLGACTHGGPVLVITEYCCYGDLLNFLRRKAEAMLGPSLSPGQDPEggvdyknihlekkyvrrdsgfssqgvdtyve 725
Cdd:cd05098   81 IINLLGACTQDGPLYVIVEYASKGNLREYLQARRPPGMEYCYNPSHNPE------------------------------- 129
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 726 mrpvstssndsfseqdldkedgRPLELRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDIMN 805
Cdd:cd05098  130 ----------------------EQLSSKDLVSCAYQVARGMEYLASKKCIHRDLAARNVLVTEDNVMKIADFGLARDIHH 187
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 806 DSNYIVKGNARLPVKWMAPESIFDCVYTVQSDVWSYGILLWEIFSLGLNPYPGILVnSKFYKLVKDGYQMAQPAFAPKNI 885
Cdd:cd05098  188 IDYYKKTTNGRLPVKWMAPEALFDRIYTHQSDVWSFGVLLWEIFTLGGSPYPGVPV-EELFKLLKEGHRMDKPSNCTNEL 266
                        330       340
                 ....*....|....*....|.
gi 569026720 886 YSIMQACWALEPTHRPTFQQI 906
Cdd:cd05098  267 YMMMRDCWHAVPSQRPTFKQL 287
PTKc_FGFR3 cd05100
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 3; PTKs ...
569-906 1.65e-91

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: 294.24  E-value: 1.65e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 569 LPYNEKWEFPRNNLQFGKTLGAGAFGKVVEATAFGLGKE--DAVLKVAVKMLKSTAHADEKEALMSELKIMSHLGQHENI 646
Cdd:cd05100    1 LPADPKWELSRTRLTLGKPLGEGCFGQVVMAEAIGIDKDkpNKPVTVAVKMLKDDATDKDLSDLVSEMEMMKMIGKHKNI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 647 VNLLGACTHGGPVLVITEYCCYGDLLNFLRRKaeamlgpslspgQDPegGVDYknihlekkyvrrdsgfssqgvdtyvem 726
Cdd:cd05100   81 INLLGACTQDGPLYVLVEYASKGNLREYLRAR------------RPP--GMDY--------------------------- 119
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 727 rpvstssndSFSEQDLDKEDgrpLELRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDIMND 806
Cdd:cd05100  120 ---------SFDTCKLPEEQ---LTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLVTEDNVMKIADFGLARDVHNI 187
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 807 SNYIVKGNARLPVKWMAPESIFDCVYTVQSDVWSYGILLWEIFSLGLNPYPGILVnSKFYKLVKDGYQMAQPAFAPKNIY 886
Cdd:cd05100  188 DYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTLGGSPYPGIPV-EELFKLLKEGHRMDKPANCTHELY 266
                        330       340
                 ....*....|....*....|
gi 569026720 887 SIMQACWALEPTHRPTFQQI 906
Cdd:cd05100  267 MIMRECWHAVPSQRPTFKQL 286
PTKc_RET cd05045
Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs ...
581-912 3.90e-88

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: 283.78  E-value: 3.90e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 581 NLQFGKTLGAGAFGKVVEATAFGLGKEDAVLKVAVKMLKSTAHADEKEALMSELKIMSHLgQHENIVNLLGACTHGGPVL 660
Cdd:cd05045    1 NLVLGKTLGEGEFGKVVKATAFRLKGRAGYTTVAVKMLKENASSSELRDLLSEFNLLKQV-NHPHVIKLYGACSQDGPLL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 661 VITEYCCYGDLLNFLR--RKAEamlgpslspgqdpeggvdyknihlekkyvrrdsgfssqgvdtyvemrPVSTSSNDSFS 738
Cdd:cd05045   80 LIVEYAKYGSLRSFLResRKVG-----------------------------------------------PSYLGSDGNRN 112
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 739 EQDLDKEDGRPLELRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDIMNDSNYIVKGNARLP 818
Cdd:cd05045  113 SSYLDNPDERALTMGDLISFAWQISRGMQYLAEMKLVHRDLAARNVLVAEGRKMKISDFGLSRDVYEEDSYVKRSKGRIP 192
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 819 VKWMAPESIFDCVYTVQSDVWSYGILLWEIFSLGLNPYPGIlVNSKFYKLVKDGYQMAQPAFAPKNIYSIMQACWALEPT 898
Cdd:cd05045  193 VKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTLGGNPYPGI-APERLFNLLKTGYRMERPENCSEEMYNLMLTCWKQEPD 271
                        330
                 ....*....|....
gi 569026720 899 HRPTFQQICSFLQE 912
Cdd:cd05045  272 KRPTFADISKELEK 285
PTKc_InsR_like cd05032
Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer ...
575-912 2.37e-76

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: 251.49  E-value: 2.37e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 575 WEFPRNNLQFGKTLGAGAFGKVVEATAFGLGKEDAVLKVAVKMLKSTAHADEKEALMSELKIMSHLGQHeNIVNLLGACT 654
Cdd:cd05032    1 WELPREKITLIRELGQGSFGMVYEGLAKGVVKGEPETRVAIKTVNENASMRERIEFLNEASVMKEFNCH-HVVRLLGVVS 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 655 HGGPVLVITEYCCYGDLLNFLRrkaeamlgpSLSPGQDPEGGVDyknihlekkyvrrdsgfssqgvdtyvemrpvstssn 734
Cdd:cd05032   80 TGQPTLVVMELMAKGDLKSYLR---------SRRPEAENNPGLG------------------------------------ 114
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 735 dsfseqdldkedgrPLELRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDIMNDSNYIVKGN 814
Cdd:cd05032  115 --------------PPTLQKFIQMAAEIADGMAYLAAKKFVHRDLAARNCMVAEDLTVKIGDFGMTRDIYETDYYRKGGK 180
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 815 ARLPVKWMAPESIFDCVYTVQSDVWSYGILLWEIFSLGLNPYPGiLVNSKFYKLVKDGYQMAQPAFAPKNIYSIMQACWA 894
Cdd:cd05032  181 GLLPVRWMAPESLKDGVFTTKSDVWSFGVVLWEMATLAEQPYQG-LSNEEVLKFVIDGGHLDLPENCPDKLLELMRMCWQ 259
                        330
                 ....*....|....*...
gi 569026720 895 LEPTHRPTFQQICSFLQE 912
Cdd:cd05032  260 YNPKMRPTFLEIVSSLKD 277
PTKc_ALK_LTK cd05036
Catalytic domain of the Protein Tyrosine Kinases, Anaplastic Lymphoma Kinase and Leukocyte ...
576-911 6.96e-74

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: 244.60  E-value: 6.96e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 576 EFPRNNLQFGKTLGAGAFGKVVEATAFGLGKEDAVLKVAVKML-KSTAHADEKEALMSELkIMSHLgQHENIVNLLGACT 654
Cdd:cd05036    2 EVPRKNLTLIRALGQGAFGEVYEGTVSGMPGDPSPLQVAVKTLpELCSEQDEMDFLMEAL-IMSKF-NHPNIVRCIGVCF 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 655 HGGPVLVITEYCCYGDLLNFLRrkaeamlgpslspgqdpeggvdyknihlekkyvrrdsgfssqgvdtyvEMRPVSTSSN 734
Cdd:cd05036   80 QRLPRFILLELMAGGDLKSFLR------------------------------------------------ENRPRPEQPS 111
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 735 dsfseqdldkedgrPLELRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTN---GHVAKIGDFGLARDIMNDSNYIV 811
Cdd:cd05036  112 --------------SLTMLDLLQLAQDVAKGCRYLEENHFIHRDIAARNCLLTCkgpGRVAKIGDFGMARDIYRADYYRK 177
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 812 KGNARLPVKWMAPESIFDCVYTVQSDVWSYGILLWEIFSLGLNPYPGiLVNSKFYKLVKDGYQMAQPAFAPKNIYSIMQA 891
Cdd:cd05036  178 GGKAMLPVKWMPPEAFLDGIFTSKTDVWSFGVLLWEIFSLGYMPYPG-KSNQEVMEFVTSGGRMDPPKNCPGPVYRIMTQ 256
                        330       340
                 ....*....|....*....|
gi 569026720 892 CWALEPTHRPTFQQICSFLQ 911
Cdd:cd05036  257 CWQHIPEDRPNFSTILERLN 276
PTKc_Src_like cd05034
Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
586-910 7.13e-74

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: 243.34  E-value: 7.13e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 586 KTLGAGAFGKVVEatafglGKEDAVLKVAVKMLKStaHADEKEALMSELKIMSHLgQHENIVNLLGACTHGGPVLVITEY 665
Cdd:cd05034    1 KKLGAGQFGEVWM------GVWNGTTKVAVKTLKP--GTMSPEAFLQEAQIMKKL-RHDKLVQLYAVCSDEEPIYIVTEL 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 666 CCYGDLLNFLRrkaeamlgpslspgqdpeggvdyknihlekkyvrrdsgfssqgvdtyvemrpvstssndsfseqdldKE 745
Cdd:cd05034   72 MSKGSLLDYLR-------------------------------------------------------------------TG 84
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 746 DGRPLELRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDIMNDSnYIVKGNARLPVKWMAPE 825
Cdd:cd05034   85 EGRALRLPQLIDMAAQIASGMAYLESRNYIHRDLAARNILVGENNVCKVADFGLARLIEDDE-YTAREGAKFPIKWTAPE 163
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 826 SIFDCVYTVQSDVWSYGILLWEIFSLGLNPYPGiLVNSKFYKLVKDGYQMAQPAFAPKNIYSIMQACWALEPTHRPTFQQ 905
Cdd:cd05034  164 AALYGRFTIKSDVWSFGILLYEIVTYGRVPYPG-MTNREVLEQVERGYRMPKPPGCPDELYDIMLQCWKKEPEERPTFEY 242

                 ....*
gi 569026720 906 ICSFL 910
Cdd:cd05034  243 LQSFL 247
PTKc_Ror cd05048
Catalytic Domain of the Protein Tyrosine Kinases, Receptor tyrosine kinase-like Orphan ...
576-911 1.18e-71

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: 238.81  E-value: 1.18e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 576 EFPRNNLQFGKTLGAGAFGKVVEATAFGLGKEDAVLKVAVKMLKSTAHADEKEALMSELKIMSHLgQHENIVNLLGACTH 655
Cdd:cd05048    1 EIPLSAVRFLEELGEGAFGKVYKGELLGPSSEESAISVAIKTLKENASPKTQQDFRREAELMSDL-QHPNIVCLLGVCTK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 656 GGPVLVITEYCCYGDLLNFLRRKaeamlgpslSPGQDPEGGVDyknihlekkyvrrdsgfssqgvdtyvemrpvstssnd 735
Cdd:cd05048   80 EQPQCMLFEYMAHGDLHEFLVRH---------SPHSDVGVSSD------------------------------------- 113
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 736 sfseqdlDKEDGRPLELRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDIMNDSNYIVKGNA 815
Cdd:cd05048  114 -------DDGTASSLDQSDFLHIAIQIAAGMEYLSSHHYVHRDLAARNCLVGDGLTVKISDFGLSRDIYSSDYYRVQSKS 186
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 816 RLPVKWMAPESIFDCVYTVQSDVWSYGILLWEIFSLGLNPYPGiLVNSKFYKLVKDGYQMAQPAFAPKNIYSIMQACWAL 895
Cdd:cd05048  187 LLPVRWMPPEAILYGKFTTESDVWSFGVVLWEIFSYGLQPYYG-YSNQEVIEMIRSRQLLPCPEDCPARVYSLMVECWHE 265
                        330
                 ....*....|....*.
gi 569026720 896 EPTHRPTFQQICSFLQ 911
Cdd:cd05048  266 IPSRRPRFKEIHTRLR 281
PTKc_Csk_like cd05039
Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
575-911 1.26e-71

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: 237.63  E-value: 1.26e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 575 WEFPRNNLQFGKTLGAGAFGKVVEATAFGLgkedavlKVAVKMLKStaHADEKEALMSELKIMSHLgQHENIVNLLGACT 654
Cdd:cd05039    1 WAINKKDLKLGELIGKGEFGDVMLGDYRGQ-------KVAVKCLKD--DSTAAQAFLAEASVMTTL-RHPNLVQLLGVVL 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 655 HGGPVLVITEYCCYGDLLNFLRrkaeamlgpslspgqdpeggvdyknihlekkyvrrdsgfsSQGvdtyvemRPVstssn 734
Cdd:cd05039   71 EGNGLYIVTEYMAKGSLVDYLR----------------------------------------SRG-------RAV----- 98
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 735 dsfseqdldkedgrpLELRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDimndSNYIVKGn 814
Cdd:cd05039   99 ---------------ITRKDQLGFALDVCEGMEYLESKKFVHRDLAARNVLVSEDNVAKVSDFGLAKE----ASSNQDG- 158
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 815 ARLPVKWMAPESIFDCVYTVQSDVWSYGILLWEIFSLGLNPYPGILVnSKFYKLVKDGYQMAQPAFAPKNIYSIMQACWA 894
Cdd:cd05039  159 GKLPIKWTAPEALREKKFSTKSDVWSFGILLWEIYSFGRVPYPRIPL-KDVVPHVEKGYRMEAPEGCPPEVYKVMKNCWE 237
                        330
                 ....*....|....*..
gi 569026720 895 LEPTHRPTFQQICSFLQ 911
Cdd:cd05039  238 LDPAKRPTFKQLREKLE 254
PTKc_Musk cd05050
Catalytic domain of the Protein Tyrosine Kinase, Muscle-specific kinase; PTKs catalyze the ...
576-911 3.78e-71

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: 237.42  E-value: 3.78e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 576 EFPRNNLQFGKTLGAGAFGKVVEATAFGLGKEDAVLKVAVKMLKSTAHADEKEALMSELKIMSHLgQHENIVNLLGACTH 655
Cdd:cd05050    1 EYPRNNIEYVRDIGQGAFGRVFQARAPGLLPYEPFTMVAVKMLKEEASADMQADFQREAALMAEF-DHPNIVKLLGVCAV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 656 GGPVLVITEYCCYGDLLNFLRRKaeamlgpslSPgqdpeggvdyknihlekkyvrrdsgfssqgvdtyvemRPVSTSSND 735
Cdd:cd05050   80 GKPMCLLFEYMAYGDLNEFLRHR---------SP-------------------------------------RAQCSLSHS 113
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 736 SFSeqdLDKEDGRPLELR--DLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDIMNDSNYIVKG 813
Cdd:cd05050  114 TSS---ARKCGLNPLPLSctEQLCIAKQVAAGMAYLSERKFVHRDLATRNCLVGENMVVKIADFGLSRNIYSADYYKASE 190
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 814 NARLPVKWMAPESIFDCVYTVQSDVWSYGILLWEIFSLGLNPYPGiLVNSKFYKLVKDGYQMAQPAFAPKNIYSIMQACW 893
Cdd:cd05050  191 NDAIPIRWMPPESIFYNRYTTESDVWAYGVVLWEIFSYGMQPYYG-MAHEEVIYYVRDGNVLSCPDNCPLELYNLMRLCW 269
                        330
                 ....*....|....*...
gi 569026720 894 ALEPTHRPTFQQICSFLQ 911
Cdd:cd05050  270 SKLPSDRPSFASINRILQ 287
PTKc_Frk_like cd05068
Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
573-912 8.13e-70

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: 233.07  E-value: 8.13e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 573 EKWEFPRNNLQFGKTLGAGAFGKVVEatafglGKEDAVLKVAVKMLKsTAHADEKEALmSELKIMSHLgQHENIVNLLGA 652
Cdd:cd05068    1 DQWEIDRKSLKLLRKLGSGQFGEVWE------GLWNNTTPVAVKTLK-PGTMDPEDFL-REAQIMKKL-RHPKLIQLYAV 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 653 CTHGGPVLVITEYCCYGDLLNFLRRKaeamlgpslspgqdpeggvdyknihlekkyvrrdsgfssqgvdtyvemrpvsts 732
Cdd:cd05068   72 CTLEEPIYIITELMKHGSLLEYLQGK------------------------------------------------------ 97
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 733 sndsfseqdldkedGRPLELRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDIMNDSNYIVK 812
Cdd:cd05068   98 --------------GRSLQLPQLIDMAAQVASGMAYLESQNYIHRDLAARNVLVGENNICKVADFGLARVIKVEDEYEAR 163
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 813 GNARLPVKWMAPESIFDCVYTVQSDVWSYGILLWEIFSLGLNPYPGiLVNSKFYKLVKDGYQMAQPAFAPKNIYSIMQAC 892
Cdd:cd05068  164 EGAKFPIKWTAPEAANYNRFSIKSDVWSFGILLTEIVTYGRIPYPG-MTNAEVLQQVERGYRMPCPPNCPPQLYDIMLEC 242
                        330       340
                 ....*....|....*....|
gi 569026720 893 WALEPTHRPTFQQICSFLQE 912
Cdd:cd05068  243 WKADPMERPTFETLQWKLED 262
PTKc_DDR cd05051
Catalytic domain of the Protein Tyrosine Kinases, Discoidin Domain Receptors; PTKs catalyze ...
576-912 6.77e-68

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: 228.76  E-value: 6.77e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 576 EFPRNNLQFGKTLGAGAFGKVVEATAFGL-----------GKEDAVLKVAVKMLKSTAHADEKEALMSELKIMSHLgQHE 644
Cdd:cd05051    1 EFPREKLEFVEKLGEGQFGEVHLCEANGLsdltsddfignDNKDEPVLVAVKMLRPDASKNAREDFLKEVKIMSQL-KDP 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 645 NIVNLLGACTHGGPVLVITEYCCYGDLLNFLRrkaeamlgpslspgqdpeggvdyknihlekKYVrrdsgfssqgvdtyv 724
Cdd:cd05051   80 NIVRLLGVCTRDEPLCMIVEYMENGDLNQFLQ------------------------------KHE--------------- 114
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 725 emrpvstssndsFSEQDLDKEDGRPLELRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDIM 804
Cdd:cd05051  115 ------------AETQGASATNSKTLSYGTLLYMATQIASGMKYLESLNFVHRDLATRNCLVGPNYTIKIADFGMSRNLY 182
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 805 NDSNYIVKGNARLPVKWMAPESIFDCVYTVQSDVWSYGILLWEIFSLG-LNPYP-----GILVN-SKFYKlvKDGYQ--M 875
Cdd:cd05051  183 SGDYYRIEGRAVLPIRWMAWESILLGKFTTKSDVWAFGVTLWEILTLCkEQPYEhltdeQVIENaGEFFR--DDGMEvyL 260
                        330       340       350
                 ....*....|....*....|....*....|....*..
gi 569026720 876 AQPAFAPKNIYSIMQACWALEPTHRPTFQQICSFLQE 912
Cdd:cd05051  261 SRPPNCPKEIYELMLECWRRDEEDRPTFREIHLFLQR 297
PTKc_Trk cd05049
Catalytic domain of the Protein Tyrosine Kinases, Tropomyosin Related Kinases; PTKs catalyze ...
576-912 1.26e-67

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: 227.73  E-value: 1.26e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 576 EFPRNNLQFGKTLGAGAFGKVVEATAFGLGKEDAVLKVAVKMLKSTAHADEKEALMSELKIMSHLgQHENIVNLLGACTH 655
Cdd:cd05049    1 HIKRDTIVLKRELGEGAFGKVFLGECYNLEPEQDKMLVAVKTLKDASSPDARKDFEREAELLTNL-QHENIVKFYGVCTE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 656 GGPVLVITEYCCYGDLLNFLRRKaeamlGPSLspgqdpeggvdyknihlekkyvrrdsgfssqgvdtyvemrpVSTSSND 735
Cdd:cd05049   80 GDPLLMVFEYMEHGDLNKFLRSH-----GPDA-----------------------------------------AFLASED 113
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 736 SfseqdldkeDGRPLELRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDIMNDSNYIVKGNA 815
Cdd:cd05049  114 S---------APGELTLSQLLHIAVQIASGMVYLASQHFVHRDLATRNCLVGTNLVVKIGDFGMSRDIYSTDYYRVGGHT 184
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 816 RLPVKWMAPESIFDCVYTVQSDVWSYGILLWEIFSLGLNPYPGiLVNSKFYKLVKDGYQMAQPAFAPKNIYSIMQACWAL 895
Cdd:cd05049  185 MLPIRWMPPESILYRKFTTESDVWSFGVVLWEIFTYGKQPWFQ-LSNTEVIECITQGRLLQRPRTCPSEVYAVMLGCWKR 263
                        330
                 ....*....|....*..
gi 569026720 896 EPTHRPTFQQICSFLQE 912
Cdd:cd05049  264 EPQQRLNIKDIHKRLQE 280
PTKc_c-ros cd05044
Catalytic domain of the Protein Tyrosine Kinase, C-ros; PTKs catalyze the transfer of the ...
586-912 2.33e-67

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: 226.53  E-value: 2.33e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 586 KTLGAGAFGKVVEATAFG-LGKEDAVLKVAVKMLKSTAHADEKEALMSELKIMSHLgQHENIVNLLGACTHGGPVLVITE 664
Cdd:cd05044    1 KFLGSGAFGEVFEGTAKDiLGDGSGETKVAVKTLRKGATDQEKAEFLKEAHLMSNF-KHPNILKLLGVCLDNDPQYIILE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 665 YCCYGDLLNFLRR-KAEAMLGPSLSpgqdpeggvdyknihlekkyvrrdsgfssqgvdtyvemrpvstssndsfseqdld 743
Cdd:cd05044   80 LMEGGDLLSYLRAaRPTAFTPPLLT------------------------------------------------------- 104
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 744 kedgrpleLRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLT--NGH--VAKIGDFGLARDIMNDSNYIVKGNARLPV 819
Cdd:cd05044  105 --------LKDLLSICVDVAKGCVYLEDMHFVHRDLAARNCLVSskDYRerVVKIGDFGLARDIYKNDYYRKEGEGLLPV 176
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 820 KWMAPESIFDCVYTVQSDVWSYGILLWEIFSLGLNPYPGiLVNSKFYKLVKDGYQMAQPAFAPKNIYSIMQACWALEPTH 899
Cdd:cd05044  177 RWMAPESLVDGVFTTQSDVWAFGVLMWEILTLGQQPYPA-RNNLEVLHFVRAGGRLDQPDNCPDDLYELMLRCWSTDPEE 255
                        330
                 ....*....|...
gi 569026720 900 RPTFQQICSFLQE 912
Cdd:cd05044  256 RPSFARILEQLQN 268
PTKc_Srm_Brk cd05148
Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal ...
575-903 2.26e-65

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: 220.77  E-value: 2.26e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 575 WEFPRNNLQFGKTLGAGAFGKVVEatafglGKEDAVLKVAVKMLKS--TAHADEkeaLMSELKIMSHLgQHENIVNLLGA 652
Cdd:cd05148    1 WERPREEFTLERKLGSGYFGEVWE------GLWKNRVRVAIKILKSddLLKQQD---FQKEVQALKRL-RHKHLISLFAV 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 653 CTHGGPVLVITEYCCYGDLLNFLRrkaeamlgpslspgqDPEGgvdyknihlekkyvrrdsgfssqgvdtyvemrpvsts 732
Cdd:cd05148   71 CSVGEPVYIITELMEKGSLLAFLR---------------SPEG------------------------------------- 98
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 733 sndsfseqdldkedgRPLELRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARdIMNDSNYIVK 812
Cdd:cd05148   99 ---------------QVLPVASLIDMACQVAEGMAYLEEQNSIHRDLAARNILVGEDLVCKVADFGLAR-LIKEDVYLSS 162
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 813 gNARLPVKWMAPESIFDCVYTVQSDVWSYGILLWEIFSLGLNPYPGILvNSKFYKLVKDGYQMAQPAFAPKNIYSIMQAC 892
Cdd:cd05148  163 -DKKIPYKWTAPEAASHGTFSTKSDVWSFGILLYEMFTYGQVPYPGMN-NHEVYDQITAGYRMPCPAKCPQEIYKIMLEC 240
                        330
                 ....*....|.
gi 569026720 893 WALEPTHRPTF 903
Cdd:cd05148  241 WAAEPEDRPSF 251
PTKc_Fes_like cd05041
Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; ...
588-911 3.08e-65

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: 220.01  E-value: 3.08e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 588 LGAGAFGKVVEATAFGLGkedavLKVAVKMLKSTAHADEKEALMSELKIMSHLgQHENIVNLLGACTHGGPVLVITEYCC 667
Cdd:cd05041    3 IGRGNFGDVYRGVLKPDN-----TEVAVKTCRETLPPDLKRKFLQEARILKQY-DHPNIVKLIGVCVQKQPIMIVMELVP 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 668 YGDLLNFLRRKaeamlGPSLSPGQdpeggvdyknihlekkyvrrdsgfssqgvdtyvemrpvstssndsfseqdldkedg 747
Cdd:cd05041   77 GGSLLTFLRKK-----GARLTVKQ-------------------------------------------------------- 95
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 748 rplelrdLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDiMNDSNYIVKGNAR-LPVKWMAPES 826
Cdd:cd05041   96 -------LLQMCLDAAAGMEYLESKNCIHRDLAARNCLVGENNVLKISDFGMSRE-EEDGEYTVSDGLKqIPIKWTAPEA 167
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 827 IFDCVYTVQSDVWSYGILLWEIFSLGLNPYPGiLVNSKFYKLVKDGYQMAQPAFAPKNIYSIMQACWALEPTHRPTFQQI 906
Cdd:cd05041  168 LNYGRYTSESDVWSFGILLWEIFSLGATPYPG-MSNQQTREQIESGYRMPAPELCPEAVYRLMLQCWAYDPENRPSFSEI 246

                 ....*
gi 569026720 907 CSFLQ 911
Cdd:cd05041  247 YNELQ 251
PTKc_InsR cd05061
Catalytic domain of the Protein Tyrosine Kinase, Insulin Receptor; PTKs catalyze the transfer ...
575-912 8.50e-64

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: 217.14  E-value: 8.50e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 575 WEFPRNNLQFGKTLGAGAFGKVVEATAFGLGKEDAVLKVAVKMLKSTAHADEKEALMSELKIMSHLGQHeNIVNLLGACT 654
Cdd:cd05061    1 WEVSREKITLLRELGQGSFGMVYEGNARDIIKGEAETRVAVKTVNESASLRERIEFLNEASVMKGFTCH-HVVRLLGVVS 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 655 HGGPVLVITEYCCYGDLLNFLRrkaeamlgpslspgqdpeggvdyknihlekkyvrrdsgfssqgvdtyvEMRPvstssn 734
Cdd:cd05061   80 KGQPTLVVMELMAHGDLKSYLR------------------------------------------------SLRP------ 105
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 735 dsfseqDLDKEDGRPL-ELRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDIMNDSNYIVKG 813
Cdd:cd05061  106 ------EAENNPGRPPpTLQEMIQMAAEIADGMAYLNAKKFVHRDLAARNCMVAHDFTVKIGDFGMTRDIYETDYYRKGG 179
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 814 NARLPVKWMAPESIFDCVYTVQSDVWSYGILLWEIFSLGLNPYPGiLVNSKFYKLVKDGYQMAQPAFAPKNIYSIMQACW 893
Cdd:cd05061  180 KGLLPVRWMAPESLKDGVFTTSSDMWSFGVVLWEITSLAEQPYQG-LSNEQVLKFVMDGGYLDQPDNCPERVTDLMRMCW 258
                        330
                 ....*....|....*....
gi 569026720 894 ALEPTHRPTFQQICSFLQE 912
Cdd:cd05061  259 QFNPKMRPTFLEIVNLLKD 277
PTKc_Abl cd05052
Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase; PTKs catalyze the transfer of ...
575-906 5.99e-63

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: 213.82  E-value: 5.99e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 575 WEFPRNNLQFGKTLGAGAFGKVVEATAFGLGKedavlKVAVKMLKSTAHADE---KEA-LMSELKimshlgqHENIVNLL 650
Cdd:cd05052    1 WEIERTDITMKHKLGGGQYGEVYEGVWKKYNL-----TVAVKTLKEDTMEVEeflKEAaVMKEIK-------HPNLVQLL 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 651 GACTHGGPVLVITEYCCYGDLLNFLRRKAEAMLGPSLspgqdpeggvdyknihlekkyvrrdsgfssqgvdtyvemrpvs 730
Cdd:cd05052   69 GVCTREPPFYIITEFMPYGNLLDYLRECNREELNAVV------------------------------------------- 105
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 731 tssndsfseqdldkedgrplelrdLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARdIMNDSNYI 810
Cdd:cd05052  106 ------------------------LLYMATQIASAMEYLEKKNFIHRDLAARNCLVGENHLVKVADFGLSR-LMTGDTYT 160
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 811 VKGNARLPVKWMAPESIFDCVYTVQSDVWSYGILLWEIFSLGLNPYPGILVnSKFYKLVKDGYQMAQPAFAPKNIYSIMQ 890
Cdd:cd05052  161 AHAGAKFPIKWTAPESLAYNKFSIKSDVWAFGVLLWEIATYGMSPYPGIDL-SQVYELLEKGYRMERPEGCPPKVYELMR 239
                        330
                 ....*....|....*.
gi 569026720 891 ACWALEPTHRPTFQQI 906
Cdd:cd05052  240 ACWQWNPSDRPSFAEI 255
PTKc_Tie cd05047
Catalytic domain of Tie Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
588-906 6.36e-63

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: 214.13  E-value: 6.36e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 588 LGAGAFGKVVEATafgLGKEDAVLKVAVKMLKSTAHADEKEALMSELKIMSHLGQHENIVNLLGACTHGGPVLVITEYCC 667
Cdd:cd05047    3 IGEGNFGQVLKAR---IKKDGLRMDAAIKRMKEYASKDDHRDFAGELEVLCKLGHHPNIINLLGACEHRGYLYLAIEYAP 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 668 YGDLLNFLRRKaeamlgpslspgqdpeggvdyknihlekKYVRRDSGFSSQGvdtyvemrpvSTSSNdsfseqdldkedg 747
Cdd:cd05047   80 HGNLLDFLRKS----------------------------RVLETDPAFAIAN----------STAST------------- 108
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 748 rpLELRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARdimNDSNYIVKGNARLPVKWMAPESI 827
Cdd:cd05047  109 --LSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGLSR---GQEVYVKKTMGRLPVRWMAIESL 183
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 569026720 828 FDCVYTVQSDVWSYGILLWEIFSLGLNPYPGiLVNSKFYKLVKDGYQMAQPAFAPKNIYSIMQACWALEPTHRPTFQQI 906
Cdd:cd05047  184 NYSVYTTNSDVWSYGVLLWEIVSLGGTPYCG-MTCAELYEKLPQGYRLEKPLNCDDEVYDLMRQCWREKPYERPSFAQI 261
PTKc_Syk_like cd05060
Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
586-910 1.17e-60

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: 207.20  E-value: 1.17e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 586 KTLGAGAFGKVVEATAfgLGKEDAVLKVAVKMLKSTAHADEKEALMSELKIMSHLgQHENIVNLLGACThGGPVLVITEY 665
Cdd:cd05060    1 KELGHGNFGSVRKGVY--LMKSGKEVEVAVKTLKQEHEKAGKKEFLREASVMAQL-DHPCIVRLIGVCK-GEPLMLVMEL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 666 CCYGDLLNFLRrkaeamlgpslspgqdpeggvDYKNIhlekkyvrrdsgfssqgvdtyvemrPVStssndsfseqdldke 745
Cdd:cd05060   77 APLGPLLKYLK---------------------KRREI-------------------------PVS--------------- 95
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 746 dgrplelrDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDIMNDSNYIVKGNA-RLPVKWMAP 824
Cdd:cd05060   96 --------DLKELAHQVAMGMAYLESKHFVHRDLAARNVLLVNRHQAKISDFGMSRALGAGSDYYRATTAgRWPLKWYAP 167
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 825 ESIFDCVYTVQSDVWSYGILLWEIFSLGLNPYPGIlVNSKFYKLVKDGYQMAQPAFAPKNIYSIMQACWALEPTHRPTFQ 904
Cdd:cd05060  168 ECINYGKFSSKSDVWSYGVTLWEAFSYGAKPYGEM-KGPEVIAMLESGERLPRPEECPQEIYSIMLSCWKYRPEDRPTFS 246

                 ....*.
gi 569026720 905 QICSFL 910
Cdd:cd05060  247 ELESTF 252
PTKc_Tie1 cd05089
Catalytic domain of the Protein Tyrosine Kinase, Tie1; Protein Tyrosine Kinase (PTK) family; ...
575-926 1.66e-60

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: 208.31  E-value: 1.66e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 575 WEfprnNLQFGKTLGAGAFGKVVEATafgLGKEDAVLKVAVKMLKSTAHADEKEALMSELKIMSHLGQHENIVNLLGACT 654
Cdd:cd05089    1 WE----DIKFEDVIGEGNFGQVIKAM---IKKDGLKMNAAIKMLKEFASENDHRDFAGELEVLCKLGHHPNIINLLGACE 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 655 HGGPVLVITEYCCYGDLLNFLRRKAEAMLGPSLSpgqdpeggvdyknihlekkyvrRDSGFSSQgvdtyvemrpvstssn 734
Cdd:cd05089   74 NRGYLYIAIEYAPYGNLLDFLRKSRVLETDPAFA----------------------KEHGTAST---------------- 115
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 735 dsfseqdldkedgrpLELRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARdimNDSNYIVKGN 814
Cdd:cd05089  116 ---------------LTSQQLLQFASDVAKGMQYLSEKQFIHRDLAARNVLVGENLVSKIADFGLSR---GEEVYVKKTM 177
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 815 ARLPVKWMAPESIFDCVYTVQSDVWSYGILLWEIFSLGLNPYPGiLVNSKFYKLVKDGYQMAQPAFAPKNIYSIMQACWA 894
Cdd:cd05089  178 GRLPVRWMAIESLNYSVYTTKSDVWSFGVLLWEIVSLGGTPYCG-MTCAELYEKLPQGYRMEKPRNCDDEVYELMRQCWR 256
                        330       340       350
                 ....*....|....*....|....*....|..
gi 569026720 895 LEPTHRPTFQQIcSFLQEQAQEDRRErdYTNL 926
Cdd:cd05089  257 DRPYERPPFSQI-SVQLSRMLEARKA--YVNM 285
PTKc_TrkA cd05092
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase A; PTKs catalyze ...
574-911 1.17e-59

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: 205.59  E-value: 1.17e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 574 KWEfprnnlqfgktLGAGAFGKVVEATAFGLGKEDAVLKVAVKMLKStAHADEKEALMSELKIMSHLgQHENIVNLLGAC 653
Cdd:cd05092   10 KWE-----------LGEGAFGKVFLAECHNLLPEQDKMLVAVKALKE-ATESARQDFQREAELLTVL-QHQHIVRFYGVC 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 654 THGGPVLVITEYCCYGDLLNFLRrkaeamlgpslspgqdpeggvdyknihlekkyvrrdsgfsSQGVDTYVemrpvstss 733
Cdd:cd05092   77 TEGEPLIMVFEYMRHGDLNRFLR----------------------------------------SHGPDAKI--------- 107
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 734 ndsfseqdLDKEDGRP---LELRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDIMNDSNYI 810
Cdd:cd05092  108 --------LDGGEGQApgqLTLGQMLQIASQIASGMVYLASLHFVHRDLATRNCLVGQGLVVKIGDFGMSRDIYSTDYYR 179
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 811 VKGNARLPVKWMAPESIFDCVYTVQSDVWSYGILLWEIFSLGLNPYPGiLVNSKFYKLVKDGYQMAQPAFAPKNIYSIMQ 890
Cdd:cd05092  180 VGGRTMLPIRWMPPESILYRKFTTESDIWSFGVVLWEIFTYGKQPWYQ-LSNTEAIECITQGRELERPRTCPPEVYAIMQ 258
                        330       340
                 ....*....|....*....|.
gi 569026720 891 ACWALEPTHRPTFQQICSFLQ 911
Cdd:cd05092  259 GCWQREPQQRHSIKDIHSRLQ 279
IgI_3_CSF-1R cd20936
Third immunoglobulin domain of the hematopoietic colony-stimulating factor 1 receptor (CSF-1R), ...
203-295 1.64e-59

Third immunoglobulin domain of the hematopoietic colony-stimulating factor 1 receptor (CSF-1R), and similar domains; member of the I-set of IgSF domains; The members here are composed of the third immunoglobulin domain of the hematopoietic colony-stimulating factor 1 receptor (CSF-1R) and similar proteins. CSF-1R, a class III receptor tyrosine kinase (RTKIII), is critical to the survival, proliferation, and differentiation of mononuclear phagocytic cells such as monocytes, tissue macrophages, muscularis macrophages, microglia, osteoclasts, Paneth cells, and myeloid dendritic cells. Human colony-stimulating factor 1 receptor (hCSF-1R) is unique among the hematopoietic receptors because it is activated by two distinct cytokines, CSF-1 and interleukin-34 (IL-34). The Ig superfamily (IgSF) 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, such as, T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, such as, 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. 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 I-set of IgSF domains.


Pssm-ID: 409530  Cd Length: 93  Bit Score: 197.87  E-value: 1.64e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 203 PALTLVPAELVRIRGEAAQIVCSASSVDVNFDVFLQHNNTKLAIPQQSDFHNNRYQKVLTLNLDQVDFQHAGNYSCVASN 282
Cdd:cd20936    1 PALTLEPAELVRIRGEAAQIVCSASNVDVNFDVFLQHGDTKLAIPQQSDFHDNRYQKVLTLNLDQVDFQDAGNYSCVASN 80
                         90
                 ....*....|...
gi 569026720 283 VQGKHSTSMFFRV 295
Cdd:cd20936   81 VQGKHSASMFFRV 93
PTKc_Lyn cd05072
Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the ...
575-912 6.20e-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: 203.35  E-value: 6.20e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 575 WEFPRNNLQFGKTLGAGAFGKVveatafGLGKEDAVLKVAVKMLKSTAHAdeKEALMSELKIMSHLgQHENIVNLLGACT 654
Cdd:cd05072    2 WEIPRESIKLVKKLGAGQFGEV------WMGYYNNSTKVAVKTLKPGTMS--VQAFLEEANLMKTL-QHDKLVRLYAVVT 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 655 HGGPVLVITEYCCYGDLLNFLRrkaeamlgpslspgqdpeggvdyknihlekkyvrrdsgfssqgvdtyvemrpvstssn 734
Cdd:cd05072   73 KEEPIYIITEYMAKGSLLDFLK---------------------------------------------------------- 94
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 735 dsfseqdldKEDGRPLELRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARdIMNDSNYIVKGN 814
Cdd:cd05072   95 ---------SDEGGKVLLPKLIDFSAQIAEGMAYIERKNYIHRDLRAANVLVSESLMCKIADFGLAR-VIEDNEYTAREG 164
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 815 ARLPVKWMAPESIFDCVYTVQSDVWSYGILLWEIFSLGLNPYPGiLVNSKFYKLVKDGYQMAQPAFAPKNIYSIMQACWA 894
Cdd:cd05072  165 AKFPIKWTAPEAINFGSFTIKSDVWSFGILLYEIVTYGKIPYPG-MSNSDVMSALQRGYRMPRMENCPDELYDIMKTCWK 243
                        330
                 ....*....|....*...
gi 569026720 895 LEPTHRPTFQQICSFLQE 912
Cdd:cd05072  244 EKAEERPTFDYLQSVLDD 261
PTKc_Fer cd05085
Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; ...
585-906 7.31e-59

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: 202.16  E-value: 7.31e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 585 GKTLGAGAFGKVVEATAfglgkEDAVlKVAVKMLKSTAHADEKEALMSELKIMSHLgQHENIVNLLGACTHGGPVLVITE 664
Cdd:cd05085    1 GELLGKGNFGEVYKGTL-----KDKT-PVAVKTCKEDLPQELKIKFLSEARILKQY-DHPNIVKLIGVCTQRQPIYIVME 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 665 YCCYGDLLNFLRRKAEAmlgpslspgqdpeggvdyknihlekkyvrrdsgfssqgvdtyvemrpvstssndsfseqdldk 744
Cdd:cd05085   74 LVPGGDFLSFLRKKKDE--------------------------------------------------------------- 90
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 745 edgrpLELRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDiMNDSNYIVKGNARLPVKWMAP 824
Cdd:cd05085   91 -----LKTKQLVKFSLDAAAGMAYLESKNCIHRDLAARNCLVGENNALKISDFGMSRQ-EDDGVYSSSGLKQIPIKWTAP 164
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 825 ESIFDCVYTVQSDVWSYGILLWEIFSLGLNPYPGiLVNSKFYKLVKDGYQMAQPAFAPKNIYSIMQACWALEPTHRPTFQ 904
Cdd:cd05085  165 EALNYGRYSSESDVWSFGILLWETFSLGVCPYPG-MTNQQAREQVEKGYRMSAPQRCPEDIYKIMQRCWDYNPENRPKFS 243

                 ..
gi 569026720 905 QI 906
Cdd:cd05085  244 EL 245
PTKc_Tec_like cd05059
Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
582-910 1.29e-58

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: 201.52  E-value: 1.29e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 582 LQFGKTLGAGAFGKVVeatafgLGKEDAVLKVAVKMLKSTAHADEKeaLMSELKIMSHLgQHENIVNLLGACTHGGPVLV 661
Cdd:cd05059    6 LTFLKELGSGQFGVVH------LGKWRGKIDVAIKMIKEGSMSEDD--FIEEAKVMMKL-SHPKLVQLYGVCTKQRPIFI 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 662 ITEYCCYGDLLNFLRRkaeamlgpslspgqdpeggvdykNIHLEKKyvrrdsgfssqgvdtyvEMrpvstssndsfseqd 741
Cdd:cd05059   77 VTEYMANGCLLNYLRE-----------------------RRGKFQT-----------------EQ--------------- 101
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 742 ldkedgrplelrdLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDIMNDSnYIVKGNARLPVKW 821
Cdd:cd05059  102 -------------LLEMCKDVCEAMEYLESNGFIHRDLAARNCLVGEQNVVKVSDFGLARYVLDDE-YTSSVGTKFPVKW 167
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 822 MAPESIFDCVYTVQSDVWSYGILLWEIFSLGLNPYPGiLVNSKFYKLVKDGYQMAQPAFAPKNIYSIMQACWALEPTHRP 901
Cdd:cd05059  168 SPPEVFMYSKFSSKSDVWSFGVLMWEVFSEGKMPYER-FSNSEVVEHISQGYRLYRPHLAPTEVYTIMYSCWHEKPEERP 246

                 ....*....
gi 569026720 902 TFQQICSFL 910
Cdd:cd05059  247 TFKILLSQL 255
PTK_CCK4 cd05046
Pseudokinase domain of the Protein Tyrosine Kinase, Colon Carcinoma Kinase 4; CCK4, also ...
577-912 3.82e-58

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: 201.15  E-value: 3.82e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 577 FPRNNLQFGKTLGAGAFGKVVEATAFGLGKEDAVLKVAVKMLKSTahaDEKEALMS---ELKIMSHLgQHENIVNLLGAC 653
Cdd:cd05046    2 FPRSNLQEITTLGRGEFGEVFLAKAKGIEEEGGETLVLVKALQKT---KDENLQSEfrrELDMFRKL-SHKNVVRLLGLC 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 654 THGGPVLVITEYCCYGDLLNFLRrkaeamlgpslspgqdpeggvdyknihlekkyvrrdsgfSSQGVDTYVEMRPVSTSS 733
Cdd:cd05046   78 REAEPHYMILEYTDLGDLKQFLR---------------------------------------ATKSKDEKLKPPPLSTKQ 118
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 734 ndsfseqdldkedgrplelrdLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDIMNDSNYIVKg 813
Cdd:cd05046  119 ---------------------KVALCTQIALGMDHLSNARFVHRDLAARNCLVSSQREVKVSLLSLSKDVYNSEYYKLR- 176
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 814 NARLPVKWMAPESIFDCVYTVQSDVWSYGILLWEIFSLGLNPYPGiLVNSKFYKLVKDG-YQMAQPAFAPKNIYSIMQAC 892
Cdd:cd05046  177 NALIPLRWLAPEAVQEDDFSTKSDVWSFGVLMWEVFTQGELPFYG-LSDEEVLNRLQAGkLELPVPEGCPSRLYKLMTRC 255
                        330       340
                 ....*....|....*....|
gi 569026720 893 WALEPTHRPTFQQICSFLQE 912
Cdd:cd05046  256 WAVNPKDRPSFSELVSALGE 275
PTKc_Tie2 cd05088
Catalytic domain of the Protein Tyrosine Kinase, Tie2; PTKs catalyze the transfer of the ...
580-918 4.02e-58

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: 202.15  E-value: 4.02e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 580 NNLQFGKTLGAGAFGKVVEATafgLGKEDAVLKVAVKMLKSTAHADEKEALMSELKIMSHLGQHENIVNLLGACTHGGPV 659
Cdd:cd05088    7 NDIKFQDVIGEGNFGQVLKAR---IKKDGLRMDAAIKRMKEYASKDDHRDFAGELEVLCKLGHHPNIINLLGACEHRGYL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 660 LVITEYCCYGDLLNFLRRKaeamlgpslspgqdpeggvdyknihlekKYVRRDSGFSsqgvdtyvemrpVSTSSNDSFSE 739
Cdd:cd05088   84 YLAIEYAPHGNLLDFLRKS----------------------------RVLETDPAFA------------IANSTASTLSS 123
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 740 QDLdkedgrplelrdlLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARdimNDSNYIVKGNARLPV 819
Cdd:cd05088  124 QQL-------------LHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGLSR---GQEVYVKKTMGRLPV 187
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 820 KWMAPESIFDCVYTVQSDVWSYGILLWEIFSLGLNPYPGiLVNSKFYKLVKDGYQMAQPAFAPKNIYSIMQACWALEPTH 899
Cdd:cd05088  188 RWMAIESLNYSVYTTNSDVWSYGVLLWEIVSLGGTPYCG-MTCAELYEKLPQGYRLEKPLNCDDEVYDLMRQCWREKPYE 266
                        330
                 ....*....|....*....
gi 569026720 900 RPTFQQICSFLQEQAQEDR 918
Cdd:cd05088  267 RPSFAQILVSLNRMLEERK 285
PTKc_FAK cd05056
Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the ...
575-918 1.37e-57

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: 199.19  E-value: 1.37e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 575 WEFPRNNLQFGKTLGAGAFGKVVEATAfgLGKEDAVLKVAVKMLKSTAHADEKEALMSELKIMSHLgQHENIVNLLGACT 654
Cdd:cd05056    1 YEIQREDITLGRCIGEGQFGDVYQGVY--MSPENEKIAVAVKTCKNCTSPSVREKFLQEAYIMRQF-DHPHIVKLIGVIT 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 655 HGgPVLVITEYCCYGDLLNFLRRkaeamlgpslspgqdpeggvdyknihlekkyvRRDSgfssqgvdtyvemrpvstssn 734
Cdd:cd05056   78 EN-PVWIVMELAPLGELRSYLQV--------------------------------NKYS--------------------- 103
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 735 dsfseqdldkedgrpLELRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARdIMNDSNYIVKGN 814
Cdd:cd05056  104 ---------------LDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSPDCVKLGDFGLSR-YMEDESYYKASK 167
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 815 ARLPVKWMAPESIFDCVYTVQSDVWSYGILLWEIFSLGLNPYPGiLVNSKFYKLVKDGYQMAQPAFAPKNIYSIMQACWA 894
Cdd:cd05056  168 GKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMLGVKPFQG-VKNNDVIGRIENGERLPMPPNCPPTLYSLMTKCWA 246
                        330       340
                 ....*....|....*....|....
gi 569026720 895 LEPTHRPTFQQICSFLQEQAQEDR 918
Cdd:cd05056  247 YDPSKRPRFTELKAQLSDILQEEK 270
PTKc_Chk cd05083
Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the ...
575-913 1.99e-57

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: 198.17  E-value: 1.99e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 575 WEFPRNNLQFGKTLGAGAFGKVVEATAFGLgkedavlKVAVKMLKSTAHAdekEALMSELKIMSHLgQHENIVNLLGACT 654
Cdd:cd05083    1 WLLNLQKLTLGEIIGEGEFGAVLQGEYMGQ-------KVAVKNIKCDVTA---QAFLEETAVMTKL-QHKNLVRLLGVIL 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 655 HGGpVLVITEYCCYGDLLNFLRRKAEAMLGPSlspgqdpeggvdyknihlekkyvrrdsgfssqgvdtyvemrpvstssn 734
Cdd:cd05083   70 HNG-LYIVMELMSKGNLVNFLRSRGRALVPVI------------------------------------------------ 100
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 735 dsfseqdldkedgrplelrDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARdimndSNYIVKGN 814
Cdd:cd05083  101 -------------------QLLQFSLDVAEGMEYLESKKLVHRDLAARNILVSEDGVAKISDFGLAK-----VGSMGVDN 156
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 815 ARLPVKWMAPESIFDCVYTVQSDVWSYGILLWEIFSLGLNPYPGILVNsKFYKLVKDGYQMAQPAFAPKNIYSIMQACWA 894
Cdd:cd05083  157 SRLPVKWTAPEALKNKKFSSKSDVWSYGVLLWEVFSYGRAPYPKMSVK-EVKEAVEKGYRMEPPEGCPPDVYSIMTSCWE 235
                        330
                 ....*....|....*....
gi 569026720 895 LEPTHRPTFQQICSFLQEQ 913
Cdd:cd05083  236 AEPGKRPSFKKLREKLEKE 254
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
588-910 2.29e-57

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: 197.76  E-value: 2.29e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 588 LGAGAFGKVVEATAfgLGKEdavlkVAVKMLK-STAHADEKEALMSELKIMSHLgQHENIVNLLGACTHGGPVLVITEYC 666
Cdd:cd13999    1 IGSGSFGEVYKGKW--RGTD-----VAIKKLKvEDDNDELLKEFRREVSILSKL-RHPNIVQFIGACLSPPPLCIVTEYM 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 667 CYGDLLNFLRRKaeamlgpslspgqdpeggvdyknihlekkyvrrdsgfssqgvdtyvemrpvstssndsfseqdldked 746
Cdd:cd13999   73 PGGSLYDLLHKK-------------------------------------------------------------------- 84
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 747 GRPLELRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARdIMNDSN---YIVKGNARlpvkWMA 823
Cdd:cd13999   85 KIPLSWSLRLKIALDIARGMNYLHSPPIIHRDLKSLNILLDENFTVKIADFGLSR-IKNSTTekmTGVVGTPR----WMA 159
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 824 PESIFDCVYTVQSDVWSYGILLWEIFSlGLNPYPGILVNSKFYKLVKDGYQMAQPAFAPKNIYSIMQACWALEPTHRPTF 903
Cdd:cd13999  160 PEVLRGEPYTEKADVYSFGIVLWELLT-GEVPFKELSPIQIAAAVVQKGLRPPIPPDCPPELSKLIKRCWNEDPEKRPSF 238

                 ....*..
gi 569026720 904 QQICSFL 910
Cdd:cd13999  239 SEIVKRL 245
PTKc_Lck_Blk cd05067
Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs ...
574-912 3.10e-57

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: 198.19  E-value: 3.10e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 574 KWEFPRNNLQFGKTLGAGAFGKVveatafGLGKEDAVLKVAVKMLKSTAHadEKEALMSELKIMSHLgQHENIVNLLGAC 653
Cdd:cd05067    1 EWEVPRETLKLVERLGAGQFGEV------WMGYYNGHTKVAIKSLKQGSM--SPDAFLAEANLMKQL-QHQRLVRLYAVV 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 654 THGgPVLVITEYCCYGDLLNFLRrkaeamlgpslspgqdpeggvdyknihlekkyvrrdsgfssqgvdtyvemrpvstss 733
Cdd:cd05067   72 TQE-PIYIITEYMENGSLVDFLK--------------------------------------------------------- 93
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 734 ndsfseqdldKEDGRPLELRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARdIMNDSNYIVKG 813
Cdd:cd05067   94 ----------TPSGIKLTINKLLDMAAQIAEGMAFIEERNYIHRDLRAANILVSDTLSCKIADFGLAR-LIEDNEYTARE 162
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 814 NARLPVKWMAPESIFDCVYTVQSDVWSYGILLWEIFSLGLNPYPGiLVNSKFYKLVKDGYQMAQPAFAPKNIYSIMQACW 893
Cdd:cd05067  163 GAKFPIKWTAPEAINYGTFTIKSDVWSFGILLTEIVTHGRIPYPG-MTNPEVIQNLERGYRMPRPDNCPEELYQLMRLCW 241
                        330
                 ....*....|....*....
gi 569026720 894 ALEPTHRPTFQQICSFLQE 912
Cdd:cd05067  242 KERPEDRPTFEYLRSVLED 260
PTKc_Jak_rpt2 cd05038
Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily ...
577-907 2.47e-56

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: 196.06  E-value: 2.47e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 577 FPRNNLQFGKTLGAGAFGKVvEATAFGLGKEDAVLKVAVKMLKSTAHADEKEALMSELKIMSHLgQHENIVNLLGACT-- 654
Cdd:cd05038    1 FEERHLKFIKQLGEGHFGSV-ELCRYDPLGDNTGEQVAVKSLQPSGEEQHMSDFKREIEILRTL-DHEYIVKYKGVCEsp 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 655 HGGPVLVITEYCCYGDLLNFLRRKAEAmlgpslspgqdpeggvdyknihlekkyvrrdsgfssqgvdtyvemrpvstssn 734
Cdd:cd05038   79 GRRSLRLIMEYLPSGSLRDYLQRHRDQ----------------------------------------------------- 105
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 735 dsfseqdldkedgrpLELRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDIMNDSN-YIVKG 813
Cdd:cd05038  106 ---------------IDLKRLLLFASQICKGMEYLGSQRYIHRDLAARNILVESEDLVKISDFGLAKVLPEDKEyYYVKE 170
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 814 NARLPVKWMAPESIFDCVYTVQSDVWSYGILLWEIFSLG---LNPYPGILVN----------SKFYKLVKDGYQMAQPAF 880
Cdd:cd05038  171 PGESPIFWYAPECLRESRFSSASDVWSFGVTLYELFTYGdpsQSPPALFLRMigiaqgqmivTRLLELLKSGERLPRPPS 250
                        330       340
                 ....*....|....*....|....*..
gi 569026720 881 APKNIYSIMQACWALEPTHRPTFQQIC 907
Cdd:cd05038  251 CPDEVYDLMKECWEYEPQDRPSFSDLI 277
PTKc_DDR2 cd05095
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 2; PTKs catalyze ...
576-912 4.20e-56

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: 195.98  E-value: 4.20e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 576 EFPRNNLQFGKTLGAGAFGKVVEATAFGLGK-----------EDAVLKVAVKMLKSTAHADEKEALMSELKIMSHLgQHE 644
Cdd:cd05095    1 EFPRKLLTFKEKLGEGQFGEVHLCEAEGMEKfmdkdfalevsENQPVLVAVKMLRADANKNARNDFLKEIKIMSRL-KDP 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 645 NIVNLLGACTHGGPVLVITEYCCYGDLLNFLRRkaeamlgpslspgQDPEGGvdyknihlekkyvrrdsgfssqgvdtyv 724
Cdd:cd05095   80 NIIRLLAVCITDDPLCMITEYMENGDLNQFLSR-------------QQPEGQ---------------------------- 118
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 725 emrPVSTSsndsfseqdldkeDGRPLELRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDIM 804
Cdd:cd05095  119 ---LALPS-------------NALTVSYSDLRFMAAQIASGMKYLSSLNFVHRDLATRNCLVGKNYTIKIADFGMSRNLY 182
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 805 NDSNYIVKGNARLPVKWMAPESIFDCVYTVQSDVWSYGILLWEIFSLGL-NPYP-----GILVNS-KFYKLVKDGYQMAQ 877
Cdd:cd05095  183 SGDYYRIQGRAVLPIRWMSWESILLGKFTTASDVWAFGVTLWETLTFCReQPYSqlsdeQVIENTgEFFRDQGRQTYLPQ 262
                        330       340       350
                 ....*....|....*....|....*....|....*
gi 569026720 878 PAFAPKNIYSIMQACWALEPTHRPTFQQICSFLQE 912
Cdd:cd05095  263 PALCPDSVYKLMLSCWRRDTKDRPSFQEIHTLLQE 297
PTKc_Csk cd05082
Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the ...
575-912 1.68e-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: 1.68e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 575 WEFPRNNLQFGKTLGAGAFGKVVeatafgLGKEDAVlKVAVKMLKSTAHAdekEALMSELKIMSHLgQHENIVNLLGACT 654
Cdd:cd05082    1 WALNMKELKLLQTIGKGEFGDVM------LGDYRGN-KVAVKCIKNDATA---QAFLAEASVMTQL-RHSNLVQLLGVIV 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 655 H-GGPVLVITEYCCYGDLLNFLRRKAEAMLGPSLspgqdpeggvdyknihlekkyvrrdsgfssqgvdtyvemrpvstss 733
Cdd:cd05082   70 EeKGGLYIVTEYMAKGSLVDYLRSRGRSVLGGDC---------------------------------------------- 103
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 734 ndsfseqdldkedgrplelrdLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDIMNdsnyiVKG 813
Cdd:cd05082  104 ---------------------LLKFSLDVCEAMEYLEGNNFVHRDLAARNVLVSEDNVAKVSDFGLTKEASS-----TQD 157
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 814 NARLPVKWMAPESIFDCVYTVQSDVWSYGILLWEIFSLGLNPYPGILVNSKFYKlVKDGYQMAQPAFAPKNIYSIMQACW 893
Cdd:cd05082  158 TGKLPVKWTAPEALREKKFSTKSDVWSFGILLWEIYSFGRVPYPRIPLKDVVPR-VEKGYKMDAPDGCPPAVYDVMKNCW 236
                        330
                 ....*....|....*....
gi 569026720 894 ALEPTHRPTFQQICSFLQE 912
Cdd:cd05082  237 HLDAAMRPSFLQLREQLEH 255
PTKc_DDR_like cd05097
Catalytic domain of Discoidin Domain Receptor-like Protein Tyrosine Kinases; PTKs catalyze the ...
576-912 2.42e-55

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: 194.04  E-value: 2.42e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 576 EFPRNNLQFGKTLGAGAFGKVVEATAFGLGK---------EDAVLKVAVKMLKSTAHADEKEALMSELKIMSHLgQHENI 646
Cdd:cd05097    1 EFPRQQLRLKEKLGEGQFGEVHLCEAEGLAEflgegapefDGQPVLVAVKMLRADVTKTARNDFLKEIKIMSRL-KNPNI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 647 VNLLGACTHGGPVLVITEYCCYGDLLNFLRRKaeamlgpslspgqdpeggvdyknihlekkyvrrdsgfssqgvdtyvEM 726
Cdd:cd05097   80 IRLLGVCVSDDPLCMITEYMENGDLNQFLSQR----------------------------------------------EI 113
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 727 RPVSTSSNDSFSeqdldkedgrpLELRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDIMND 806
Cdd:cd05097  114 ESTFTHANNIPS-----------VSIANLLYMAVQIASGMKYLASLNFVHRDLATRNCLVGNHYTIKIADFGMSRNLYSG 182
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 807 SNYIVKGNARLPVKWMAPESIFDCVYTVQSDVWSYGILLWEIFSL-GLNPYP-----GILVNS-KFYKlvKDGYQ--MAQ 877
Cdd:cd05097  183 DYYRIQGRAVLPIRWMAWESILLGKFTTASDVWAFGVTLWEMFTLcKEQPYSllsdeQVIENTgEFFR--NQGRQiyLSQ 260
                        330       340       350
                 ....*....|....*....|....*....|....*
gi 569026720 878 PAFAPKNIYSIMQACWALEPTHRPTFQQICSFLQE 912
Cdd:cd05097  261 TPLCPSPVFKLMMRCWSRDIKDRPTFNKIHHFLRE 295
PTKc_EGFR_like cd05057
Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs ...
576-919 9.03e-55

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: 191.47  E-value: 9.03e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 576 EFPRNNLQFGKTLGAGAFGKVVEATAFGLGkEDAVLKVAVKMLKSTAHADEKEALMSELKIMSHLGqHENIVNLLGACTh 655
Cdd:cd05057    3 IVKETELEKGKVLGSGAFGTVYKGVWIPEG-EKVKIPVAIKVLREETGPKANEEILDEAYVMASVD-HPHLVRLLGICL- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 656 GGPVLVITEYCCYGDLLNFLRRKAEAmLGPslspgqdpeggvdyknihlekkyvrrdsgfssqgvdtyvemrpvstssnd 735
Cdd:cd05057   80 SSQVQLITQLMPLGCLLDYVRNHRDN-IGS-------------------------------------------------- 108
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 736 sfseqdldkedgrplelRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLL-TNGHVaKIGDFGLARDIMNDSN-YIVKG 813
Cdd:cd05057  109 -----------------QLLLNWCVQIAKGMSYLEEKRLVHRDLAARNVLVkTPNHV-KITDFGLAKLLDVDEKeYHAEG 170
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 814 nARLPVKWMAPESIFDCVYTVQSDVWSYGILLWEIFSLGLNPYPGILVnSKFYKLVKDGYQMAQPAFAPKNIYSIMQACW 893
Cdd:cd05057  171 -GKVPIKWMALESIQYRIYTHKSDVWSYGVTVWELMTFGAKPYEGIPA-VEIPDLLEKGERLPQPPICTIDVYMVLVKCW 248
                        330       340
                 ....*....|....*....|....*.
gi 569026720 894 ALEPTHRPTFQQICSFLQEQAQEDRR 919
Cdd:cd05057  249 MIDAESRPTFKELANEFSKMARDPQR 274
PTKc_Hck cd05073
Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the ...
573-912 2.28e-54

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: 190.24  E-value: 2.28e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 573 EKWEFPRNNLQFGKTLGAGAFGKVVEATAfglgkeDAVLKVAVKMLKSTAHAdeKEALMSELKIMSHLgQHENIVNLLGA 652
Cdd:cd05073    4 DAWEIPRESLKLEKKLGAGQFGEVWMATY------NKHTKVAVKTMKPGSMS--VEAFLAEANVMKTL-QHDKLVKLHAV 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 653 CTHGgPVLVITEYCCYGDLLNFLRrkaeamlgpslspgqdpeggvdyknihlekkyvrrdsgfssqgvdtyvemrpvsts 732
Cdd:cd05073   75 VTKE-PIYIITEFMAKGSLLDFLK-------------------------------------------------------- 97
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 733 sndsfseqdldKEDGRPLELRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARdIMNDSNYIVK 812
Cdd:cd05073   98 -----------SDEGSKQPLPKLIDFSAQIAEGMAFIEQRNYIHRDLRAANILVSASLVCKIADFGLAR-VIEDNEYTAR 165
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 813 GNARLPVKWMAPESIFDCVYTVQSDVWSYGILLWEIFSLGLNPYPGiLVNSKFYKLVKDGYQMAQPAFAPKNIYSIMQAC 892
Cdd:cd05073  166 EGAKFPIKWTAPEAINFGSFTIKSDVWSFGILLMEIVTYGRIPYPG-MSNPEVIRALERGYRMPRPENCPEELYNIMMRC 244
                        330       340
                 ....*....|....*....|
gi 569026720 893 WALEPTHRPTFQQICSFLQE 912
Cdd:cd05073  245 WKNRPEERPTFEYIQSVLDD 264
PTKc_EphR cd05033
Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
586-911 2.55e-54

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: 189.89  E-value: 2.55e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 586 KTLGAGAFGKVVEATAFGLGKEDavLKVAVKMLKSTAHADEKEALMSELKIMSHLgQHENIVNLLGACTHGGPVLVITEY 665
Cdd:cd05033   10 KVIGGGEFGEVCSGSLKLPGKKE--IDVAIKTLKSGYSDKQRLDFLTEASIMGQF-DHPNVIRLEGVVTKSRPVMIVTEY 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 666 CCYGDLLNFLRRKaeamlgpslspgqdpeggvdyknihlekkyvrrDSGFSsqgvdtyvemrpvstssndsfseqdldke 745
Cdd:cd05033   87 MENGSLDKFLREN---------------------------------DGKFT----------------------------- 104
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 746 dgrPLELRDLLHfssQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDIMN-DSNYIVKGnARLPVKWMAP 824
Cdd:cd05033  105 ---VTQLVGMLR---GIASGMKYLSEMNYVHRDLAARNILVNSDLVCKVSDFGLSRRLEDsEATYTTKG-GKIPIRWTAP 177
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 825 ESIFDCVYTVQSDVWSYGILLWEIFSLGLNPYPGiLVNSKFYKLVKDGYQMAQPAFAPKNIYSIMQACWALEPTHRPTFQ 904
Cdd:cd05033  178 EAIAYRKFTSASDVWSFGIVMWEVMSYGERPYWD-MSNQDVIKAVEDGYRLPPPMDCPSALYQLMLDCWQKDRNERPTFS 256

                 ....*..
gi 569026720 905 QICSFLQ 911
Cdd:cd05033  257 QIVSTLD 263
IgI_4_SCFR_like cd04975
Fourth immunoglobulin (Ig)-like domain of stem cell factor receptor (SCFR), and similar ...
299-400 3.89e-54

Fourth immunoglobulin (Ig)-like domain of stem cell factor receptor (SCFR), and similar domains; member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain of stem cell factor receptor (SCFR). In addition to SCFR, this group also includes the fourth Ig domain of macrophage colony stimulating factor receptor (M-CSF-R). SCFR, also called receptor tyrosine kinase KIT or proto-oncogene c-Kit, contains an extracellular component having five Ig-like domains, a transmembrane segment, and a cytoplasmic portion having protein tyrosine kinase activity. SCFR and its ligand SCF are critical for normal hematopoiesis, mast cell development, melanocytes, and gametogenesis. SCF binds to the second and third Ig-like domains of SCFR, this fourth Ig-like domain participates in SCFR dimerization, which follows ligand binding. Deletion of this fourth SCFR Ig-like domain abolishes the ligand-induced dimerization of SCFR and completely inhibits signal transduction. M-CSF-R, also called proto-oncogene c-Fms, acts as cell-surface receptor for CSF1 and IL34 and plays an essential role in the regulation of survival, proliferation and differentiation of hematopoietic precursor cells, such as macrophages and monocytes. 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: 409364  Cd Length: 101  Bit Score: 183.19  E-value: 3.89e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 299 AYLNLSSEQNLIQEVTVGEGLNLKVMVEAYPGLQGFNWTYLGPFSDhQPEPKLANATTKDTYRHTFTLSLPRLKPSEAGR 378
Cdd:cd04975    1 GYINLSSEQNLTVEVNVGENLDLIVEVEAYPKPEHQNWTYMGPFFT-DKWEDLPNSENESTYRYVSTLHLTRLKGSEAGT 79
                         90       100
                 ....*....|....*....|..
gi 569026720 379 YSFLARNPGGWRALTFELTLRY 400
Cdd:cd04975   80 YTFLASNSDVNAALAFEVYLNY 101
PTKc_Fes cd05084
Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the ...
585-911 1.30e-53

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: 187.45  E-value: 1.30e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 585 GKTLGAGAFGKVVEatafGLGKEDAVLkVAVKMLKSTAHADEKEALMSELKIMSHLgQHENIVNLLGACTHGGPVLVITE 664
Cdd:cd05084    1 GERIGRGNFGEVFS----GRLRADNTP-VAVKSCRETLPPDLKAKFLQEARILKQY-SHPNIVRLIGVCTQKQPIYIVME 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 665 YCCYGDLLNFLRrkaeamlgpslspgqdpeggvdyknihlekkyvrrdsgfssqgvdtyvemrpvstssndsfseqdldk 744
Cdd:cd05084   75 LVQGGDFLTFLR-------------------------------------------------------------------- 86
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 745 EDGRPLELRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDiMNDSNYIVKGNAR-LPVKWMA 823
Cdd:cd05084   87 TEGPRLKVKELIRMVENAAAGMEYLESKHCIHRDLAARNCLVTEKNVLKISDFGMSRE-EEDGVYAATGGMKqIPVKWTA 165
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 824 PESIFDCVYTVQSDVWSYGILLWEIFSLGLNPYPgILVNSKFYKLVKDGYQMAQPAFAPKNIYSIMQACWALEPTHRPTF 903
Cdd:cd05084  166 PEALNYGRYSSESDVWSFGILLWETFSLGAVPYA-NLSNQQTREAVEQGVRLPCPENCPDEVYRLMEQCWEYDPRKRPSF 244

                 ....*...
gi 569026720 904 QQICSFLQ 911
Cdd:cd05084  245 STVHQDLQ 252
PTKc_TAM cd05035
Catalytic Domain of TAM (Tyro3, Axl, Mer) Protein Tyrosine Kinases; PTKs catalyze the transfer ...
582-912 4.17e-53

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: 186.59  E-value: 4.17e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 582 LQFGKTLGAGAFGKVVEATafgLGKEDAV-LKVAVKMLKSTAHA-DEKEALMSELKIMSHLgQHENIVNLLGACTHGGPV 659
Cdd:cd05035    1 LKLGKILGEGEFGSVMEAQ---LKQDDGSqLKVAVKTMKVDIHTySEIEEFLSEAACMKDF-DHPNVMRLIGVCFTASDL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 660 ------LVITEYCCYGDLLNFLrrkaeamlgpslspgqdpeggvdyknihlekkyvrrdsgFSSQgvdtyVEMRPVStss 733
Cdd:cd05035   77 nkppspMVILPFMKHGDLHSYL---------------------------------------LYSR-----LGGLPEK--- 109
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 734 ndsfseqdldkedgrpLELRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDIMNDSNYIVKG 813
Cdd:cd05035  110 ----------------LPLQTLLKFMVDIAKGMEYLSNRNFIHRDLAARNCMLDENMTVCVADFGLSRKIYSGDYYRQGR 173
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 814 NARLPVKWMAPESIFDCVYTVQSDVWSYGILLWEIFSLGLNPYPGIlVNSKFYKLVKDGYQMAQPAFAPKNIYSIMQACW 893
Cdd:cd05035  174 ISKMPVKWIALESLADNVYTSKSDVWSFGVTMWEIATRGQTPYPGV-ENHEIYDYLRNGNRLKQPEDCLDEVYFLMYFCW 252
                        330
                 ....*....|....*....
gi 569026720 894 ALEPTHRPTFQQICSFLQE 912
Cdd:cd05035  253 TVDPKDRPTFTKLREVLEN 271
PTKc_Met_Ron cd05058
Catalytic domain of the Protein Tyrosine Kinases, Met and Ron; PTKs catalyze the transfer of ...
588-908 4.70e-53

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: 186.14  E-value: 4.70e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 588 LGAGAFGKVVEATAfgLGKEDAVLKVAVKMLKSTAHADEKEALMSELKIMSHLgQHENIVNLLGAC--THGGPvLVITEY 665
Cdd:cd05058    3 IGKGHFGCVYHGTL--IDSDGQKIHCAVKSLNRITDIEEVEQFLKEGIIMKDF-SHPNVLSLLGIClpSEGSP-LVVLPY 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 666 CCYGDLLNFLRrkaeamlgpslSPGQDPEggvdyknihlekkyvrrdsgfssqgvdtyvemrpvstssndsfseqdldke 745
Cdd:cd05058   79 MKHGDLRNFIR-----------SETHNPT--------------------------------------------------- 96
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 746 dgrpleLRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDIMNDSNYIV--KGNARLPVKWMA 823
Cdd:cd05058   97 ------VKDLIGFGLQVAKGMEYLASKKFVHRDLAARNCMLDESFTVKVADFGLARDIYDKEYYSVhnHTGAKLPVKWMA 170
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 824 PESIFDCVYTVQSDVWSYGILLWEIFSLGLNPYPGilVNSkfYKLVK---DGYQMAQPAFAPKNIYSIMQACWALEPTHR 900
Cdd:cd05058  171 LESLQTQKFTTKSDVWSFGVLLWELMTRGAPPYPD--VDS--FDITVyllQGRRLLQPEYCPDPLYEVMLSCWHPKPEMR 246

                 ....*...
gi 569026720 901 PTFQQICS 908
Cdd:cd05058  247 PTFSELVS 254
PTKc_Axl cd05075
Catalytic domain of the Protein Tyrosine Kinase, Axl; PTKs catalyze the transfer of the ...
582-906 5.77e-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: 186.37  E-value: 5.77e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 582 LQFGKTLGAGAFGKVVEATafgLGKEDAVLKVAVKMLK-STAHADEKEALMSELKIMSHLgQHENIVNLLGACTHG---- 656
Cdd:cd05075    2 LALGKTLGEGEFGSVMEGQ---LNQDDSVLKVAVKTMKiAICTRSEMEDFLSEAVCMKEF-DHPNVMRLIGVCLQNtese 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 657 ---GPVlVITEYCCYGDLLNFLRrkaeamlgpslspgqdpeggvdyknihlekkyvrrdsgFSSQGvDTYVEMrPVSTss 733
Cdd:cd05075   78 gypSPV-VILPFMKHGDLHSFLL--------------------------------------YSRLG-DCPVYL-PTQM-- 114
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 734 ndsfseqdldkedgrplelrdLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDIMNDSNYIVKG 813
Cdd:cd05075  115 ---------------------LVKFMTDIASGMEYLSSKNFIHRDLAARNCMLNENMNVCVADFGLSKKIYNGDYYRQGR 173
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 814 NARLPVKWMAPESIFDCVYTVQSDVWSYGILLWEIFSLGLNPYPGIlVNSKFYKLVKDGYQMAQPAFAPKNIYSIMQACW 893
Cdd:cd05075  174 ISKMPVKWIAIESLADRVYTTKSDVWSFGVTMWEIATRGQTPYPGV-ENSEIYDYLRQGNRLKQPPDCLDGLYELMSSCW 252
                        330
                 ....*....|...
gi 569026720 894 ALEPTHRPTFQQI 906
Cdd:cd05075  253 LLNPKDRPSFETL 265
PTKc_Ror2 cd05091
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
576-911 1.88e-52

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: 185.22  E-value: 1.88e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 576 EFPRNNLQFGKTLGAGAFGKVVEATAFGLGKEDAVLKVAVKMLKSTAHADEKEALMSELKIMSHLgQHENIVNLLGACTH 655
Cdd:cd05091    2 EINLSAVRFMEELGEDRFGKVYKGHLFGTAPGEQTQAVAIKTLKDKAEGPLREEFRHEAMLRSRL-QHPNIVCLLGVVTK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 656 GGPVLVITEYCCYGDLLNFLrrkaeAMLGPSLSPGqdpeggvdyknihlekkyvrrdsgfssqgvdtyvemrpvstSSND 735
Cdd:cd05091   81 EQPMSMIFSYCSHGDLHEFL-----VMRSPHSDVG-----------------------------------------STDD 114
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 736 sfseqdlDKEDGRPLELRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDIMNDSNYIVKGNA 815
Cdd:cd05091  115 -------DKTVKSTLEPADFLHIVTQIAAGMEYLSSHHVVHKDLATRNVLVFDKLNVKISDLGLFREVYAADYYKLMGNS 187
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 816 RLPVKWMAPESIFDCVYTVQSDVWSYGILLWEIFSLGLNPYPGiLVNSKFYKLVKDGYQMAQPAFAPKNIYSIMQACWAL 895
Cdd:cd05091  188 LLPIRWMSPEAIMYGKFSIDSDIWSYGVVLWEVFSYGLQPYCG-YSNQDVIEMIRNRQVLPCPDDCPAWVYTLMLECWNE 266
                        330
                 ....*....|....*.
gi 569026720 896 EPTHRPTFQQICSFLQ 911
Cdd:cd05091  267 FPSRRPRFKDIHSRLR 282
PTKc_Src_Fyn_like cd14203
Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
586-912 2.47e-52

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: 183.58  E-value: 2.47e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 586 KTLGAGAFGKVveatafGLGKEDAVLKVAVKMLKSTAHAdeKEALMSELKIMSHLgQHENIVNLLgACTHGGPVLVITEY 665
Cdd:cd14203    1 VKLGQGCFGEV------WMGTWNGTTKVAIKTLKPGTMS--PEAFLEEAQIMKKL-RHDKLVQLY-AVVSEEPIYIVTEF 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 666 CCYGDLLNFLRrkaeamlgpslspgqdpeggvdyknihlekkyvrrdsgfssqgvdtyvemrpvstssndsfseqdldKE 745
Cdd:cd14203   71 MSKGSLLDFLK-------------------------------------------------------------------DG 83
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 746 DGRPLELRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARdIMNDSNYIVKGNARLPVKWMAPE 825
Cdd:cd14203   84 EGKYLKLPQLVDMAAQIASGMAYIERMNYIHRDLRAANILVGDNLVCKIADFGLAR-LIEDNEYTARQGAKFPIKWTAPE 162
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 826 SIFDCVYTVQSDVWSYGILLWEIFSLGLNPYPGiLVNSKFYKLVKDGYQMAQPAFAPKNIYSIMQACWALEPTHRPTFQQ 905
Cdd:cd14203  163 AALYGRFTIKSDVWSFGILLTELVTKGRVPYPG-MNNREVLEQVERGYRMPCPPGCPESLHELMCQCWRKDPEERPTFEY 241

                 ....*..
gi 569026720 906 ICSFLQE 912
Cdd:cd14203  242 LQSFLED 248
PTKc_IGF-1R cd05062
Catalytic domain of the Protein Tyrosine Kinase, Insulin-like Growth Factor-1 Receptor; PTKs ...
575-912 3.07e-52

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: 184.47  E-value: 3.07e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 575 WEFPRNNLQFGKTLGAGAFGKVVEATAFGLGKEDAVLKVAVKMLKSTAHADEKEALMSELKIMSHLGQHeNIVNLLGACT 654
Cdd:cd05062    1 WEVAREKITMSRELGQGSFGMVYEGIAKGVVKDEPETRVAIKTVNEAASMRERIEFLNEASVMKEFNCH-HVVRLLGVVS 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 655 HGGPVLVITEYCCYGDLLNFLRrkaeamlgpslspgqdpeggvdyknihlekkyvrrdsgfssqgvdtyvEMRPvSTSSN 734
Cdd:cd05062   80 QGQPTLVIMELMTRGDLKSYLR------------------------------------------------SLRP-EMENN 110
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 735 DSFSeqdldkedgrPLELRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDIMNDSNYIVKGN 814
Cdd:cd05062  111 PVQA----------PPSLKKMIQMAGEIADGMAYLNANKFVHRDLAARNCMVAEDFTVKIGDFGMTRDIYETDYYRKGGK 180
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 815 ARLPVKWMAPESIFDCVYTVQSDVWSYGILLWEIFSLGLNPYPGiLVNSKFYKLVKDGYQMAQPAFAPKNIYSIMQACWA 894
Cdd:cd05062  181 GLLPVRWMSPESLKDGVFTTYSDVWSFGVVLWEIATLAEQPYQG-MSNEQVLRFVMEGGLLDKPDNCPDMLFELMRMCWQ 259
                        330
                 ....*....|....*...
gi 569026720 895 LEPTHRPTFQQICSFLQE 912
Cdd:cd05062  260 YNPKMRPSFLEIISSIKE 277
PTKc_Ack_like cd05040
Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs ...
586-912 3.63e-52

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: 183.31  E-value: 3.63e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 586 KTLGAGAFGKVVEATafGLGKEDAVLKVAVKMLKSTAHADEkEALMS---ELKIMsHLGQHENIVNLLG-ACTHggPVLV 661
Cdd:cd05040    1 EKLGDGSFGVVRRGE--WTTPSGKVIQVAVKCLKSDVLSQP-NAMDDflkEVNAM-HSLDHPNLIRLYGvVLSS--PLMM 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 662 ITEYCCYGDLLNFLRRKAEAMlgpslspgqdpeggvdyknihlekkyvrrdsgfssqgvdtyvemrPVSTssndsfseqd 741
Cdd:cd05040   75 VTELAPLGSLLDRLRKDQGHF---------------------------------------------LIST---------- 99
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 742 ldkedgrplelrdLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDI-MNDSNYIVKGNARLPVK 820
Cdd:cd05040  100 -------------LCDYAVQIANGMAYLESKRFIHRDLAARNILLASKDKVKIGDFGLMRALpQNEDHYVMQEHRKVPFA 166
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 821 WMAPESIFDCVYTVQSDVWSYGILLWEIFSLGLNPYPGILVNSKFYKLVKDGYQMAQPAFAPKNIYSIMQACWALEPTHR 900
Cdd:cd05040  167 WCAPESLKTRKFSHASDVWMFGVTLWEMFTYGEEPWLGLNGSQILEKIDKEGERLERPDDCPQDIYNVMLQCWAHKPADR 246
                        330
                 ....*....|..
gi 569026720 901 PTFQQICSFLQE 912
Cdd:cd05040  247 PTFVALRDFLPE 258
PTKc_TrkC cd05094
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase C; PTKs catalyze ...
579-910 7.61e-52

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: 183.67  E-value: 7.61e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 579 RNNLQFGKTLGAGAFGKVVEATAFGLGKEDAVLKVAVKMLKSTAHADEKEaLMSELKIMSHLgQHENIVNLLGACTHGGP 658
Cdd:cd05094    4 RRDIVLKRELGEGAFGKVFLAECYNLSPTKDKMLVAVKTLKDPTLAARKD-FQREAELLTNL-QHDHIVKFYGVCGDGDP 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 659 VLVITEYCCYGDLLNFLRrkaeamlgpslspgqdpeggvdyknihlekkyvrrdsgfsSQGVDTYVEMrpvstssndsfs 738
Cdd:cd05094   82 LIMVFEYMKHGDLNKFLR----------------------------------------AHGPDAMILV------------ 109
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 739 eqdldkeDGRPLE------LRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDIMNDSNYIVK 812
Cdd:cd05094  110 -------DGQPRQakgelgLSQMLHIATQIASGMVYLASQHFVHRDLATRNCLVGANLLVKIGDFGMSRDVYSTDYYRVG 182
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 813 GNARLPVKWMAPESIFDCVYTVQSDVWSYGILLWEIFSLGLNPYPGiLVNSKFYKLVKDGYQMAQPAFAPKNIYSIMQAC 892
Cdd:cd05094  183 GHTMLPIRWMPPESIMYRKFTTESDVWSFGVILWEIFTYGKQPWFQ-LSNTEVIECITQGRVLERPRVCPKEVYDIMLGC 261
                        330
                 ....*....|....*...
gi 569026720 893 WALEPTHRPTFQQICSFL 910
Cdd:cd05094  262 WQREPQQRLNIKEIYKIL 279
PTKc_Btk_Bmx cd05113
Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow ...
579-911 3.91e-51

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: 180.46  E-value: 3.91e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 579 RNNLQFGKTLGAGAFGKVveatafGLGKEDAVLKVAVKMLKSTAHADEKeaLMSELKIMSHLgQHENIVNLLGACTHGGP 658
Cdd:cd05113    3 PKDLTFLKELGTGQFGVV------KYGKWRGQYDVAIKMIKEGSMSEDE--FIEEAKVMMNL-SHEKLVQLYGVCTKQRP 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 659 VLVITEYCCYGDLLNFLRrkaeamlgpslspgqdpeggvdyknihlekkyvrrdsgfssqgvdtyvemrpvstssndsfs 738
Cdd:cd05113   74 IFIITEYMANGCLLNYLR-------------------------------------------------------------- 91
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 739 eqdldkEDGRPLELRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDIMNDSnYIVKGNARLP 818
Cdd:cd05113   92 ------EMRKRFQTQQLLEMCKDVCEAMEYLESKQFLHRDLAARNCLVNDQGVVKVSDFGLSRYVLDDE-YTSSVGSKFP 164
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 819 VKWMAPESIFDCVYTVQSDVWSYGILLWEIFSLGLNPYPgILVNSKFYKLVKDGYQMAQPAFAPKNIYSIMQACWALEPT 898
Cdd:cd05113  165 VRWSPPEVLMYSKFSSKSDVWAFGVLMWEVYSLGKMPYE-RFTNSETVEHVSQGLRLYRPHLASEKVYTIMYSCWHEKAD 243
                        330
                 ....*....|...
gi 569026720 899 HRPTFQQICSFLQ 911
Cdd:cd05113  244 ERPTFKILLSNIL 256
PTKc_Yes cd05069
Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the ...
573-912 5.24e-51

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: 181.04  E-value: 5.24e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 573 EKWEFPRNNLQFGKTLGAGAFGKVveatafGLGKEDAVLKVAVKMLKSTAHAdeKEALMSELKIMSHLgQHENIVNLLGA 652
Cdd:cd05069    5 DAWEIPRESLRLDVKLGQGCFGEV------WMGTWNGTTKVAIKTLKPGTMM--PEAFLQEAQIMKKL-RHDKLVPLYAV 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 653 CTHGgPVLVITEYCCYGDLLNFLRrkaeamlgpslspgqdpEGgvdyknihlekkyvrrdsgfssqgvdtyvemrpvsts 732
Cdd:cd05069   76 VSEE-PIYIVTEFMGKGSLLDFLK-----------------EG------------------------------------- 100
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 733 sndsfseqdldkeDGRPLELRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARdIMNDSNYIVK 812
Cdd:cd05069  101 -------------DGKYLKLPQLVDMAAQIADGMAYIERMNYIHRDLRAANILVGDNLVCKIADFGLAR-LIEDNEYTAR 166
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 813 GNARLPVKWMAPESIFDCVYTVQSDVWSYGILLWEIFSLGLNPYPGiLVNSKFYKLVKDGYQMAQPAFAPKNIYSIMQAC 892
Cdd:cd05069  167 QGAKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELVTKGRVPYPG-MVNREVLEQVERGYRMPCPQGCPESLHELMKLC 245
                        330       340
                 ....*....|....*....|
gi 569026720 893 WALEPTHRPTFQQICSFLQE 912
Cdd:cd05069  246 WKKDPDERPTFEYIQSFLED 265
PTKc_TrkB cd05093
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase B; PTKs catalyze ...
579-915 4.69e-50

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: 178.70  E-value: 4.69e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 579 RNNLQFGKTLGAGAFGKVVEATAFGLGKEDAVLKVAVKMLKSTAHADEKEaLMSELKIMSHLgQHENIVNLLGACTHGGP 658
Cdd:cd05093    4 RHNIVLKRELGEGAFGKVFLAECYNLCPEQDKILVAVKTLKDASDNARKD-FHREAELLTNL-QHEHIVKFYGVCVEGDP 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 659 VLVITEYCCYGDLLNFLRrkaeamlgpslspgqdpeggvdyknihlekkyvrrdsgfsSQGVDTYvemrpvstssndsfs 738
Cdd:cd05093   82 LIMVFEYMKHGDLNKFLR----------------------------------------AHGPDAV--------------- 106
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 739 eqdLDKEDGRPLELRD--LLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDIMNDSNYIVKGNAR 816
Cdd:cd05093  107 ---LMAEGNRPAELTQsqMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGMSRDVYSTDYYRVGGHTM 183
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 817 LPVKWMAPESIFDCVYTVQSDVWSYGILLWEIFSLGLNPYPGiLVNSKFYKLVKDGYQMAQPAFAPKNIYSIMQACWALE 896
Cdd:cd05093  184 LPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTYGKQPWYQ-LSNNEVIECITQGRVLQRPRTCPKEVYDLMLGCWQRE 262
                        330
                 ....*....|....*....
gi 569026720 897 PTHRPTFQQICSFLQEQAQ 915
Cdd:cd05093  263 PHMRLNIKEIHSLLQNLAK 281
PTKc_Mer cd14204
Catalytic Domain of the Protein Tyrosine Kinase, Mer; PTKs catalyze the transfer of the ...
579-906 7.47e-50

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: 177.82  E-value: 7.47e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 579 RNNLQFGKTLGAGAFGKVVEATafgLGKEDAV-LKVAVKMLK-STAHADEKEALMSELKIMSHLgQHENIVNLLGACTHG 656
Cdd:cd14204    6 RNLLSLGKVLGEGEFGSVMEGE---LQQPDGTnHKVAVKTMKlDNFSQREIEEFLSEAACMKDF-NHPNVIRLLGVCLEV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 657 GP-----VLVITEYCCYGDLLNFLRRKAEAMlGPSLSPgqdpeggvdyknihlekkyvrrdsgfssqgvdtyvemrpvst 731
Cdd:cd14204   82 GSqripkPMVILPFMKYGDLHSFLLRSRLGS-GPQHVP------------------------------------------ 118
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 732 ssndsfseqdldkedgrpleLRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDIMNDSNYIV 811
Cdd:cd14204  119 --------------------LQTLLKFMIDIALGMEYLSSRNFLHRDLAARNCMLRDDMTVCVADFGLSKKIYSGDYYRQ 178
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 812 KGNARLPVKWMAPESIFDCVYTVQSDVWSYGILLWEIFSLGLNPYPGILvNSKFYKLVKDGYQMAQPAFAPKNIYSIMQA 891
Cdd:cd14204  179 GRIAKMPVKWIAVESLADRVYTVKSDVWAFGVTMWEIATRGMTPYPGVQ-NHEIYDYLLHGHRLKQPEDCLDELYDIMYS 257
                        330
                 ....*....|....*
gi 569026720 892 CWALEPTHRPTFQQI 906
Cdd:cd14204  258 CWRSDPTDRPTFTQL 272
PTKc_DDR1 cd05096
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 1; PTKs catalyze ...
576-912 2.62e-49

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: 177.05  E-value: 2.62e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 576 EFPRNNLQFGKTLGAGAFGKV----VEAT--------AFGLGKEDAVLkVAVKMLKSTAHADEKEALMSELKIMSHLgQH 643
Cdd:cd05096    1 KFPRGHLLFKEKLGEGQFGEVhlceVVNPqdlptlqfPFNVRKGRPLL-VAVKILRPDANKNARNDFLKEVKILSRL-KD 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 644 ENIVNLLGACTHGGPVLVITEYCCYGDLLNFLRRKaeamlgpslspgqdpeggvdykniHLEKKyvrrdsgfSSQGVDTY 723
Cdd:cd05096   79 PNIIRLLGVCVDEDPLCMITEYMENGDLNQFLSSH------------------------HLDDK--------EENGNDAV 126
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 724 VEMRPVSTSSNDSfseqdldkedgrplelrdLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDI 803
Cdd:cd05096  127 PPAHCLPAISYSS------------------LLHVALQIASGMKYLSSLNFVHRDLATRNCLVGENLTIKIADFGMSRNL 188
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 804 MNDSNYIVKGNARLPVKWMAPESIFDCVYTVQSDVWSYGILLWEIFSL-GLNPY-----PGILVNS-KFYKLVKDGYQMA 876
Cdd:cd05096  189 YAGDYYRIQGRAVLPIRWMAWECILMGKFTTASDVWAFGVTLWEILMLcKEQPYgeltdEQVIENAgEFFRDQGRQVYLF 268
                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 569026720 877 QPAFAPKNIYSIMQACWALEPTHRPTFQQICSFLQE 912
Cdd:cd05096  269 RPPPCPQGLYELMLQCWSRDCRERPSFSDIHAFLTE 304
PTKc_Fyn cd05070
Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the ...
573-912 2.37e-48

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: 173.33  E-value: 2.37e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 573 EKWEFPRNNLQFGKTLGAGAFGKVveatafGLGKEDAVLKVAVKMLKSTAHAdeKEALMSELKIMSHLgQHENIVNLLGA 652
Cdd:cd05070    2 DVWEIPRESLQLIKRLGNGQFGEV------WMGTWNGNTKVAIKTLKPGTMS--PESFLEEAQIMKKL-KHDKLVQLYAV 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 653 CTHGgPVLVITEYCCYGDLLNFLRrkaeamlgpslspgqdpeggvdyknihlekkyvrrdsgfssqgvdtyvemrpvsts 732
Cdd:cd05070   73 VSEE-PIYIVTEYMSKGSLLDFLK-------------------------------------------------------- 95
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 733 sndsfseqdlDKEdGRPLELRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARdIMNDSNYIVK 812
Cdd:cd05070   96 ----------DGE-GRALKLPNLVDMAAQVAAGMAYIERMNYIHRDLRSANILVGNGLICKIADFGLAR-LIEDNEYTAR 163
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 813 GNARLPVKWMAPESIFDCVYTVQSDVWSYGILLWEIFSLGLNPYPGiLVNSKFYKLVKDGYQMAQPAFAPKNIYSIMQAC 892
Cdd:cd05070  164 QGAKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELVTKGRVPYPG-MNNREVLEQVERGYRMPCPQDCPISLHELMIHC 242
                        330       340
                 ....*....|....*....|
gi 569026720 893 WALEPTHRPTFQQICSFLQE 912
Cdd:cd05070  243 WKKDPEERPTFEYLQGFLED 262
PTKc_Ror1 cd05090
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
576-906 3.43e-48

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: 173.27  E-value: 3.43e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 576 EFPRNNLQFGKTLGAGAFGKVVEATAFGLGKEDAVLkVAVKMLKSTAHADEKEALMSELKIMSHLgQHENIVNLLGACTH 655
Cdd:cd05090    1 ELPLSAVRFMEELGECAFGKIYKGHLYLPGMDHAQL-VAIKTLKDYNNPQQWNEFQQEASLMTEL-HHPNIVCLLGVVTQ 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 656 GGPVLVITEYCCYGDLLNFLRRKaeamlgpslSPGQDpeggvdyknihlekkyvrrdsgfssqgvdtyvemrpVSTSSNd 735
Cdd:cd05090   79 EQPVCMLFEFMNQGDLHEFLIMR---------SPHSD------------------------------------VGCSSD- 112
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 736 sfseqdldkEDG---RPLELRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDIMNDSNYIVK 812
Cdd:cd05090  113 ---------EDGtvkSSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILVGEQLHVKISDLGLSREIYSSDYYRVQ 183
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 813 GNARLPVKWMAPESIFDCVYTVQSDVWSYGILLWEIFSLGLNPYPGiLVNSKFYKLVKDGYQMAQPAFAPKNIYSIMQAC 892
Cdd:cd05090  184 NKSLLPIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSFGLQPYYG-FSNQEVIEMVRKRQLLPCSEDCPPRMYSLMTEC 262
                        330
                 ....*....|....
gi 569026720 893 WALEPTHRPTFQQI 906
Cdd:cd05090  263 WQEIPSRRPRFKDI 276
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
583-906 1.11e-47

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 170.40  E-value: 1.11e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720   583 QFGKTLGAGAFGKVVEATAFGLGKedavlKVAVKMLKSTAHADEKEALMSELKIMSHLgQHENIVNLLGACTHGGPVLVI 662
Cdd:smart00220   2 EILEKLGEGSFGKVYLARDKKTGK-----LVAIKVIKKKKIKKDRERILREIKILKKL-KHPNIVRLYDVFEDEDKLYLV 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720   663 TEYCCYGDLLNFLRRKaeamlgpslspgqdpeggvdyknihlekkyvrrdsgfssqgvdtyvemrpvstssndsfseqdl 742
Cdd:smart00220  76 MEYCEGGDLFDLLKKR---------------------------------------------------------------- 91
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720   743 dkedgRPLELRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDIMNDSN---YIVkgnarlPV 819
Cdd:smart00220  92 -----GRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLARQLDPGEKlttFVG------TP 160
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720   820 KWMAPESIFDCVYTVQSDVWSYGILLWEIFSlGLNPYPGILVNSKFYKLVKDGY--QMAQPAFAPKNIYSIMQACWALEP 897
Cdd:smart00220 161 EYMAPEVLLGKGYGKAVDIWSLGVILYELLT-GKPPFPGDDQLLELFKKIGKPKppFPPPEWDISPEAKDLIRKLLVKDP 239

                   ....*....
gi 569026720   898 THRPTFQQI 906
Cdd:smart00220 240 EKRLTAEEA 248
PTKc_Tyro3 cd05074
Catalytic domain of the Protein Tyrosine Kinase, Tyro3; PTKs catalyze the transfer of the ...
578-911 3.26e-47

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: 170.48  E-value: 3.26e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 578 PRNNLQFGKTLGAGAFGKVVEATafgLGKED-AVLKVAVKMLKSTAHADEK-EALMSELKIMSHLgQHENIVNLLGACTH 655
Cdd:cd05074    7 QEQQFTLGRMLGKGEFGSVREAQ---LKSEDgSFQKVAVKMLKADIFSSSDiEEFLREAACMKEF-DHPNVIKLIGVSLR 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 656 GGPV------LVITEYCCYGDLLNFLrrkaeamLGPSLspGQDPeggvdyknihlekkyvrrdsgfssqgvdtyvemrpv 729
Cdd:cd05074   83 SRAKgrlpipMVILPFMKHGDLHTFL-------LMSRI--GEEP------------------------------------ 117
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 730 stssndsFSeqdldkedgrpLELRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDIMNDSNY 809
Cdd:cd05074  118 -------FT-----------LPLQTLVRFMIDIASGMEYLSSKNFIHRDLAARNCMLNENMTVCVADFGLSKKIYSGDYY 179
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 810 IVKGNARLPVKWMAPESIFDCVYTVQSDVWSYGILLWEIFSLGLNPYPGIlVNSKFYKLVKDGYQMAQPAFAPKNIYSIM 889
Cdd:cd05074  180 RQGCASKLPVKWLALESLADNVYTTHSDVWAFGVTMWEIMTRGQTPYAGV-ENSEIYNYLIKGNRLKQPPDCLEDVYELM 258
                        330       340
                 ....*....|....*....|..
gi 569026720 890 QACWALEPTHRPTFQQICSFLQ 911
Cdd:cd05074  259 CQCWSPEPKCRPSFQHLRDQLE 280
PTKc_Src cd05071
Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the ...
573-912 1.78e-46

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: 167.94  E-value: 1.78e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 573 EKWEFPRNNLQFGKTLGAGAFGKVveatafGLGKEDAVLKVAVKMLKSTAHAdeKEALMSELKIMSHLgQHENIVNLLGA 652
Cdd:cd05071    2 DAWEIPRESLRLEVKLGQGCFGEV------WMGTWNGTTRVAIKTLKPGTMS--PEAFLQEAQVMKKL-RHEKLVQLYAV 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 653 CTHGgPVLVITEYCCYGDLLNFLRrkaeamlgpslspgqdpeggvdyknihlekkyvrrdsgfssqgvdtyvemrpvsts 732
Cdd:cd05071   73 VSEE-PIYIVTEYMSKGSLLDFLK-------------------------------------------------------- 95
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 733 sndsfseqdldKEDGRPLELRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARdIMNDSNYIVK 812
Cdd:cd05071   96 -----------GEMGKYLRLPQLVDMAAQIASGMAYVERMNYVHRDLRAANILVGENLVCKVADFGLAR-LIEDNEYTAR 163
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 813 GNARLPVKWMAPESIFDCVYTVQSDVWSYGILLWEIFSLGLNPYPGiLVNSKFYKLVKDGYQMAQPAFAPKNIYSIMQAC 892
Cdd:cd05071  164 QGAKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELTTKGRVPYPG-MVNREVLDQVERGYRMPCPPECPESLHDLMCQC 242
                        330       340
                 ....*....|....*....|
gi 569026720 893 WALEPTHRPTFQQICSFLQE 912
Cdd:cd05071  243 WRKEPEERPTFEYLQAFLED 262
PTK_Ryk cd05043
Pseudokinase domain of Ryk (Receptor related to tyrosine kinase); Ryk is a receptor tyr kinase ...
591-912 1.02e-45

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: 165.70  E-value: 1.02e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 591 GAFGKVVEATafgLGKEDAVLK-VAVKMLKSTAHADEKEALMSELKIMSHLgQHENIVNLLGACTH-GGPVLVITEYCCY 668
Cdd:cd05043   17 GTFGRIFHGI---LRDEKGKEEeVLVKTVKDHASEIQVTMLLQESSLLYGL-SHQNLLPILHVCIEdGEKPMVLYPYMNW 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 669 GDLLNFLRRkaeamlgPSLSPGQDPeggvdyknihlekkyvrrdsgfssqgvdtyvemRPVSTssndsfseqdldkedgr 748
Cdd:cd05043   93 GNLKLFLQQ-------CRLSEANNP---------------------------------QALST----------------- 115
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 749 plelRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDIMNDSNYIVKGNARLPVKWMAPESIF 828
Cdd:cd05043  116 ----QQLVHMALQIACGMSYLHRRGVIHKDIAARNCVIDDELQVKITDNALSRDLFPMDYHCLGDNENRPIKWMSLESLV 191
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 829 DCVYTVQSDVWSYGILLWEIFSLGLNPYPGILVnSKFYKLVKDGYQMAQPAFAPKNIYSIMQACWALEPTHRPTFQQICS 908
Cdd:cd05043  192 NKEYSSASDVWSFGVLLWELMTLGQTPYVEIDP-FEMAAYLKDGYRLAQPINCPDELFAVMACCWALDPEERPSFQQLVQ 270

                 ....
gi 569026720 909 FLQE 912
Cdd:cd05043  271 CLTD 274
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
588-906 6.33e-45

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: 161.28  E-value: 6.33e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 588 LGAGAFGKVVEATAFGLGKedavlKVAVKMLKSTAHADEKEALMSELKIMSHLgQHENIVNLLGACTHGGPVLVITEYCC 667
Cdd:cd00180    1 LGKGSFGKVYKARDKETGK-----KVAVKVIPKEKLKKLLEELLREIEILKKL-NHPNIVKLYDVFETENFLYLVMEYCE 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 668 YGDLLNFLRRKaeamlgpslspgqdpeggvdyknihlekkyvrrdsgfssqgvdtyvemrpvstssndsfseqdldkedG 747
Cdd:cd00180   75 GGSLKDLLKEN--------------------------------------------------------------------K 86
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 748 RPLELRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDIMNDSNYIVKGNARLPVKWMAPESI 827
Cdd:cd00180   87 GPLSEEEALSILRQLLSALEYLHSNGIIHRDLKPENILLDSDGTVKLADFGLAKDLDSDDSLLKTTGGTTPPYYAPPELL 166
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 569026720 828 FDCVYTVQSDVWSYGILLWEIfslglnpypgilvnskfyklvkdgyqmaqpafapKNIYSIMQACWALEPTHRPTFQQI 906
Cdd:cd00180  167 GGRYYGPKVDIWSLGVILYEL----------------------------------EELKDLIRRMLQYDPKKRPSAKEL 211
PTKc_Tec_Rlk cd05114
Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular ...
582-915 1.24e-44

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: 161.95  E-value: 1.24e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 582 LQFGKTLGAGAFGKVveatafGLGKEDAVLKVAVKMLKSTAHADEKeaLMSELKIMSHLgQHENIVNLLGACTHGGPVLV 661
Cdd:cd05114    6 LTFMKELGSGLFGVV------RLGKWRAQYKVAIKAIREGAMSEED--FIEEAKVMMKL-THPKLVQLYGVCTQQKPIYI 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 662 ITEYCCYGDLLNFLRRKaeamlgpslspgqdpeggvdyknihleKKYVRRDSgfssqgvdtyvemrpvstssndsfseqd 741
Cdd:cd05114   77 VTEFMENGCLLNYLRQR---------------------------RGKLSRDM---------------------------- 101
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 742 ldkedgrplelrdLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDIMNDsNYIVKGNARLPVKW 821
Cdd:cd05114  102 -------------LLSMCQDVCEGMEYLERNNFIHRDLAARNCLVNDTGVVKVSDFGMTRYVLDD-QYTSSSGAKFPVKW 167
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 822 MAPESIFDCVYTVQSDVWSYGILLWEIFSLGLNPYPGiLVNSKFYKLVKDGYQMAQPAFAPKNIYSIMQACWALEPTHRP 901
Cdd:cd05114  168 SPPEVFNYSKFSSKSDVWSFGVLMWEVFTEGKMPFES-KSNYEVVEMVSRGHRLYRPKLASKSVYEVMYSCWHEKPEGRP 246
                        330
                 ....*....|....
gi 569026720 902 TFQQICSFLQEQAQ 915
Cdd:cd05114  247 TFADLLRTITEIAE 260
PTKc_EphR_A2 cd05063
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the ...
586-912 4.68e-43

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: 157.83  E-value: 4.68e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 586 KTLGAGAFGKVVEATAFGLGKEDAVlkVAVKMLKSTAHADEKEALMSELKIMSHLGqHENIVNLLGACTHGGPVLVITEY 665
Cdd:cd05063   11 KVIGAGEFGEVFRGILKMPGRKEVA--VAIKTLKPGYTEKQRQDFLSEASIMGQFS-HHNIIRLEGVVTKFKPAMIITEY 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 666 CCYGDLLNFLRRKaeamlgpslspgqdpeggvdyknihlekkyvrrDSGFSsqgvdtyvemrpvstssndsfseqdldke 745
Cdd:cd05063   88 MENGALDKYLRDH---------------------------------DGEFS----------------------------- 105
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 746 dgrPLELRDLLHfssQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDIMND--SNYIVKGnARLPVKWMA 823
Cdd:cd05063  106 ---SYQLVGMLR---GIAAGMKYLSDMNYVHRDLAARNILVNSNLECKVSDFGLSRVLEDDpeGTYTTSG-GKIPIRWTA 178
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 824 PESIFDCVYTVQSDVWSYGILLWEIFSLGLNPYPGiLVNSKFYKLVKDGYQMAQPAFAPKNIYSIMQACWALEPTHRPTF 903
Cdd:cd05063  179 PEAIAYRKFTSASDVWSFGIVMWEVMSFGERPYWD-MSNHEVMKAINDGFRLPAPMDCPSAVYQLMLQCWQQDRARRPRF 257

                 ....*....
gi 569026720 904 QQICSFLQE 912
Cdd:cd05063  258 VDIVNLLDK 266
PTKc_EphR_A cd05066
Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors; PTKs catalyze ...
580-910 5.29e-43

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: 157.72  E-value: 5.29e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 580 NNLQFGKTLGAGAFGKVVEATAFGLGKEDavLKVAVKMLKSTAHADEKEALMSELKIMSHLgQHENIVNLLGACTHGGPV 659
Cdd:cd05066    4 SCIKIEKVIGAGEFGEVCSGRLKLPGKRE--IPVAIKTLKAGYTEKQRRDFLSEASIMGQF-DHPNIIHLEGVVTRSKPV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 660 LVITEYCCYGDLLNFLRrkaeamlgpslspgqdpeggvdyknihlekkyvrrdsgfssqgvdtyvemrpvstssndsfse 739
Cdd:cd05066   81 MIVTEYMENGSLDAFLR--------------------------------------------------------------- 97
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 740 qdldKEDGRpLELRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDIMND--SNYIVKGnARL 817
Cdd:cd05066   98 ----KHDGQ-FTVIQLVGMLRGIASGMKYLSDMGYVHRDLAARNILVNSNLVCKVSDFGLSRVLEDDpeAAYTTRG-GKI 171
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 818 PVKWMAPESIFDCVYTVQSDVWSYGILLWEIFSLGLNPYPGiLVNSKFYKLVKDGYQMAQPAFAPKNIYSIMQACWALEP 897
Cdd:cd05066  172 PIRWTAPEAIAYRKFTSASDVWSYGIVMWEVMSYGERPYWE-MSNQDVIKAIEEGYRLPAPMDCPAALHQLMLDCWQKDR 250
                        330
                 ....*....|...
gi 569026720 898 THRPTFQQICSFL 910
Cdd:cd05066  251 NERPKFEQIVSIL 263
PTKc_EGFR cd05108
Catalytic domain of the Protein Tyrosine Kinase, Epidermal Growth Factor Receptor; PTKs ...
586-919 1.97e-42

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: 157.49  E-value: 1.97e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 586 KTLGAGAFGKVVEATAFGLGkEDAVLKVAVKMLKSTAHADEKEALMSELKIMSHLgQHENIVNLLGACTHGGpVLVITEY 665
Cdd:cd05108   13 KVLGSGAFGTVYKGLWIPEG-EKVKIPVAIKELREATSPKANKEILDEAYVMASV-DNPHVCRLLGICLTST-VQLITQL 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 666 CCYGDLLNFLRRKAEAMLGpslspgqdpeggvdyknihlekkyvrrdsgfssqgvdtyvemrpvstssndsfseqdldke 745
Cdd:cd05108   90 MPFGCLLDYVREHKDNIGS------------------------------------------------------------- 108
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 746 dgrplelRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDIMNDSNYIVKGNARLPVKWMAPE 825
Cdd:cd05108  109 -------QYLLNWCVQIAKGMNYLEDRRLVHRDLAARNVLVKTPQHVKITDFGLAKLLGAEEKEYHAEGGKVPIKWMALE 181
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 826 SIFDCVYTVQSDVWSYGILLWEIFSLGLNPYPGILVnSKFYKLVKDGYQMAQPAFAPKNIYSIMQACWALEPTHRPTFQQ 905
Cdd:cd05108  182 SILHRIYTHQSDVWSYGVTVWELMTFGSKPYDGIPA-SEISSILEKGERLPQPPICTIDVYMIMVKCWMIDADSRPKFRE 260
                        330
                 ....*....|....
gi 569026720 906 ICSFLQEQAQEDRR 919
Cdd:cd05108  261 LIIEFSKMARDPQR 274
PTKc_Itk cd05112
Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs ...
580-903 2.34e-42

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: 155.49  E-value: 2.34e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 580 NNLQFGKTLGAGAFGKVVeatafgLGKEDAVLKVAVKMLKSTAHADEKeaLMSELKIMSHLgQHENIVNLLGACTHGGPV 659
Cdd:cd05112    4 SELTFVQEIGSGQFGLVH------LGYWLNKDKVAIKTIREGAMSEED--FIEEAEVMMKL-SHPKLVQLYGVCLEQAPI 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 660 LVITEYCCYGDLLNFLRrkaeamlgpslspgqdpeggvdyknihlekkyvrrdsgfssqgvdtyvemrpvstSSNDSFSE 739
Cdd:cd05112   75 CLVFEFMEHGCLSDYLR-------------------------------------------------------TQRGLFSA 99
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 740 QDLdkedgrplelrdlLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDIMNDsNYIVKGNARLPV 819
Cdd:cd05112  100 ETL-------------LGMCLDVCEGMAYLEEASVIHRDLAARNCLVGENQVVKVSDFGMTRFVLDD-QYTSSTGTKFPV 165
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 820 KWMAPESIFDCVYTVQSDVWSYGILLWEIFSLGLNPYPGiLVNSKFYKLVKDGYQMAQPAFAPKNIYSIMQACWALEPTH 899
Cdd:cd05112  166 KWSSPEVFSFSRYSSKSDVWSFGVLMWEVFSEGKIPYEN-RSNSEVVEDINAGFRLYKPRLASTHVYEIMNHCWKERPED 244

                 ....
gi 569026720 900 RPTF 903
Cdd:cd05112  245 RPSF 248
PTKc_Syk cd05116
Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; PTKs catalyze the ...
586-903 8.85e-42

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: 153.96  E-value: 8.85e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 586 KTLGAGAFGKVVEatafGLGKEDAVLK-VAVKMLKSTAH-ADEKEALMSELKIMSHLgQHENIVNLLGACtHGGPVLVIT 663
Cdd:cd05116    1 GELGSGNFGTVKK----GYYQMKKVVKtVAVKILKNEANdPALKDELLREANVMQQL-DNPYIVRMIGIC-EAESWMLVM 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 664 EYCCYGDLLNFLRrkaeamlgpslspgqdpeggvdyKNIHLEKKyvrrdsgfssqgvdtyvemrpvstssndsfseqdld 743
Cdd:cd05116   75 EMAELGPLNKFLQ-----------------------KNRHVTEK------------------------------------ 95
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 744 kedgrplELRDLLHfssQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDIMNDSNYI-VKGNARLPVKWM 822
Cdd:cd05116   96 -------NITELVH---QVSMGMKYLEESNFVHRDLAARNVLLVTQHYAKISDFGLSKALRADENYYkAQTHGKWPVKWY 165
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 823 APESIFDCVYTVQSDVWSYGILLWEIFSLGLNPYPGiLVNSKFYKLVKDGYQMAQPAFAPKNIYSIMQACWALEPTHRPT 902
Cdd:cd05116  166 APECMNYYKFSSKSDVWSFGVLMWEAFSYGQKPYKG-MKGNEVTQMIEKGERMECPAGCPPEMYDLMKLCWTYDVDERPG 244

                 .
gi 569026720 903 F 903
Cdd:cd05116  245 F 245
Pkinase pfam00069
Protein kinase domain;
582-908 1.11e-41

Protein kinase domain;


Pssm-ID: 425449 [Multi-domain]  Cd Length: 254  Bit Score: 153.53  E-value: 1.11e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720  582 LQFGKTLGAGAFGKVVEATAFGLGKedavlKVAVKML-KSTAHADEKEALMSELKIMSHLgQHENIVNLLGACTHGGPVL 660
Cdd:pfam00069   1 YEVLEKLGSGSFGTVYKAKHRDTGK-----IVAIKKIkKEKIKKKKDKNILREIKILKKL-NHPNIVRLYDAFEDKDNLY 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720  661 VITEYCCYGDLLNFLRRKAeamlgpslspgqdpeggvdyknihlekkyvrrdsgfssqgvdtyvemrpvstssndSFSEq 740
Cdd:pfam00069  75 LVLEYVEGGSLFDLLSEKG--------------------------------------------------------AFSE- 97
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720  741 dldkedgrplelRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLL-TNGHVaKIGDFGLARDIMNDSNY-IVKGNARlp 818
Cdd:pfam00069  98 ------------REAKFIMKQILEGLEYLHSNGIVHRDLKPENILIdEDGNL-KITDFGLARQLNSGSSLtTFVGTPW-- 162
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720  819 vkWMAPESIFDCVYTVQSDVWSYGILLWEIFSlGLNPYPGILVNSKFYKLVKDGYQMAQPAF-APKNIYSIMQACWALEP 897
Cdd:pfam00069 163 --YMAPEVLGGNPYGPKVDVWSLGCILYELLT-GKPPFPGINGNEIYELIIDQPYAFPELPSnLSEEAKDLLKKLLKKDP 239
                         330
                  ....*....|.
gi 569026720  898 THRPTFQQICS 908
Cdd:pfam00069 240 SKRLTATEALQ 250
PTKc_HER2 cd05109
Catalytic domain of the Protein Tyrosine Kinase, HER2; PTKs catalyze the transfer of the ...
586-919 6.39e-41

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: 152.10  E-value: 6.39e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 586 KTLGAGAFGKVVEATAFGLGkEDAVLKVAVKMLKSTAHADEKEALMSELKIMSHLGQhENIVNLLGACThGGPVLVITEY 665
Cdd:cd05109   13 KVLGSGAFGTVYKGIWIPDG-ENVKIPVAIKVLRENTSPKANKEILDEAYVMAGVGS-PYVCRLLGICL-TSTVQLVTQL 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 666 CCYGDLLNFLRrkaeamlgpslspgqdpeggvdyknihlekkyvrrdsgfssqgvdtyvemrpvstssndsfseqdldkE 745
Cdd:cd05109   90 MPYGCLLDYVR--------------------------------------------------------------------E 101
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 746 DGRPLELRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDI-MNDSNYIVKGnARLPVKWMAP 824
Cdd:cd05109  102 NKDRIGSQDLLNWCVQIAKGMSYLEEVRLVHRDLAARNVLVKSPNHVKITDFGLARLLdIDETEYHADG-GKVPIKWMAL 180
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 825 ESIFDCVYTVQSDVWSYGILLWEIFSLGLNPYPGILVNsKFYKLVKDGYQMAQPAFAPKNIYSIMQACWALEPTHRPTFQ 904
Cdd:cd05109  181 ESILHRRFTHQSDVWSYGVTVWELMTFGAKPYDGIPAR-EIPDLLEKGERLPQPPICTIDVYMIMVKCWMIDSECRPRFR 259
                        330
                 ....*....|....*
gi 569026720 905 QICSFLQEQAQEDRR 919
Cdd:cd05109  260 ELVDEFSRMARDPSR 274
PTKc_EphR_B cd05065
Catalytic domain of the Protein Tyrosine Kinases, Class EphB Ephrin Receptors; PTKs catalyze ...
586-910 7.79e-40

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


Pssm-ID: 173638 [Multi-domain]  Cd Length: 269  Bit Score: 148.48  E-value: 7.79e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 586 KTLGAGAFGKVVEATAFGLGKEDAVlkVAVKMLKSTAHADEKEALMSELKIMSHLgQHENIVNLLGACTHGGPVLVITEY 665
Cdd:cd05065   10 EVIGAGEFGEVCRGRLKLPGKREIF--VAIKTLKSGYTEKQRRDFLSEASIMGQF-DHPNIIHLEGVVTKSRPVMIITEF 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 666 CCYGDLLNFLRRKaeamlgpslspgqdpeggvdyknihlekkyvrrDSGFSsqgvdtyvemrpvstssndsfseqdldke 745
Cdd:cd05065   87 MENGALDSFLRQN---------------------------------DGQFT----------------------------- 104
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 746 dgrPLELRDLLHfssQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDIMNDSN---YIVKGNARLPVKWM 822
Cdd:cd05065  105 ---VIQLVGMLR---GIAAGMKYLSEMNYVHRDLAARNILVNSNLVCKVSDFGLSRFLEDDTSdptYTSSLGGKIPIRWT 178
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 823 APESIFDCVYTVQSDVWSYGILLWEIFSLGLNPYPGiLVNSKFYKLVKDGYQMAQPAFAPKNIYSIMQACWALEPTHRPT 902
Cdd:cd05065  179 APEAIAYRKFTSASDVWSYGIVMWEVMSYGERPYWD-MSNQDVINAIEQDYRLPPPMDCPTALHQLMLDCWQKDRNLRPK 257

                 ....*...
gi 569026720 903 FQQICSFL 910
Cdd:cd05065  258 FGQIVNTL 265
PTKc_Tyk2_rpt2 cd05080
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze ...
577-912 8.29e-40

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: 148.89  E-value: 8.29e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 577 FPRNNLQFGKTLGAGAFGKVVeATAFGLGKEDAVLKVAVKMLKSTAHADEKEALMSELKIMSHLgQHENIVNLLGACTHG 656
Cdd:cd05080    1 FHKRYLKKIRDLGEGHFGKVS-LYCYDPTNDGTGEMVAVKALKADCGPQHRSGWKQEIDILKTL-YHENIVKYKGCCSEQ 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 657 GP--VLVITEYCCYGDLLNFLRRKAeamlgpslspgqdpeggvdyknihlekkyvrrdsgfssqgvdtyvemrpvstssn 734
Cdd:cd05080   79 GGksLQLIMEYVPLGSLRDYLPKHS------------------------------------------------------- 103
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 735 dsfseqdldkedgrpLELRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDIMNDSNYI-VKG 813
Cdd:cd05080  104 ---------------IGLAQLLLFAQQICEGMAYLHSQHYIHRDLAARNVLLDNDRLVKIGDFGLAKAVPEGHEYYrVRE 168
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 814 NARLPVKWMAPESIFDCVYTVQSDVWSYGILLWEI-------------FSLGLNPYPGILVNSKFYKLVKDGYQMAQPAF 880
Cdd:cd05080  169 DGDSPVFWYAPECLKEYKFYYASDVWSFGVTLYELlthcdssqspptkFLEMIGIAQGQMTVVRLIELLERGERLPCPDK 248
                        330       340       350
                 ....*....|....*....|....*....|..
gi 569026720 881 APKNIYSIMQACWALEPTHRPTFQQICSFLQE 912
Cdd:cd05080  249 CPQEVYHLMKNCWETEASFRPTFENLIPILKT 280
PTKc_Zap-70 cd05115
Catalytic domain of the Protein Tyrosine Kinase, Zeta-chain-associated protein of 70kDa; PTKs ...
588-906 8.87e-40

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: 148.56  E-value: 8.87e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 588 LGAGAFGkVVEATAFGLGKEDavLKVAVKMLKSTAHADEKEALMSELKIMSHLgQHENIVNLLGACTHGGPVLVItEYCC 667
Cdd:cd05115   12 LGSGNFG-CVKKGVYKMRKKQ--IDVAIKVLKQGNEKAVRDEMMREAQIMHQL-DNPYIVRMIGVCEAEALMLVM-EMAS 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 668 YGDLLNFLRRKAEAMlgpslspgqdpeggvdyknihlekkyvrrdsgfssqgvdtyvemrpvsTSSNdsfseqdldkedg 747
Cdd:cd05115   87 GGPLNKFLSGKKDEI------------------------------------------------TVSN------------- 105
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 748 rpleLRDLLHfssQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDI-MNDSNYIVKGNARLPVKWMAPES 826
Cdd:cd05115  106 ----VVELMH---QVSMGMKYLEEKNFVHRDLAARNVLLVNQHYAKISDFGLSKALgADDSYYKARSAGKWPLKWYAPEC 178
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 827 IFDCVYTVQSDVWSYGILLWEIFSLGLNPYPGiLVNSKFYKLVKDGYQMAQPAFAPKNIYSIMQACWALEPTHRPTFQQI 906
Cdd:cd05115  179 INFRKFSSRSDVWSYGVTMWEAFSYGQKPYKK-MKGPEVMSFIEQGKRMDCPAECPPEMYALMSDCWIYKWEDRPNFLTV 257
STKc_TAK1 cd14058
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated ...
588-915 2.33e-39

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: 146.81  E-value: 2.33e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 588 LGAGAFGKVVEATAFGLgkedavlKVAVKMLKSTAhadEKEALMSELKIMSHLgQHENIVNLLGACTHGGPVLVITEYCC 667
Cdd:cd14058    1 VGRGSFGVVCKARWRNQ-------IVAVKIIESES---EKKAFEVEVRQLSRV-DHPNIIKLYGACSNQKPVCLVMEYAE 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 668 YGDLLNFLRrkaeamlgpslspGQDPEggvdyknihlekkyvrrdsgfssqgvdtyvemrPVSTSSNdsfseqdldkedg 747
Cdd:cd14058   70 GGSLYNVLH-------------GKEPK---------------------------------PIYTAAH------------- 90
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 748 rplelrdLLHFSSQVAQGMAFLAS---KNCIHRDVAARNVLLTNGH-VAKIGDFGLARDImndSNYIV--KGNARlpvkW 821
Cdd:cd14058   91 -------AMSWALQCAKGVAYLHSmkpKALIHRDLKPPNLLLTNGGtVLKICDFGTACDI---STHMTnnKGSAA----W 156
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 822 MAPESIFDCVYTVQSDVWSYGILLWEIFSLGLnPYPGI-LVNSKFYKLVKDGYQMAQPAFAPKNIYSIMQACWALEPTHR 900
Cdd:cd14058  157 MAPEVFEGSKYSEKCDVFSWGIILWEVITRRK-PFDHIgGPAFRIMWAVHNGERPPLIKNCPKPIESLMTRCWSKDPEKR 235
                        330
                 ....*....|....*
gi 569026720 901 PTFQQICSFLQEQAQ 915
Cdd:cd14058  236 PSMKEIVKIMSHLMQ 250
PTKc_Jak1_rpt2 cd05079
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the ...
577-906 2.71e-39

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: 147.38  E-value: 2.71e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 577 FPRNNLQFGKTLGAGAFGKVvEATAFGLGKEDAVLKVAVKMLKSTAHADEKEALMSELKIMSHLgQHENIVNLLGACTHG 656
Cdd:cd05079    1 FEKRFLKRIRDLGEGHFGKV-ELCRYDPEGDNTGEQVAVKSLKPESGGNHIADLKKEIEILRNL-YHENIVKYKGICTED 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 657 G--PVLVITEYCCYGDLlnflrrkaeamlgpslspgqdpeggvdyknihleKKYVRRDSGfssqgvdtyvemrpvstssn 734
Cdd:cd05079   79 GgnGIKLIMEFLPSGSL----------------------------------KEYLPRNKN-------------------- 104
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 735 dsfseqdldkedgrPLELRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDIMNDSN-YIVKG 813
Cdd:cd05079  105 --------------KINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIETDKEyYTVKD 170
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 814 NARLPVKWMAPESIFDCVYTVQSDVWSYGILLWEI-------------FSLGLNPYPGILVNSKFYKLVKDGYQMAQPAF 880
Cdd:cd05079  171 DLDSPVFWYAPECLIQSKFYIASDVWSFGVTLYELltycdsesspmtlFLKMIGPTHGQMTVTRLVRVLEEGKRLPRPPN 250
                        330       340
                 ....*....|....*....|....*.
gi 569026720 881 APKNIYSIMQACWALEPTHRPTFQQI 906
Cdd:cd05079  251 CPEEVYQLMRKCWEFQPSKRTTFQNL 276
PTK_HER3 cd05111
Pseudokinase domain of the Protein Tyrosine Kinase, HER3; HER3 (ErbB3) is a member of the EGFR ...
577-919 8.45e-39

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: 145.87  E-value: 8.45e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 577 FPRNNLQFGKTLGAGAFGKVVEAtaFGLGKEDAV-LKVAVKMLKSTAHADEKEALMSELKIMSHLgQHENIVNLLGACTh 655
Cdd:cd05111    4 FKETELRKLKVLGSGVFGTVHKG--IWIPEGDSIkIPVAIKVIQDRSGRQSFQAVTDHMLAIGSL-DHAYIVRLLGICP- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 656 GGPVLVITEYCCYGDLLNFLRRKAEAmLGPSLspgqdpeggvdyknihlekkyvrrdsgfssqgvdtyvemrpvstssnd 735
Cdd:cd05111   80 GASLQLVTQLLPLGSLLDHVRQHRGS-LGPQL------------------------------------------------ 110
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 736 sfseqdldkedgrplelrdLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDIMNDSNYIVKGNA 815
Cdd:cd05111  111 -------------------LLNWCVQIAKGMYYLEEHRMVHRNLAARNVLLKSPSQVQVADFGVADLLYPDDKKYFYSEA 171
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 816 RLPVKWMAPESIFDCVYTVQSDVWSYGILLWEIFSLGLNPYPGILVnSKFYKLVKDGYQMAQPAFAPKNIYSIMQACWAL 895
Cdd:cd05111  172 KTPIKWMALESIHFGKYTHQSDVWSYGVTVWEMMTFGAEPYAGMRL-AEVPDLLEKGERLAQPQICTIDVYMVMVKCWMI 250
                        330       340
                 ....*....|....*....|....
gi 569026720 896 EPTHRPTFQQICSFLQEQAQEDRR 919
Cdd:cd05111  251 DENIRPTFKELANEFTRMARDPPR 274
PTKc_Jak2_rpt2 cd14205
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the ...
577-906 1.39e-38

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: 145.54  E-value: 1.39e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 577 FPRNNLQFGKTLGAGAFGKVvEATAFGLGKEDAVLKVAVKMLKSTAhADEKEALMSELKIMSHLgQHENIVNLLGACTHG 656
Cdd:cd14205    1 FEERHLKFLQQLGKGNFGSV-EMCRYDPLQDNTGEVVAVKKLQHST-EEHLRDFEREIEILKSL-QHDNIVKYKGVCYSA 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 657 G--PVLVITEYCCYGDLLNFLRRKAEAmlgpslspgqdpeggvdyknihlekkyvrrdsgfssqgvdtyvemrpvstssn 734
Cdd:cd14205   78 GrrNLRLIMEYLPYGSLRDYLQKHKER----------------------------------------------------- 104
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 735 dsfseqdldkedgrpLELRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDIMNDSNYI-VKG 813
Cdd:cd14205  105 ---------------IDHIKLLQYTSQICKGMEYLGTKRYIHRDLATRNILVENENRVKIGDFGLTKVLPQDKEYYkVKE 169
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 814 NARLPVKWMAPESIFDCVYTVQSDVWSYGILLWEIFS---------------LGlNPYPGILVNSKFYKLVKDGYQMAQP 878
Cdd:cd14205  170 PGESPIFWYAPESLTESKFSVASDVWSFGVVLYELFTyieksksppaefmrmIG-NDKQGQMIVFHLIELLKNNGRLPRP 248
                        330       340
                 ....*....|....*....|....*...
gi 569026720 879 AFAPKNIYSIMQACWALEPTHRPTFQQI 906
Cdd:cd14205  249 DGCPDEIYMIMTECWNNNVNQRPSFRDL 276
PTKc_Jak3_rpt2 cd05081
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the ...
577-906 1.40e-37

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: 142.34  E-value: 1.40e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 577 FPRNNLQFGKTLGAGAFGKVVEATAFGLGKEDAVLkVAVKMLKSTAhADEKEALMSELKIMSHLgQHENIVNLLGAC-TH 655
Cdd:cd05081    1 FEERHLKYISQLGKGNFGSVELCRYDPLGDNTGAL-VAVKQLQHSG-PDQQRDFQREIQILKAL-HSDFIVKYRGVSyGP 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 656 GGPVL-VITEYCCYGDLLNFLRRKaEAMLGPslspgqdpeggvdyknihlekkyvrrdsgfssqgvdtyvemrpvstssn 734
Cdd:cd05081   78 GRRSLrLVMEYLPSGCLRDFLQRH-RARLDA------------------------------------------------- 107
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 735 dsfseqdldkedgrplelRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDIMNDSN-YIVKG 813
Cdd:cd05081  108 ------------------SRLLLYSSQICKGMEYLGSRRCVHRDLAARNILVESEAHVKIADFGLAKLLPLDKDyYVVRE 169
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 814 NARLPVKWMAPESIFDCVYTVQSDVWSYGILLWEIFSLG-------------LNPYPGILVNSKFYKLVKDGYQMAQPAF 880
Cdd:cd05081  170 PGQSPIFWYAPESLSDNIFSRQSDVWSFGVVLYELFTYCdkscspsaeflrmMGCERDVPALCRLLELLEEGQRLPAPPA 249
                        330       340
                 ....*....|....*....|....*.
gi 569026720 881 APKNIYSIMQACWALEPTHRPTFQQI 906
Cdd:cd05081  250 CPAEVHELMKLCWAPSPQDRPSFSAL 275
PTKc_HER4 cd05110
Catalytic domain of the Protein Tyrosine Kinase, HER4; PTKs catalyze the transfer of the ...
586-919 5.01e-35

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: 135.58  E-value: 5.01e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 586 KTLGAGAFGKVVEATAFGLGkEDAVLKVAVKMLKSTAHADEKEALMSELKIMSHLgQHENIVNLLGACThGGPVLVITEY 665
Cdd:cd05110   13 KVLGSGAFGTVYKGIWVPEG-ETVKIPVAIKILNETTGPKANVEFMDEALIMASM-DHPHLVRLLGVCL-SPTIQLVTQL 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 666 CCYGDLLNFLRRKAEAmLGPSLspgqdpeggvdyknihlekkyvrrdsgfssqgvdtyvemrpvstssndsfseqdldke 745
Cdd:cd05110   90 MPHGCLLDYVHEHKDN-IGSQL---------------------------------------------------------- 110
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 746 dgrplelrdLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDIMNDSNYIVKGNARLPVKWMAPE 825
Cdd:cd05110  111 ---------LLNWCVQIAKGMMYLEERRLVHRDLAARNVLVKSPNHVKITDFGLARLLEGDEKEYNADGGKMPIKWMALE 181
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 826 SIFDCVYTVQSDVWSYGILLWEIFSLGLNPYPGIlVNSKFYKLVKDGYQMAQPAFAPKNIYSIMQACWALEPTHRPTFQQ 905
Cdd:cd05110  182 CIHYRKFTHQSDVWSYGVTIWELMTFGGKPYDGI-PTREIPDLLEKGERLPQPPICTIDVYMVMVKCWMIDADSRPKFKE 260
                        330
                 ....*....|....
gi 569026720 906 ICSFLQEQAQEDRR 919
Cdd:cd05110  261 LAAEFSRMARDPQR 274
PTKc_EphR_A10 cd05064
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A10; PTKs catalyze the ...
576-912 6.27e-34

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: 131.58  E-value: 6.27e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 576 EFPRNNLQFGKTLGAGAFGKVVEATAFGLGKEDavLKVAVKMLKSTAHADEKEALMSELKIMSHLgQHENIVNLLGACTH 655
Cdd:cd05064    1 ELDNKSIKIERILGTGRFGELCRGCLKLPSKRE--LPVAIHTLRAGCSDKQRRGFLAEALTLGQF-DHSNIVRLEGVITR 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 656 GGPVLVITEYCCYGDLLNFLRRKAEamlgpSLSPGQdpeggvdyknihlekkyvrrdsgfssqgvdtyvemrpvstssnd 735
Cdd:cd05064   78 GNTMMIVTEYMSNGALDSFLRKHEG-----QLVAGQ-------------------------------------------- 108
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 736 sfseqdldkedgrpleLRDLLhfsSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFG-LARDIMNDSNYIVKGn 814
Cdd:cd05064  109 ----------------LMGML---PGLASGMKYLSEMGYVHKGLAAHKVLVNSDLVCKISGFRrLQEDKSEAIYTTMSG- 168
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 815 aRLPVKWMAPESIFDCVYTVQSDVWSYGILLWEIFSLGLNPYPGiLVNSKFYKLVKDGYQMAQPAFAPKNIYSIMQACWA 894
Cdd:cd05064  169 -KSPVLWAAPEAIQYHHFSSASDVWSFGIVMWEVMSYGERPYWD-MSGQDVIKAVEDGFRLPAPRNCPNLLHQLMLDCWQ 246
                        330
                 ....*....|....*...
gi 569026720 895 LEPTHRPTFQQICSFLQE 912
Cdd:cd05064  247 KERGERPRFSQIHSILSK 264
PTKc_Aatyk3 cd14206
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 3; PTKs ...
588-911 1.29e-33

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: 130.84  E-value: 1.29e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 588 LGAGAFGKVVEATAFGlgkEDAVLKVAVKMLKSTAHADEKEALMSELKIMSHLgQHENIVNLLGACTHGGPVLVITEYCC 667
Cdd:cd14206    5 IGNGWFGKVILGEIFS---DYTPAQVVVKELRVSAGPLEQRKFISEAQPYRSL-QHPNILQCLGLCTETIPFLLIMEFCQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 668 YGDLLNFLR--RKAEAMlGPSLSPgqdpeggvdyknihlekkyvrRDsgfssqgvdtyvemrpvstssndsfseqdldke 745
Cdd:cd14206   81 LGDLKRYLRaqRKADGM-TPDLPT---------------------RD--------------------------------- 105
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 746 dgrpleLRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDIMNDSNYIVKGNARLPVKWMAPE 825
Cdd:cd14206  106 ------LRTLQRMAYEITLGLLHLHKNNYIHSDLALRNCLLTSDLTVRIGDYGLSHNNYKEDYYLTPDRLWIPLRWVAPE 179
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 826 -------SIFDCVYTVQSDVWSYGILLWEIFSLGLNPYPGILVNSKFYKLVKDGY-QMAQPAFAPKNI---YSIMQACWa 894
Cdd:cd14206  180 lldelhgNLIVVDQSKESNVWSLGVTIWELFEFGAQPYRHLSDEEVLTFVVREQQmKLAKPRLKLPYAdywYEIMQSCW- 258
                        330
                 ....*....|....*..
gi 569026720 895 LEPTHRPTFQQIcsFLQ 911
Cdd:cd14206  259 LPPSQRPSVEEL--HLQ 273
STKc_MAP3K12_13 cd14059
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase ...
588-910 2.51e-32

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: 125.68  E-value: 2.51e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 588 LGAGAFGKVVeatafgLGKEDAVlKVAVKMLKstahaDEKEalmSELKIMSHLgQHENIVNLLGACTHGGPVLVITEYCC 667
Cdd:cd14059    1 LGSGAQGAVF------LGKFRGE-EVAVKKVR-----DEKE---TDIKHLRKL-NHPNIIKFKGVCTQAPCYCILMEYCP 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 668 YGDLLNFLRrkaeamlgpslspgqdpeggvdyknihlekkyvrrdsgfssqgvdtyvemrpvstssndsfseqdldkeDG 747
Cdd:cd14059   65 YGQLYEVLR---------------------------------------------------------------------AG 75
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 748 RPLELRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDIMNDSnyiVKGNARLPVKWMAPESI 827
Cdd:cd14059   76 REITPSLLVDWSKQIASGMNYLHLHKIIHRDLKSPNVLVTYNDVLKISDFGTSKELSEKS---TKMSFAGTVAWMAPEVI 152
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 828 FDCVYTVQSDVWSYGILLWEIFSlGLNPYPGILVNSKFYKLVKDGYQMAQPAFAPKNIYSIMQACWALEPTHRPTFQQIC 907
Cdd:cd14059  153 RNEPCSEKVDIWSFGVVLWELLT-GEIPYKDVDSSAIIWGVGSNSLQLPVPSTCPDGFKLLMKQCWNSKPRNRPSFRQIL 231

                 ...
gi 569026720 908 SFL 910
Cdd:cd14059  232 MHL 234
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
585-857 6.32e-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: 6.32e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 585 GKTLGAGAFGKVVEATAFGLGKEdavlkVAVKMLKSTAHADEK-EALMSELKIMSHLgQHENIVNLLGACTHGGPVLVIT 663
Cdd:cd06606    5 GELLGKGSFGSVYLALNLDTGEL-----MAVKEVELSGDSEEElEALEREIRILSSL-KHPNIVRYLGTERTENTLNIFL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 664 EYCCYGDLLNFLRRKaeamlgpslspGQDPEGGVdyknihleKKYVRrdsgfssqgvdtyvemrpvstssndsfseqdld 743
Cdd:cd06606   79 EYVPGGSLASLLKKF-----------GKLPEPVV--------RKYTR--------------------------------- 106
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 744 kedgrplelrdllhfssQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDI----MNDSNYIVKGNARlpv 819
Cdd:cd06606  107 -----------------QILEGLEYLHSNGIVHRDIKGANILVDSDGVVKLADFGCAKRLaeiaTGEGTKSLRGTPY--- 166
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 569026720 820 kWMAPESIFDCVYTVQSDVWSYGILLWEIFSlGLNPYP 857
Cdd:cd06606  167 -WMAPEVIRGEGYGRAADIWSLGCTVIEMAT-GKPPWS 202
PTKc_Aatyk cd05042
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinases; PTKs ...
586-906 1.98e-31

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: 124.24  E-value: 1.98e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 586 KTLGAGAFGKVVEATAFglgKEDAVLKVAVKMLKSTAHADEKEALMSELKIMSHLgQHENIVNLLGACTHGGPVLVITEY 665
Cdd:cd05042    1 QEIGNGWFGKVLLGEIY---SGTSVAQVVVKELKASANPKEQDTFLKEGQPYRIL-QHPNILQCLGQCVEAIPYLLVMEF 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 666 CCYGDLLNFLRRKAEAMLGPSlspgqdpeggvdyknihlekkyvrrdsgfssqgvdtyvemrpvstssndsfseqdldke 745
Cdd:cd05042   77 CDLGDLKAYLRSEREHERGDS----------------------------------------------------------- 97
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 746 dgrplELRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDIMNDSNYIVKGNARLPVKWMAPE 825
Cdd:cd05042   98 -----DTRTLQRMACEVAAGLAHLHKLNFVHSDLALRNCLLTSDLTVKIGDYGLAHSRYKEDYIETDDKLWFPLRWTAPE 172
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 826 ---SIFDCVYTV----QSDVWSYGILLWEIFSLGLNPYPGI--------LVNSKFYKLVKDgyQMAQPafAPKNIYSIMQ 890
Cdd:cd05042  173 lvtEFHDRLLVVdqtkYSNIWSLGVTLWELFENGAQPYSNLsdldvlaqVVREQDTKLPKP--QLELP--YSDRWYEVLQ 248
                        330
                 ....*....|....*.
gi 569026720 891 ACWaLEPTHRPTFQQI 906
Cdd:cd05042  249 FCW-LSPEQRPAAEDV 263
PTKc_Aatyk1 cd05087
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 1; PTKs ...
586-906 6.20e-31

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: 122.79  E-value: 6.20e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 586 KTLGAGAFGKVVeatafgLGKEDAVL---KVAVKMLKSTAHADEKEALMSELKIMSHLgQHENIVNLLGACTHGGPVLVI 662
Cdd:cd05087    3 KEIGHGWFGKVF------LGEVNSGLsstQVVVKELKASASVQDQMQFLEEAQPYRAL-QHTNLLQCLAQCAEVTPYLLV 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 663 TEYCCYGDLLNFLR--RKAEAMLgpslspgqdPEggvdyknihlekkyvrrdsgfssqgvdtyvemrpvstssndsfseq 740
Cdd:cd05087   76 MEFCPLGDLKGYLRscRAAESMA---------PD---------------------------------------------- 100
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 741 dldkedgrPLELRDLlhfSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDIMNDSNYIVKGNARLPVK 820
Cdd:cd05087  101 --------PLTLQRM---ACEVACGLLHLHRNNFVHSDLALRNCLLTADLTVKIGDYGLSHCKYKEDYFVTADQLWVPLR 169
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 821 WMAPESIfDCVY--------TVQSDVWSYGILLWEIFSLGLNPYPG-----ILVnskfYKLVKDGYQMAQPAFA---PKN 884
Cdd:cd05087  170 WIAPELV-DEVHgnllvvdqTKQSNVWSLGVTIWELFELGNQPYRHysdrqVLT----YTVREQQLKLPKPQLKlslAER 244
                        330       340
                 ....*....|....*....|..
gi 569026720 885 IYSIMQACWaLEPTHRPTFQQI 906
Cdd:cd05087  245 WYEVMQFCW-LQPEQRPTAEEV 265
STKc_MLK cd14061
Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the ...
588-912 2.60e-28

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: 114.80  E-value: 2.60e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 588 LGAGAFGKVVEAtaFGLGKEdavlkVAVKMLKSTA---HADEKEALMSELKIMSHLgQHENIVNLLGACTHGGPVLVITE 664
Cdd:cd14061    2 IGVGGFGKVYRG--IWRGEE-----VAVKAARQDPdedISVTLENVRQEARLFWML-RHPNIIALRGVCLQPPNLCLVME 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 665 YCCYGDLlnflrrkaeamlgpslspgqdpeggvdykNIHLEKKYVrrdsgfssqgvdtyvemrpvstssndsfseqdldk 744
Cdd:cd14061   74 YARGGAL-----------------------------NRVLAGRKI----------------------------------- 89
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 745 edgrPLELrdLLHFSSQVAQGMAFLASKN---CIHRDVAARNVLLTNG--------HVAKIGDFGLARDIMNDSNYIVKG 813
Cdd:cd14061   90 ----PPHV--LVDWAIQIARGMNYLHNEApvpIIHRDLKSSNILILEAienedlenKTLKITDFGLAREWHKTTRMSAAG 163
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 814 NarlpVKWMAPESIFDCVYTVQSDVWSYGILLWEIFSlGLNPYPGILVNSKFYKLVKDGYQMAQPAFAPKNIYSIMQACW 893
Cdd:cd14061  164 T----YAWMAPEVIKSSTFSKASDVWSYGVLLWELLT-GEVPYKGIDGLAVAYGVAVNKLTLPIPSTCPEPFAQLMKDCW 238
                        330
                 ....*....|....*....
gi 569026720 894 ALEPTHRPTFQQICSFLQE 912
Cdd:cd14061  239 QPDPHDRPSFADILKQLEN 257
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
588-903 1.34e-27

Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RIP kinases serve as essential sensors of cellular stress. They are involved in regulating NF-kappaB and MAPK signaling, and are implicated in mediating cellular processes such as apoptosis, necroptosis, differentiation, and survival. RIP kinases contain a homologous N-terminal kinase domain and varying C-terminal domains. Higher vertebrates contain multiple RIP kinases, with mammals harboring at least five members. RIP1 and RIP2 harbor C-terminal domains from the Death domain (DD) superfamily while RIP4 contains ankyrin (ANK) repeats. RIP3 contain a RIP homotypic interaction motif (RHIM) that facilitates binding to RIP1. RIP1 and RIP3 are important in apoptosis and necroptosis, while RIP2 and RIP4 play roles in keratinocyte differentiation and inflammatory immune responses. The RIP subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270880 [Multi-domain]  Cd Length: 263  Bit Score: 112.93  E-value: 1.34e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 588 LGAGAFGKVVEA---TAFGLgkedavlkVAVKMLKS-TAHADEKEALMSELKIMsHLGQHENIVNLLGACTHGGPVLVIT 663
Cdd:cd13978    1 LGSGGFGTVSKArhvSWFGM--------VAIKCLHSsPNCIEERKALLKEAEKM-ERARHSYVLPLLGVCVERRSLGLVM 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 664 EYCCYGDLLNFLRRKAeamlgpslspgQDPeggvdyknihlekkyvrrdsgfssqgvdtyvemrpvstssndsfseqdld 743
Cdd:cd13978   72 EYMENGSLKSLLEREI-----------QDV-------------------------------------------------- 90
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 744 kedgrPLELRdlLHFSSQVAQGMAFL--ASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDIM----NDSNYIVKGNARL 817
Cdd:cd13978   91 -----PWSLR--FRIIHEIALGMNFLhnMDPPLLHHDLKPENILLDNHFHVKISDFGLSKLGMksisANRRRGTENLGGT 163
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 818 PVkWMAPESIFDCVY--TVQSDVWSYGILLWEIFSlGLNPYPG-ILVNSKFYKLVK------DGYQMAQPAFAPKNIYSI 888
Cdd:cd13978  164 PI-YMAPEAFDDFNKkpTSKSDVYSFAIVIWAVLT-RKEPFENaINPLLIMQIVSKgdrpslDDIGRLKQIENVQELISL 241
                        330
                 ....*....|....*
gi 569026720 889 MQACWALEPTHRPTF 903
Cdd:cd13978  242 MIRCWDGNPDARPTF 256
STKc_Raf cd14062
Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) ...
588-911 5.41e-27

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: 110.95  E-value: 5.41e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 588 LGAGAFGKVVEATAFGlgkedavlKVAVKMLKSTAHADEK-EALMSELKIMSHLgQHENIVNLLGACTHggPVL-VITEY 665
Cdd:cd14062    1 IGSGSFGTVYKGRWHG--------DVAVKKLNVTDPTPSQlQAFKNEVAVLRKT-RHVNILLFMGYMTK--PQLaIVTQW 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 666 CcygdllnflrrkaeamlgpslspgqdpEGGVDYKNIH-LEKKYvrrdsgfssqgvdtyvemrpvstssndsfseqdldk 744
Cdd:cd14062   70 C---------------------------EGSSLYKHLHvLETKF------------------------------------ 86
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 745 edgrplELRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLArdiMNDSNYIVKGNARLP---VKW 821
Cdd:cd14062   87 ------EMLQLIDIARQTAQGMDYLHAKNIIHRDLKSNNIFLHEDLTVKIGDFGLA---TVKTRWSGSQQFEQPtgsILW 157
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 822 MAPESIF---DCVYTVQSDVWSYGILLWEIFSLGLnPYPGILVNSKFYKLVKDGYqmAQPAF------APKNIYSIMQAC 892
Cdd:cd14062  158 MAPEVIRmqdENPYSFQSDVYAFGIVLYELLTGQL-PYSHINNRDQILFMVGRGY--LRPDLskvrsdTPKALRRLMEDC 234
                        330
                 ....*....|....*....
gi 569026720 893 WALEPTHRPTFQQICSFLQ 911
Cdd:cd14062  235 IKFQRDERPLFPQILASLE 253
STKc_MLTK cd14060
Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated ...
589-911 7.78e-27

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: 110.05  E-value: 7.78e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 589 GAGAFGKVVEATAFGLGKEdavlkVAVKMLKSTahadEKEAlmselKIMSHLgQHENIVNLLGACTHGGPVLVITEYCCY 668
Cdd:cd14060    2 GGGSFGSVYRAIWVSQDKE-----VAVKKLLKI----EKEA-----EILSVL-SHRNIIQFYGAILEAPNYGIVTEYASY 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 669 GDLLNFLrrkaeamlgpslspgqdpeggvdyknihlekkyvrrdsgfssqgvdtyvemrpvstSSNDSfSEQDLDKedgr 748
Cdd:cd14060   67 GSLFDYL--------------------------------------------------------NSNES-EEMDMDQ---- 85
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 749 plelrdLLHFSSQVAQGMAFL---ASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDIMNDSNYIVKGNarlpVKWMAPE 825
Cdd:cd14060   86 ------IMTWATDIAKGMHYLhmeAPVKVIHRDLKSRNVVIAADGVLKICDFGASRFHSHTTHMSLVGT----FPWMAPE 155
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 826 SIFDCVYTVQSDVWSYGILLWEIFSLGLnPYPGILVNSKFYKLVKDGYQMAQPAFAPKNIYSIMQACWALEPTHRPTFQQ 905
Cdd:cd14060  156 VIQSLPVSETCDTYSYGVVLWEMLTREV-PFKGLEGLQVAWLVVEKNERPTIPSSCPRSFAELMRRCWEADVKERPSFKQ 234

                 ....*.
gi 569026720 906 ICSFLQ 911
Cdd:cd14060  235 IIGILE 240
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
581-908 1.05e-25

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: 107.31  E-value: 1.05e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 581 NLQFGKTLGAGAFGKVVEATAFGLGkedavLKVAVKMLKSTAHADEK-EALMSELKIMSHLgQHENIVNLLGACTHGGPV 659
Cdd:cd06627    1 NYQLGDLIGRGAFGSVYKGLNLNTG-----EFVAIKQISLEKIPKSDlKSVMGEIDLLKKL-NHPNIVKYIGSVKTKDSL 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 660 LVITEYCCYGDLLNFLRRKaeamlgpslspGQDPEggvdykniHLEKKYVrrdsgfssqgvdtyvemrpvstssndsfse 739
Cdd:cd06627   75 YIILEYVENGSLASIIKKF-----------GKFPE--------SLVAVYI------------------------------ 105
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 740 qdldkedgrplelrdllhfsSQVAQGMAFLASKNCIHRDVAARNVLLT-NGHVaKIGDFGLARDIMNdsnyiVKGNARLP 818
Cdd:cd06627  106 --------------------YQVLEGLAYLHEQGVIHRDIKGANILTTkDGLV-KLADFGVATKLNE-----VEKDENSV 159
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 819 V---KWMAPESIFDCVYTVQSDVWSYGILLWEIFSlGLNPYPGILVNSKFYKLVKDgyqmAQPAFaPKNIYS-----IMQ 890
Cdd:cd06627  160 VgtpYWMAPEVIEMSGVTTASDIWSVGCTVIELLT-GNPPYYDLQPMAALFRIVQD----DHPPL-PENISPelrdfLLQ 233
                        330
                 ....*....|....*...
gi 569026720 891 aCWALEPTHRPTFQQICS 908
Cdd:cd06627  234 -CFQKDPTLRPSAKELLK 250
STKc_MLK4 cd14146
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the ...
588-906 1.24e-25

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: 107.43  E-value: 1.24e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 588 LGAGAFGKVVEATAFGLgkedavlKVAVKMLKSTAHADEK---EALMSELKIMSHLgQHENIVNLLGACTHGGPVLVITE 664
Cdd:cd14146    2 IGVGGFGKVYRATWKGQ-------EVAVKAARQDPDEDIKataESVRQEAKLFSML-RHPNIIKLEGVCLEEPNLCLVME 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 665 YCcYGDLLNflrrkaEAMLGPSLSPGqdpeggvdyknihlekkyvrrdsgfssqgvdtyvemrpvstssndsfseqdldK 744
Cdd:cd14146   74 FA-RGGTLN------RALAAANAAPG-----------------------------------------------------P 93
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 745 EDGRPLELRDLLHFSSQVAQGMAFL---ASKNCIHRDVAARNVLLTN--------GHVAKIGDFGLARDIMNDSNYIVKG 813
Cdd:cd14146   94 RRARRIPPHILVNWAVQIARGMLYLheeAVVPILHRDLKSSNILLLEkiehddicNKTLKITDFGLAREWHRTTKMSAAG 173
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 814 NarlpVKWMAPESIFDCVYTVQSDVWSYGILLWEIFSlGLNPYPGILVNSKFYKLVKDGYQMAQPAFAPKNIYSIMQACW 893
Cdd:cd14146  174 T----YAWMAPEVIKSSLFSKGSDIWSYGVLLWELLT-GEVPYRGIDGLAVAYGVAVNKLTLPIPSTCPEPFAKLMKECW 248
                        330
                 ....*....|...
gi 569026720 894 ALEPTHRPTFQQI 906
Cdd:cd14146  249 EQDPHIRPSFALI 261
PTKc_Aatyk2 cd05086
Catalytic domain of the Protein Tyrosine Kinase, Apoptosis-associated tyrosine kinase 2; PTKs ...
588-906 5.89e-24

Catalytic domain of the Protein Tyrosine Kinase, Apoptosis-associated tyrosine kinase 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Aatyk2 is a member of the Aatyk subfamily of proteins, which are receptor kinases containing a transmembrane segment and a long C-terminal cytoplasmic tail with a catalytic domain. Aatyk2 is also called lemur tyrosine kinase 2 (Lmtk2) or brain-enriched kinase (Brek). It is expressed at high levels in early postnatal brain, and has been shown to play a role in nerve growth factor (NGF) signaling. Studies with knockout mice reveal that Aatyk2 is essential for late stage spermatogenesis. Although it is classified as a PTK based on sequence similarity and the phylogenetic tree, Aatyk2 has been functionally characterized as a serine/threonine kinase. The Aatyk2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270669 [Multi-domain]  Cd Length: 271  Bit Score: 102.64  E-value: 5.89e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 588 LGAGAFGKVVEATAFglgKEDAVLKVAVKMLKSTAHADEKEALMSELKIMSHLgQHENIVNLLGACTHGGPVLVITEYCC 667
Cdd:cd05086    5 IGNGWFGKVLLGEIY---TGTSVARVVVKELKASANPKEQDDFLQQGEPYYIL-QHPNILQCVGQCVEAIPYLLVFEFCD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 668 YGDLLNFLRRkaeamlgpslspgqdpeggvdyknihlEKKYVRRDSgfssqgvdtyvemrpvstssndsfseqdldkedg 747
Cdd:cd05086   81 LGDLKTYLAN---------------------------QQEKLRGDS---------------------------------- 99
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 748 rplELRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDIMNDSNYIVKGNARLPVKWMAPE-- 825
Cdd:cd05086  100 ---QIMLLQRMACEIAAGLAHMHKHNFLHSDLALRNCYLTSDLTVKVGDYGIGFSRYKEDYIETDDKKYAPLRWTAPElv 176
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 826 -SIFDCVYTVQ----SDVWSYGILLWEIFSLGLNPYPGI--------LVNSKFYKLVKDgyQMAQPafAPKNIYSIMQAC 892
Cdd:cd05086  177 tSFQDGLLAAEqtkySNIWSLGVTLWELFENAAQPYSDLsdrevlnhVIKERQVKLFKP--HLEQP--YSDRWYEVLQFC 252
                        330
                 ....*....|....
gi 569026720 893 WaLEPTHRPTFQQI 906
Cdd:cd05086  253 W-LSPEKRPTAEEV 265
STKc_A-Raf cd14150
Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) ...
586-916 2.05e-23

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: 100.86  E-value: 2.05e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 586 KTLGAGAFGKVVEATAFGlgkedavlKVAVKMLKSTAHADEK-EALMSELKIMSHLgQHENIVNLLGACTHGGpVLVITE 664
Cdd:cd14150    6 KRIGTGSFGTVFRGKWHG--------DVAVKILKVTEPTPEQlQAFKNEMQVLRKT-RHVNILLFMGFMTRPN-FAIITQ 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 665 YCcygdllnflrrkaeamlgpslspgqdpEGGVDYKNIHlekkyvrrdsgfssqgvdtyvemrpVSTSSNDSFSeqdldk 744
Cdd:cd14150   76 WC---------------------------EGSSLYRHLH-------------------------VTETRFDTMQ------ 97
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 745 edgrplelrdLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDIMNDSNYIVKGNARLPVKWMAP 824
Cdd:cd14150   98 ----------LIDVARQTAQGMDYLHAKNIIHRDLKSNNIFLHEGLTVKIGDFGLATVKTRWSGSQQVEQPSGSILWMAP 167
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 825 ESIF---DCVYTVQSDVWSYGILLWEIFSlGLNPYPGILVNSKFYKLVKDGYqmAQPAFA------PKNIYSIMQACWAL 895
Cdd:cd14150  168 EVIRmqdTNPYSFQSDVYAYGVVLYELMS-GTLPYSNINNRDQIIFMVGRGY--LSPDLSklssncPKAMKRLLIDCLKF 244
                        330       340
                 ....*....|....*....|.
gi 569026720 896 EPTHRPTFQQICSFLqEQAQE 916
Cdd:cd14150  245 KREERPLFPQILVSI-ELLQR 264
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
588-902 3.12e-23

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: 99.97  E-value: 3.12e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 588 LGAGAFGKVVEATAFGLGKEdavlkVAVKMLKSTAHADE--KEALMSELKIMSHLgQHENIVNLLGACTHGGPVLVITEY 665
Cdd:cd14014    8 LGRGGMGEVYRARDTLLGRP-----VAIKVLRPELAEDEefRERFLREARALARL-SHPNIVRVYDVGEDDGRPYIVMEY 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 666 CCYGDLLNFLRRkaeamlgpslspgqdpeggvdyknihlekkyvrrdsgfssqgvdtyvemrpvstssndsfseqdldke 745
Cdd:cd14014   82 VEGGSLADLLRE-------------------------------------------------------------------- 93
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 746 dGRPLELRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDImnDSNYIVKGNARL--PVkWMA 823
Cdd:cd14014   94 -RGPLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGRVKLTDFGIARAL--GDSGLTQTGSVLgtPA-YMA 169
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 824 PESIFDCVYTVQSDVWSYGILLWEIFSlGLNPYPGILVNSKFYKLVKDGYQM--AQPAFAPKNIYSIMQACWALEPTHRP 901
Cdd:cd14014  170 PEQARGGPVDPRSDIYSLGVVLYELLT-GRPPFDGDSPAAVLAKHLQEAPPPpsPLNPDVPPALDAIILRALAKDPEERP 248

                 .
gi 569026720 902 T 902
Cdd:cd14014  249 Q 249
PKc_LIMK_like cd14065
Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of ...
588-910 3.38e-23

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: 99.87  E-value: 3.38e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 588 LGAGAFGKVVEATAFGLGKedavlkvaVKMLKSTAHADEKEALMSELKIMSHLgQHENIVNLLGACTHGGPVLVITEYCC 667
Cdd:cd14065    1 LGKGFFGEVYKVTHRETGK--------VMVMKELKRFDEQRSFLKEVKLMRRL-SHPNILRFIGVCVKDNKLNFITEYVN 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 668 YGDLLNFLRRKAEamlgpslspgqdpeggvdyknihlekkyvrrdsgfssqgvdtyvemrpvstssndsfseqdldkedg 747
Cdd:cd14065   72 GGTLEELLKSMDE------------------------------------------------------------------- 84
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 748 rPLELRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLL---TNGHVAKIGDFGLARDIMNDSN--------YIVKGNAR 816
Cdd:cd14065   85 -QLPWSQRVSLAKDIASGMAYLHSKNIIHRDLNSKNCLVreaNRGRNAVVADFGLAREMPDEKTkkpdrkkrLTVVGSPY 163
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 817 lpvkWMAPESIFDCVYTVQSDVWSYGILLWEIFSLgLNPYPGILVNSKFYKLVKDGYQMAQPAFAPKNIYSIMQACWALE 896
Cdd:cd14065  164 ----WMAPEMLRGESYDEKVDVFSFGIVLCEIIGR-VPADPDYLPRTMDFGLDVRAFRTLYVPDCPPSFLPLAIRCCQLD 238
                        330
                 ....*....|....
gi 569026720 897 PTHRPTFQQICSFL 910
Cdd:cd14065  239 PEKRPSFVELEHHL 252
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
581-888 4.39e-23

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 223589 [Multi-domain]  Cd Length: 384  Bit Score: 102.51  E-value: 4.39e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 581 NLQFGKTLGAGAFGKVVEATAfglgkedaVLKVAVKMLKSTAHADEKEA--LMSELKIMSHLGQHENIVNLLGACTHGGP 658
Cdd:COG0515    1 SYRILRKLGEGSFGEVYLARD--------RKLVALKVLAKKLESKSKEVerFLREIQILASLNHPPNIVKLYDFFQDEGS 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 659 VLVITEYCCYGDLLNFLRRKaeamlgpslspgqdpeggvdyknihlekkyvrrdsgfssqgvdtyvemrpvstssndsfs 738
Cdd:COG0515   73 LYLVMEYVDGGSLEDLLKKI------------------------------------------------------------ 92
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 739 eqdldkEDGRPLELRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLT-NGHVAKIGDFGLARdIMNDSNYIVKGNARL 817
Cdd:COG0515   93 ------GRKGPLSESEALFILAQILSALEYLHSKGIIHRDIKPENILLDrDGRVVKLIDFGLAK-LLPDPGSTSSIPALP 165
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 569026720 818 PVK-----WMAPESIFDCV---YTVQSDVWSYGILLWEIFsLGLNPYPGILVNSKFYKLVKDGYQMAQPAFAPKNIYSI 888
Cdd:COG0515  166 STSvgtpgYMAPEVLLGLSlayASSSSDIWSLGITLYELL-TGLPPFEGEKNSSATSQTLKIILELPTPSLASPLSPSN 243
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
586-909 6.96e-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: 99.07  E-value: 6.96e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 586 KTLGAGAFGKVVEATafglGKEDAVLKVAVKMLKSTAHADEKEALMSELKIMSHLgQHENIVNLLGACTHGGPVLVITEY 665
Cdd:cd08215    6 RVIGKGSFGSAYLVR----RKSDGKLYVLKEIDLSNMSEKEREEALNEVKLLSKL-KHPNIVKYYESFEENGKLCIVMEY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 666 CCYGDLLNFLRRKaeamlgpslspgqdpeggvdyknihlekkyvrrdsgfssqgvdtyvemrpvstssndsfseqdldKE 745
Cdd:cd08215   81 ADGGDLAQKIKKQ-----------------------------------------------------------------KK 95
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 746 DGRPLELRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARdIMNDSN-----------Yivkgn 814
Cdd:cd08215   96 KGQPFPEEQILDWFVQICLALKYLHSRKILHRDLKTQNIFLTKDGVVKLGDFGISK-VLESTTdlaktvvgtpyY----- 169
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 815 arlpvkwMAPESIFDCVYTVQSDVWSYGILLWEIFSL-----GLNpypgilVNSKFYKLVKDGYQMaqpafaPKNIYS-- 887
Cdd:cd08215  170 -------LSPELCENKPYNYKSDIWALGCVLYELCTLkhpfeANN------LPALVYKIVKGQYPP------IPSQYSse 230
                        330       340
                 ....*....|....*....|....*
gi 569026720 888 ---IMQACWALEPTHRPTFQQICSF 909
Cdd:cd08215  231 lrdLVNSMLQKDPEKRPSANEILSS 255
STKc_MLK2 cd14148
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the ...
747-906 1.37e-22

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: 98.14  E-value: 1.37e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 747 GRPLELRDLLHFSSQVAQGMAFLASKN---CIHRDVAARNVLLTN--------GHVAKIGDFGLARDIMNDSnyivKGNA 815
Cdd:cd14148   86 GKKVPPHVLVNWAVQIARGMNYLHNEAivpIIHRDLKSSNILILEpienddlsGKTLKITDFGLAREWHKTT----KMSA 161
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 816 RLPVKWMAPESIFDCVYTVQSDVWSYGILLWEIFSlGLNPYPGILVNSKFYKLVKDGYQMAQPAFAPKNIYSIMQACWAL 895
Cdd:cd14148  162 AGTYAWMAPEVIRLSLFSKSSDVWSFGVLLWELLT-GEVPYREIDALAVAYGVAMNKLTLPIPSTCPEPFARLLEECWDP 240
                        170
                 ....*....|.
gi 569026720 896 EPTHRPTFQQI 906
Cdd:cd14148  241 DPHGRPDFGSI 251
STKc_MLK3 cd14147
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the ...
747-911 1.57e-22

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: 98.18  E-value: 1.57e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 747 GRPLELRDLLHFSSQVAQGMAFLASKN---CIHRDVAARNVLLTNGHVA--------KIGDFGLARDIMNDSNYIVKGNa 815
Cdd:cd14147   95 GRRVPPHVLVNWAVQIARGMHYLHCEAlvpVIHRDLKSNNILLLQPIENddmehktlKITDFGLAREWHKTTQMSAAGT- 173
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 816 rlpVKWMAPESIFDCVYTVQSDVWSYGILLWEIFSlGLNPYPGILVNSKFYKLVKDGYQMAQPAFAPKNIYSIMQACWAL 895
Cdd:cd14147  174 ---YAWMAPEVIKASTFSKGSDVWSFGVLLWELLT-GEVPYRGIDCLAVAYGVAVNKLTLPIPSTCPEPFAQLMADCWAQ 249
                        170
                 ....*....|....*.
gi 569026720 896 EPTHRPTFQQICSFLQ 911
Cdd:cd14147  250 DPHRRPDFASILQQLE 265
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
583-856 1.90e-22

Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. This family is composed of STKs, and some dual-specificity PKs that phosphorylate both threonine and tyrosine residues of target proteins. Most members are kinases involved in mitogen-activated protein kinase (MAPK) signaling cascades, acting as MAPK kinases (MAPKKs), MAPKK kinases (MAPKKKs), or MAPKKK kinases (MAP4Ks). The MAPK signaling pathways are important mediators of cellular responses to extracellular signals. The pathways involve a triple kinase core cascade comprising of the MAPK, which is phosphorylated and activated by a MAPKK, which itself is phosphorylated and activated by a MAPKKK. Each MAPK cascade is activated either by a small GTP-binding protein or by an adaptor protein, which transmits the signal either directly to a MAPKKK to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. Other STE family members include p21-activated kinases (PAKs) and class III myosins, among others. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. Class III myosins are motor proteins containing an N-terminal kinase catalytic domain and a C-terminal actin-binding domain, which can phosphorylate several cytoskeletal proteins, conventional myosin regulatory light chains, as well as autophosphorylate the C-terminal motor domain. They play an important role in maintaining the structural integrity of photoreceptor cell microvilli. The STE family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270692 [Multi-domain]  Cd Length: 254  Bit Score: 97.66  E-value: 1.90e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 583 QFGKTLGAGAFGKVVEATAFGLGKEdavlkVAVKMLKSTAhADEKEALMSELKIMSHLgQHENIVNLLGACTHGGPVLVI 662
Cdd:cd05122    3 EILEKIGKGGFGVVYKARHKKTGQI-----VAIKKINLES-KEKKESILNEIAILKKC-KHPNIVKYYGSYLKKDELWIV 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 663 TEYCCYGDLLNflrrkaeamlgpslspgqdpeggvdyknihlekkyvrrdsgfssqgvdtyvemrpVSTSSNDSFSEQDL 742
Cdd:cd05122   76 MEFCSGGSLKD-------------------------------------------------------LLKNTNKTLTEQQI 100
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 743 DKEdgrpleLRDLLhfssqvaQGMAFLASKNCIHRDVAARNVLLT-NGHVaKIGDFGLA--------RDIMNDSNYivkg 813
Cdd:cd05122  101 AYV------CKEVL-------KGLEYLHSHGIIHRDIKAANILLTsDGEV-KLIDFGLSaqlsdgktRNTFVGTPY---- 162
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 569026720 814 narlpvkWMAPESIFDCVYTVQSDVWSYGILLWEIFsLGLNPY 856
Cdd:cd05122  163 -------WMAPEVIQGKPYGFKADIWSLGITAIEMA-EGKPPY 197
STKc_B-Raf cd14151
Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) ...
573-916 2.18e-22

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


Pssm-ID: 271053 [Multi-domain]  Cd Length: 274  Bit Score: 98.21  E-value: 2.18e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 573 EKWEFPRNNLQFGKTLGAGAFGKVVEATAFGlgkedavlKVAVKMLKSTAHADEK-EALMSELKIMSHLgQHENIVNLLG 651
Cdd:cd14151    1 DDWEIPDGQITVGQRIGSGSFGTVYKGKWHG--------DVAVKMLNVTAPTPQQlQAFKNEVGVLRKT-RHVNILLFMG 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 652 ACTHggPVL-VITEYCcygdllnflrrkaeamlgpslspgqdpEGGVDYKNIHL-EKKYvrrdsgfssqgvdtyvemrpv 729
Cdd:cd14151   72 YSTK--PQLaIVTQWC---------------------------EGSSLYHHLHIiETKF--------------------- 101
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 730 stssndsfseqdldkedgrplELRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDIMNDSNY 809
Cdd:cd14151  102 ---------------------EMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVKSRWSGS 160
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 810 IVKGNARLPVKWMAPESIF---DCVYTVQSDVWSYGILLWEIFSlGLNPYPGILVNSKFYKLVKDGYqmAQPAFA----- 881
Cdd:cd14151  161 HQFEQLSGSILWMAPEVIRmqdKNPYSFQSDVYAFGIVLYELMT-GQLPYSNINNRDQIIFMVGRGY--LSPDLSkvrsn 237
                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 569026720 882 -PKNIYSIMQACWALEPTHRPTFQQICSFLQEQAQE 916
Cdd:cd14151  238 cPKAMKRLMAECLKKKRDERPLFPQILASIELLARS 273
STKc_MLK1 cd14145
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the ...
755-906 2.71e-22

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: 97.81  E-value: 2.71e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 755 LLHFSSQVAQGMAFL---ASKNCIHRDVAARNVLL----TNGHVA----KIGDFGLARDIMNDSnyivKGNARLPVKWMA 823
Cdd:cd14145  106 LVNWAVQIARGMNYLhceAIVPVIHRDLKSSNILIlekvENGDLSnkilKITDFGLAREWHRTT----KMSAAGTYAWMA 181
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 824 PESIFDCVYTVQSDVWSYGILLWEIFSlGLNPYPGILVNSKFYKLVKDGYQMAQPAFAPKNIYSIMQACWALEPTHRPTF 903
Cdd:cd14145  182 PEVIRSSMFSKGSDVWSYGVLLWELLT-GEVPFRGIDGLAVAYGVAMNKLSLPIPSTCPEPFARLMEDCWNPDPHSRPPF 260

                 ...
gi 569026720 904 QQI 906
Cdd:cd14145  261 TNI 263
PKc_TESK cd14155
Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; ...
588-912 6.73e-22

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: 96.01  E-value: 6.73e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 588 LGAGAFGKVVEATAFGLGKedavlKVAVKMLKSTAHadeKEALMSELKIMSHLgQHENIVNLLGACTHGGPVLVITEYCC 667
Cdd:cd14155    1 IGSGFFSEVYKVRHRTSGQ-----VMALKMNTLSSN---RANMLREVQLMNRL-SHPNILRFMGVCVHQGQLHALTEYIN 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 668 YGDLlnflrrkaeamlgpslspgqdpeggvdyknihlekkyvrrdsgfssqgvdtyvemrpvstssndsfsEQDLDKEDG 747
Cdd:cd14155   72 GGNL-------------------------------------------------------------------EQLLDSNEP 84
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 748 RPLELRdlLHFSSQVAQGMAFLASKNCIHRDVAARNVLL---TNGHVAKIGDFGLARDIMNDSNyivkGNARLPV----K 820
Cdd:cd14155   85 LSWTVR--VKLALDIARGLSYLHSKGIFHRDLTSKNCLIkrdENGYTAVVGDFGLAEKIPDYSD----GKEKLAVvgspY 158
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 821 WMAPESIFDCVYTVQSDVWSYGILLWEIFSLgLNPYPGILVNSKFYKLVKDGYQ----MAQPAFAPKNIYsimqaCWALE 896
Cdd:cd14155  159 WMAPEVLRGEPYNEKADVFSYGIILCEIIAR-IQADPDYLPRTEDFGLDYDAFQhmvgDCPPDFLQLAFN-----CCNMD 232
                        330
                 ....*....|....*.
gi 569026720 897 PTHRPTFQQICSFLQE 912
Cdd:cd14155  233 PKSRPSFHDIVKTLEE 248
PTK_Jak_rpt1 cd05037
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak ...
582-910 2.18e-21

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: 94.85  E-value: 2.18e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 582 LQFGKTLGAGAFGKVVE----ATAFGLGKEDAVLKvavKMLKStAHADEKEALMSELKIMSHLgQHENIVNLLGACTHGG 657
Cdd:cd05037    1 ITFHEHLGQGTFTNIYDgilrEVGDGRVQEVEVLL---KVLDS-DHRDISESFFETASLMSQI-SHKHLVKLYGVCVADE 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 658 PVLViTEYCCYGDLLNFLRRKaeamlgpslspgqdpeggvdyknihlekkyvrrdsgfssqgvdtyvemrpvstssndsf 737
Cdd:cd05037   76 NIMV-QEYVRYGPLDKYLRRM----------------------------------------------------------- 95
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 738 seqdldkedGRPLELRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLT----NGHV--AKIGDFGLARDIMNDSnYIV 811
Cdd:cd05037   96 ---------GNNVPLSWKLQVAKQLASALHYLEDKKLIHGNVRGRNILLAreglDGYPpfIKLSDPGVPITVLSRE-ERV 165
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 812 kgnarLPVKWMAPESIFDCV--YTVQSDVWSYGILLWEIFSLGLNPYPGILVNSK--FYklvKDGYQMAQPAFAPknIYS 887
Cdd:cd05037  166 -----DRIPWIAPECLRNLQanLTIAADKWSFGTTLWEICSGGEEPLSALSSQEKlqFY---EDQHQLPAPDCAE--LAE 235
                        330       340
                 ....*....|....*....|...
gi 569026720 888 IMQACWALEPTHRPTFQQICSFL 910
Cdd:cd05037  236 LIMQCWTYEPTKRPSFRAILRDL 258
STKc_IRAK4 cd14158
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; ...
585-912 2.48e-21

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: 95.26  E-value: 2.48e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 585 GKTLGAGAFGKVVEatafGLGKEdavLKVAVKMLKSTAHA---DEKEALMSELKIMSHLgQHENIVNLLGACTHGGPVLV 661
Cdd:cd14158   20 GNKLGEGGFGVVFK----GYIND---KNVAVKKLAAMVDIsteDLTKQFEQEIQVMAKC-QHENLVELLGYSCDGPQLCL 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 662 ITEYCCYGDLLNFLRRKaeamlgpslspgqdpeggvdyknihlekkyvrrdsgfssqgvdtyvemrpvstssndsfseqd 741
Cdd:cd14158   92 VYTYMPNGSLLDRLACL--------------------------------------------------------------- 108
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 742 ldkEDGRPLELRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDIMNDSNYIVKGNARLPVKW 821
Cdd:cd14158  109 ---NDTPPLSWHMRCKIAQGTANGINYLHENNHIHRDIKSANILLDETFVPKISDFGLARASEKFSQTIMTERIVGTTAY 185
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 822 MAPESIFDCVyTVQSDVWSYGILLWEIFSlGLNPY-----PGILVNSK---------FYKLVKDGYQMAQPAFAPKnIYS 887
Cdd:cd14158  186 MAPEALRGEI-TPKSDIFSFGVVLLEIIT-GLPPVdenrdPQLLLDIKeeiedeektIEDYVDKKMGDWDSTSIEA-MYS 262
                        330       340
                 ....*....|....*....|....*
gi 569026720 888 IMQACWALEPTHRPTFQQICSFLQE 912
Cdd:cd14158  263 VASQCLNDKKNRRPDIAKVQQLLQE 287
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
581-906 8.82e-21

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: 92.58  E-value: 8.82e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 581 NLQFGKTLGAGAFGKVVEATAFGLGKedavlKVAVKML-KSTAHADEKEALMSELKIMSHLgQHENIVNLLGACTHGGPV 659
Cdd:cd14003    1 NYELGKTLGEGSFGKVKLARHKLTGE-----KVAIKIIdKSKLKEEIEEKIKREIEIMKLL-NHPNIIKLYEVIETENKI 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 660 LVITEYCCYGDLLNFLRRKaeamlgpslspgqdpeggvdyknihlekkyvRRdsgfssqgvdtyvemrpvstssndsfse 739
Cdd:cd14003   75 YLVMEYASGGELFDYIVNN-------------------------------GR---------------------------- 95
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 740 qdLDKEDGRplelrdllHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDIMNDS---------NYi 810
Cdd:cd14003   96 --LSEDEAR--------RFFQQLISAVDYCHSNGIVHRDLKLENILLDKNGNLKIIDFGLSNEFRGGSllktfcgtpAY- 164
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 811 vkgnarlpvkwMAPEsIFDC--VYTVQSDVWSYGILLweiFSL--GLNPYPGILVNSKFYKLVKDGYQMaqPAFAPKNIY 886
Cdd:cd14003  165 -----------AAPE-VLLGrkYDGPKADVWSLGVIL---YAMltGYLPFDDDNDSKLFRKILKGKYPI--PSHLSPDAR 227
                        330       340
                 ....*....|....*....|
gi 569026720 887 SIMQACWALEPTHRPTFQQI 906
Cdd:cd14003  228 DLIRRMLVVDPSKRITIEEI 247
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
583-845 2.32e-20

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: 91.77  E-value: 2.32e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 583 QFGKTLGAGAFGKVVEATAFGLGKEdavlkVAVKML-KSTAHADEKEALMSELKIMSHLgQHENIVNLLGACTHGGPVLV 661
Cdd:cd05117    3 ELGKVLGRGSFGVVRLAVHKKTGEE-----YAVKIIdKKKLKSEDEEMLRREIEILKRL-DHPNIVKLYEVFEDDKNLYL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 662 ITEYCCYGDLLNFLrrkaeamlgpslspgqdpeggvdyknihlekkyvrrdsgfssqgvdtyvemrpvstSSNDSFSEQd 741
Cdd:cd05117   77 VMELCTGGELFDRI--------------------------------------------------------VKKGSFSER- 99
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 742 ldkedgrplELRDLLHfssQVAQGMAFLASKNCIHRDVAARNVLLT----NGHVaKIGDFGLARDIMNDSnyivkgNARL 817
Cdd:cd05117  100 ---------EAAKIMK---QILSAVAYLHSQGIVHRDLKPENILLAskdpDSPI-KIIDFGLAKIFEEGE------KLKT 160
                        250       260       270
                 ....*....|....*....|....*....|.
gi 569026720 818 PV---KWMAPESIFDCVYTVQSDVWSYGILL 845
Cdd:cd05117  161 VCgtpYYVAPEVLKGKGYGKKCDIWSLGVIL 191
PK_KSR cd14063
Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to ...
582-910 3.76e-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: 3.76e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 582 LQFGKTLGAGAFGKVVEATAFGlgkedavlKVAVKMLKSTAHADEK-EALMSELKIMSHLgQHENIVNLLGACTHGGPVL 660
Cdd:cd14063    2 LEIKEVIGKGRFGRVHRGRWHG--------DVAIKLLNIDYLNEEQlEAFKEEVAAYKNT-RHDNLVLFMGACMDPPHLA 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 661 VITEYCcygdllnflrrkaeamLGPSLspgqdpeggvdYKNIHLEKkyvrrdsgfssqgvdtyvemrpvstsSNDSFSEq 740
Cdd:cd14063   73 IVTSLC----------------KGRTL-----------YSLIHERK--------------------------EKFDFNK- 98
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 741 dldkedgrplelrdLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAkIGDFGLARdiMNDSNYIVKGNARL--P 818
Cdd:cd14063   99 --------------TVQIAQQICQGMGYLHAKGIIHKDLKSKNIFLENGRVV-ITDFGLFS--LSGLLQPGRREDTLviP 161
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 819 VKW---MAPESI----FDCV------YTVQSDVWSYGILLWEIFSLGLnPYPGILVNSKFYKlVKDGYQMAQPAFA-PKN 884
Cdd:cd14063  162 NGWlcyLAPEIIralsPDLDfeeslpFTKASDVYAFGTVWYELLAGRW-PFKEQPAESIIWQ-VGCGKKQSLSQLDiGRE 239
                        330       340
                 ....*....|....*....|....*.
gi 569026720 885 IYSIMQACWALEPTHRPTFQQICSFL 910
Cdd:cd14063  240 VKDILMQCWAYDPEKRPTFSDLLRML 265
PK_GC cd13992
Pseudokinase domain of membrane Guanylate Cyclase receptors; The pseudokinase domain shows ...
626-912 4.21e-20

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: 91.30  E-value: 4.21e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 626 EKEALMSELKIMSHLgQHENIVNLLGACTHGGPVLVITEYCCYGDLLNFLRRKAEAMlgpslspgqdpeggvdyknihle 705
Cdd:cd13992   39 EKRTILQELNQLKEL-VHDNLNKFIGICINPPNIAVVTEYCTRGSLQDVLLNREIKM----------------------- 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 706 kkyvrrDSGFSSqgvdtyvemrpvstssndSFseqdldkedgrpleLRDLLHfssqvaqGMAFL-ASKNCIHRDVAARNV 784
Cdd:cd13992   95 ------DWMFKS------------------SF--------------IKDIVK-------GMNYLhSSSIGYHGRLKSSNC 129
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 785 LLTNGHVAKIGDFGLARdIMNDSNYIVKGNARLPVK--WMAPESIFDCVY----TVQSDVWSYGILLWEIFsLGLNPYPG 858
Cdd:cd13992  130 LVDSRWVVKLTDFGLRN-LLEEQTNHQLDEDAQHKKllWTAPELLRGSLLevrgTQKGDVYSFAIILYEIL-FRSDPFAL 207
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 859 ILVNSKFYKLVKDGYQMAQPAFA------PKNIYSIMQACWALEPTHRPTFQQICSFLQE 912
Cdd:cd13992  208 EREVAIVEKVISGGNKPFRPELAvlldefPPRLVLLVKQCWAENPEKRPSFKQIKKTLTE 267
STKc_C-Raf cd14149
Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) ...
575-911 5.54e-20

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: 91.25  E-value: 5.54e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 575 WEFPRNNLQFGKTLGAGAFGKVVEATAFGlgkedavlKVAVKMLKSTAHADEK-EALMSELKIMSHLgQHENIVNLLGAC 653
Cdd:cd14149    7 WEIEASEVMLSTRIGSGSFGTVYKGKWHG--------DVAVKILKVVDPTPEQfQAFRNEVAVLRKT-RHVNILLFMGYM 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 654 THGGpVLVITEYCcygdllnflrrkaeamlgpslspgqdpEGGVDYKNIH-LEKKYvrrdsgfssqgvdtyvemrpvsts 732
Cdd:cd14149   78 TKDN-LAIVTQWC---------------------------EGSSLYKHLHvQETKF------------------------ 105
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 733 sndsfseqdldkedgrplELRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDIMNDSNYIVK 812
Cdd:cd14149  106 ------------------QMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVKSRWSGSQQV 167
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 813 GNARLPVKWMAPESIF---DCVYTVQSDVWSYGILLWEIFSlGLNPYPGILVNSKFYKLVKDGYqmAQPAFA------PK 883
Cdd:cd14149  168 EQPTGSILWMAPEVIRmqdNNPFSFQSDVYSYGIVLYELMT-GELPYSHINNRDQIIFMVGRGY--ASPDLSklykncPK 244
                        330       340
                 ....*....|....*....|....*...
gi 569026720 884 NIYSIMQACWALEPTHRPTFQQICSFLQ 911
Cdd:cd14149  245 AMKRLVADCIKKVKEERPLFPQILSSIE 272
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
588-850 9.72e-20

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: 90.41  E-value: 9.72e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 588 LGAGAFGKVVEATaFGLGKedavlKVAVKMLKST-AHADEKEALmSELKIMSHLgQHENIVNLLGACTHGGPVLVITEYC 666
Cdd:cd14066    1 IGSGGFGTVYKGV-LENGT-----VVAVKRLNEMnCAASKKEFL-TELEMLGRL-RHPNLVRLLGYCLESDEKLLVYEYM 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 667 CYGDLLNFLRRKaeamlgpslspgqdpeggvdyknihlekkyvrrdsgfssqgvdtyvemrpvstssndsfseqdldkED 746
Cdd:cd14066   73 PNGSLEDRLHCH------------------------------------------------------------------KG 86
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 747 GRPLELRDLLHFSSQVAQGMAFL---ASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDIMNDSNYIVKGNARLPVKWMA 823
Cdd:cd14066   87 SPPLPWPQRLKIAKGIARGLEYLheeCPPPIIHGDIKSSNILLDEDFEPKLTDFGLARLIPPSESVSKTSAVKGTIGYLA 166
                        250       260
                 ....*....|....*....|....*..
gi 569026720 824 PESIFDCVYTVQSDVWSYGILLWEIFS 850
Cdd:cd14066  167 PEYIRTGRVSTKSDVYSFGVVLLELLT 193
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
582-848 1.11e-19

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: 89.58  E-value: 1.11e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 582 LQFGKTLGAGAFGKVVEATAFGLGKEdavlkVAVKMLKSTAhaDEKEALMSELKIMSHLgQHENIVNLLGACTHGGPVLV 661
Cdd:cd06614    2 YKNLEKIGEGASGEVYKATDRATGKE-----VAIKKMRLRK--QNKELIINEILIMKEC-KHPNIVDYYDSYLVGDELWV 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 662 ITEYCCYGDLLNFLRRKAEAMLGPSLSpgqdpeggvdyknihlekkYVRRdsgfssqgvdtyvemrpvstssndsfseqd 741
Cdd:cd06614   74 VMEYMDGGSLTDIITQNPVRMNESQIA-------------------YVCR------------------------------ 104
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 742 ldkedgrplelrdllhfssQVAQGMAFLASKNCIHRDVAARNVLLT-NGHVaKIGDFGLA---------RDIMNDSNYiv 811
Cdd:cd06614  105 -------------------EVLQGLEYLHSQNVIHRDIKSDNILLSkDGSV-KLADFGFAaqltkekskRNSVVGTPY-- 162
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 569026720 812 kgnarlpvkWMAPESIFDCVYTVQSDVWSYGILLWEI 848
Cdd:cd06614  163 ---------WMAPEVIKRKDYGPKVDIWSLGIMCIEM 190
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
585-902 2.07e-19

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: 89.36  E-value: 2.07e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 585 GKTLGAGAFGKVVEATAFGLGKEDAVLKVAVKMLKSTAHADEK----EALMSELKIMSHLgQHENIVNLLGActhggpvl 660
Cdd:cd06629    6 GELIGKGTYGRVYLAMNATTGEMLAVKQVELPKTSSDRADSRQktvvDALKSEIDTLKDL-DHPNIVQYLGF-------- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 661 viteyccygdllnflrrkaeamlgpslspgqdpEGGVDYKNIHLEkkYV---------RRDSGFssqgvdtyvemrpvst 731
Cdd:cd06629   77 ---------------------------------EETEDYFSIFLE--YVpggsigsclRKYGKF---------------- 105
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 732 ssndsfsEQDLDKedgrplelrdllHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLAR---DIM-NDS 807
Cdd:cd06629  106 -------EEDLVR------------FFTRQILDGLAYLHSKGILHRDLKADNILVDLEGICKISDFGISKksdDIYgNNG 166
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 808 NYIVKGNarlpVKWMAPEsIFDCV---YTVQSDVWSYGILLWEIFSlGLNPYPGILVNSKFYKL--------VKDGYQMA 876
Cdd:cd06629  167 ATSMQGS----VFWMAPE-VIHSQgqgYSAKVDIWSLGCVVLEMLA-GRRPWSDDEAIAAMFKLgnkrsappVPEDVNLS 240
                        330       340
                 ....*....|....*....|....*.
gi 569026720 877 QPAFAPKNiysimqACWALEPTHRPT 902
Cdd:cd06629  241 PEALDFLN------ACFAIDPRDRPT 260
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
582-902 2.93e-19

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: 88.59  E-value: 2.93e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 582 LQFGKTLGAGAFGKVVEATAFGLgkedavlKVAVKMLK-STAHADEKEALMSELKImSHLgQHENIVNLLGA---CTHGG 657
Cdd:cd13979    5 LRLQEPLGSGGFGSVYKATYKGE-------TVAVKIVRrRRKNRASRQSFWAELNA-ARL-RHENIVRVLAAetgTDFAS 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 658 PVLVITEYCcygdllnflrrkaeamlgpslspgqdpeggvdyknihlekkyvrrdsgfssqgvdtyvemrpvstssnDSF 737
Cdd:cd13979   76 LGLIIMEYC--------------------------------------------------------------------GNG 87
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 738 SEQDLDKEDGRPLELRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARdIMNDSNyiVKGNARL 817
Cdd:cd13979   88 TLQQLIYEGSEPLPLAHRILISLDIARALRFCHSHGIVHLDVKPANILISEQGVCKLCDFGCSV-KLGEGN--EVGTPRS 164
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 818 PVK----WMAPESIFDCVYTVQSDVWSYGILLWEIFSlGLNPYPG----ILVNSKFYKLVKDGYQMAQPAFApKNIYSIM 889
Cdd:cd13979  165 HIGgtytYRAPELLKGERVTPKADIYSFGITLWQMLT-RELPYAGlrqhVLYAVVAKDLRPDLSGLEDSEFG-QRLRSLI 242
                        330
                 ....*....|...
gi 569026720 890 QACWALEPTHRPT 902
Cdd:cd13979  243 SRCWSAQPAERPN 255
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
586-906 3.58e-19

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: 88.09  E-value: 3.58e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 586 KTLGAGAFGKVVEATafglGKEDAVLKVAVKMLKSTAHADEKEALMSELKIMSHLgQHENIVNLLGACTHGGPVLVITEY 665
Cdd:cd08225    6 KKIGEGSFGKIYLAK----AKSDSEHCVIKEIDLTKMPVKEKEASKKEVILLAKM-KHPNIVTFFASFQENGRLFIVMEY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 666 CCYGDLLNFLRRKAEAMlgpslspgqdpeggvdyknihlekkyvrrdsgfssqgvdtyvemrpvstssndsFSEQDLdke 745
Cdd:cd08225   81 CDGGDLMKRINRQRGVL------------------------------------------------------FSEDQI--- 103
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 746 dgrplelrdlLHFSSQVAQGMAFLASKNCIHRDVAARNVLLT-NGHVAKIGDFGLARdIMNDSNYIVKGNARLPVkWMAP 824
Cdd:cd08225  104 ----------LSWFVQISLGLKHIHDRKILHRDIKSQNIFLSkNGMVAKLGDFGIAR-QLNDSMELAYTCVGTPY-YLSP 171
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 825 ESIFDCVYTVQSDVWSYGILLWEIFSLGlNPYPGilvnSKFYKLVkdgYQMAQPAFAP------KNIYSIMQACWALEPT 898
Cdd:cd08225  172 EICQNRPYNNKTDIWSLGCVLYELCTLK-HPFEG----NNLHQLV---LKICQGYFAPispnfsRDLRSLISQLFKVSPR 243

                 ....*...
gi 569026720 899 HRPTFQQI 906
Cdd:cd08225  244 DRPSITSI 251
PKc_TNNI3K cd14064
Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; ...
742-912 3.96e-19

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: 87.97  E-value: 3.96e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 742 LDKEDGRPLELRDLLHFSSQVAQGMAFL--ASKNCIHRDVAARNVLL-TNGHvAKIGDFGLARDI--MNDSNYIVK-GNA 815
Cdd:cd14064   82 LLHEQKRVIDLQSKLIIAVDVAKGMEYLhnLTQPIIHRDLNSHNILLyEDGH-AVVADFGESRFLqsLDEDNMTKQpGNL 160
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 816 RlpvkWMAPESIFDCV-YTVQSDVWSYGILLWEIFSlGLNPY----PGILVNSKFYKLVKD--GYQMaqpafaPKNIYSI 888
Cdd:cd14064  161 R----WMAPEVFTQCTrYSIKADVFSYALCLWELLT-GEIPFahlkPAAAAADMAYHHIRPpiGYSI------PKPISSL 229
                        170       180
                 ....*....|....*....|....
gi 569026720 889 MQACWALEPTHRPTFQQICSFLQE 912
Cdd:cd14064  230 LMRGWNAEPESRPSFVEIVALLEP 253
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
585-906 4.92e-19

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: 87.97  E-value: 4.92e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 585 GKTLGAGAFGKVVEATAFGLGKEDAVLKVAVKMLKSTAHADEK---EALMSELKIMSHLgQHENIVNLLGACTHGgpvlv 661
Cdd:cd06628    5 GALIGSGSFGSVYLGMNASSGELMAVKQVELPSVSAENKDRKKsmlDALQREIALLREL-QHENIVQYLGSSSDA----- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 662 iteyccygdllnflrrkaeamlgpslspgqdpeggvDYKNIHLEkkYVrrdSGFSSQGVdtyvemrpvsTSSNDSFSEqd 741
Cdd:cd06628   79 ------------------------------------NHLNIFLE--YV---PGGSVATL----------LNNYGAFEE-- 105
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 742 ldkedgrPLelrdLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDIMNDSNYIVKGNARL---- 817
Cdd:cd06628  106 -------SL----VRNFVRQILKGLNYLHNRGIIHRDIKGANILVDNKGGIKISDFGISKKLEANSLSTKNNGARPslqg 174
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 818 PVKWMAPESIFDCVYTVQSDVWSYGILLWEIFSlGLNPYPGIlvnSKFYKLVKDGyQMAQPAFaPKNIYS----IMQACW 893
Cdd:cd06628  175 SVFWMAPEVVKQTSYTRKADIWSLGCLVVEMLT-GTHPFPDC---TQMQAIFKIG-ENASPTI-PSNISSeardFLEKTF 248
                        330
                 ....*....|...
gi 569026720 894 ALEPTHRPTFQQI 906
Cdd:cd06628  249 EIDHNKRPTADEL 261
STKc_LIMK cd14154
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer ...
588-911 1.96e-18

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: 86.41  E-value: 1.96e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 588 LGAGAFGKVVEATAFGLGKedavlkvaVKMLKSTAHADE--KEALMSELKIMSHLgQHENIVNLLGACTHGGPVLVITEY 665
Cdd:cd14154    1 LGKGFFGQAIKVTHRETGE--------VMVMKELIRFDEeaQRNFLKEVKVMRSL-DHPNVLKFIGVLYKDKKLNLITEY 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 666 CCYGDLLNFLRRKAeamlgpslspgqdpeggvdyknihlekkyvrrdsgfssqgvdtyvemrpvstssndsfseqdldke 745
Cdd:cd14154   72 IPGGTLKDVLKDMA------------------------------------------------------------------ 85
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 746 dgRPLELRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDIMND------------------- 806
Cdd:cd14154   86 --RPLPWAQRVRFAKDIASGMAYLHSMNIIHRDLNSHNCLVREDKTVVVADFGLARLIVEErlpsgnmspsetlrhlksp 163
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 807 ---SNYIVKGNARlpvkWMAPESIFDCVYTVQSDVWSYGILLWEIFSLgLNPYPGILVNSKFYKLVKDGYQMAQPAFAPK 883
Cdd:cd14154  164 drkKRYTVVGNPY----WMAPEMLNGRSYDEKVDIFSFGIVLCEIIGR-VEADPDYLPRTKDFGLNVDSFREKFCAGCPP 238
                        330       340
                 ....*....|....*....|....*...
gi 569026720 884 NIYSIMQACWALEPTHRPTFQQICSFLQ 911
Cdd:cd14154  239 PFFKLAFLCCDLDPEKRPPFETLEEWLE 266
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
586-850 2.92e-18

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: 85.36  E-value: 2.92e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 586 KTLGAGAFGKVVEAtafglgkEDAVL--KVAVKMLKstAHADEKEALMSELKIMSHLG---QHENIVNLLGACTHGGPVL 660
Cdd:cd05118    5 RKIGEGAFGTVWLA-------RDKVTgeKVAIKKIK--NDFRHPKAALREIKLLKHLNdveGHPNIVKLLDVFEHRGGNH 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 661 V--ITEYCCYgDLLNFLRRKaeamlgpslspgqdpeggvdyknihlekkyvrrdsgfssqgvdtyvemrpvstssndsfs 738
Cdd:cd05118   76 LclVFELMGM-NLYELIKDY------------------------------------------------------------ 94
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 739 eqdldkedGRPLELRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGH-VAKIGDFGLARdIMNDSNYIVKGNARl 817
Cdd:cd05118   95 --------PRGLPLDLIKSYLYQLLQALDFLHSNGIIHRDLKPENILINLELgQLKLADFGLAR-SFTSPPYTPYVATR- 164
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 569026720 818 pvkW-MAPESIFDC-VYTVQSDVWSYGILLWEIFS 850
Cdd:cd05118  165 ---WyRAPEVLLGAkPYGSSIDIWSLGCILAELLT 196
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
588-905 3.16e-18

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: 85.42  E-value: 3.16e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 588 LGAGAFGKVVEAtafgLGKEDAVLKVAVK-MLKSTAHADEKEALMSELKIMSHLgQHENIVNLLGACTHGGPVLVITEYC 666
Cdd:cd14121    3 LGSGTYATVYKA----YRKSGAREVVAVKcVSKSSLNKASTENLLTEIELLKKL-KHPHIVELKDFQWDEEHIYLIMEYC 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 667 CYGDLLNFLRrkaeamlgpslspgqdpeggvdyKNIHLEKKYVRRdsgfssqgvdtyvemrpvstssndsfseqdldked 746
Cdd:cd14121   78 SGGDLSRFIR-----------------------SRRTLPESTVRR----------------------------------- 99
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 747 grplelrdllhFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGH--VAKIGDFGLARDIM-NDSNYIVKGNarlPVkWMA 823
Cdd:cd14121  100 -----------FLQQLASALQFLREHNISHMDLKPQNLLLSSRYnpVLKLADFGFAQHLKpNDEAHSLRGS---PL-YMA 164
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 824 PESIFDCVYTVQSDVWSYGILLWEIFsLGLNPYpgilvNSKFYKLVKDGYQMAQPAFAPKNIySIMQACWAL-------E 896
Cdd:cd14121  165 PEMILKKKYDARVDLWSVGVILYECL-FGRAPF-----ASRSFEELEEKIRSSKPIEIPTRP-ELSADCRDLllrllqrD 237

                 ....*....
gi 569026720 897 PTHRPTFQQ 905
Cdd:cd14121  238 PDRRISFEE 246
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
583-906 3.18e-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: 85.70  E-value: 3.18e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 583 QFGKTLGAGAFGKVVEATAFGLGKEDavlKVAVKML-KSTAHADEKEALM-SELKIMSHLgQHENIVNLLGACTHGGPVL 660
Cdd:cd14080    3 RLGKTIGEGSYSKVKLAEYTKSGLKE---KVACKIIdKKKAPKDFLEKFLpRELEILRKL-RHPNIIQVYSIFERGSKVF 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 661 VITEYCCYGDLLNFLRRKaeamlgpslspGQDPEggvdykniHLEKKYVRrdsgfssqgvdtyvemrpvstssndsfseq 740
Cdd:cd14080   79 IFMEYAEHGDLLEYIQKR-----------GALSE--------SQARIWFR------------------------------ 109
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 741 dldkedgrplelrdllhfssQVAQGMAFLASKNCIHRDVAARNVLLT-NGHVaKIGDFGLARDIMNDSN----------- 808
Cdd:cd14080  110 --------------------QLALAVQYLHSLDIAHRDLKCENILLDsNNNV-KLSDFGFARLCPDDDGdvlsktfcgsa 168
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 809 -Y----IVKGNARLPVKwmapesifdcvytvqSDVWSYGILLWeifslglnpypgILVNSK--F-----YKLVKDgyQMA 876
Cdd:cd14080  169 aYaapeILQGIPYDPKK---------------YDIWSLGVILY------------IMLCGSmpFddsniKKMLKD--QQN 219
                        330       340       350
                 ....*....|....*....|....*....|....*..
gi 569026720 877 QPAFAPKNIYSIMQAC-----WALEP--THRPTFQQI 906
Cdd:cd14080  220 RKVRFPSSVKKLSPECkdlidQLLEPdpTKRATIEEI 256
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
580-902 3.31e-18

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: 85.73  E-value: 3.31e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 580 NNLQFGKTLGAGAFGKVVEATAFGLGKEdavlkVAVKMLkstahadEKEALMSELK---------IMSHLGqHENIVNLl 650
Cdd:cd05581    1 NDFKFGKPLGEGSYSTVVLAKEKETGKE-----YAIKVL-------DKRHIIKEKKvkyvtiekeVLSRLA-HPGIVKL- 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 651 gACTHGGP-----VLvitEYCCYGDLLNFLRRKAeamlgpslspgqdpeggvdyknihlekkyvrrdsgfssqgvdtyve 725
Cdd:cd05581   67 -YYTFQDEsklyfVL---EYAPNGDLLEYIRKYG---------------------------------------------- 96
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 726 mrpvstssndSFSEQDLDkedgrplelrdllHFSSQVAQGMAFLASKNCIHRDVAARNVLLT-NGHVaKIGDFGLArDIM 804
Cdd:cd05581   97 ----------SLDEKCTR-------------FYTAEIVLALEYLHSKGIIHRDLKPENILLDeDMHI-KITDFGTA-KVL 151
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 805 --NDSNYIVKGNARLPVKWM--------------APESIFDCVYTVQSDVWSYGILLWEIFSlGLNPYPGILVNSKFYKL 868
Cdd:cd05581  152 gpDSSPESTKGDADSQIAYNqaraasfvgtaeyvSPELLNEKPAGKSSDLWALGCIIYQMLT-GKPPFRGSNEYLTFQKI 230
                        330       340       350
                 ....*....|....*....|....*....|....
gi 569026720 869 VKDGYQMaqPAFAPKNIYSIMQACWALEPTHRPT 902
Cdd:cd05581  231 VKLEYEF--PENFPPDAKDLIQKLLVLDPSKRLG 262
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
583-906 3.60e-18

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: 85.15  E-value: 3.60e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 583 QFGKTLGAGAFGKVVEATAFGLGKEDAVlKVaVKMLKSTAHADEK-EALMSELKIMSHLgQHENIVNLLGACTHGGPVLV 661
Cdd:cd06632    3 QKGQLLGSGSFGSVYEGFNGDTGDFFAV-KE-VSLVDDDKKSRESvKQLEQEIALLSKL-RHPNIVQYYGTEREEDNLYI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 662 ITEYCCYGDLLNFLRRKaeamlgpslspgqdpeGGVDYKNIHLekkYVRrdsgfssqgvdtyvemrpvstssndsfseqd 741
Cdd:cd06632   80 FLEYVPGGSIHKLLQRY----------------GAFEEPVIRL---YTR------------------------------- 109
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 742 ldkedgrplelrdllhfssQVAQGMAFLASKNCIHRDVAARNVLL-TNGHVaKIGDFGLARDIMNDSNYI-VKGNARlpv 819
Cdd:cd06632  110 -------------------QILSGLAYLHSRNTVHRDIKGANILVdTNGVV-KLADFGMAKHVEAFSFAKsFKGSPY--- 166
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 820 kWMAPESI--FDCVYTVQSDVWSYGILLWEIfSLGLNPYPGILVNSKFYKLVKDGYQMAQPAFAPKNIYSIMQACWALEP 897
Cdd:cd06632  167 -WMAPEVImqKNSGYGLAVDIWSLGCTVLEM-ATGKPPWSQYEGVAAIFKIGNSGELPPIPDHLSPDAKDFIRLCLQRDP 244

                 ....*....
gi 569026720 898 THRPTFQQI 906
Cdd:cd06632  245 EDRPTASQL 253
PKc_LIMK_like_unk cd14156
Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs ...
749-915 6.19e-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: 84.49  E-value: 6.19e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 749 PLELRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLL---TNGHVAKIGDFGLARDIMN------DSNYIVKGNARlpv 819
Cdd:cd14156   85 PLSWREKVELACDISRGMVYLHSKNIYHRDLNSKNCLIrvtPRGREAVVTDFGLAREVGEmpandpERKLSLVGSAF--- 161
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 820 kWMAPESIFDCVYTVQSDVWSYGILLWEIfsLGLNPY-PGILVNSKFYKLVKDGYQMAQPAfAPKNIYSIMQACWALEPT 898
Cdd:cd14156  162 -WMAPEMLRGEPYDRKVDVFSFGIVLCEI--LARIPAdPEVLPRTGDFGLDVQAFKEMVPG-CPEPFLDLAASCCRMDAF 237
                        170
                 ....*....|....*..
gi 569026720 899 HRPTFQQICSFLQEQAQ 915
Cdd:cd14156  238 KRPSFAELLDELEDIAE 254
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
580-905 7.04e-18

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: 84.57  E-value: 7.04e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 580 NNLQFGKTLGAGAFGKVVEATAFGLGKEdavlkVAVKMLKSTAHADEKEALMSELKIMsHLGQHENIVNLLGACTHGGPV 659
Cdd:cd06623    1 SDLERVKVLGQGSSGVVYKVRHKPTGKI-----YALKKIHVDGDEEFRKQLLRELKTL-RSCESPYVVKCYGAFYKEGEI 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 660 LVITEYCCYGDLLNFLRRKaeamlgpslspgqdpeggvdyknihleKKyvrrdsgfssqgvdtyvemrpvstssndsFSE 739
Cdd:cd06623   75 SIVLEYMDGGSLADLLKKV---------------------------GK-----------------------------IPE 98
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 740 QDLDKedgrplelrdllhFSSQVAQGMAFL-ASKNCIHRDVAARNVLL-TNGHVaKIGDFGLARDIMN----DSNYIvkG 813
Cdd:cd06623   99 PVLAY-------------IARQILKGLDYLhTKRHIIHRDIKPSNLLInSKGEV-KIADFGISKVLENtldqCNTFV--G 162
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 814 NarlpVKWMAPESIFDCVYTVQSDVWSYGILLWEiFSLGLNPYPGILVNSKF---YKLVKDgyqmaQPAFAPKNIYS--- 887
Cdd:cd06623  163 T----VTYMSPERIQGESYSYAADIWSLGLTLLE-CALGKFPFLPPGQPSFFelmQAICDG-----PPPSLPAEEFSpef 232
                        330       340
                 ....*....|....*....|
gi 569026720 888 --IMQACWALEPTHRPTFQQ 905
Cdd:cd06623  233 rdFISACLQKDPKKRPSAAE 252
PKc_Dusty cd13975
Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze ...
750-912 1.12e-17

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: 84.08  E-value: 1.12e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 750 LELRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARD--IMNDSnyIVKgnarLPVKwMAPEsI 827
Cdd:cd13975   99 LSLEERLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKKNRAKITDLGFCKPeaMMSGS--IVG----TPIH-MAPE-L 170
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 828 FDCVYTVQSDVWSYGILLWEIFSLGLN-PYPGILVNSK--FYKLVKDGYQMAQPAFAPKNIYSIMQACWALEPTHRPTFQ 904
Cdd:cd13975  171 FSGKYDNSVDVYAFGILFWYLCAGHVKlPEAFEQCASKdhLWNNVRKGVRPERLPVFDEECWNLMEACWSGDPSQRPLLG 250

                 ....*...
gi 569026720 905 QICSFLQE 912
Cdd:cd13975  251 IVQPKLQG 258
STKc_LIMK1 cd14221
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the ...
758-911 1.93e-17

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: 83.47  E-value: 1.93e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 758 FSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDIMNDSN----------------YIVKGNARlpvkW 821
Cdd:cd14221   96 FAKDIASGMAYLHSMNIIHRDLNSHNCLVRENKSVVVADFGLARLMVDEKTqpeglrslkkpdrkkrYTVVGNPY----W 171
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 822 MAPESIFDCVYTVQSDVWSYGILLWEIFSLgLNPYPGILVNSKFYKLVKDGY-QMAQPAFAPKNIYSIMQACWALEPTHR 900
Cdd:cd14221  172 MAPEMINGRSYDEKVDVFSFGIVLCEIIGR-VNADPDYLPRTMDFGLNVRGFlDRYCPPNCPPSFFPIAVLCCDLDPEKR 250
                        170
                 ....*....|.
gi 569026720 901 PTFQQICSFLQ 911
Cdd:cd14221  251 PSFSKLEHWLE 261
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
588-906 1.98e-17

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: 82.82  E-value: 1.98e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 588 LGAGAFGKVVEATAfglgKEDAVLKVAVKMLKSTAHADEKEALMSELKIMSHLGQHENIVNLLGACTHGGPVLVITEYCC 667
Cdd:cd13997    8 IGSGSFSEVFKVRS----KVDGCLYAVKKSKKPFRGPKERARALREVEAHAALGQHPNIVRYYSSWEEGGHLYIQMELCE 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 668 YGDLLNFLrrkaeamlgpslspgqdpeggvdyknihlekkyvrrdsgfSSQGVDTYVemrpvstssndsfSEqdldkedg 747
Cdd:cd13997   84 NGSLQDAL----------------------------------------EELSPISKL-------------SE-------- 102
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 748 rpLELRDLLHfssQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARdIMNDSNYIVKGNARlpvkWMAPESI 827
Cdd:cd13997  103 --AEVWDLLL---QVALGLAFIHSKGIVHLDIKPDNIFISNKGTCKIGDFGLAT-RLETSGDVEEGDSR----YLAPELL 172
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 828 FD-CVYTVQSDVWSYGILLWEIfsLGLNPYPGilvNSKFYKLVKDGYqmaqPAFAPKNIYS-----IMQACWALEPTHRP 901
Cdd:cd13997  173 NEnYTHLPKADIFSLGVTVYEA--ATGEPLPR---NGQQWQQLRQGK----LPLPPGLVLSqeltrLLKVMLDPDPTRRP 243

                 ....*
gi 569026720 902 TFQQI 906
Cdd:cd13997  244 TADQL 248
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
585-908 2.25e-17

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: 82.99  E-value: 2.25e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 585 GKTLGAGAFGKVVEATAFGLGKEDAVLKVAVKMLKStAHADEKeaLMSELKIMSHLgQHENIVNLLGACTHGGPVLVITE 664
Cdd:cd14099    6 GKFLGKGGFAKCYEVTDMSTGKVYAGKVVPKSSLTK-PKQREK--LKSEIKIHRSL-KHPNIVKFHDCFEDEENVYILLE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 665 YCCYGDLLNFLRRkaeamlgpslspgqdpeggvdyknihlekkyvRRdsgfssqgvdtyvemrpvstssndSFSEQdldk 744
Cdd:cd14099   82 LCSNGSLMELLKR--------------------------------RK------------------------ALTEP---- 101
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 745 edgrplELRdllHFSSQVAQGMAFLASKNCIHRDVAARNVLLT-NGHVaKIGDFGLARDIMNDS----------NYIvkg 813
Cdd:cd14099  102 ------EVR---YFMRQILSGVKYLHSNRIIHRDLKLGNLFLDeNMNV-KIGDFGLAARLEYDGerkktlcgtpNYI--- 168
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 814 narlpvkwmAPESIFDCV-YTVQSDVWSYGILLWEIFsLGLNPYPGILVNSKFYKLVKDGYQMAQPAFAPKNIYSIMQAC 892
Cdd:cd14099  169 ---------APEVLEKKKgHSFEVDIWSLGVILYTLL-VGKPPFETSDVKETYKRIKKNEYSFPSHLSISDEAKDLIRSM 238
                        330
                 ....*....|....*.
gi 569026720 893 WALEPTHRPTFQQICS 908
Cdd:cd14099  239 LQPDPTKRPSLDEILS 254
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
574-856 2.76e-17

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: 82.75  E-value: 2.76e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 574 KWEFPRNNLqfgktLGAGAFGKVVEatafGLGKEDAVLKVAVKMLKSTAHADEKEALMSELKIMSHLgQHENIVNLLGAC 653
Cdd:cd14202    1 KFEFSRKDL-----IGHGAFAVVFK----GRHKEKHDLEVAVKCINKKNLAKSQTLLGKEIKILKEL-KHENIVALYDFQ 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 654 THGGPVLVITEYCCYGDLLNFLRRKaeamlgpslspgqdpeggvdyknihlekkyvrrdsgfssqgvdtyvemrpvSTSS 733
Cdd:cd14202   71 EIANSVYLVMEYCNGGDLADYLHTM---------------------------------------------------RTLS 99
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 734 NDSfseqdldkedgrpleLRDLLHfssQVAQGMAFLASKNCIHRDVAARNVLLT---------NGHVAKIGDFGLARDIM 804
Cdd:cd14202  100 EDT---------------IRLFLQ---QIAGAMKMLHSKGIIHRDLKPQNILLSysggrksnpNNIRIKIADFGFARYLQ 161
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 569026720 805 NdsNYIVKGNARLPVkWMAPESIFDCVYTVQSDVWSYGILLWEIFSlGLNPY 856
Cdd:cd14202  162 N--NMMAATLCGSPM-YMAPEVIMSQHYDAKADLWSIGTIIYQCLT-GKAPF 209
STKc_myosinIII_N_like cd06608
N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze ...
578-906 6.74e-17

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: 81.96  E-value: 6.74e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 578 PRNNLQFGKTLGAGAFGKVVEATAFGLGKedavlKVAVKMLKSTAhaDEKEALMSELKIMSHLGQHENIVNLLGA----- 652
Cdd:cd06608    4 PAGIFELVEVIGEGTYGKVYKARHKKTGQ-----LAAIKIMDIIE--DEEEEIKLEINILRKFSNHPNIATFYGAfikkd 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 653 -CTHGGPVLVITEYCCYG---DLLNFLRRKaeamlgpslspgqdpeggvdyknihlekkyvrrdsgfssqgvdtyvemrp 728
Cdd:cd06608   77 pPGGDDQLWLVMEYCGGGsvtDLVKGLRKK-------------------------------------------------- 106
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 729 vstssndsfseqdldkedGRPLELRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLT-NGHVaKIGDFGLARDImnDS 807
Cdd:cd06608  107 ------------------GKRLKEEWIAYILRETLRGLAYLHENKVIHRDIKGQNILLTeEAEV-KLVDFGVSAQL--DS 165
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 808 NYIVKGNARLPVKWMAPESI-----FDCVYTVQSDVWSYGILLWE----------------IFSLGLNPYPgilvnskfy 866
Cdd:cd06608  166 TLGRRNTFIGTPYWMAPEVIacdqqPDASYDARCDVWSLGITAIEladgkpplcdmhpmraLFKIPRNPPP--------- 236
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 569026720 867 klvkdgyQMAQPAFAPKNIYSIMQACWALEPTHRPTFQQI 906
Cdd:cd06608  237 -------TLKSPEKWSKEFNDFISECLIKNYEQRPFTEEL 269
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
586-914 1.15e-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: 80.90  E-value: 1.15e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 586 KTLGAGAFGKVVEATAFGLGKEDAVLKVAvkmLKSTAHAdEKEALMSELKIMSHLgQHENIVNLLGACTHGGPVLVITEY 665
Cdd:cd08530    6 KKLGKGSYGSVYKVKRLSDNQVYALKEVN---LGSLSQK-EREDSVNEIRLLASV-NHPNIIRYKEAFLDGNRLCIVMEY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 666 CCYGDLLNFLRRKaeamlgpslspgqdpeggvdyknihlekkyvrrdsgfssqgvdtyvemrpvstssndsfseqdldKE 745
Cdd:cd08530   81 APFGDLSKLISKR-----------------------------------------------------------------KK 95
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 746 DGRPLELRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDIMNDSNYIVKGNarlPVkWMAPE 825
Cdd:cd08530   96 KRRLFPEDDIWRIFIQMLRGLKALHDQKILHRDLKSANILLSAGDLVKIGDLGISKVLKKNLAKTQIGT---PL-YAAPE 171
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 826 SIFDCVYTVQSDVWSYGILLWEIFSLGLnPYPGILVNSKFYKlVKDGYQMAQPAFAPKNIYSIMQACWALEPTHRPTFQQ 905
Cdd:cd08530  172 VWKGRPYDYKSDIWSLGCLLYEMATFRP-PFEARTMQELRYK-VCRGKFPPIPPVYSQDLQQIIRSLLQVNPKKRPSCDK 249

                 ....*....
gi 569026720 906 IcsfLQEQA 914
Cdd:cd08530  250 L---LQSPA 255
PTK_Jak2_rpt1 cd05078
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 2; Jak2 is widely ...
582-906 1.72e-16

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: 80.38  E-value: 1.72e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 582 LQFGKTLGAGAFGKVVEATAFGLGK--EDAVLKVAVKMLKSTaHADEKEALMSELKIMSHLgQHENIVNLLGACTHGGPV 659
Cdd:cd05078    1 LIFNESLGQGTFTKIFKGIRREVGDygQLHETEVLLKVLDKA-HRNYSESFFEAASMMSQL-SHKHLVLNYGVCVCGDEN 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 660 LVITEYCCYGDLLNFLRRKAEAMlgpslspgqdpeggvdykNIHLEkkyvrrdsgfssqgvdtyvemrpvstssndsfse 739
Cdd:cd05078   79 ILVQEYVKFGSLDTYLKKNKNCI------------------NILWK---------------------------------- 106
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 740 qdldkedgrplelrdlLHFSSQVAQGMAFLASKNCIHRDVAARNVLLT--------NGHVAKIGDFG-----LARDIMND 806
Cdd:cd05078  107 ----------------LEVAKQLAWAMHFLEEKTLVHGNVCAKNILLIreedrktgNPPFIKLSDPGisitvLPKDILLE 170
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 807 snyivkgnaRLPvkWMAPESIFDCVY-TVQSDVWSYGILLWEIFSLGLNPYPGiLVNSKFYKLVKDGYQMAQPAFApkNI 885
Cdd:cd05078  171 ---------RIP--WVPPECIENPKNlSLATDKWSFGTTLWEICSGGDKPLSA-LDSQRKLQFYEDRHQLPAPKWT--EL 236
                        330       340
                 ....*....|....*....|.
gi 569026720 886 YSIMQACWALEPTHRPTFQQI 906
Cdd:cd05078  237 ANLINNCMDYEPDHRPSFRAI 257
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
583-908 1.81e-16

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: 80.21  E-value: 1.81e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 583 QFGKTLGAGAFGKVVEA----TAFglgkedavlKVAVKML-KST-AHADEKEALMSELKIMSHLgQHENIVNLLGACTHG 656
Cdd:cd14007    3 EIGKPLGKGKFGNVYLArekkSGF---------IVALKVIsKSQlQKSGLEHQLRREIEIQSHL-RHPNILRLYGYFEDK 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 657 GPVLVITEYCCYGDLLNFLRRKaeamlgpslspgqdpeggvdyknihleKKyvrrdsgFSSQGVDTYVemrpvstssnds 736
Cdd:cd14007   73 KRIYLILEYAPNGELYKELKKQ---------------------------KR-------FDEKEAAKYI------------ 106
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 737 fseqdldkedgrplelrdllhfsSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDIMNdsnyivkgNAR 816
Cdd:cd14007  107 -----------------------YQLALALDYLHSKNIIHRDIKPENILLGSNGELKLADFGWSVHAPS--------NRR 155
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 817 LPV----KWMAPESIFDCVYTVQSDVWSYGILLWEIFSlGLNPYPGILVNSKFYKLVKDGYQMaqpafaPKNIYSIMQ-- 890
Cdd:cd14007  156 KTFcgtlDYLPPEMVEGKEYDYKVDIWSLGVLCYELLV-GKPPFESKSHQETYKRIQNVDIKF------PSSVSPEAKdl 228
                        330       340
                 ....*....|....*....|
gi 569026720 891 ACWAL--EPTHRPTFQQICS 908
Cdd:cd14007  229 ISKLLqkDPSKRLSLEQVLN 248
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
578-906 2.32e-16

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: 80.56  E-value: 2.32e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 578 PRNNLQFGKTLGAGAFGKVVEATafglgKEDAVLKVAVKMLKsTAHADEKEALMSELKIMSHLgQHENIVNLLGACTHGG 657
Cdd:cd06611    3 PNDIWEIIGELGDGAFGKVYKAQ-----HKETGLFAAAKIIQ-IESEEELEDFMVEIDILSEC-KHPNIVGLYEAYFYEN 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 658 PVLVITEYCcygdllnflrrkaeamlgpslspgqdPEGGVDYKNIHLEKkyvrrdsGFssqgvdTYVEMRPVStssndsf 737
Cdd:cd06611   76 KLWILIEFC--------------------------DGGALDSIMLELER-------GL------TEPQIRYVC------- 109
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 738 seqdldkedgrplelrdllhfsSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFG----LARDIMNDSNYIvkG 813
Cdd:cd06611  110 ----------------------RQMLEALNFLHSHKVIHRDLKAGNILLTLDGDVKLADFGvsakNKSTLQKRDTFI--G 165
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 814 NARlpvkWMAPESIF-----DCVYTVQSDVWSYGILLWEIFSL-----GLNPYPGILvnskfyKLVK-DGYQMAQPAFAP 882
Cdd:cd06611  166 TPY----WMAPEVVAcetfkDNPYDYKADIWSLGITLIELAQMepphhELNPMRVLL------KILKsEPPTLDQPSKWS 235
                        330       340
                 ....*....|....*....|....
gi 569026720 883 KNIYSIMQACWALEPTHRPTFQQI 906
Cdd:cd06611  236 SSFNDFLKSCLVKDPDDRPTAAEL 259
STKc_RIP1 cd14027
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze ...
588-910 2.68e-16

Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RIP1 harbors a C-terminal Death domain (DD), which binds death receptors (DRs) including TNF receptor 1, Fas, TNF-related apoptosis-inducing ligand receptor 1 (TRAILR1), and TRAILR2. It also interacts with other DD-containing adaptor proteins such as TRADD and FADD. RIP1 can also recruit other kinases including MEKK1, MEKK3, and RIP3 through an intermediate domain (ID) that bears a RIP homotypic interaction motif (RHIM). RIP1 plays a crucial role in determining a cell's fate, between survival or death, following exposure to stress signals. It is important in the signaling of NF-kappaB and MAPKs, and it links DR-associated signaling to reactive oxygen species (ROS) production. Abnormal RIP1 function may result in ROS accummulation affecting inflammatory responses, innate immunity, stress responses, and cell survival. RIP kinases serve as essential sensors of cellular stress. The RIP1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270929 [Multi-domain]  Cd Length: 267  Bit Score: 79.85  E-value: 2.68e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 588 LGAGAFGKVVEATAFGLGKedAVLKVavkMLKSTAHADEKEALMSELKIMSHLgQHENIVNLLGACTHGGPVLVITEYCC 667
Cdd:cd14027    1 LDSGGFGKVSLCFHRTQGL--VVLKT---VYTGPNCIEHNEALLEEGKMMNRL-RHSRVVKLLGVILEEGKYSLVMEYME 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 668 YGDLLNFLrrkaeamlgpslspgqdpeggvdyknihlEKKYVrrdsgfssqgvdtyvemrPVSTSsndsfseqdldkedG 747
Cdd:cd14027   75 KGNLMHVL-----------------------------KKVSV------------------PLSVK--------------G 93
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 748 RplelrdllhFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARdiMNDSNYIVKGNARLPVK------- 820
Cdd:cd14027   94 R---------IILEIIEGMAYLHGKGVIHKDLKPENILVDNDFHIKIADLGLAS--FKMWSKLTKEEHNEQREvdgtakk 162
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 821 ------WMAPESIFD--CVYTVQSDVWSYGILLWEIFSlGLNPYPGILVNSKFYKLVKDGYQMAQ---PAFAPKNIYSIM 889
Cdd:cd14027  163 nagtlyYMAPEHLNDvnAKPTEKSDVYSFAIVLWAIFA-NKEPYENAINEDQIIMCIKSGNRPDVddiTEYCPREIIDLM 241
                        330       340
                 ....*....|....*....|..
gi 569026720 890 QACWALEPTHRPTFQQI-CSFL 910
Cdd:cd14027  242 KLCWEANPEARPTFPGIeEKFR 263
STKc_LRRK cd14000
Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the ...
588-910 3.92e-16

Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LRRKs are also classified as ROCO proteins because they contain a ROC (Ras of complex proteins)/GTPase domain followed by a COR (C-terminal of ROC) domain of unknown function. In addition, LRRKs contain a catalytic kinase domain and protein-protein interaction motifs including a WD40 domain, LRRs and ankyrin (ANK) repeats. LRRKs possess both GTPase and kinase activities, with the ROC domain acting as a molecular switch for the kinase domain, cycling between a GTP-bound state which drives kinase activity and a GDP-bound state which decreases the activity. Vertebrates contain two members, LRRK1 and LRRK2, which show complementary expression in the brain. Mutations in LRRK2 are linked to both familial and sporadic forms of Parkinson's disease. The normal roles of LRRKs are not clearly defined. They may be involved in mitogen-activated protein kinase (MAPK) pathways, protein translation control, programmed cell death pathways, and cytoskeletal dynamics. The LRRK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270902 [Multi-domain]  Cd Length: 275  Bit Score: 79.58  E-value: 3.92e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 588 LGAGAFGKVVEATAFGlgkEDavlkVAVKML---KSTAHADEKEALM-----------------SELKIMSHLgQHENIV 647
Cdd:cd14000    2 LGDGGFGSVYRASYKG---EP----VAVKIFnkhTSSNFANVPADTMlrhlratdamknfrllrQELTVLSHL-HHPSIV 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 648 NLLGACTHggPVLVITEYCCYGDLLNFLR--RKAEAMLGPslspgqdpeggvdykniHLEKKYVRrdsgfssqgvdtyve 725
Cdd:cd14000   74 YLLGIGIH--PLMLVLELAPLGSLDHLLQqdSRSFASLGR-----------------TLQQRIAL--------------- 119
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 726 mrpvstssndsfseqdldkedgrplelrdllhfssQVAQGMAFLASKNCIHRDVAARNVLL----TNGHV-AKIGDFGLA 800
Cdd:cd14000  120 -----------------------------------QVADGLRYLHSAMIIYRDLKSHNVLVwtlyPNSAIiIKIADYGIS 164
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 801 RDIMNDSnyiVKGNARLPvKWMAPESI-FDCVYTVQSDVWSYGILLWEIFSLGlNPYPG---ILVNSKFYKLVKDGYQMA 876
Cdd:cd14000  165 RQCCRMG---AKGSEGTP-GFRAPEIArGNVIYNEKVDVFSFGMLLYEILSGG-APMVGhlkFPNEFDIHGGLRPPLKQY 239
                        330       340       350
                 ....*....|....*....|....*....|....
gi 569026720 877 QPAFaPKNIYSIMQACWALEPTHRPTFQQICSFL 910
Cdd:cd14000  240 ECAP-WPEVEVLMKKCWKENPQQRPTAVTVVSIL 272
STKc_LIMK2 cd14222
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the ...
588-906 5.87e-16

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: 79.22  E-value: 5.87e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 588 LGAGAFGKVVEATAFGLGKedavlkvaVKMLKSTAHADE--KEALMSELKIMSHLgQHENIVNLLGACTHGGPVLVITEY 665
Cdd:cd14222    1 LGKGFFGQAIKVTHKATGK--------VMVMKELIRCDEetQKTFLTEVKVMRSL-DHPNVLKFIGVLYKDKRLNLLTEF 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 666 CCYGDLLNFLRrkaeamlgpslspgqdpeggvdyknihlekkyvrrdsgfssqgvdtyvemrpvstsSNDSFseqdldke 745
Cdd:cd14222   72 IEGGTLKDFLR--------------------------------------------------------ADDPF-------- 87
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 746 dgrPLELRdlLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDIMND------------------- 806
Cdd:cd14222   88 ---PWQQK--VSFAKGIASGMAYLHSMSIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEEkkkpppdkpttkkrtlrkn 162
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 807 ---SNYIVKGNARlpvkWMAPESIFDCVYTVQSDVWSYGILLWEIFSlGLNPYPGILVNSKFYKL-VKDGYQMAQPAFAP 882
Cdd:cd14222  163 drkKRYTVVGNPY----WMAPEMLNGKSYDEKVDIFSFGIVLCEIIG-QVYADPDCLPRTLDFGLnVRLFWEKFVPKDCP 237
                        330       340
                 ....*....|....*....|....
gi 569026720 883 KNIYSIMQACWALEPTHRPTFQQI 906
Cdd:cd14222  238 PAFFPLAAICCRLEPDSRPAFSKL 261
STKc_STK10 cd06644
Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase ...
564-906 7.72e-16

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: 79.31  E-value: 7.72e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 564 IDPtqlpyNEKWEFprnnlqFGKtLGAGAFGKVVEATafglGKEDAVLkVAVKMLKsTAHADEKEALMSELKIMSHLgQH 643
Cdd:cd06644    8 LDP-----NEVWEI------IGE-LGDGAFGKVYKAK----NKETGAL-AAAKVIE-TKSEEELEDYMVEIEILATC-NH 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 644 ENIVNLLGACTHGGPVLVITEYCcygdllnflrrkaeamlgpslspgqdPEGGVDYKNIHLekkyvrrDSGFSSQGVDTy 723
Cdd:cd06644   69 PYIVKLLGAFYWDGKLWIMIEFC--------------------------PGGAVDAIMLEL-------DRGLTEPQIQV- 114
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 724 vemrpvstssndsfseqdldkedgrplelrdllhFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLA--- 800
Cdd:cd06644  115 ----------------------------------ICRQMLEALQYLHSMKIIHRDLKAGNVLLTLDGDIKLADFGVSakn 160
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 801 ------RDIMNDSNYivkgnarlpvkWMAPESIF-----DCVYTVQSDVWSYGILLWEIFSL-----GLNPYPGILVNSK 864
Cdd:cd06644  161 vktlqrRDSFIGTPY-----------WMAPEVVMcetmkDTPYDYKADIWSLGITLIEMAQIepphhELNPMRVLLKIAK 229
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 569026720 865 fyklvKDGYQMAQPAFAPKNIYSIMQACWALEPTHRPTFQQI 906
Cdd:cd06644  230 -----SEPPTLSQPSKWSMEFRDFLKTALDKHPETRPSAAQL 266
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
586-907 1.31e-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: 77.97  E-value: 1.31e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 586 KTLGAGAFGKVVEAtafgLGKEDAVLKVAVKMLKSTAHADEKEALMSELKIMSHLgQHENIVNLLG------ACThggpV 659
Cdd:cd08217    6 ETIGKGSFGTVRKV----RRKSDGKILVWKEIDYGKMSEKEKQQLVSEVNILREL-KHPNIVRYYDrivdraNTT----L 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 660 LVITEYCCYGDLLNFLRRKaeamlgpslspgqdpeggvdyknihlekkyvrrdsgfssqgvdtyvemrpvstssndsfse 739
Cdd:cd08217   77 YIVMEYCEGGDLAQLIKKC------------------------------------------------------------- 95
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 740 qdldKEDGRPLELRDLLHFSSQVAqgmafLASKNC----------IHRDVAARNVLLTNGHVAKIGDFGLARdIMNDSNY 809
Cdd:cd08217   96 ----KKENQYIPEEFIWKIFTQLL-----LALYEChnrsvgggkiLHRDLKPANIFLDSDNNVKLGDFGLAR-VLSHDSS 165
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 810 IVKGNARLPVkWMAPESIFDCVYTVQSDVWSYGILLWEIFSLGLnPYPGilvnSKFYKL---VKDGYQMAQPAFAPKNIY 886
Cdd:cd08217  166 FAKTYVGTPY-YMSPELLNEQSYDEKSDIWSLGCLIYELCALHP-PFQA----ANQLELakkIKEGKFPRIPSRYSSELN 239
                        330       340
                 ....*....|....*....|.
gi 569026720 887 SIMQACWALEPTHRPTFQQIC 907
Cdd:cd08217  240 EVIKSMLNVDPDKRPSVEELL 260
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
588-847 1.69e-15

Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes yeast ATG1 and metazoan homologs including vertebrate ULK1-3. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. It is involved in nutrient sensing and signaling, the assembly of autophagy factors and the execution of autophagy. In metazoans, ATG1 homologs display additional functions. Unc-51 and ULKs have been implicated in neuronal and axonal development. The ATG1/ULK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270911 [Multi-domain]  Cd Length: 251  Bit Score: 77.26  E-value: 1.69e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 588 LGAGAFGKVVEATAFGLGKEdavlkVAVK-MLKSTAHADEKEALMSELKIMSHLgQHENIVNLLGACTHGGPVLVITEYC 666
Cdd:cd14009    1 IGRGSFATVWKGRHKQTGEV-----VAIKeISRKKLNKKLQENLESEIAILKSI-KHPNIVRLYDVQKTEDFIYLVLEYC 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 667 CYGDLLNFLRRKaeamlgpslspgqdpeGGvdyknihLEKKYVRrdsgfssqgvdtyvemrpvstssndsfseqdldked 746
Cdd:cd14009   75 AGGDLSQYIRKR----------------GR-------LPEAVAR------------------------------------ 95
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 747 grplelrdllHFSSQVAQGMAFLASKNCIHRDVAARNVLL-TNGHVA--KIGDFGLARDIMNDS-NYIVKGNarlPVkWM 822
Cdd:cd14009   96 ----------HFMQQLASGLKFLRSKNIIHRDLKPQNLLLsTSGDDPvlKIADFGFARSLQPASmAETLCGS---PL-YM 161
                        250       260
                 ....*....|....*....|....*
gi 569026720 823 APESIFDCVYTVQSDVWSYGILLWE 847
Cdd:cd14009  162 APEILQFQKYDAKADLWSVGAILFE 186
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
588-858 1.90e-15

Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of CDK9 and CDK12 from higher eukaryotes, yeast BUR1, C-type plant CDKs (CdkC), and similar proteins. CDK9, BUR1, and CdkC are functionally equivalent. They act as a kinase for the C-terminal domain of RNA polymerase II and participate in regulating mutliple steps of gene expression including transcription elongation and RNA processing. CDK9 and CdkC associate with T-type cyclins while BUR1 associates with the cyclin BUR2. CDK12 is a unique CDK that contains an arginine/serine-rich (RS) domain, which is predominantly found in splicing factors. CDK12 interacts with cyclins L1 and L2, and participates in regulating transcription and alternative splicing. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK9-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270832 [Multi-domain]  Cd Length: 291  Bit Score: 77.99  E-value: 1.90e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 588 LGAGAFGKVVEATAFGLGKedavlKVAVKMLKSTahaDEKEAL----MSELKIMSHLgQHENIVNLLGACT------HGG 657
Cdd:cd07840    7 IGEGTYGQVYKARNKKTGE-----LVALKKIRME---NEKEGFpitaIREIKLLQKL-DHPNVVRLKEIVTskgsakYKG 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 658 PVLVITEYCCYgDLLNFLRRKaeamlGPSLSPGQdpeggvdyknihlekkyvrrdsgfssqgvdtyvemrpvstssndsf 737
Cdd:cd07840   78 SIYMVFEYMDH-DLTGLLDNP-----EVKFTESQ---------------------------------------------- 105
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 738 seqdldkedgrplelrdLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARdimndsNYIVKGNARL 817
Cdd:cd07840  106 -----------------IKCYMKQLLEGLQYLHSNGILHRDIKGSNILINNDGVLKLADFGLAR------PYTKENNADY 162
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 569026720 818 PVK----WM-APESIFDCV-YTVQSDVWSYGILLWEIFsLGLNPYPG 858
Cdd:cd07840  163 TNRvitlWYrPPELLLGATrYGPEVDMWSVGCILAELF-TGKPIFQG 208
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
581-904 2.09e-15

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: 77.39  E-value: 2.09e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 581 NLQFGKTLGAGAFGKVVEATAFglgKEDavLKVAVKMLKsTAHADEKEAL-------MSELKIMSHLGQHENIVNLLGAC 653
Cdd:cd13993    1 RYQLISPIGEGAYGVVYLAVDL---RTG--RKYAIKCLY-KSGPNSKDGNdfqklpqLREIDLHRRVSRHPNIITLHDVF 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 654 THGGPVLVITEYCCYGDLlnflrrkaeamlgpslspgqdpeggvdYKNIHLEKKYVrrdsgfssqgvdtyvemrpvstss 733
Cdd:cd13993   75 ETEVAIYIVLEYCPNGDL---------------------------FEAITENRIYV------------------------ 103
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 734 ndsfseqdldkedGRPLELRdllHFSSQVAQGMAFLASKNCIHRDVAARNVLLT-NGHVAKIGDFGLARDIMNDSNYIVk 812
Cdd:cd13993  104 -------------GKTELIK---NVFLQLIDAVKHCHSLGIYHRDIKPENILLSqDEGTVKLCDFGLATTEKISMDFGV- 166
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 813 GNARlpvkWMAPESI---------FDCVYtvqSDVWSYGILLWEIFSlGLNP--YPGILVNSKFYKLVKDG--YQMAQPA 879
Cdd:cd13993  167 GSEF----YMAPECFdevgrslkgYPCAA---GDIWSLGIILLNLTF-GRNPwkIASESDPIFYDYYLNSPnlFDVILPM 238
                        330       340
                 ....*....|....*....|....*
gi 569026720 880 FapKNIYSIMQACWALEPTHRPTFQ 904
Cdd:cd13993  239 S--DDFYNLLRQIFTVNPNNRILLP 261
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
580-926 2.71e-15

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: 77.36  E-value: 2.71e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 580 NNLQFGKTLGAGAFGKVVEATAFGLGKedavlKVAVKMLKsTAHADE--KEALMSELKIMSHLgQHENIVNLLGACTHGG 657
Cdd:cd07833    1 NKYEVLGVVGEGAYGVVLKCRNKATGE-----IVAIKKFK-ESEDDEdvKKTALREVKVLRQL-RHENIVNLKEAFRRKG 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 658 PVLVITEYCcYGDLLNFLRRkaeamlgpslSPGqdpegGVDYKnihlekkYVRRdsgfssqgvdtyvemrpvstssndsf 737
Cdd:cd07833   74 RLYLVFEYV-ERTLLELLEA----------SPG-----GLPPD-------AVRS-------------------------- 104
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 738 seqdldkedgrplelrdllhFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDIMNDSN-----YIVk 812
Cdd:cd07833  105 --------------------YIWQLLQAIAYCHSHNIIHRDIKPENILVSESGVLKLCDFGFARALTARPAspltdYVA- 163
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 813 gnarlpVKWM-APESIF-DCVYTVQSDVWSYGILLWEIFslglnpypgilvnskfyklvkDGyqmaQPAFAPKN----IY 886
Cdd:cd07833  164 ------TRWYrAPELLVgDTNYGKPVDVWAIGCIMAELL---------------------DG----EPLFPGDSdidqLY 212
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 569026720 887 SIMQACWALEPTHRPTFQQICSF----LQEQAQEDRRERDYTNL 926
Cdd:cd07833  213 LIQKCLGPLPPSHQELFSSNPRFagvaFPEPSQPESLERRYPGK 256
STKc_FA2-like cd08529
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar ...
585-906 2.96e-15

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: 76.68  E-value: 2.96e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 585 GKTLGAGAFGKVVEATAfglgKEDAVLKVAVKMLKSTAHADEKEALMSELKIMSHLgQHENIVNLLGACTHGGPVLVITE 664
Cdd:cd08529    5 LNKLGKGSFGVVYKVVR----KVDGRVYALKQIDISRMSRKMREEAIDEARVLSKL-NSPYVIKYYDSFVDKGKLNIVME 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 665 YCCYGDLLNFLRRKAeamlgpslspgqdpeggvdyknihlekkyvrrdsgfssqgvdtyvemrpvstssndsfseqdldk 744
Cdd:cd08529   80 YAENGDLHSLIKSQR----------------------------------------------------------------- 94
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 745 edGRPLELRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARdIMNDSNYIVKGNARLPVkWMAP 824
Cdd:cd08529   95 --GRPLPEDQIWKFFIQTLLGLSHLHSKKILHRDIKSMNIFLDKGDNVKIGDLGVAK-ILSDTTNFAQTIVGTPY-YLSP 170
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 825 ESIFDCVYTVQSDVWSYGILLWEIfSLGLNPYP----GILVnskfYKLVKDGYQmAQPAFAPKNIYSIMQACWALEPTHR 900
Cdd:cd08529  171 ELCEDKPYNEKSDVWALGCVLYEL-CTGKHPFEaqnqGALI----LKIVRGKYP-PISASYSQDLSQLIDSCLTKDYRQR 244

                 ....*.
gi 569026720 901 PTFQQI 906
Cdd:cd08529  245 PDTTEL 250
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
589-921 3.05e-15

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: 76.52  E-value: 3.05e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 589 GAGAFGKVVEATAFGLGKEDAvLKVAVKMLKSTahaDEKEALMSELKIMSHLgQHENIVNLLGACTHGGPVLVITEYCcY 668
Cdd:cd14002   10 GEGSFGKVYKGRRKYTGQVVA-LKFIPKRGKSE---KELRNLRQEIEILRKL-NHPNIIEMLDSFETKKEFVVVTEYA-Q 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 669 GDLLNFLrrkaeamlgpslspgqdpeggvdyknihlekkyvrrdsgfssqgvdtyvemrpvstssndsfseqdldkEDGR 748
Cdd:cd14002   84 GELFQIL---------------------------------------------------------------------EDDG 94
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 749 PLELRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDImnDSNYIV----KGNarlPVkWMAP 824
Cdd:cd14002   95 TLPEEEVRSIAKQLVSALHYLHSNRIIHRDMKPQNILIGKGGVVKLCDFGFARAM--SCNTLVltsiKGT---PL-YMAP 168
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 825 ESIFDCVYTVQSDVWSYGILLWEIFsLGLNPYpgiLVNSkFYKLVkdgyQM--AQPAFAPKNIYsimqacwalepthrPT 902
Cdd:cd14002  169 ELVQEQPYDHTADLWSLGCILYELF-VGQPPF---YTNS-IYQLV----QMivKDPVKWPSNMS--------------PE 225
                        330
                 ....*....|....*....
gi 569026720 903 FQqicSFLQEQAQEDRRER 921
Cdd:cd14002  226 FK---SFLQGLLNKDPSKR 241
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
588-889 4.48e-15

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: 76.75  E-value: 4.48e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 588 LGAGAFGKVVEATafglGKEDAVLkVAVKMLKstaHADEKEAL----MSELKIMSHLgQHENIVNLLGACTHGGPVLVIT 663
Cdd:cd07829    7 LGEGTYGVVYKAK----DKKTGEI-VALKKIR---LDNEEEGIpstaLREISLLKEL-KHPNIVKLLDVIHTENKLYLVF 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 664 EYCCYgDLLNFLRRKAeamlgpslspgqdpeggvdyknihlekkyvrrdsgfssqgvdtyvemrpvstssndsfseqdld 743
Cdd:cd07829   78 EYCDQ-DLKKYLDKRP---------------------------------------------------------------- 92
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 744 kedgRPLELRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDIMNDSNYIVKGNARLpvkWM- 822
Cdd:cd07829   93 ----GPLPPNLIKSIMYQLLRGLAYCHSHRILHRDLKPQNLLINRDGVLKLADFGLARAFGIPLRTYTHEVVTL---WYr 165
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 823 APESIFDC-VYTVQSDVWSYG-IL------------------LWEIFS-LGL-NP--YPGilvnskFYKLVKdgYQMAQP 878
Cdd:cd07829  166 APEILLGSkHYSTAVDIWSVGcIFaelitgkplfpgdseidqLFKIFQiLGTpTEesWPG------VTKLPD--YKPTFP 237
                        330
                 ....*....|.
gi 569026720 879 AFAPKNIYSIM 889
Cdd:cd07829  238 KWPKNDLEKVL 248
STKc_Nek4 cd08223
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
742-906 1.07e-14

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: 75.17  E-value: 1.07e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 742 LDKEDGRPLELRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARdIMNDSNYIVKGNARLPVkW 821
Cdd:cd08223   91 LKEQKGVLLEERQVVEWFVQIAMALQYMHERNILHRDLKTQNIFLTKSNIIKVGDLGIAR-VLESSSDMATTLIGTPY-Y 168
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 822 MAPESIFDCVYTVQSDVWSYGILLWEIFSLGlNPYPGILVNSKFYKLVKdGYQMAQPAFAPKNIYSIMQACWALEPTHRP 901
Cdd:cd08223  169 MSPELFSNKPYNHKSDVWALGCCVYEMATLK-HAFNAKDMNSLVYKILE-GKLPPMPKQYSPELGELIKAMLHQDPEKRP 246

                 ....*
gi 569026720 902 TFQQI 906
Cdd:cd08223  247 SVKRI 251
PK_GC-A_B cd14042
Pseudokinase domain of the membrane Guanylate Cyclase receptors, GC-A and GC-B; The ...
613-910 1.60e-14

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: 74.94  E-value: 1.60e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 613 VAVKMLKSTAHADEKEALMsELKIMSHLgQHENIVNLLGACTHGGPVLVITEYCCYGDLlnflrrkaeamlgpslspgQD 692
Cdd:cd14042   33 VAIKKVNKKRIDLTREVLK-ELKHMRDL-QHDNLTRFIGACVDPPNICILTEYCPKGSL-------------------QD 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 693 peggvdyknIhLEkkyvrrdsgfssqgvdtyvemrpvstssNDSfseqdldkedgrpLELRDLLHFS--SQVAQGMAF-- 768
Cdd:cd14042   92 ---------I-LE----------------------------NED-------------IKLDWMFRYSliHDIVKGMHYlh 120
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 769 ---------LASKNCIhrdVAARNVLltnghvaKIGDFGLAR------DIMNDSNYIVKgnaRLpvkWMAPESIFDCVY- 832
Cdd:cd14042  121 dseikshgnLKSSNCV---VDSRFVL-------KITDFGLHSfrsgqePPDDSHAYYAK---LL---WTAPELLRDPNPp 184
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 833 ---TVQSDVWSYGILLWEIFS---------LGLNPyPGILVnskfyKLVKDGYQmaqPAF--------APKNIYSIMQAC 892
Cdd:cd14042  185 ppgTQKGDVYSFGIILQEIATrqgpfyeegPDLSP-KEIIK-----KKVRNGEK---PPFrpsldeleCPDEVLSLMQRC 255
                        330
                 ....*....|....*...
gi 569026720 893 WALEPTHRPTFQQICSFL 910
Cdd:cd14042  256 WAEDPEERPDFSTLRNKL 273
PTKc_Wee1_fungi cd14052
Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the ...
586-848 3.24e-14

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: 74.00  E-value: 3.24e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 586 KTLGAGAFGKVVEATAfglgKEDAVLKVAVKMLK-STAHADEKEALMSELKIMSHLGQ--HENIVNLLGACTHGGPVLVI 662
Cdd:cd14052    6 ELIGSGEFSQVYKVSE----RVPTGKVYAVKKLKpNYAGAKDRLRRLEEVSILRELTLdgHDNIVQLIDSWEYHGHLYIQ 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 663 TEYCCYGDLlnflrrkaeamlgpslspgqdpeggvdyknihlekkyvrrdsgfssqgvdtyvemrpvstssnDSFSEQDL 742
Cdd:cd14052   82 TELCENGSL---------------------------------------------------------------DVFLSELG 98
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 743 DKEDGRPLELRDLLhfsSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLA--------RDIMNDSNYIvkgn 814
Cdd:cd14052   99 LLGRLDEFRVWKIL---VELSLGLRFIHDHHFVHLDLKPANVLITFEGTLKIGDFGMAtvwplirgIEREGDREYI---- 171
                        250       260       270
                 ....*....|....*....|....*....|....
gi 569026720 815 arlpvkwmAPESIFDCVYTVQSDVWSYGILLWEI 848
Cdd:cd14052  172 --------APEILSEHMYDKPADIFSLGLILLEA 197
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
583-907 3.36e-14

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: 74.11  E-value: 3.36e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 583 QFGKTLGAGAFGKVVEATAFGLGKedavlKVAVKMLKSTAHADEKEALMSELKIMSHLGQHENIVNLlgacthggpvlvi 662
Cdd:cd07830    2 KVIKQLGDGTFGSVYLARNKETGE-----LVAIKKMKKKFYSWEECMNLREVKSLRKLNEHPNIVKL------------- 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 663 teyccygdllnflrrkaeamlgpslspgqdpeggvdyKNIHLEKKYVrrdsgfssqgvdtYVEMRPVstssndsfsEQDL 742
Cdd:cd07830   64 -------------------------------------KEVFRENDEL-------------YFVFEYM---------EGNL 84
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 743 ----DKEDGRPLELRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDIMNDSNYIVKGNARlp 818
Cdd:cd07830   85 yqlmKDRKGKPFSESVIRSIIYQILQGLAHIHKHGFFHRDLKPENLLVSGPEVVKIADFGLAREIRSRPPYTDYVSTR-- 162
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 819 vkWM-APESIFDC-VYTVQSDVWSYGILLWEIFSlgLNP-YPGilvNS---KFYKLVK-----------DGYQMAQ---- 877
Cdd:cd07830  163 --WYrAPEILLRStSYSSPVDIWALGCIMAELYT--LRPlFPG---SSeidQLYKICSvlgtptkqdwpEGYKLASklgf 235
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 569026720 878 --PAFAPKNIYSI-----------MQACWALEPTHRPTFQQIC 907
Cdd:cd07830  236 rfPQFAPTSLHQLipnaspeaidlIKDMLRWDPKKRPTASQAL 278
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
588-906 4.44e-14

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: 73.48  E-value: 4.44e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 588 LGAGAFGKVVEATafglGKEDAVLkVAVKMLKSTAHADEKEALMSELKIMSHLgQHENIVNLLGACTHGGPVLVITEYCC 667
Cdd:cd13996   14 LGSGGFGSVYKVR----NKVDGVT-YAIKKIRLTEKSSASEKVLREVKALAKL-NHPNIVRYYTAWVEEPPLYIQMELCE 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 668 YGDLlnflrrkaeamlgpslspgqdpeggvdyknihlekkyvrrdsgfssqgvdtyvemrpvstssndsfsEQDLDKEDG 747
Cdd:cd13996   88 GGTL-------------------------------------------------------------------RDWIDRRNS 100
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 748 RPLELRDL-LHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNG-HVAKIGDFGLARDI-------MNDSNYIVKGNARLP 818
Cdd:cd13996  101 SSKNDRKLaLELFKQILKGVSYIHSKGIVHRDLKPSNIFLDNDdLQVKIGDFGLATSIgnqkrelNNLNNNNNGNTSNNS 180
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 819 VK-----WMAPESIFDCVYTVQSDVWSYGILLWEIFSlglnPYPGILVNSKFYKLVKDG----YQMAQpafaPKNIYSIM 889
Cdd:cd13996  181 VGigtplYASPEQLDGENYNEKADIYSLGIILFEMLH----PFKTAMERSTILTDLRNGilpeSFKAK----HPKEADLI 252
                        330
                 ....*....|....*..
gi 569026720 890 QACWALEPTHRPTFQQI 906
Cdd:cd13996  253 QSLLSKNPEERPSAEQL 269
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
585-845 5.44e-14

Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Chk1 is implicated in many major checkpoints of the cell cycle, providing a link between upstream sensors and the cell cycle engine. It plays an important role in DNA damage response and maintaining genomic stability. Chk1 acts as an effector of the sensor kinase, ATR (ATM and Rad3-related), a member of the PI3K family, which is activated upon DNA replication stress. Chk1 delays mitotic entry in response to replication blocks by inhibiting cyclin dependent kinase (Cdk) activity. In addition, Chk1 contributes to the function of centrosome and spindle-based checkpoints, inhibits firing of origins of DNA replication (Ori), and represses transcription of cell cycle proteins including cyclin B and Cdk1. The Chk1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270971 [Multi-domain]  Cd Length: 261  Bit Score: 73.13  E-value: 5.44e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 585 GKTLGAGAFGKVveataFGLGKEDAVLKVAVKML-KSTAHADEKEALMSELKIMSHLgQHENIVNLLGACTHGGPVLVIT 663
Cdd:cd14069    6 VQTLGEGAFGEV-----FLAVNRNTEEAVAVKFVdMKRAPGDCPENIKKEVCIQKML-SHKNVVRFYGHRREGEFQYLFL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 664 EYCCYGDLLNFLrrkaeamlgpslspgqDPEGGVDYKNIHLekkyvrrdsgfssqgvdtyvemrpvstssndsfseqdld 743
Cdd:cd14069   80 EYASGGELFDKI----------------EPDVGMPEDVAQF--------------------------------------- 104
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 744 kedgrplelrdllhFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLArdimndSNYIVKGNARLPVK--- 820
Cdd:cd14069  105 --------------YFQQLMAGLKYLHSCGITHRDIKPENLLLDENDNLKISDFGLA------TVFRYKGKERLLNKmcg 164
                        250       260
                 ....*....|....*....|....*....
gi 569026720 821 ---WMAPESIFDCVYTVQ-SDVWSYGILL 845
Cdd:cd14069  165 tlpYVAPELLAKKKYRAEpVDVWSCGIVL 193
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
744-912 8.68e-14

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: 72.30  E-value: 8.68e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 744 KEDGRPLELRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARdIMNDSNYIVKGNARLPVkWMA 823
Cdd:cd08224   95 KKQKRLIPERTIWKYFVQLCSALEHMHSKRIMHRDIKPANVFITANGVVKLGDLGLGR-FFSSKTTAAHSLVGTPY-YMS 172
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 824 PESIFDCVYTVQSDVWSYGILLWEIFSLGlNPYPGILVNskFYKLVKDGYQMAQPAFaPKNIYS-----IMQACWALEPT 898
Cdd:cd08224  173 PERIREQGYDFKSDIWSLGCLLYEMAALQ-SPFYGEKMN--LYSLCKKIEKCEYPPL-PADLYSqelrdLVAACIQPDPE 248
                        170
                 ....*....|....
gi 569026720 899 HRPTFQQICSFLQE 912
Cdd:cd08224  249 KRPDISYVLDVAKR 262
STKc_PLK4 cd14186
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the ...
744-906 1.03e-13

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: 72.20  E-value: 1.03e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 744 KEDGRPLELRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDIM--NDSNYIVKGNArlpvKW 821
Cdd:cd14186   93 KNRKKPFTEDEARHFMHQIVTGMLYLHSHGILHRDLTLSNLLLTRNMNIKIADFGLATQLKmpHEKHFTMCGTP----NY 168
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 822 MAPESIFDCVYTVQSDVWSYGILLWeIFSLGLNPYPGILVNSKFYKLVKDGYQMaqPAFAPKNIYSIMQACWALEPTHRP 901
Cdd:cd14186  169 ISPEIATRSAHGLESDVWSLGCMFY-TLLVGRPPFDTDTVKNTLNKVVLADYEM--PAFLSREAQDLIHQLLRKNPADRL 245

                 ....*
gi 569026720 902 TFQQI 906
Cdd:cd14186  246 SLSSV 250
STKc_KSR1 cd14152
Catalytic domain of the Serine/Threonine Kinase, Kinase Suppressor of Ras 1; STKs catalyze the ...
582-919 1.43e-13

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


Pssm-ID: 271054 [Multi-domain]  Cd Length: 279  Bit Score: 72.31  E-value: 1.43e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 582 LQFGKTLGAGAFGKVVEATAFGlgkedavlKVAVKMLKSTAHADEKEALMSELKIMSHLGQHENIVNLLGACTHGGPVLV 661
Cdd:cd14152    2 IELGELIGQGRWGKVHRGRWHG--------EVAIRLLEIDGNNQDHLKLFKKEVMNYRQTRHENVVLFMGACMHPPHLAI 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 662 ITEYCCYGDLLNFLRrkaeamlgpslspgqDPEGGVDYKNIHlekkyvrrdsgfssqgvdtyvemrpvstssndsfseqd 741
Cdd:cd14152   74 ITSFCKGRTLYSFVR---------------DPKTSLDINKTR-------------------------------------- 100
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 742 ldkedgrplelrdllHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAkIGDFGLardiMNDSNYIVKG----NARL 817
Cdd:cd14152  101 ---------------QIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDNGKVV-ITDFGL----FGISGVVQEGrrenELKL 160
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 818 PVKW---MAPESIF--------DCV-YTVQSDVWSYGILLWEifsLGLNPYPgiLVNSKFYKLV---KDGYQMAQ---PA 879
Cdd:cd14152  161 PHDWlcyLAPEIVRemtpgkdeDCLpFSKAADVYAFGTIWYE---LQARDWP--LKNQPAEALIwqiGSGEGMKQvltTI 235
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 569026720 880 FAPKNIYSIMQACWALEPTHRPTFQQICSFLQEQAQEDRR 919
Cdd:cd14152  236 SLGKEVTEILSACWAFDLEERPSFTLLMDMLEKLPKLNRR 275
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
586-849 1.47e-13

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: 72.94  E-value: 1.47e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 586 KTLGAGAFGKVVEATafglgkeDAVL--KVAVKML-KSTAHA-DEKEALmSELKIMSHLgQHENIVNLLgacthggpvlv 661
Cdd:cd07834    6 KPIGSGAYGVVCSAY-------DKRTgrKVAIKKIsNVFDDLiDAKRIL-REIKILRHL-KHENIIGLL----------- 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 662 iteyccygdllNFLRrkaeamlgpslspgqdPEGGVDYKnihlekkyvrrdsgfssqgvDTYVEMrpvstssndSFSEQD 741
Cdd:cd07834   66 -----------DILR----------------PPSPEEFN--------------------DVYIVT---------ELMETD 89
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 742 LDK--EDGRPLELRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLL-TNGHVaKIGDFGLARDIMNDSN------YIVk 812
Cdd:cd07834   90 LHKviKSPQPLTDDHIQYFLYQILRGLKYLHSAGVIHRDLKPSNILVnSNCDL-KICDFGLARGVDPDEDkgflteYVV- 167
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 569026720 813 gnarlpVKWM-APESIFDCV-YTVQSDVWSYGILLWEIF 849
Cdd:cd07834  168 ------TRWYrAPELLLSSKkYTKAIDIWSVGCIFAELL 200
PTK_Jak3_rpt1 cd14208
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 3; Jak3 is ...
582-906 1.62e-13

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: 71.47  E-value: 1.62e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 582 LQFGKTLGAGAFGKVVEATAFGLGKEDAV-LKVAVKMLKSTaHADEKEALMSELKIMSHLgQHENIVNLLGACThGGPVL 660
Cdd:cd14208    1 LTFMESLGKGSFTKIYRGLRTDEEDDERCeTEVLLKVMDPT-HGNCQESFLEAASIMSQI-SHKHLVLLHGVCV-GKDSI 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 661 VITEYCCYGDLLNFLRRkaeamlgpslspgQDPEGgvdyknihlekkyvrrdsgfssqgvdtyvemrPVSTSSNdsfseq 740
Cdd:cd14208   78 MVQEFVCHGALDLYLKK-------------QQQKG--------------------------------PVAISWK------ 106
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 741 dldkedgrplelrdlLHFSSQVAQGMAFLASKNCIHRDVAARNVLLT------NGHVAKIGDFGLARDIMnDSNYIVKgn 814
Cdd:cd14208  107 ---------------LQVVKQLAYALNYLEDKQLVHGNVSAKKVLLSregdkgSPPFIKLSDPGVSIKVL-DEELLAE-- 168
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 815 aRLPvkWMAPESIFDC-VYTVQSDVWSYGILLWEIFSLGLNPYpGILVNSKFYKLVKDGYQMAQPAFApkNIYSIMQACW 893
Cdd:cd14208  169 -RIP--WVAPECLSDPqNLALEADKWGFGATLWEIFSGGHMPL-SALDPSKKLQFYNDRKQLPAPHWI--ELASLIQQCM 242
                        330
                 ....*....|...
gi 569026720 894 ALEPTHRPTFQQI 906
Cdd:cd14208  243 SYNPLLRPSFRAI 255
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
761-859 1.86e-13

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: 71.53  E-value: 1.86e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 761 QVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLA---RDIMNDSNYIVkGNarlPVkWMAPESIFDCVYTVQSD 837
Cdd:cd06612  107 QTLKGLEYLHSNKKIHRDIKAGNILLNEEGQAKLADFGVSgqlTDTMAKRNTVI-GT---PF-WMAPEVIQEIGYNNKAD 181
                         90       100
                 ....*....|....*....|..
gi 569026720 838 VWSYGILLWEIFSlGLNPYPGI 859
Cdd:cd06612  182 IWSLGITAIEMAE-GKPPYSDI 202
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
585-848 2.05e-13

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: 71.31  E-value: 2.05e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 585 GKTLGAGAFGKVveatAFGL---GKEDAVLKVAVKMLKSTAHADEKEALMSELKIMSHLgQHENIVNLLGACTHGGPVLV 661
Cdd:cd06631    6 GNVLGKGAYGTV----YCGLtstGQLIAVKQVELDTSDKEKAEKEYEKLQEEVDLLKTL-KHVNIVGYLGTCLEDNVVSI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 662 ITEYCCYGDLLNFLRRkaeamLGPslspgqdpeggvdyknihLEKKYVRRdsgfssqgvdtyvemrpvstssndsfseqd 741
Cdd:cd06631   81 FMEFVPGGSIASILAR-----FGA------------------LEEPVFCR------------------------------ 107
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 742 ldkedgrplelrdllhFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDIMNDSNYIVKGNARLPVK- 820
Cdd:cd06631  108 ----------------YTKQILEGVAYLHNNNVIHRDIKGNNIMLMPNGVIKLIDFGCAKRLCINLSSGSQSQLLKSMRg 171
                        250       260       270
                 ....*....|....*....|....*....|.
gi 569026720 821 ---WMAPESIFDCVYTVQSDVWSYGILLWEI 848
Cdd:cd06631  172 tpyWMAPEVINETGHGRKSDIWSIGCTVFEM 202
STKc_MLCK cd14103
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the ...
588-858 2.60e-13

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: 70.72  E-value: 2.60e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 588 LGAGAFGKVVEATAFGLGKEdavlkVAVKMLKsTAHADEKEALMSELKIMSHLgQHENIVNLLGACTHGGPVLVITEYCC 667
Cdd:cd14103    1 LGRGKFGTVYRCVEKATGKE-----LAAKFIK-CRKAKDREDVRNEIEIMNQL-RHPRLLQLYDAFETPREMVLVMEYVA 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 668 YGDLLnflrrkaeamlgpslspgqdpEGGVDyknihlekkyvrrdsgfssqgvDTYVemrpvstssndsfseqdldkedg 747
Cdd:cd14103   74 GGELF---------------------ERVVD----------------------DDFE----------------------- 87
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 748 rpLELRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTN--GHVAKIGDFGLARDImnDSNYIVKGNARLPvKWMAPE 825
Cdd:cd14103   88 --LTERDCILFMRQICEGVQYMHKQGILHLDLKPENILCVSrtGNQIKIIDFGLARKY--DPDKKLKVLFGTP-EFVAPE 162
                        250       260       270
                 ....*....|....*....|....*....|....
gi 569026720 826 SI-FDCVyTVQSDVWSYGILLWEIFSlGLNPYPG 858
Cdd:cd14103  163 VVnYEPI-SYATDMWSVGVICYVLLS-GLSPFMG 194
STKc_MST3 cd06641
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs ...
742-906 2.87e-13

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: 71.26  E-value: 2.87e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 742 LDKEDGRPLELRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDIMNDSnyiVKGNARLPVK- 820
Cdd:cd06641   90 LDLLEPGPLDETQIATILREILKGLDYLHSEKKIHRDIKAANVLLSEHGEVKLADFGVAGQLTDTQ---IKRN*FVGTPf 166
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 821 WMAPESIFDCVYTVQSDVWSYGILLWEIfSLGLNPYPGILVNSKFYKLVKDGYQMAQPAFApKNIYSIMQACWALEPTHR 900
Cdd:cd06641  167 WMAPEVIKQSAYDSKADIWSLGITAIEL-ARGEPPHSELHPMKVLFLIPKNNPPTLEGNYS-KPLKEFVEACLNKEPSFR 244

                 ....*.
gi 569026720 901 PTFQQI 906
Cdd:cd06641  245 PTAKEL 250
STKc_MAP4K3_like cd06613
Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like ...
588-902 3.78e-13

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: 70.41  E-value: 3.78e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 588 LGAGAFGKVVEATAFGLGKedavlKVAVKMLKSTAhADEKEALMSELKIMSHLgQHENIVNLLGACTHGGPVLVITEYCc 667
Cdd:cd06613    8 IGSGTYGDVYKARNIATGE-----LAAVKVIKLEP-GDDFEIIQQEISMLKEC-RHPNIVAYFGSYLRRDKLWIVMEYC- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 668 ygdllnflrrkaeamlgpslspgqdpEGGvdyknihlekkyvrrdsgfssqgvdtyvemrpvstssndsfSEQDLDKEDG 747
Cdd:cd06613   80 --------------------------GGG-----------------------------------------SLQDIYQVTG 92
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 748 rPLELRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLT-NGHVaKIGDFGLARDImndSNYIVKGNARL--PVkWMAP 824
Cdd:cd06613   93 -PLSELQIAYVCRETLKGLAYLHSTGKIHRDIKGANILLTeDGDV-KLADFGVSAQL---TATIAKRKSFIgtPY-WMAP 166
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 825 ESIfdCV-----YTVQSDVWSYGILLWEIfSLGLNPYPGILVNSKFYKLVKDGYQmaQPAFAPKNIYS-----IMQACWA 894
Cdd:cd06613  167 EVA--AVerkggYDGKCDIWALGITAIEL-AELQPPMFDLHPMRALFLIPKSNFD--PPKLKDKEKWSpdfhdFIKKCLT 241

                 ....*...
gi 569026720 895 LEPTHRPT 902
Cdd:cd06613  242 KNPKKRPT 249
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
580-907 3.91e-13

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase Kinase; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MAPKKs are dual-specificity PKs that phosphorylate their downstream targets, MAPKs, at specific threonine and tyrosine residues. The MAPK signaling pathways are important mediators of cellular responses to extracellular signals. The pathways involve a triple kinase core cascade comprising the MAPK, which is phosphorylated and activated by a MAPK kinase (MAPKK or MKK or MAP2K), which itself is phosphorylated and activated by a MAPKK kinase (MAPKKK or MKKK or MAP3K). There are three MAPK subfamilies: extracellular signal-regulated kinase (ERK), c-Jun N-terminal kinase (JNK), and p38. In mammalian cells, there are seven MAPKKs (named MKK1-7) and 20 MAPKKKs. Each MAPK subfamily can be activated by at least two cognate MAPKKs and by multiple MAPKKKs. The MAPKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270782 [Multi-domain]  Cd Length: 265  Bit Score: 70.45  E-value: 3.91e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 580 NNLQFGKTLGAGAFGKVVEATAFGLGKedavlKVAVKMLKSTAHADEKEALMSELKImSHLGQHENIVNLLGACTHGGPV 659
Cdd:cd06605    1 DDLEYLGELGEGNGGVVSKVRHRPSGQ-----IMAVKVIRLEIDEALQKQILRELDV-LHKCNSPYIVGFYGAFYSEGDI 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 660 LVITEYCCYGDLLNFLRRkaeamlgpslspgqdpeggvdyknihlekkyvrrdsgfssqgvdtyvemrpvstssndsfse 739
Cdd:cd06605   75 SICMEYMDGGSLDKILKE-------------------------------------------------------------- 92
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 740 qdldkedGRPLELRDLLHFSSQVAQGMAFLASK-NCIHRDVAARNVLLTNGHVAKIGDFGLARDIMNDSNYIVKGNArlp 818
Cdd:cd06605   93 -------VGRIPERILGKIAVAVVKGLIYLHEKhKIIHRDVKPSNILVNSRGQVKLCDFGVSGQLVDSLAKTFVGTR--- 162
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 819 vKWMAPESIFDCVYTVQSDVWSYGILLWEIfSLGLNPYPGIlvNSKFYKLVKDgyQMAQ-----PAFAPKNIYS-----I 888
Cdd:cd06605  163 -SYMAPERISGGKYTVKSDIWSLGLSLVEL-ATGRFPYPPP--NAKPSMMIFE--LLSYivdepPPLLPSGKFSpdfqdF 236
                        330
                 ....*....|....*....
gi 569026720 889 MQACWALEPTHRPTFQQIC 907
Cdd:cd06605  237 VSQCLQKDPTERPSYKELM 255
PKc_MKK5 cd06619
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
762-902 4.84e-13

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


Pssm-ID: 132950 [Multi-domain]  Cd Length: 279  Bit Score: 70.68  E-value: 4.84e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 762 VAQGMAFLASKNCIHRDVAARNVLL-TNGHVaKIGDFGLARDIMND-SNYIVKGNArlpvkWMAPESIFDCVYTVQSDVW 839
Cdd:cd06619  104 VVKGLTYLWSLKILHRDVKPSNMLVnTRGQV-KLCDFGVSTQLVNSiAKTYVGTNA-----YMAPERISGEQYGIHSDVW 177
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 569026720 840 SYGILLWEIfSLGLNPYPGILVNSKFY---KLVKDGYQMAQPA-----FAPKNIYSIMQaCWALEPTHRPT 902
Cdd:cd06619  178 SLGISFMEL-ALGRFPYPQIQKNQGSLmplQLLQCIVDEDPPVlpvgqFSEKFVHFITQ-CMRKQPKERPA 246
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
588-900 4.87e-13

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: 69.85  E-value: 4.87e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 588 LGAGAFGKVVEATAFGLGKedavlKVAVKMLKSTAHADEKEAL--MSELKIMSHLgQHENIVNLLGACTHGGPVLVITEY 665
Cdd:cd05123    1 LGKGSFGKVLLVRKKDTGK-----LYAMKVLRKKEIIKRKEVEhtLNERNILERV-NHPFIVKLHYAFQTEEKLYLVLDY 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 666 CCYGDLLNFLRRKAeamlgpslspgqdpeggvdyknihlekkyvrrdsgfssqgvdtyvemrpvstssndSFSEQDLdke 745
Cdd:cd05123   75 VPGGELFSHLSKEG--------------------------------------------------------RFPEERA--- 95
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 746 dgrplelrdlLHFSSQVAQGMAFLASKNCIHRDVAARNVLLT-NGHVaKIGDFGLARDIMNDSNYIVK--GNArlpvKWM 822
Cdd:cd05123   96 ----------RFYAAEIVLALEYLHSLGIIYRDLKPENILLDsDGHI-KLTDFGLAKELSSDGDRTYTfcGTP----EYL 160
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 569026720 823 APESIFDCVYTVQSDVWSYGILLWEIFSlGLNPYPGILVNSKFYKLVKDGYQMaqPAFAPKNIYSIMQACWALEPTHR 900
Cdd:cd05123  161 APEVLLGKGYGKAVDWWSLGVLLYEMLT-GKPPFYAENRKEIYEKILKSPLKF--PEYVSPEAKSLISGLLQKDPTKR 235
STKc_TAO2 cd06634
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze ...
738-902 6.18e-13

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


Pssm-ID: 270804 [Multi-domain]  Cd Length: 308  Bit Score: 70.82  E-value: 6.18e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 738 SEQDLDKEDGRPLELRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLArDIMNDSNYIVKgnarL 817
Cdd:cd06634  100 SASDLLEVHKKPLQEVEIAAITHGALQGLAYLHSHNMIHRDVKAGNILLTEPGLVKLGDFGSA-SIMAPANSFVG----T 174
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 818 PVkWMAPESIF---DCVYTVQSDVWSYGILLWEifsLGLNPYPGILVN--SKFYKLVKDGYQMAQPAFAPKNIYSIMQAC 892
Cdd:cd06634  175 PY-WMAPEVILamdEGQYDGKVDVWSLGITCIE---LAERKPPLFNMNamSALYHIAQNESPALQSGHWSEYFRNFVDSC 250
                        170
                 ....*....|
gi 569026720 893 WALEPTHRPT 902
Cdd:cd06634  251 LQKIPQDRPT 260
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
581-850 6.55e-13

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


Pssm-ID: 270795 [Multi-domain]  Cd Length: 260  Bit Score: 69.69  E-value: 6.55e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 581 NLQFGKTLGAGAFGKVVEATAFGLGKEDAVLKVAVKMLKSTAhADEKEALMSELKIMSHLgQHENIVNLLGACTHGGPVL 660
Cdd:cd06625    1 NWKQGKLLGQGAFGQVYLCYDADTGRELAVKQVEIDPINTEA-SKEVKALECEIQLLKNL-QHERIVQYYGCLQDEKSLS 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 661 VITEYCCYGDLLNFLrrKAEAMLGPSLSpgqdpeggvdyknihleKKYVRrdsgfssqgvdtyvemrpvstssndsfseq 740
Cdd:cd06625   79 IFMEYMPGGSVKDEI--KAYGALTENVT-----------------RKYTR------------------------------ 109
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 741 dldkedgrplelrdllhfssQVAQGMAFLASKNCIHRDVAARNVLL-TNGHVaKIGDFGLARDIMNdsnyIVKGNARLPV 819
Cdd:cd06625  110 --------------------QILEGLAYLHSNMIVHRDIKGANILRdSNGNV-KLGDFGASKRLQT----ICSSTGMKSV 164
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 569026720 820 K----WMAPESIFDCVYTVQSDVWSYGILLWEIFS 850
Cdd:cd06625  165 TgtpyWMSPEVINGEGYGRKADIWSVGCTVVEMLT 199
STKc_ULK2 cd14201
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the ...
575-856 7.32e-13

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: 70.04  E-value: 7.32e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 575 WEFPRNNLqfgktLGAGAFGKVVEatafGLGKEDAVLKVAVKMLKSTAHADEKEALMSELKIMSHLgQHENIVNLLGACT 654
Cdd:cd14201    6 FEYSRKDL-----VGHGAFAVVFK----GRHRKKTDWEVAIKSINKKNLSKSQILLGKEIKILKEL-QHENIVALYDVQE 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 655 HGGPVLVITEYCCYGDLLNFLRRKAeamlgpslspgqdpeggvdyknihlekkyvrrdsgfssqgvdtyvemrpvsTSSN 734
Cdd:cd14201   76 MPNSVFLVMEYCNGGDLADYLQAKG---------------------------------------------------TLSE 104
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 735 DSfseqdldkedgrpleLRDLLHfssQVAQGMAFLASKNCIHRDVAARNVLLT---------NGHVAKIGDFGLARDImn 805
Cdd:cd14201  105 DT---------------IRVFLQ---QIAAAMRILHSKGIIHRDLKPQNILLSyasrkkssvSGIRIKIADFGFARYL-- 164
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 569026720 806 DSNYIVKGNARLPVkWMAPESIFDCVYTVQSDVWSYGILLWEIFsLGLNPY 856
Cdd:cd14201  165 QSNMMAATLCGSPM-YMAPEVIMSQHYDAKADLWSIGTVIYQCL-VGKPPF 213
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
207-293 8.68e-13

Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of proteins of different functions. Examples include antibodies, the giant muscle kinase titin and receptor tyrosine kinases. Immunoglobulin-like domains may be involved in protein-protein and protein-ligand interactions.


Pssm-ID: 395002  Cd Length: 86  Bit Score: 64.91  E-value: 8.68e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720  207 LVPAELVRIRGEAAQIVCSASSVDVNFDVFLQHNNTKLAIPQQsDFHNNRYQKVLTLNLDQVDFQHAGNYSCVASNVQGK 286
Cdd:pfam00047   1 SAPPTVTVLEGDSATLTCSASTGSPGPDVTWSKEGGTLIESLK-VKHDNGRTTQSSLLISNVTKEDAGTYTCVVNNPGGS 79

                  ....*..
gi 569026720  287 HSTSMFF 293
Cdd:pfam00047  80 ATLSTSL 86
STKc_ULK1_2-like cd14120
Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar ...
588-847 1.31e-12

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: 68.93  E-value: 1.31e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 588 LGAGAFGKVVEatafGLGKEDAVLKVAVKMLKSTAHADEKEALMSELKIMSHLgQHENIVNLLGACTHGGPVLVITEYCC 667
Cdd:cd14120    1 IGHGAFAVVFK----GRHRKKPDLPVAIKCITKKNLSKSQNLLGKEIKILKEL-SHENVVALLDCQETSSSVYLVMEYCN 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 668 YGDLLNFLRRKAeamlgpslspgqdpeggvdyknihlekkyvrrdsgfssqgvdtyvemrpvsTSSNDSFSeqdldkedg 747
Cdd:cd14120   76 GGDLADYLQAKG---------------------------------------------------TLSEDTIR--------- 95
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 748 rplelrdllHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGH---------VAKIGDFGLAR----DIMndsnyivkgN 814
Cdd:cd14120   96 ---------VFLQQIAAAMKALHSKGIVHRDLKPQNILLSHNSgrkpspndiRLKIADFGFARflqdGMM---------A 157
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 569026720 815 ARL---PVkWMAPESIFDCVYTVQSDVWSYGILLWE 847
Cdd:cd14120  158 ATLcgsPM-YMAPEVIMSLQYDAKADLWSIGTIVYQ 192
PK_SCY1_like cd14011
Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein ...
761-906 2.06e-12

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: 68.89  E-value: 2.06e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 761 QVAQGMAFL-ASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDIMN---DSNYIVKGNARLPV------KWMAPESIFDC 830
Cdd:cd14011  122 QISEALSFLhNDVKLVHGNICPESVVINSNGEWKLAGFDFCISSEQatdQFPYFREYDPNLPPlaqpnlNYLAPEYILSK 201
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 569026720 831 VYTVQSDVWSYGILLWEIFSLGLNPYPGILVNSKFYKLVKDGYQMAQPAFA--PKNIYSIMQACWALEPTHRPTFQQI 906
Cdd:cd14011  202 TCDPASDMFSLGVLIYAIYNKGKPLFDCVNNLLSYKKNSNQLRQLSLSLLEkvPEELRDHVKTLLNVTPEVRPDAEQL 279
STKc_TAO cd06607
Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs ...
748-843 2.32e-12

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: 68.25  E-value: 2.32e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 748 RPLELRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLArDIMNDSNYIVKgnarLPVkWMAPESI 827
Cdd:cd06607   96 KPLQEVEIAAICHGALQGLAYLHSHNRIHRDVKAGNILLTEPGTVKLADFGSA-SLVCPANSFVG----TPY-WMAPEVI 169
                         90
                 ....*....|....*....
gi 569026720 828 F---DCVYTVQSDVWSYGI 843
Cdd:cd06607  170 LamdEGQYDGKVDVWSLGI 188
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
749-919 2.40e-12

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: 68.55  E-value: 2.40e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 749 PLELRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDIMNDSnyiVKGNARLPVK-WMAPESI 827
Cdd:cd06642   97 PLEETYIATILREILKGLDYLHSERKIHRDIKAANVLLSEQGDVKLADFGVAGQLTDTQ---IKRNTFVGTPfWMAPEVI 173
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 828 FDCVYTVQSDVWSYGILLWEIfSLGLNPYPGILVNSKFYKLVKDGYQMAQPAFApKNIYSIMQACWALEPTHRPTFQQI- 906
Cdd:cd06642  174 KQSAYDFKADIWSLGITAIEL-AKGEPPNSDLHPMRVLFLIPKNSPPTLEGQHS-KPFKEFVEACLNKDPRFRPTAKELl 251
                        170       180
                 ....*....|....*....|....
gi 569026720 907 -----------CSFLQEQAQEDRR 919
Cdd:cd06642  252 khkfitrytkkTSFLTELIDRYKR 275
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
588-856 2.55e-12

Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of MST3, MST4, STK25, Schizosaccharomyces pombe Nak1 and Sid1, Saccharomyces cerevisiae sporulation-specific protein 1 (SPS1), and related proteins. Nak1 is required by fission yeast for polarizing the tips of actin cytoskeleton and is involved in cell growth, cell separation, cell morphology and cell-cycle progression. Sid1 is a component in the septation initiation network (SIN) signaling pathway, and plays a role in cytokinesis. SPS1 plays a role in regulating proteins required for spore wall formation. MST4 plays a role in mitogen-activated protein kinase (MAPK) signaling during cytoskeletal rearrangement, morphogenesis, and apoptosis. MST3 phosphorylates the STK NDR and may play a role in cell cycle progression and cell morphology. STK25 may play a role in the regulation of cell migration and polarization. The MST3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270786 [Multi-domain]  Cd Length: 274  Bit Score: 68.43  E-value: 2.55e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 588 LGAGAFGKVVEATAFGLGKEdavlkVAVKMLKSTAHADEKEALMSELKIMSHLgQHENIVNLLGACTHGGPVLVITEYCC 667
Cdd:cd06609    9 IGKGSFGEVYKGIDKRTNQV-----VAIKVIDLEEAEDEIEDIQQEIQFLSQC-DSPYITKYYGSFLKGSKLWIIMEYCG 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 668 YGDLLNFLRrkaeamlgpslsPGQDPEGGVDYknIhlekkyvrrdsgfssqgvdtyvemrpvstssndsfseqdldkedg 747
Cdd:cd06609   83 GGSVLDLLK------------PGPLDETYIAF--I--------------------------------------------- 103
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 748 rpleLRDLLHfssqvaqGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLA---RDIMNDSNYIVkGNarlPVkWMAP 824
Cdd:cd06609  104 ----LREVLL-------GLEYLHSEGKIHRDIKAANILLSEEGDVKLADFGVSgqlTSTMSKRNTFV-GT---PF-WMAP 167
                        250       260       270
                 ....*....|....*....|....*....|..
gi 569026720 825 ESIFDCVYTVQSDVWSYGILLWEIFSlGLNPY 856
Cdd:cd06609  168 EVIKQSGYDEKADIWSLGITAIELAK-GEPPL 198
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
744-906 3.25e-12

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: 68.22  E-value: 3.25e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 744 KEDGRPLElRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDIMNDSNYIVKGNARlpvkWMA 823
Cdd:cd06621   97 KKGGRIGE-KVLGKIAESVLKGLSYLHSRKIIHRDIKPSNILLTRKGQVKLCDFGVSGELVNSLAGTFTGTSY----YMA 171
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 824 PESIFDCVYTVQSDVWSYGILLWEIfSLGLNPYP-------------GILVNSKFYKLVKDgyqMAQPAFAPKNIYSIMQ 890
Cdd:cd06621  172 PERIQGGPYSITSDVWSLGLTLLEV-AQNRFPFPpegepplgpiellSYIVNMPNPELKDE---PENGIKWSESFKDFIE 247
                        170
                 ....*....|....*.
gi 569026720 891 ACWALEPTHRPTFQQI 906
Cdd:cd06621  248 KCLEKDGTRRPGPWQM 263
STKc_ACVR2 cd14053
Catalytic domain of the Serine/Threonine Kinase, Activin Type II Receptor; STKs catalyze the ...
591-850 3.25e-12

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: 68.12  E-value: 3.25e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 591 GAFGKVVEATafgLGKEDavlkVAVKMLKSTahadEKEALMSELKIMSHLG-QHENIVNLLGACTHGGPVLV----ITEY 665
Cdd:cd14053    6 GRFGAVWKAQ---YLNRL----VAVKIFPLQ----EKQSWLTEREIYSLPGmKHENILQFIGAEKHGESLEAeywlITEF 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 666 CCYGDLLNFLRrkaeamlgpslspgqdpeggvdyknihlekkyvrrdsgfssqgvdtyvemrpvstssndsfseqdldke 745
Cdd:cd14053   75 HERGSLCDYLK--------------------------------------------------------------------- 85
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 746 dGRPLELRDLLHFSSQVAQGMAFL---------ASKNCI-HRDVAARNVLLTNGHVAKIGDFGLARDIMNDsnyIVKGNA 815
Cdd:cd14053   86 -GNVISWNELCKIAESMARGLAYLhedipatngGHKPSIaHRDFKSKNVLLKSDLTACIADFGLALKFEPG---KSCGDT 161
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 569026720 816 RLPV---KWMAPESI----------FDCVytvqsDVWSYGILLWEIFS 850
Cdd:cd14053  162 HGQVgtrRYMAPEVLegainftrdaFLRI-----DMYAMGLVLWELLS 204
STKc_Nek11 cd08222
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
586-906 4.76e-12

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: 67.06  E-value: 4.76e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 586 KTLGAGAFGKV--VEATAFGLGKEDAVLK-VAVKMLKStahaDEKEALMSELKIMSHLgQHENIVNLLGACTHGGPVLVI 662
Cdd:cd08222    6 RKLGSGNFGTVylVSDLKATADEELKVLKeISVGELQP----DETVDANREAKLLSKL-DHPAIVKFHDSFVEKESFCIV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 663 TEYCCYGDLlnflrrkaeamlgpslspgqdpeggvDYKnihlekkyvrrdsgfssqgVDTYvemrpvstssndsfseqdl 742
Cdd:cd08222   81 TEYCEGGDL--------------------------DDK-------------------ISEY------------------- 96
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 743 dKEDGRPLELRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGhVAKIGDFGLARDIMNDSNyIVKGNARLPVkWM 822
Cdd:cd08222   97 -KKSGTTIDENQILDWFIQLLLAVQYMHERRILHRDLKAKNIFLKNN-VIKVGDFGISRILMGTSD-LATTFTGTPY-YM 172
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 823 APESIFDCVYTVQSDVWSYGILLWEIFSLGlNPYPGILVNSKFYKLVkDGYQMAQPAFAPKNIYSIMQACWALEPTHRPT 902
Cdd:cd08222  173 SPEVLKHEGYNSKSDIWSLGCILYEMCCLK-HAFDGQNLLSVMYKIV-EGETPSLPDKYSKELNAIYSRMLNKDPALRPS 250

                 ....
gi 569026720 903 FQQI 906
Cdd:cd08222  251 AAEI 254
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
588-858 5.19e-12

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: 66.91  E-value: 5.19e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 588 LGAGAFGKVVEATAFGLGKEdavlkVAVKMLKStaHADEKEALMSELKIMSHLgQHENIVNLLGACTHGGPVLVITEYCC 667
Cdd:cd14006    1 LGRGRFGVVKRCIEKATGRE-----FAAKFIPK--RDKKKEAVLREISILNQL-QHPRIIQLHEAYESPTELVLILELCS 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 668 YGDLLNFLRRKAEamlgpslspgqdpeggvdyknihlekkyvrrdsgfssqgvdtyvemrpvstssndsFSEQdldkedg 747
Cdd:cd14006   73 GGELLDRLAERGS--------------------------------------------------------LSEE------- 89
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 748 rplELRDLLHfssQVAQGMAFLASKNCIHRDVAARNVLLTNGHVA--KIGDFGLARDImNDSNYIV--KGNArlpvKWMA 823
Cdd:cd14006   90 ---EVRTYMR---QLLEGLQYLHNHHILHLDLKPENILLADRPSPqiKIIDFGLARKL-NPGEELKeiFGTP----EFVA 158
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 569026720 824 PESIFDCVYTVQSDVWSYGILLWEIFSlGLNPYPG 858
Cdd:cd14006  159 PEIVNGEPVSLATDMWSIGVLTYVLLS-GLSPFLG 192
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
581-914 5.27e-12

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: 67.36  E-value: 5.27e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 581 NLQFGKTLGAGAFGKVVEATAFGLGKEdavlkVAVKMLKSTAHADEKEAlMSELKIMSHLGQHENIVNLLGACTHGGP-- 658
Cdd:cd13985    1 RYQVTKQLGEGGFSYVYLAHDVNTGRR-----YALKRMYFNDEEQLRVA-IKEIEIMKRLCGHPNIVQYYDSAILSSEgr 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 659 --VLVITEYCcygdllnflrrkaeamlGPSLspgqdpeggVDYknihLEKKYvrrdsgfssqgvdtyvemrpvstssnds 736
Cdd:cd13985   75 keVLLLMEYC-----------------PGSL---------VDI----LEKSP---------------------------- 96
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 737 fseqdldkedGRPLELRDLLHFSSQVAQGMAFLASKN--CIHRDVAARNVLLTNGHVAKIGDFGLA---------RDIMN 805
Cdd:cd13985   97 ----------PSPLSEEEVLRIFYQICQAVGHLHSQSppIIHRDIKIENILFSNTGRFKLCDFGSAttehyplerAEEVN 166
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 806 DSNYIVKGNARLpvKWMAPESIfDcVY-----TVQSDVWSYGILLWEI--FSLGLNPYPGILVNSKFYKLVKDGYQmaqp 878
Cdd:cd13985  167 IIEEEIQKNTTP--MYRAPEMI-D-LYskkpiGEKADIWALGCLLYKLcfFKLPFDESSKLAIVAGKYSIPEQPRY---- 238
                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 569026720 879 afaPKNIYSIMQACWALEPTHRPTFQQICSFLQEQA 914
Cdd:cd13985  239 ---SPELHDLIRHMLTPDPAERPDIFQVINIITKDT 271
STKc_MLCK2 cd14190
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze ...
581-858 5.44e-12

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: 67.25  E-value: 5.44e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 581 NLQFGKTLGAGAFGKVVEATAFGLGkedavLKVAVKMLKsTAHADEKEALMSELKIMSHLgQHENIVNLLGACTHGGPVL 660
Cdd:cd14190    5 SIHSKEVLGGGKFGKVHTCTEKRTG-----LKLAAKVIN-KQNSKDKEMVLLEIQVMNQL-NHRNLIQLYEAIETPNEIV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 661 VITEYCcygdllnflrrkaeamlgpslspgqdpEGGVDYKNIhlekkyvrrdsgfssqgVDtyvemrpvstssndsfseq 740
Cdd:cd14190   78 LFMEYV---------------------------EGGELFERI-----------------VD------------------- 94
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 741 dldkeDGRPLELRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTN--GHVAKIGDFGLARDImnDSNYIVKGNARLP 818
Cdd:cd14190   95 -----EDYHLTEVDAMVFVRQICEGIQFMHQMRVLHLDLKPENILCVNrtGHQVKIIDFGLARRY--NPREKLKVNFGTP 167
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 569026720 819 vKWMAPESI-FDCVyTVQSDVWSYGILLWEIFSlGLNPYPG 858
Cdd:cd14190  168 -EFLSPEVVnYDQV-SFPTDMWSMGVITYMLLS-GLSPFLG 205
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
586-842 5.47e-12

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: 67.53  E-value: 5.47e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 586 KTLGAGAFGKVVEATAFGLGKEDAVLKV-AVKMLKStahadekealmSELKIMSHLgQHENIVNLLGACTHggpvlvite 664
Cdd:cd14137   10 KVIGSGSFGVVYQAKLLETGEVVAIKKVlQDKRYKN-----------RELQIMRRL-KHPNIVKLKYFFYS--------- 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 665 yccygdllnflrrkaeamlgpslspgQDPEGGVDYKNIHLE----------KKYVRRdsgfssqgvdtyvemrpvstssn 734
Cdd:cd14137   69 --------------------------SGEKKDEVYLNLVMEympetlyrviRHYSKN----------------------- 99
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 735 dsfseqdldkedGRPLELRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLL-TNGHVAKIGDFGLARDI-MNDSN--YI 810
Cdd:cd14137  100 ------------KQTIPIIYVKLYSYQLFRGLAYLHSLGICHRDIKPQNLLVdPETGVLKLCDFGSAKRLvPGEPNvsYI 167
                        250       260       270
                 ....*....|....*....|....*....|...
gi 569026720 811 VKGNARlpvkwmAPESIFDCV-YTVQSDVWSYG 842
Cdd:cd14137  168 CSRYYR------APELIFGATdYTTAIDIWSAG 194
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
761-900 5.75e-12

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: 67.11  E-value: 5.75e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 761 QVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLA---------RDIMNDSNYivkgnarlpvkWMAPESIFDCV 831
Cdd:cd06917  109 EVLVALKFIHKDGIIHRDIKAANILVTNTGNVKLCDFGVAaslnqnsskRSTFVGTPY-----------WMAPEVITEGK 177
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 569026720 832 -YTVQSDVWSYGILLWEIfSLGLNPYPGILVNSKFYKLVKdgyqmAQPAFAPKNIYS-----IMQACWALEPTHR 900
Cdd:cd06917  178 yYDTKADIWSLGITTYEM-ATGNPPYSDVDALRAVMLIPK-----SKPPRLEGNGYSpllkeFVAACLDEEPKDR 246
PKc_Mps1 cd14131
Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle ...
742-906 5.92e-12

Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle 1 (also called TTK); Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. TTK/Mps1 is a spindle checkpoint kinase that was first discovered due to its necessity in centrosome duplication in budding yeast. It was later found to function in the spindle assembly checkpoint, which monitors the proper attachment of chromosomes to the mitotic spindle. In yeast, substrates of Mps1 include the spindle pole body components Spc98p, Spc110p, and Spc42p. The TTK/Mps1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271033 [Multi-domain]  Cd Length: 271  Bit Score: 67.24  E-value: 5.92e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 742 LDKEDGRPLELRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVaKIGDFGLARDIMNDSNYIVKGNARLPVKW 821
Cdd:cd14131   92 LKKKRPKPIDPNFIRYYWKQMLEAVHTIHEEGIVHSDLKPANFLLVKGRL-KLIDFGIAKAIQNDTTSIVRDSQVGTLNY 170
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 822 MAPESIFDCVYTVQ----------SDVWSYGILLWEiFSLGLNPYPGI-LVNSKFYKLVKDGYQMAQPAFAPKNIYSIMQ 890
Cdd:cd14131  171 MSPEAIKDTSASGEgkpkskigrpSDVWSLGCILYQ-MVYGKTPFQHItNPIAKLQAIIDPNHEIEFPDIPNPDLIDVMK 249
                        170
                 ....*....|....*.
gi 569026720 891 ACWALEPTHRPTFQQI 906
Cdd:cd14131  250 RCLQRDPKKRPSIPEL 265
STKc_SLK cd06643
Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer ...
588-892 6.76e-12

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: 67.36  E-value: 6.76e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 588 LGAGAFGKVVEATafglGKEDAVLkVAVKMLkSTAHADEKEALMSELKIMSHLgQHENIVNLLGACTHGGPVLVITEYCC 667
Cdd:cd06643   13 LGDGAFGKVYKAQ----NKETGIL-AAAKVI-DTKSEEELEDYMVEIDILASC-DHPNIVKLLDAFYYENNLWILIEFCA 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 668 ygdllnflrrkaeamlgpslspgqdpEGGVDYKNIHLEkkyvrrdsgfssqgvdtyvemRPVSTSSNDSFSEQDLDkedg 747
Cdd:cd06643   86 --------------------------GGAVDAVMLELE---------------------RPLTEPQIRVVCKQTLE---- 114
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 748 rplelrdllhfssqvaqGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLA----RDIMNDSNYIvkGNARlpvkWMA 823
Cdd:cd06643  115 -----------------ALVYLHENKIIHRDLKAGNILFTLDGDIKLADFGVSakntRTLQRRDSFI--GTPY----WMA 171
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 569026720 824 PESIF-----DCVYTVQSDVWSYGILLWEIFSL-----GLNPYPGILVNSKfyklvKDGYQMAQPAFAPKNIYSIMQAC 892
Cdd:cd06643  172 PEVVMcetskDRPYDYKADVWSLGVTLIEMAQIepphhELNPMRVLLKIAK-----SEPPTLAQPSRWSPEFKDFLRKC 245
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
585-848 7.58e-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: 7.58e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 585 GKTLGAGAFGKVVEATAFGLGKEDAVLKVAVKMLKSTAHADEKEALMSELKIMSHLgQHENIVNLLGACTHGGPVLVITE 664
Cdd:cd06630    5 GPLLGTGAFSSCYQARDVKTGTLMAVKQVSFCRNSSSEQEEVVEAIREEIRMMARL-NHPNIVRMLGATQHKSHFNIFVE 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 665 YccygdllnflrrkaeaMLGPSLSpgqdpeggvdykniHLEKKYvrrdsgfssqgvdtyvemrpvstssnDSFSEQDLdk 744
Cdd:cd06630   84 W----------------MAGGSVA--------------SLLSKY--------------------------GAFSENVI-- 105
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 745 edgrplelrdlLHFSSQVAQGMAFLASKNCIHRDVAARNVLL-TNGHVAKIGDFG----LARDIMNDSNYivKGNARLPV 819
Cdd:cd06630  106 -----------INYTLQILRGLAYLHDNQIIHRDLKGANLLVdSTGQRLRIADFGaaarLASKGTGAGEF--QGQLLGTI 172
                        250       260
                 ....*....|....*....|....*....
gi 569026720 820 KWMAPESIFDCVYTVQSDVWSYGILLWEI 848
Cdd:cd06630  173 AFMAPEVLRGEQYGRSCDVWSVGCVIIEM 201
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
742-906 8.94e-12

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 8; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek8 contains an N-terminal kinase catalytic domain and a C-terminal RCC1 (regulator of chromosome condensation) domain. A double point mutation in Nek8 causes cystic kidney disease in mice that genetically resembles human autosomal recessive polycystic kidney disease (ARPKD). Nek8 is also associated with a rare form of juvenile renal cystic disease, nephronophthisis type 9. It has been suggested that a defect in the ciliary localization of Nek8 contributes to the development of cysts manifested by these diseases. Nek8 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270859 [Multi-domain]  Cd Length: 256  Bit Score: 66.29  E-value: 8.94e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 742 LDKEDGRPLELRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGH-VAKIGDFGLARDIMNDSN-YIVKGNarlPV 819
Cdd:cd08220   90 IQQRKGSLLSEEEILHFFVQILLALHHVHSKQILHRDLKTQNILLNKKRtVVKIGDFGISKILSSKSKaYTVVGT---PC 166
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 820 kWMAPESIFDCVYTVQSDVWSYGILLWEIFSL-----GLNpYPGILVnskfyKLVKDGYQMAQPAFAPkNIYSIMQACWA 894
Cdd:cd08220  167 -YISPELCEGKPYNQKSDIWALGCVLYELASLkrafeAAN-LPALVL-----KIMRGTFAPISDRYSE-ELRHLILSMLH 238
                        170
                 ....*....|..
gi 569026720 895 LEPTHRPTFQQI 906
Cdd:cd08220  239 LDPNKRPTLSEI 250
STKc_AMPK_alpha cd14079
Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein ...
581-846 9.00e-12

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: 66.52  E-value: 9.00e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 581 NLQFGKTLGAGAFGKVVEATAFGLGKedavlKVAVKML--KSTAHADEKEALMSELKIMsHLGQHENIVNLLGACTHGGP 658
Cdd:cd14079    3 NYILGKTLGVGSFGKVKLAEHELTGH-----KVAVKILnrQKIKSLDMEEKIRREIQIL-KLFRHPHIIRLYEVIETPTD 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 659 VLVITEYCCYGDLLNFLRRKaeamlgpslspGQDPEggvdyknihlekkyvrrdsgfssqgvdtyVEMRpvstssndsfs 738
Cdd:cd14079   77 IFMVMEYVSGGELFDYIVQK-----------GRLSE-----------------------------DEAR----------- 105
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 739 eqdldkedgrplelrdllHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLArDIMNDSNYIvKGNARLP 818
Cdd:cd14079  106 ------------------RFFQQIISGVEYCHRHMVVHRDLKPENLLLDSNMNVKIADFGLS-NIMRDGEFL-KTSCGSP 165
                        250       260
                 ....*....|....*....|....*....
gi 569026720 819 vKWMAPESIFDCVYT-VQSDVWSYGILLW 846
Cdd:cd14079  166 -NYAAPEVISGKLYAgPEVDVWSCGVILY 193
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
583-908 9.79e-12

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: 66.26  E-value: 9.79e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 583 QFGKTLGAGAFGKVVEATAFGLGKEdavlkVAVKMLKSTAHADEKEA--LMSELKIMSHLgQHENIVNLLGACTHGGPVL 660
Cdd:cd14073    4 ELLETLGKGTYGKVKLAIERATGRE-----VAIKSIKKDKIEDEQDMvrIRREIEIMSSL-NHPHIIRIYEVFENKDKIV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 661 VITEYCCYGDLLNFLRRKaeamlgpslspgqdpeggvdyknihlekkyvrrdsgfssqgvdtyvemrpvstssndsfseQ 740
Cdd:cd14073   78 IVMEYASGGELYDYISER-------------------------------------------------------------R 96
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 741 DLDKEDGRplelrdllHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDIMND-------------S 807
Cdd:cd14073   97 RLPEREAR--------RIFRQIVSAVHYCHKNGVVHRDLKLENILLDQNGNAKIADFGLSNLYSKDkllqtfcgsplyaS 168
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 808 NYIVKGnarLPvkWMAPEsiFDCvytvqsdvWSYGILLWeIFSLGLNPYPGilvnSKFYKLVKdgyQMAQPAF----APK 883
Cdd:cd14073  169 PEIVNG---TP--YQGPE--VDC--------WSLGVLLY-TLVYGTMPFDG----SDFKRLVK---QISSGDYreptQPS 225
                        330       340
                 ....*....|....*....|....*
gi 569026720 884 NIYSIMQACWALEPTHRPTFQQICS 908
Cdd:cd14073  226 DASGLIRWMLTVNPKRRATIEDIAN 250
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
586-907 1.03e-11

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: 66.69  E-value: 1.03e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 586 KTLGAGAFGKVVEATAFGLGKedavlkvavKMLKSTAHADEKEA----LMSELKIMsHLGQHENIVNLLGACTHGGPVLV 661
Cdd:cd06620   11 KDLGAGNGGSVSKVLHIPTGT---------IMAKKVIHIDAKSSvrkqILRELQIL-HECHSPYIVSFYGAFLNENNNII 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 662 I-TEYCCYGDLLNFLRRKAeamlgpslspgqdpeggvdyknihlekkyvrrdsgfssqgvdtyvemrpvstssndsfseq 740
Cdd:cd06620   81 IcMEYMDCGSLDKILKKKG------------------------------------------------------------- 99
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 741 dldkedgrPLELRDLLHFSSQVAQGMAFLASK-NCIHRDVAARNVLLTN-GHVaKIGDFGLARDIMNDSNYIVKGNArlp 818
Cdd:cd06620  100 --------PFPEEVLGKIAVAVLEGLTYLYNVhRIIHRDIKPSNILVNSkGQI-KLCDFGVSGELINSIADTFVGTS--- 167
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 819 vKWMAPESIFDCVYTVQSDVWSYGILLWEifsLGLNPYP---------------GIL------VNSKFYKLVKDgyqmaq 877
Cdd:cd06620  168 -TYMSPERIQGGKYSVKSDVWSLGLSIIE---LALGEFPfagsnddddgyngpmGILdllqriVNEPPPRLPKD------ 237
                        330       340       350
                 ....*....|....*....|....*....|
gi 569026720 878 PAFaPKNIYSIMQACWALEPTHRPTFQQIC 907
Cdd:cd06620  238 RIF-PKDLRDFVDRCLLKDPRERPSPQLLL 266
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
757-906 1.06e-11

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: 66.13  E-value: 1.06e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 757 HFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDI-MNDSNYIVKGNARLPvKWMAPESIFDCVY--T 833
Cdd:cd14119  101 GYFVQLIDGLEYLHSQGIIHKDIKPGNLLLTTDGTLKISDFGVAEALdLFAEDDTCTTSQGSP-AFQPPEIANGQDSfsG 179
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 569026720 834 VQSDVWSYGILLWEIFSlGLNPYPGILVNSKFYKLVKDGYQMaqPAFAPKNIYSIMQACWALEPTHRPTFQQI 906
Cdd:cd14119  180 FKVDIWSAGVTLYNMTT-GKYPFEGDNIYKLFENIGKGEYTI--PDDVDPDLQDLLRGMLEKDPEKRFTIEQI 249
PKc_PBS2_like cd06622
Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
762-906 1.36e-11

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: 66.41  E-value: 1.36e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 762 VAQGMAFLASK-NCIHRDVAARNVLL-TNGHVaKIGDFGLardimndSNYIVKGNARLPV---KWMAPESIF------DC 830
Cdd:cd06622  111 VVKGLKFLKEEhNIIHRDVKPTNVLVnGNGQV-KLCDFGV-------SGNLVASLAKTNIgcqSYMAPERIKsggpnqNP 182
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 569026720 831 VYTVQSDVWSYGILLWEIfSLGLNPYPGILVNSKFYKL--VKDGYQMAQPAFAPKNIYSIMQACWALEPTHRPTFQQI 906
Cdd:cd06622  183 TYTVQSDVWSLGLSILEM-ALGRYPYPPETYANIFAQLsaIVDGDPPTLPSGYSDDAQDFVAKCLNKIPNRRPTYAQL 259
STK_BAK1_like cd14664
Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; ...
588-912 1.82e-11

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


Pssm-ID: 271134 [Multi-domain]  Cd Length: 270  Bit Score: 65.59  E-value: 1.82e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 588 LGAGAFGKVVEatafglGKEDAVLKVAVKMLKSTAHADEKEALMSELKIMSHLgQHENIVNLLGACTHGGPVLVITEYCC 667
Cdd:cd14664    1 IGRGGAGTVYK------GVMPNGTLVAVKRLKGEGTQGGDHGFQAEIQTLGMI-RHRNIVRLRGYCSNPTTNLLVYEYMP 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 668 YGDLLNFLRRKAEAmlGPSLspgqdpeggvDYknihlEKKYvrrdsgfssqgvdtyvemrpvstssndsfseqdldkedg 747
Cdd:cd14664   74 NGSLGELLHSRPES--QPPL----------DW-----ETRQ--------------------------------------- 97
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 748 rplelrdllHFSSQVAQGMAFL---ASKNCIHRDVAARNVLLTNGHVAKIGDFGLARdIMNDSNYIVKGNARLPVKWMAP 824
Cdd:cd14664   98 ---------RIALGSARGLAYLhhdCSPLIIHRDVKSNNILLDEEFEAHVADFGLAK-LMDDKDSHVMSSVAGSYGYIAP 167
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 825 ESIFDCVYTVQSDVWSYGILLWEIFSlGLNPY------PGILVNSKFYKLVKDGYQMAqpAFAP-----------KNIYS 887
Cdd:cd14664  168 EYAYTGKVSEKSDVYSYGVVLLELIT-GKRPFdeafldDGVDIVDWVRGLLEEKKVEA--LVDPdlqgvykleevEQVFQ 244
                        330       340
                 ....*....|....*....|....*
gi 569026720 888 IMQACWALEPTHRPTFQQICSFLQE 912
Cdd:cd14664  245 VALLCTQSSPMERPTMREVVRMLEG 269
IgI_4_SCFR cd05860
Fourth immunoglobulin (Ig)-like domain of stem cell factor receptor (SCFR); member of the ...
300-396 2.04e-11

Fourth immunoglobulin (Ig)-like domain of stem cell factor receptor (SCFR); member of the I-set of IgSF domains; The members here are composed of the fourth Immunoglobulin (Ig)-like domain in stem cell factor receptor (SCFR). SCFR is organized as an extracellular component having five IG-like domains, a transmembrane segment, and a cytoplasmic portion having protein tyrosine kinase activity. SCFR and its ligand SCF are critical for normal hematopoiesis, mast cell development, melanocytes, and gametogenesis. SCF binds to the second and third Ig-like domains of SCFR. This fourth Ig-like domain participates in SCFR dimerization, which follows ligand binding. Deletion of this fourth domain abolishes the ligand-induced dimerization of SCFR and completely inhibits signal transduction. 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: 409446  Cd Length: 101  Bit Score: 61.41  E-value: 2.04e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 300 YLNLSSEQNLIQEVTVGEGLNLKVMVEAYPGLQGFNWTYLGPF----SDHQPEPKlanatTKDTYRHTFTLSLPRLKPSE 375
Cdd:cd05860    2 FINITPVDNTTIFVNAGENLDLRVEYEAYPKPEHQVWIYMNETltntSDHYVKSK-----TEGNNRYVSELHLTRLKGTE 76
                         90       100
                 ....*....|....*....|.
gi 569026720 376 AGRYSFLARNPGGWRALTFEL 396
Cdd:cd05860   77 GGIYTFLVSNSDASASVTFNV 97
PKc_Myt1 cd14050
Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze ...
583-848 2.09e-11

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: 65.02  E-value: 2.09e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 583 QFGKTLGAGAFGKVVEATAfglgKEDAVLkVAVKMLKS--TAHADEKEALmSELKIMSHLGQHENIVNLLGACTHGGPVL 660
Cdd:cd14050    4 TILSKLGEGSFGEVFKVRS----REDGKL-YAVKRSRSrfRGEKDRKRKL-EEVERHEKLGEHPNCVRFIKAWEEKGILY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 661 VITEYCCygdllnflrrkaeamlgPSLSPgqdpeggvdykniHLEKkyvrrdsgfssqgvdtyvemrpvstssNDSFSEQ 740
Cdd:cd14050   78 IQTELCD-----------------TSLQQ-------------YCEE---------------------------THSLPES 100
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 741 DLDKEdgrpleLRDLLhfssqvaQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDI-MNDSNYIVKGNARlpv 819
Cdd:cd14050  101 EVWNI------LLDLL-------KGLKHLHDHGLIHLDIKPANIFLSKDGVCKLGDFGLVVELdKEDIHDAQEGDPR--- 164
                        250       260
                 ....*....|....*....|....*....
gi 569026720 820 kWMAPEsIFDCVYTVQSDVWSYGILLWEI 848
Cdd:cd14050  165 -YMAPE-LLQGSFTKAADIFSLGITILEL 191
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
583-906 2.93e-11

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: 64.76  E-value: 2.93e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 583 QFGKTLGAGAFGkvvEATAFgLGKEDAVLKVAVKMLKSTAHADEKEALMSELKIMSHLgQHENIVNLLGACTHGGPVLVI 662
Cdd:cd08221    3 IPVRVLGRGAFG---EAVLY-RKTEDNSLVVWKEVNLSRLSEKERRDALNEIDILSLL-NHDNIITYYNHFLDGESLFIE 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 663 TEYCcygdllnflrrkaeamlgpslspgqdpEGGVDYKNIHLEKkyvrrdsgfssqgvdtyvemrpvstssNDSFSEQDL 742
Cdd:cd08221   78 MEYC---------------------------NGGNLHDKIAQQK---------------------------NQLFPEEVV 103
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 743 dkedgrplelrdlLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARdIMNDSNYIVKGNARLPVkWM 822
Cdd:cd08221  104 -------------LWYLYQIVSAVSHIHKAGILHRDIKTLNIFLTKADLVKLGDFGISK-VLDSESSMAESIVGTPY-YM 168
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 823 APESIFDCVYTVQSDVWSYGILLWEIFSL-----GLNPYpgilvnSKFYKLVKDGYQMAQPAFApKNIYSIMQACWALEP 897
Cdd:cd08221  169 SPELVQGVKYNFKSDIWAVGCVLYELLTLkrtfdATNPL------RLAVKIVQGEYEDIDEQYS-EEIIQLVHDCLHQDP 241

                 ....*....
gi 569026720 898 THRPTFQQI 906
Cdd:cd08221  242 EDRPTAEEL 250
PK_GC_unk cd14045
Pseudokinase domain of the unknown subfamily of membrane Guanylate Cyclase receptors; The ...
613-910 3.70e-11

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: 64.88  E-value: 3.70e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 613 VAVKMLKSTAHADEKeALMSELKIMSHLgQHENIVNLLGACTHGGPVLVITEYCcygdllnflrrkaeamlgpslspgqd 692
Cdd:cd14045   33 VAIKKIAKKSFTLSK-RIRKEVKQVREL-DHPNLCKFIGGCIEVPNVAIITEYC-------------------------- 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 693 PEGgvdyknihlekkyvrrdsgfssqgvdtyvemrpvstSSNDSFSEQDLdkedgrPLELRDLLHFSSQVAQGMAFLASK 772
Cdd:cd14045   85 PKG------------------------------------SLNDVLLNEDI------PLNWGFRFSFATDIARGMAYLHQH 122
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 773 NCIHRDVAARNVLLTNGHVAKIGDFGLARDIMNDSNYIVKG-NARLPVKWMAPE--SIFDCVYTVQSDVWSYGILLWEIF 849
Cdd:cd14045  123 KIYHGRLKSSNCVIDDRWVCKIADYGLTTYRKEDGSENASGyQQRLMQVYLPPEnhSNTDTEPTQATDVYSYAIILLEIA 202
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 569026720 850 SLGlNPYPGILVNSK------FYKLVKDGYQMAQPafAPKNIYSIMQACWALEPTHRPTFQQICSFL 910
Cdd:cd14045  203 TRN-DPVPEDDYSLDeawcppLPELISGKTENSCP--CPADYVELIRRCRKNNPAQRPTFEQIKKTL 266
STKc_Yank1 cd05578
Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the ...
757-858 3.74e-11

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: 64.59  E-value: 3.74e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 757 HFSSQVAQGMAFLASKNCIHRDVAARNVLLTN-GHVaKIGDFGLARdIMNDSNYIVKGNARLPvkWMAPESIFDCVYTVQ 835
Cdd:cd05578  104 FYICEIVLALDYLHSKNIIHRDIKPDNILLDEqGHV-HITDFNIAT-KLTDGTLATSTSGTKP--YMAPEVFMRAGYSFA 179
                         90       100
                 ....*....|....*....|...
gi 569026720 836 SDVWSYGILLWEiFSLGLNPYPG 858
Cdd:cd05578  180 VDWWSLGVTAYE-MLRGKRPYEI 201
STKc_EIF2AK3_PERK cd14048
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
750-906 4.03e-11

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: 64.90  E-value: 4.03e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 750 LELRDL---LHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLA---------RDIMNDSNYIVKGNARL 817
Cdd:cd14048  112 MESRELfvcLNIFKQIASAVEYLHSKGLIHRDLKPSNVFFSLDDVVKVGDFGLVtamdqgepeQTVLTPMPAYAKHTGQV 191
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 818 PVK-WMAPESIFDCVYTVQSDVWSYGILLWE-IFSLGlnpypgilVNSKFYKLVKDGYQMAQPAFAPKNI---YSIMQAC 892
Cdd:cd14048  192 GTRlYMSPEQIHGNQYSEKVDIFALGLILFElIYSFS--------TQMERIRTLTDVRKLKFPALFTNKYpeeRDMVQQM 263
                        170
                 ....*....|....
gi 569026720 893 WALEPTHRPTFQQI 906
Cdd:cd14048  264 LSPSPSERPEAHEV 277
STKc_TAO3 cd06633
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze ...
738-848 4.12e-11

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: 65.06  E-value: 4.12e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 738 SEQDLDKEDGRPLELRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLArDIMNDSNYIVKgnarL 817
Cdd:cd06633  106 SASDLLEVHKKPLQEVEIAAITHGALQGLAYLHSHNMIHRDIKAGNILLTEPGQVKLADFGSA-SIASPANSFVG----T 180
                         90       100       110
                 ....*....|....*....|....*....|....
gi 569026720 818 PVkWMAPESIF---DCVYTVQSDVWSYGILLWEI 848
Cdd:cd06633  181 PY-WMAPEVILamdEGQYDGKVDIWSLGITCIEL 213
STKc_RIP4_like cd14025
Catalytic domain of the Serine/Threonine kinases, Receptor Interacting Protein 4 and similar ...
749-908 4.43e-11

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


Pssm-ID: 270927 [Multi-domain]  Cd Length: 267  Bit Score: 64.44  E-value: 4.43e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 749 PLELR-DLLHfssQVAQGMAFLASKN--CIHRDVAARNVLLTNGHVAKIGDFGLAR-DIMNDSNYIVKGNARLPVKWMAP 824
Cdd:cd14025   90 PWELRfRIIH---ETAVGMNFLHCMKppLLHLDLKPANILLDAHYHVKISDFGLAKwNGLSHSHDLSRDGLRGTIAYLPP 166
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 825 ESI------FDCVYtvqsDVWSYGILLWEIFSLGlNPYPGilVNSKFYKLVKDGYQMaQPAFAP---------KNIYSIM 889
Cdd:cd14025  167 ERFkeknrcPDTKH----DVYSFAIVIWGILTQK-KPFAG--ENNILHIMVKVVKGH-RPSLSPiprqrpsecQQMICLM 238
                        170
                 ....*....|....*....
gi 569026720 890 QACWALEPTHRPTFQQICS 908
Cdd:cd14025  239 KRCWDQDPRKRPTFQDITS 257
STKc_ERK5 cd07855
Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; ...
586-858 4.64e-11

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: 65.46  E-value: 4.64e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 586 KTLGAGAFGKVVEATAFGLGKedavlKVAVKMLkstAHADEKEAL----MSELKIMSHLgQHENIVNLLgacthggpvlv 661
Cdd:cd07855   11 ETIGSGAYGVVCSAIDTKSGQ-----KVAIKKI---PNAFDVVTTakrtLRELKILRHF-KHDNIIAIR----------- 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 662 iteyccygDLLnflrrkaeamlgpslspgqdpeggvdyknihlekkyvrRDSGFSSQGVDTYVEMrpvstssndSFSEQD 741
Cdd:cd07855   71 --------DIL--------------------------------------RPKVPYADFKDVYVVL---------DLMESD 95
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 742 LDK--EDGRPLELRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLT-NGHVaKIGDFGLARDIMNDS----NYIVKGN 814
Cdd:cd07855   96 LHHiiHSDQPLTLEHIRYFLYQLLRGLKYIHSANVIHRDLKPSNLLVNeNCEL-KIGDFGMARGLCTSPeehkYFMTEYV 174
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 569026720 815 ARLPVKwmAPESIFDC-VYTVQSDVWSYGILLWEIfsLGLNP-YPG 858
Cdd:cd07855  175 ATRWYR--APELMLSLpEYTQAIDMWSVGCIFAEM--LGRRQlFPG 216
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
580-848 4.71e-11

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: 64.91  E-value: 4.71e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 580 NNLQFGKTLGAGAFGKVVEATAFGLGKedavlKVAVKMLKST--AHADEKEALMSELKIMSHLgQHENIVNLLGACTHGG 657
Cdd:cd05580    1 DDFEFLKTLGTGSFGRVRLVKHKDSGK-----YYALKILKKAkiIKLKQVEHVLNEKRILSEV-RHPFIVNLLGSFQDDR 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 658 PVLVITEYCCYGDLLNFLRRkaeamlgpslspgqdpeggvdyknihlekkyvrrdsgfssqgvdtyvemrpvstssNDSF 737
Cdd:cd05580   75 NLYMVMEYVPGGELFSLLRR--------------------------------------------------------SGRF 98
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 738 SEQDLdkedgrplelrdlLHFSSQVAQGMAFLASKNCIHRDVAARNVLL-TNGHVaKIGDFGLARDImNDSNYIVKGNAr 816
Cdd:cd05580   99 PNDVA-------------KFYAAEVVLALEYLHSLDIVYRDLKPENLLLdSDGHI-KITDFGFAKRV-KDRTYTLCGTP- 162
                        250       260       270
                 ....*....|....*....|....*....|..
gi 569026720 817 lpvKWMAPESIFDCVYTVQSDVWSYGILLWEI 848
Cdd:cd05580  163 ---EYLAPEIILSKGHGKAVDWWALGILIYEM 191
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
588-848 4.72e-11

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


Pssm-ID: 270826 [Multi-domain]  Cd Length: 287  Bit Score: 64.66  E-value: 4.72e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 588 LGAGAFGKVVEATAFGLGKEDAVLKVAVKmlksTAHADEKEALMSELKIMSHLGQHENIVNLLGACTHGGPVLVITEYcc 667
Cdd:cd07832    8 IGEGAHGIVFKAKDRETGETVALKKVALR----KLEGGIPNQALREIKALQACQGHPYVVKLRDVFPHGTGFVLVFEY-- 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 668 ygdllnflrrkaeamLGPSLSPgqdpeggvdyknihlekkyVRRDsgfssqgvdtyvEMRPVSTSSNDSFSEQDLDkedg 747
Cdd:cd07832   82 ---------------MLSSLSE-------------------VLRD------------EERPLTEAQVKRYMRMLLK---- 111
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 748 rplelrdllhfssqvaqGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARdIMNDsnyivkGNARLP-----VKW- 821
Cdd:cd07832  112 -----------------GVAYMHANRIMHRDLKPANLLISSTGVLKIADFGLAR-LFSE------EDPRLYshqvaTRWy 167
                        250       260
                 ....*....|....*....|....*...
gi 569026720 822 MAPESIFDC-VYTVQSDVWSYGILLWEI 848
Cdd:cd07832  168 RAPELLYGSrKYDEGVDLWAVGCIFAEL 195
STKc_PKN cd05589
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer ...
588-858 5.27e-11

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: 65.01  E-value: 5.27e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 588 LGAGAFGKVVEATAFGLGKedavlKVAVKMLKS--TAHADEKEALMSELKIM--SHLGQHENIVNLLGACTHGGPVLVIT 663
Cdd:cd05589    7 LGRGHFGKVLLAEYKPTGE-----LFAIKALKKgdIIARDEVESLMCEKRIFetVNSARHPFLVNLFACFQTPEHVCFVM 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 664 EYCCYGDLlnflrrkaeaMLgpslspgqdpeggvdykNIHlekkyvrrdsgfssqgvdtyvemrpvstssNDSFSEQdld 743
Cdd:cd05589   82 EYAAGGDL----------MM-----------------HIH------------------------------EDVFSEP--- 101
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 744 kedgrplelRDLLhFSSQVAQGMAFLASKNCIHRDVAARNVLL-TNGHVaKIGDFGLARDIM--NDSNYIVKGNArlpvK 820
Cdd:cd05589  102 ---------RAVF-YAACVVLGLQFLHEHKIVYRDLKLDNLLLdTEGYV-KIADFGLCKEGMgfGDRTSTFCGTP----E 166
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 569026720 821 WMAPESIFDCVYTVQSDVWSYGILLWEIFsLGLNPYPG 858
Cdd:cd05589  167 FLAPEVLTDTSYTRAVDWWGLGVLIYEML-VGESPFPG 203
STKc_STK33 cd14097
Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the ...
583-906 6.04e-11

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: 64.11  E-value: 6.04e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 583 QFGKTLGAGAFGKVVEATAFGLGKEDAVLKV--------AVKMLKStahadekealmsELKIMSHLgQHENIVNLLGACT 654
Cdd:cd14097    4 TFGRKLGQGSFGVVIEATHKETQTKWAIKKInrekagssAVKLLER------------EVDILKHV-NHAHIIHLEEVFE 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 655 HGGPVLVITEYCCYGDLLNFLRRKaeamlgpslspgqdpeggvdyknihlekkyvrrdsGFssqgvdtyvemrpvstssn 734
Cdd:cd14097   71 TPKRMYLVMELCEDGELKELLLRK-----------------------------------GF------------------- 96
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 735 dsFSEQDLDkedgrplelrdllHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHV-------AKIGDFGLARDIMNDS 807
Cdd:cd14097   97 --FSENETR-------------HIIQSLASAVAYLHKNDIVHRDLKLENILVKSSIIdnndklnIKVTDFGLSVQKYGLG 161
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 808 NYIVKGNARLPVkWMAPESIFDCVYTVQSDVWSYGILLWeIFSLGLNPYPGiLVNSKFYKLVKDG-YQMAQPAF-----A 881
Cdd:cd14097  162 EDMLQETCGTPI-YMAPEVISAHGYSQQCDIWSIGVIMY-MLLCGEPPFVA-KSEEKLFEEIRKGdLTFTQSVWqsvsdA 238
                        330       340
                 ....*....|....*....|....*
gi 569026720 882 PKNiysIMQACWALEPTHRPTFQQI 906
Cdd:cd14097  239 AKN---VLQQLLKVDPAHRMTASEL 260
STKc_TGFbR-like cd13998
Catalytic domain of Transforming Growth Factor beta Receptor-like Serine/Threonine Kinases; ...
750-850 6.51e-11

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: 64.38  E-value: 6.51e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 750 LELRDLLHFSSQVAQGMAFLAS--------KNCI-HRDVAARNVLLTNGHVAKIGDFGLArdIMNDSNYIVKGNARLP-- 818
Cdd:cd13998   89 IDWVSLCRLALSVARGLAHLHSeipgctqgKPAIaHRDLKSKNILVKNDGTCCIADFGLA--VRLSPSTGEEDNANNGqv 166
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 569026720 819 --VKWMAPESIFDCVYT------VQSDVWSYGILLWEIFS 850
Cdd:cd13998  167 gtKRYMAPEVLEGAINLrdfesfKRVDIYAMGLVLWEMAS 206
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
744-901 6.67e-11

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


Pssm-ID: 270865 [Multi-domain]  Cd Length: 268  Bit Score: 63.89  E-value: 6.67e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 744 KEDGRPLELRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARdIMNDSNYIVKGNARLPVkWMA 823
Cdd:cd08228   97 KKQKRLIPERTVWKYFVQLCSAVEHMHSRRVMHRDIKPANVFITATGVVKLGDLGLGR-FFSSKTTAAHSLVGTPY-YMS 174
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 824 PESIFDCVYTVQSDVWSYGILLWEIFSLGlNPYPGILVNskFYKLVKDGYQMAQPAFaPKNIYS-----IMQACWALEPT 898
Cdd:cd08228  175 PERIHENGYNFKSDIWSLGCLLYEMAALQ-SPFYGDKMN--LFSLCQKIEQCDYPPL-PTEHYSeklreLVSMCIYPDPD 250

                 ...
gi 569026720 899 HRP 901
Cdd:cd08228  251 QRP 253
STKc_Nek1 cd08218
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
586-906 6.72e-11

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: 63.68  E-value: 6.72e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 586 KTLGAGAFGKVVEATAFGLGKEDAVLKVAVKMLKSTahadEKEALMSELKIMSHLgQHENIVNLLGACTHGGPVLVITEY 665
Cdd:cd08218    6 KKIGEGSFGKALLVKSKEDGKQYVIKEINISKMSPK----EREESRKEVAVLSKM-KHPNIVQYQESFEENGNLYIVMDY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 666 CCYGDLlnflrrkaeamlgpslspgqdpeggvdYKNIHLEKkyvrrdsgfssqGVdtyvemrpvstssndSFSEqdldke 745
Cdd:cd08218   81 CDGGDL---------------------------YKRINAQR------------GV---------------LFPE------ 100
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 746 dgrplelRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARdIMNDSNYIVKGNARLPVkWMAPE 825
Cdd:cd08218  101 -------DQILDWFVQLCLALKHVHDRKILHRDIKSQNIFLTKDGIIKLGDFGIAR-VLNSTVELARTCIGTPY-YLSPE 171
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 826 SIFDCVYTVQSDVWSYGILLWEIFSLGlNPYPGILVNSKFYKLVKDGYQMAqPAFAPKNIYSIMQACWALEPTHRPTFQQ 905
Cdd:cd08218  172 ICENKPYNNKSDIWALGCVLYEMCTLK-HAFEAGNMKNLVLKIIRGSYPPV-PSRYSYDLRSLVSQLFKRNPRDRPSINS 249

                 .
gi 569026720 906 I 906
Cdd:cd08218  250 I 250
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
761-906 8.53e-11

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: 63.92  E-value: 8.53e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 761 QVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDIMNDSnyiVKGNARLPVK-WMAPESIFDCVYTVQSDVW 839
Cdd:cd06640  109 EILKGLDYLHSEKKIHRDIKAANVLLSEQGDVKLADFGVAGQLTDTQ---IKRNTFVGTPfWMAPEVIQQSAYDSKADIW 185
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 569026720 840 SYGILLWEIfSLGLNPYPGILVNSKFYKLVKDGYQMAQPAFApKNIYSIMQACWALEPTHRPTFQQI 906
Cdd:cd06640  186 SLGITAIEL-AKGEPPNSDMHPMRVLFLIPKNNPPTLVGDFS-KPFKEFIDACLNKDPSFRPTAKEL 250
STKc_MAPK4_6 cd07854
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also ...
586-848 9.10e-11

Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also called ERK4) and 6 (also called ERK3); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK4 (also called ERK4 or p63MAPK) and MAPK6 (also called ERK3 or p97MAPK) are atypical MAPKs that are not regulated by MAPK kinases. MAPK6 is expressed ubiquitously with highest amounts in brain and skeletal muscle. It may be involved in the control of cell differentiation by negatively regulating cell cycle progression in certain conditions. It may also play a role in glucose-induced insulin secretion. MAPK6 and MAPK4 cooperate to regulate the activity of MAPK-activated protein kinase 5 (MK5), leading to its relocation to the cytoplasm and exclusion from the nucleus. The MAPK6/MK5 and MAPK4/MK5 pathways may play critical roles in embryonic and post-natal development. MAPKs are important mediators of cellular responses to extracellular signals. The MAPK4/6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143359 [Multi-domain]  Cd Length: 342  Bit Score: 64.41  E-value: 9.10e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 586 KTLGAGAFGKVVEATAFGLGKEDAVLKVAVKMLKSTAHAdekealMSELKIMSHLgQHENIVnllgacthggpvlvitey 665
Cdd:cd07854   11 RPLGCGSNGLVFSAVDSDCDKRVAVKKIVLTDPQSVKHA------LREIKIIRRL-DHDNIV------------------ 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 666 ccygdllnflrrKAEAMLGPSLSPGQDPeggvdyknihlekkyVRRDSGFSSqgvdTYVEMRPVSTSSNDSFSEQDLDKE 745
Cdd:cd07854   66 ------------KVYEVLGPSGSDLTED---------------VGSLTELNS----VYIVQEYMETDLANVLEQGPLSEE 114
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 746 DGRplelrdllHFSSQVAQGMAFLASKNCIHRDVAARNVLL-TNGHVAKIGDFGLARdIMnDSNYIVKG--NARLPVKWM 822
Cdd:cd07854  115 HAR--------LFMYQLLRGLKYIHSANVLHRDLKPANVFInTEDLVLKIGDFGLAR-IV-DPHYSHKGylSEGLVTKWY 184
                        250       260
                 ....*....|....*....|....*...
gi 569026720 823 -APESIFDCV-YTVQSDVWSYGILLWEI 848
Cdd:cd07854  185 rSPRLLLSPNnYTKAIDMWAAGCIFAEM 212
PKc_MKK3_6 cd06617
Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase ...
721-917 1.02e-10

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: 1.02e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 721 DTYVEMRPVSTSSnDSFSEQDLDKEDGRPLELRDLLHFSsqVAQGMAFLASK-NCIHRDVAARNVLLT-NGHVaKIGDFG 798
Cdd:cd06617   74 DVWICMEVMDTSL-DKFYKKVYDKGLTIPEDILGKIAVS--IVKALEYLHSKlSVIHRDVKPSNVLINrNGQV-KLCDFG 149
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 799 LARDIMNDSNYIVKGNARlpvKWMAPESI----FDCVYTVQSDVWSYGILLWEIfSLGLNPYPGILVNSKFYKLVKDGYQ 874
Cdd:cd06617  150 ISGYLVDSVAKTIDAGCK---PYMAPERInpelNQKGYDVKSDVWSLGITMIEL-ATGRFPYDSWKTPFQQLKQVVEEPS 225
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 569026720 875 MAQPA--FAPKNIYSIMQaCWALEPTHRPTFQQIC--SFLQEQAQED 917
Cdd:cd06617  226 PQLPAekFSPEFQDFVNK-CLKKNYKERPNYPELLqhPFFELHLSKN 271
STKc_CDKL1_4 cd07847
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; ...
761-906 1.02e-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: 63.54  E-value: 1.02e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 761 QVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARdIMN--DSNYivkgNARLPVKWM-APESIF-DCVYTVQS 836
Cdd:cd07847  108 QTLQAVNFCHKHNCIHRDVKPENILITKQGQIKLCDFGFAR-ILTgpGDDY----TDYVATRWYrAPELLVgDTQYGPPV 182
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 837 DVWSYGILLWEIFSlGLNPYPG-----------------------ILVNSKFYKLVK-------DGYQMAQPAFAPKNIy 886
Cdd:cd07847  183 DVWAIGCVFAELLT-GQPLWPGksdvdqlylirktlgdliprhqqIFSTNQFFKGLSipepetrEPLESKFPNISSPAL- 260
                        170       180
                 ....*....|....*....|
gi 569026720 887 SIMQACWALEPTHRPTFQQI 906
Cdd:cd07847  261 SFLKGCLQMDPTERLSCEEL 280
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
588-846 1.15e-10

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: 63.34  E-value: 1.15e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 588 LGAGAFGKVVEAtafgLGKEDAVLkVAVKMLK---------STAHADEKEALMS----ELKIMSHLgQHENIVNLLGACT 654
Cdd:cd14008    1 LGRGSFGKVKLA----LDTETGQL-YAIKIFNksrlrkrreGKNDRGKIKNALDdvrrEIAIMKKL-DHPNIVRLYEVID 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 655 --HGGPVLVITEYCCYGDLlnflrrkaeamlgpslspgqdpeggvdyknihlekkyvrrdsgfssqgvdtyveMRPVSTS 732
Cdd:cd14008   75 dpESDKLYLVLEYCEGGPV------------------------------------------------------MELDSGD 100
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 733 SNDSFSEQDLDKEdgrpleLRDLLHfssqvaqGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARdIMNDSNYIVK 812
Cdd:cd14008  101 RVPPLPEETARKY------FRDLVL-------GLEYLHENGIVHRDIKPENLLLTADGTVKISDFGVSE-MFEDGNDTLQ 166
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 569026720 813 GNARLPVkWMAPEsIFDCVYTVQS----DVWSYGILLW 846
Cdd:cd14008  167 KTAGTPA-FLAPE-LCDGDSKTYSgkaaDIWALGVTLY 202
STKc_PAK_II cd06648
Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze ...
578-848 1.20e-10

Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Group II PAKs, also called non-conventional PAKs, include PAK4, PAK5, and PAK6. Group II PAKs contain PBD (p21-binding domain) and catalytic domains, but lack other motifs found in group I PAKs, such as an AID (autoinhibitory domain) and SH3 binding sites. Since group II PAKs do not contain an obvious AID, they may be regulated differently from group I PAKs. While group I PAKs interact with the SH3 containing proteins Nck, Grb2 and PIX, no such binding has been demonstrated for group II PAKs. Some known substrates of group II PAKs are also substrates of group I PAKs such as Raf, BAD, LIMK and GEFH1. Unique group II substrates include MARK/Par-1 and PDZ-RhoGEF. Group II PAKs play important roles in filopodia formation, neuron extension, cytoskeletal organization, and cell survival. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270815 [Multi-domain]  Cd Length: 261  Bit Score: 63.23  E-value: 1.20e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 578 PRNNLQFGKTLGAGAFGKVVEATAFGLGKedavlKVAVKMLKSTAHaDEKEALMSELKIMSHLgQHENIVNLLGACTHGG 657
Cdd:cd06648    5 PRSDLDNFVKIGEGSTGIVCIATDKSTGR-----QVAVKKMDLRKQ-QRRELLFNEVVIMRDY-QHPNIVEMYSSYLVGD 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 658 PVLVITEYCcygdllnflrrkaeamlgpslspgqdpEGGvdyknihlekkyvrrdsgfssqgvdtyvemrpvstSSNDSF 737
Cdd:cd06648   78 ELWVVMEFL---------------------------EGG-----------------------------------ALTDIV 95
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 738 SEQDLDKEDgrplelrdLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDIMNDsnyivkgnarL 817
Cdd:cd06648   96 THTRMNEEQ--------IATVCRAVLKALSFLHSQGVIHRDIKSDSILLTSDGRVKLSDFGFCAQVSKE----------V 157
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 569026720 818 PVK--------WMAPESIFDCVYTVQSDVWSYGILLWEI 848
Cdd:cd06648  158 PRRkslvgtpyWMAPEVISRLPYGTEVDIWSLGIMVIEM 196
PHA03209 PHA03209
serine/threonine kinase US3; Provisional
742-860 1.24e-10

serine/threonine kinase US3; Provisional


Pssm-ID: 177557 [Multi-domain]  Cd Length: 357  Bit Score: 64.13  E-value: 1.24e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 742 LDKEDgRPLELRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDIMNDSNYI-VKGNarlpVK 820
Cdd:PHA03209 147 LTKRS-RPLPIDQALIIEKQILEGLRYLHAQRIIHRDVKTENIFINDVDQVCIGDLGAAQFPVVAPAFLgLAGT----VE 221
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 569026720 821 WMAPESIFDCVYTVQSDVWSYGILLWEIFSlglnpYPGIL 860
Cdd:PHA03209 222 TNAPEVLARDKYNSKADIWSAGIVLFEMLA-----YPSTI 256
STKc_CDK4 cd07863
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs ...
747-849 1.52e-10

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


Pssm-ID: 143368 [Multi-domain]  Cd Length: 288  Bit Score: 63.06  E-value: 1.52e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 747 GRPLE-LRDLLHfssQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDImndSNYIVKGNARLPVKWMAPE 825
Cdd:cd07863  104 GLPAEtIKDLMR---QFLRGLDFLHANCIVHRDLKPENILVTSGGQVKLADFGLARIY---SCQMALTPVVVTLWYRAPE 177
                         90       100
                 ....*....|....*....|....
gi 569026720 826 SIFDCVYTVQSDVWSYGILLWEIF 849
Cdd:cd07863  178 VLLQSTYATPVDMWSVGCIFAEMF 201
STKc_LRRK2 cd14068
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze ...
588-910 1.67e-10

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


Pssm-ID: 270970 [Multi-domain]  Cd Length: 252  Bit Score: 62.66  E-value: 1.67e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 588 LGAGAFGKVVEATAFGlgkEDavlkVAVKMLKStaHADEKeALMSELKIMSHLgQHENIVNLLGACTHggPVLVITEYCc 667
Cdd:cd14068    2 LGDGGFGSVYRAVYRG---ED----VAVKIFNK--HTSFR-LLRQELVVLSHL-HHPSLVALLAAGTA--PRMLVMELA- 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 668 ygdllnflrrkaeamlgpslspgqdPEGGVDykniHLekkyVRRDSGFSSqgvdtyvemrpvstssndsfseqdldkedg 747
Cdd:cd14068   68 -------------------------PKGSLD----AL----LQQDNASLT------------------------------ 84
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 748 RPLELRDLLHfssqVAQGMAFLASKNCIHRDVAARNVLLTNGH-----VAKIGDFGLARDIMNDSNYIVKGNArlpvKWM 822
Cdd:cd14068   85 RTLQHRIALH----VADGLRYLHSAMIIYRDLKPHNVLLFTLYpncaiIAKIADYGIAQYCCRMGIKTSEGTP----GFR 156
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 823 APE-SIFDCVYTVQSDVWSYGILLWEIFSLGLNPYPGILVNSKFYKLVKDGyQMAQPA----FAP-KNIYSIMQACWALE 896
Cdd:cd14068  157 APEvARGNVIYNQQADVYSFGLLLYDILTCGERIVEGLKFPNEFDELAIQG-KLPDPVkeygCAPwPGVEALIKDCLKEN 235
                        330
                 ....*....|....
gi 569026720 897 PTHRPTFQQICSFL 910
Cdd:cd14068  236 PQCRPTSAQVFDIL 249
STKc_TAO1 cd06635
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze ...
738-906 1.75e-10

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: 63.53  E-value: 1.75e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 738 SEQDLDKEDGRPLELRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLArDIMNDSNYIVKgnarL 817
Cdd:cd06635  110 SASDLLEVHKKPLQEIEIAAITHGALQGLAYLHSHNMIHRDIKAGNILLTEPGQVKLADFGSA-SIASPANSFVG----T 184
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 818 PVkWMAPESIF---DCVYTVQSDVWSYGILLWEIFSLGlNPYPGILVNSKFYKLVKDGYQMAQPAFAPKNIYSIMQACWA 894
Cdd:cd06635  185 PY-WMAPEVILamdEGQYDGKVDVWSLGITCIELAERK-PPLFNMNAMSALYHIAQNESPTLQSNEWSDYFRNFVDSCLQ 262
                        170
                 ....*....|..
gi 569026720 895 LEPTHRPTFQQI 906
Cdd:cd06635  263 KIPQDRPTSEEL 274
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
584-847 2.00e-10

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: 62.97  E-value: 2.00e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 584 FGKTLGAGAFGKVVEATAFGLGKedavlKVAVKMLKSTAHADEKEAL-MS---ELKIMSHLgQHENIVNLLGACTHGGPV 659
Cdd:cd07841    4 KGKKLGEGTYAVVYKARDKETGR-----IVAIKKIKLGERKEAKDGInFTalrEIKLLQEL-KHPNIIGLLDVFGHKSNI 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 660 LVITEYCcYGDLLNFLRRKAeamlgPSLSPGqdpeggvDYKNIHLekkyvrrdsgfssqgvdtyvemrpvstssndsfse 739
Cdd:cd07841   78 NLVFEFM-ETDLEKVIKDKS-----IVLTPA-------DIKSYML----------------------------------- 109
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 740 qdldkedgrplelrdllhfssQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDIMNDS-NYIVKGNARlp 818
Cdd:cd07841  110 ---------------------MTLRGLEYLHSNWILHRDLKPNNLLIASDGVLKLADFGLARSFGSPNrKMTHQVVTR-- 166
                        250       260       270
                 ....*....|....*....|....*....|.
gi 569026720 819 vkWM-APESIFDC-VYTVQSDVWSYGILLWE 847
Cdd:cd07841  167 --WYrAPELLFGArHYGVGVDMWSVGCIFAE 195
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
588-850 2.25e-10

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: 62.51  E-value: 2.25e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 588 LGAGAFGKVVEATAFGLGKEDAVLKVAVkmlkstaHADEKEalmSELKIMSHLgQHENIVNLlgacthggpvlviteYCC 667
Cdd:cd14047   14 IGSGGFGQVFKAKHRIDGKTYAIKRVKL-------NNEKAE---REVKALAKL-DHPNIVRY---------------NGC 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 668 YGDLLNFlrrkaeamlgPSLSPGQDPEGGVDYKNIHLEkkyvrrdsgFSSQGVdtyvemrpvstssndsfSEQDLDKEDG 747
Cdd:cd14047   68 WDGFDYD----------PETSSSNSSRSKTKCLFIQME---------FCEKGT-----------------LESWIEKRNG 111
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 748 RPLELRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLardIMNDSNYIVKGNARLPVKWMAPESI 827
Cdd:cd14047  112 EKLDKVLALEIFEQITKGVEYIHSKKLIHRDLKPSNIFLVDTGKVKIGDFGL---VTSLKNDGKRTKSKGTLSYMSPEQI 188
                        250       260
                 ....*....|....*....|...
gi 569026720 828 FDCVYTVQSDVWSYGILLWEIFS 850
Cdd:cd14047  189 SSQDYGKEVDIYALGLILFELLH 211
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
588-798 2.33e-10

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: 59.38  E-value: 2.33e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 588 LGAGAFGKVVEATAFGLGKEdavlkVAVKMLKSTAhADEKEALMSELKIMSHLGQHE-NIVNLLGACTHGGPVLVITEYC 666
Cdd:cd13968    1 MGEGASAKVFWAEGECTTIG-----VAVKIGDDVN-NEEGEDLESEMDILRRLKGLElNIPKVLVTEDVDGPNILLMELV 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 667 cygdllnflrrkaeamlgpslspgqdpeggvdyknihlekkyvrrdSGFSSQGVDTYVEMrpvstssndsfSEQDLDKed 746
Cdd:cd13968   75 ----------------------------------------------KGGTLIAYTQEEEL-----------DEKDVES-- 95
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 569026720 747 grplelrdllhFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFG 798
Cdd:cd13968   96 -----------IMYQLAECMRLLHSFHLIHRDLNNDNILLSEDGNVKLIDFG 136
STKc_IRE1 cd13982
Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze ...
740-906 3.47e-10

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: 61.90  E-value: 3.47e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 740 QDLDKEDGRP-LELRDLLHfssQVAQGMAFLASKNCIHRDVAARNVLLT----NGHV-AKIGDFGLARDI-MNDSNYIVK 812
Cdd:cd13982   88 PRESKLFLRPgLEPVRLLR---QIASGLAHLHSLNIVHRDLKPQNILIStpnaHGNVrAMISDFGLCKKLdVGRSSFSRR 164
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 813 GNARLPVKWMAPESIFDCVYTVQS---DVWSYGILLWEIFSLGLNPYPGIL-----VNSKFYKLVKDGYQMAQPAFAPKN 884
Cdd:cd13982  165 SGVAGTSGWIAPEMLSGSTKRRQTravDIFSLGCVFYYVLSGGSHPFGDKLereanILKGKYSLDKLLSLGEHGPEAQDL 244
                        170       180
                 ....*....|....*....|..
gi 569026720 885 IYSIMQAcwalEPTHRPTFQQI 906
Cdd:cd13982  245 IERMIDF----DPEKRPSAEEV 262
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
740-908 3.48e-10

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: 61.53  E-value: 3.48e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 740 QDLDKEDGRPLELRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDIMNDSNYIVkgnARLPV 819
Cdd:cd08219   87 QKIKLQRGKLFPEDTILQWFVQMCLGVQHIHEKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLTSPGAYAC---TYVGT 163
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 820 KWMAPESIFDCV-YTVQSDVWSYGILLWEIFSLGlNPYPGILVNSKFYKLVKDGYQmAQPAFAPKNIYSIMQACWALEPT 898
Cdd:cd08219  164 PYYVPPEIWENMpYNNKSDIWSLGCILYELCTLK-HPFQANSWKNLILKVCQGSYK-PLPSHYSYELRSLIKQMFKRNPR 241
                        170
                 ....*....|
gi 569026720 899 HRPTFQQICS 908
Cdd:cd08219  242 SRPSATTILS 251
STKc_nPKC_theta cd05619
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze ...
758-900 3.76e-10

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: 62.63  E-value: 3.76e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 758 FSSQVAQGMAFLASKNCIHRDVAARNVLL-TNGHVaKIGDFGLARDIMndsnyivKGNARLPV-----KWMAPESIFDCV 831
Cdd:cd05619  111 YAAEIICGLQFLHSKGIVYRDLKLDNILLdKDGHI-KIADFGMCKENM-------LGDAKTSTfcgtpDYIAPEILLGQK 182
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 569026720 832 YTVQSDVWSYGILLWEIFsLGLNPYPGILVNSKFYKLVKDgyQMAQPAFAPKNIYSIMQACWALEPTHR 900
Cdd:cd05619  183 YNTSVDWWSFGVLLYEML-IGQSPFHGQDEEELFQSIRMD--NPFYPRWLEKEAKDILVKLFVREPERR 248
STKc_CDK6 cd07862
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs ...
742-849 3.81e-10

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK6 is regulated by D-type cyclins and INK4 inhibitors. It is active towards the retinoblastoma (pRb) protein, implicating it to function in regulating the early G1 phase of the cell cycle. It is expressed ubiquitously and is localized in the cytoplasm. It is also present in the ruffling edge of spreading fibroblasts and may play a role in cell spreading. It binds to the p21 inhibitor without any effect on its own activity and it is overexpressed in squamous cell carcinomas and neuroblastomas. CDK6 has also been shown to inhibit cell differentiation in many cell types. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270846 [Multi-domain]  Cd Length: 290  Bit Score: 61.97  E-value: 3.81e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 742 LDK--EDGRPLE-LRDLLHfssQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDI---MNDSNYIVKgna 815
Cdd:cd07862   99 LDKvpEPGVPTEtIKDMMF---QLLRGLDFLHSHRVVHRDLKPQNILVTSSGQIKLADFGLARIYsfqMALTSVVVT--- 172
                         90       100       110
                 ....*....|....*....|....*....|....
gi 569026720 816 rlpVKWMAPESIFDCVYTVQSDVWSYGILLWEIF 849
Cdd:cd07862  173 ---LWYRAPEVLLQSSYATPVDLWSVGCIFAEMF 203
STKc_cPKC_beta cd05616
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs ...
758-900 4.91e-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: 61.94  E-value: 4.91e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 758 FSSQVAQGMAFLASKNCIHRDVAARNVLL-TNGHVaKIGDFGLARDIMNDSnYIVKGNARLPvKWMAPESIFDCVYTVQS 836
Cdd:cd05616  106 YAAEIAIGLFFLQSKGIIYRDLKLDNVMLdSEGHI-KIADFGMCKENIWDG-VTTKTFCGTP-DYIAPEIIAYQPYGKSV 182
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 569026720 837 DVWSYGILLWEIFSlGLNPYPGILVNSKFYKLVKdgYQMAQPAFAPKNIYSIMQACWALEPTHR 900
Cdd:cd05616  183 DWWAFGVLLYEMLA-GQAPFEGEDEDELFQSIME--HNVAYPKSMSKEAVAICKGLMTKHPGKR 243
STKc_PAK6 cd06659
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the ...
762-856 5.48e-10

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: 61.54  E-value: 5.48e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 762 VAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDIMNDsnyIVKGNARLPVK-WMAPESIFDCVYTVQSDVWS 840
Cdd:cd06659  126 VLQALAYLHSQGVIHRDIKSDSILLTLDGRVKLSDFGFCAQISKD---VPKRKSLVGTPyWMAPEVISRCPYGTEVDIWS 202
                         90
                 ....*....|....*.
gi 569026720 841 YGILLWEIFSlGLNPY 856
Cdd:cd06659  203 LGIMVIEMVD-GEPPY 217
STKc_Nek7 cd08229
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
744-901 6.97e-10

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


Pssm-ID: 270866 [Multi-domain]  Cd Length: 292  Bit Score: 61.20  E-value: 6.97e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 744 KEDGRPLELRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARdIMNDSNYIVKGNARLPVkWMA 823
Cdd:cd08229  119 KKQKRLIPEKTVWKYFVQLCSALEHMHSRRVMHRDIKPANVFITATGVVKLGDLGLGR-FFSSKTTAAHSLVGTPY-YMS 196
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 824 PESIFDCVYTVQSDVWSYGILLWEIFSLGlNPYPGILVNskFYKLVKDGYQMAQPAFaPKNIYS-----IMQACWALEPT 898
Cdd:cd08229  197 PERIHENGYNFKSDIWSLGCLLYEMAALQ-SPFYGDKMN--LYSLCKKIEQCDYPPL-PSDHYSeelrqLVNMCINPDPE 272

                 ...
gi 569026720 899 HRP 901
Cdd:cd08229  273 KRP 275
STKc_TEY_MAPK cd07858
Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; ...
757-858 7.76e-10

Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Plant MAPKs are typed based on the conserved phosphorylation motif present in the activation loop, TEY and TDY. This subfamily represents the TEY subtype of plant MAPKs and is further subdivided into three groups (A, B, and C). Group A is represented by AtMPK3, AtMPK6, Nicotiana tabacum BTF4 (NtNTF4), among others. They are mostly involved in environmental and hormonal responses. AtMPK3 and AtMPK6 are also key regulators for stomatal development and patterning. Group B is represented by AtMPK4, AtMPK13, and NtNTF6, among others. They may be involved in both cell division and environmental stress response. AtMPK4 also participates in regulating innate immunity. Group C is represented by AtMPK1, AtMPK2, NtNTF3, Oryza sativa MAPK4 (OsMAPK4), among others. They may also be involved in stress responses. AtMPK1 and AtMPK2 are activated following mechanical injury and in the presence of stress chemicals such as jasmonic acid, hydrogen peroxide and abscisic acid. OsMAPK4 is also called OsMSRMK3 for Multiple Stress-Responsive MAPK3. In plants, MAPKs are associated with physiological, developmental, hormonal, and stress responses. Some plants show numerous gene duplications of MAPKs; Arabidopsis thaliana harbors at least 20 MAPKs, named AtMPK1-20. The TEY MAPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143363 [Multi-domain]  Cd Length: 337  Bit Score: 61.62  E-value: 7.76e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 757 HFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLAR------DIMNDsnYIVkgnarlpVKWM-APESIFD 829
Cdd:cd07858  112 YFLYQLLRGLKYIHSANVLHRDLKPSNLLLNANCDLKICDFGLARttsekgDFMTE--YVV-------TRWYrAPELLLN 182
                         90       100       110
                 ....*....|....*....|....*....|.
gi 569026720 830 CV-YTVQSDVWSYGILLWEIfsLGLNP-YPG 858
Cdd:cd07858  183 CSeYTTAIDVWSVGCIFAEL--LGRKPlFPG 211
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
581-906 8.23e-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: 60.36  E-value: 8.23e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 581 NLQFGKTLGAGAFGKVVEA----TAFGLGkedavLKVAVKmlKSTAHADEKEALMSELKIMSHLgQHENIVNLLGACTHG 656
Cdd:cd14116    6 DFEIGRPLGKGKFGNVYLArekqSKFILA-----LKVLFK--AQLEKAGVEHQLRREVEIQSHL-RHPNILRLYGYFHDA 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 657 GPVLVITEYCCYGDLLNFLRRKaeamlgpslspgqdpeggvdyknihlekkyvrrdSGFSSQGVDTYVemrpvstssnds 736
Cdd:cd14116   78 TRVYLILEYAPLGTVYRELQKL----------------------------------SKFDEQRTATYI------------ 111
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 737 fseqdldkedgrplelrdllhfsSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDIMNDSNYIVKGNar 816
Cdd:cd14116  112 -----------------------TELANALSYCHSKRVIHRDIKPENLLLGSAGELKIADFGWSVHAPSSRRTTLCGT-- 166
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 817 lpVKWMAPESIFDCVYTVQSDVWSYGILLWEiFSLGLNPYPGILVNSKFYKLVKDGYQMaqPAFAPKNIYSIMQACWALE 896
Cdd:cd14116  167 --LDYLPPEMIEGRMHDEKVDLWSLGVLCYE-FLVGKPPFEANTYQETYKRISRVEFTF--PDFVTEGARDLISRLLKHN 241
                        330
                 ....*....|
gi 569026720 897 PTHRPTFQQI 906
Cdd:cd14116  242 PSQRPMLREV 251
STKc_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
757-906 8.28e-10

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


Pssm-ID: 271089 [Multi-domain]  Cd Length: 265  Bit Score: 60.72  E-value: 8.28e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 757 HFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDIMNDSNYiVKGNARLPvKWMAPESIFDCVYTVQS 836
Cdd:cd14187  111 YYLRQIILGCQYLHRNRVIHRDLKLGNLFLNDDMEVKIGDFGLATKVEYDGER-KKTLCGTP-NYIAPEVLSKKGHSFEV 188
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 569026720 837 DVWSYGILLWEIFsLGLNPYPGILVNSKFYKLVKDGYQMaqpafaPKNI----YSIMQACWALEPTHRPTFQQI 906
Cdd:cd14187  189 DIWSIGCIMYTLL-VGKPPFETSCLKETYLRIKKNEYSI------PKHInpvaASLIQKMLQTDPTARPTINEL 255
STKc_nPKC_delta cd05620
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze ...
744-926 9.25e-10

Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-delta plays a role in cell cycle regulation and programmed cell death in many cell types. It slows down cell proliferation, inducing cell cycle arrest and enhancing cell differentiation. PKC-delta is also involved in the regulation of transcription as well as immune and inflammatory responses. It plays a central role in the genotoxic stress response that leads to DNA damaged-induced apoptosis. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. The nPKC-delta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173710 [Multi-domain]  Cd Length: 316  Bit Score: 61.11  E-value: 9.25e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 744 KEDGRpLELRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLT-NGHVaKIGDFGLARDimndsnyIVKGNARLPV--- 819
Cdd:cd05620   88 QDKGR-FDLYRATFYAAEIVCGLQFLHSKGIIYRDLKLDNVMLDrDGHI-KIADFGMCKE-------NVFGDNRASTfcg 158
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 820 --KWMAPESIFDCVYTVQSDVWSYGILLWEIFsLGLNPYPGILVNSKFYKLVKDGYQMaqPAFAPKNIYSIMQACWALEP 897
Cdd:cd05620  159 tpDYIAPEILQGLKYTFSVDWWSFGVLLYEML-IGQSPFHGDDEDELFESIRVDTPHY--PRWITKESKDILEKLFERDP 235
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 569026720 898 THR----------PTFQQICSFLQEQAQED-------RRERDYTNL 926
Cdd:cd05620  236 TRRlgvvgnirghPFFKTINWTALEKRELDppfkpkvKSPSDYSNF 281
PTK_Jak1_rpt1 cd05077
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 1; Jak1 is widely ...
759-906 9.77e-10

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: 60.34  E-value: 9.77e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 759 SSQVAQGMAFLASKNCIHRDVAARNVLLTN-------GHVAKIGDFGLARDIMNDSNYIvkgnARLPvkWMAPESIFDC- 830
Cdd:cd05077  115 AKQLASALSYLEDKDLVHGNVCTKNILLARegidgecGPFIKLSDPGIPITVLSRQECV----ERIP--WIAPECVEDSk 188
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 569026720 831 VYTVQSDVWSYGILLWEIFSLGLNPYPGILVNSK--FYklvKDGYQMAQPAFapKNIYSIMQACWALEPTHRPTFQQI 906
Cdd:cd05077  189 NLSIAADKWSFGTTLWEICYNGEIPLKDKTLAEKerFY---EGQCMLVTPSC--KELADLMTHCMNYDPNQRPFFRAI 261
STKc_myosinIIIA_N cd06638
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze ...
578-848 1.11e-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: 1.11e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 578 PRNNLQFGKTLGAGAFGKVVEAtafgLGKEDAVlKVAVKMLKSTAHADEKeaLMSELKIMSHLGQHENIVNLLGA----- 652
Cdd:cd06638   16 PSDTWEIIETIGKGTYGKVFKV----LNKKNGS-KAAVKILDPIHDIDEE--IEAEYNILKALSDHPNVVKFYGMyykkd 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 653 CTHGGPVLVITEYCCYGDLLNFLRrkaeamlgpslspgqdpeggvdyknihlekkyvrrdsGFSSQGvdtyvemrpvsts 732
Cdd:cd06638   89 VKNGDQLWLVLELCNGGSVTDLVK-------------------------------------GFLKRG------------- 118
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 733 snDSFSEqdldkedgrPLeLRDLLHfssQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDIMNDSnyiVK 812
Cdd:cd06638  119 --ERMEE---------PI-IAYILH---EALMGLQHLHVNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQLTSTR---LR 180
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 569026720 813 GNARLPVK-WMAPESI-----FDCVYTVQSDVWSYGILLWEI 848
Cdd:cd06638  181 RNTSVGTPfWMAPEVIaceqqLDSTYDARCDVWSLGITAIEL 222
STKc_CDK4_6_like cd07838
Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; ...
588-851 1.21e-09

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: 60.37  E-value: 1.21e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 588 LGAGAFGKVVEATAFGLGKEDAVLKVAVkmlkstaHADEKEALMS---ELKIMSHLGQ--HENIVNLLGACThggpvlvi 662
Cdd:cd07838    7 IGEGAYGTVYKARDLQDGRFVALKKVRV-------PLSEEGIPLStirEIALLKQLESfeHPNVVRLLDVCH-------- 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 663 teyccygdllnflrrkaeamlgpslspGQDPEGGVDyknIHLEKKYVRRDsgfssqgVDTYVEMRPvstssndsfsEQDL 742
Cdd:cd07838   72 ---------------------------GPRTDRELK---LTLVFEHVDQD-------LATYLDKCP----------KPGL 104
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 743 DKEdgrplELRDLLHfssQVAQGMAFLASKNCIHRDVAARNVLLTN-GHVaKIGDFGLARDIMNDSnyivkgnARLPVK- 820
Cdd:cd07838  105 PPE-----TIKDLMR---QLLRGLDFLHSHRIVHRDLKPQNILVTSdGQV-KLADFGLARIYSFEM-------ALTSVVv 168
                        250       260       270
                 ....*....|....*....|....*....|....
gi 569026720 821 --WM-APESIFDCVYTVQSDVWSYGILLWEIFSL 851
Cdd:cd07838  169 tlWYrAPEVLLQSSYATPVDMWSVGCIFAELFNR 202
PKc_MKK4 cd06616
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
773-868 1.64e-09

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase Kinase 4; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MKK4 is a dual-specificity PK that phosphorylates and activates the downstream targets, c-Jun N-terminal kinase (JNK) and p38 MAPK, on specific threonine and tyrosine residues. JNK and p38 are collectively known as stress-activated MAPKs, as they are activated in response to a variety of environmental stresses and pro-inflammatory cytokines. Their activation is associated with the induction of cell death. Mice deficient in MKK4 die during embryogenesis and display anemia, severe liver hemorrhage, and abnormal hepatogenesis. MKK4 may also play roles in the immune system and in cardiac hypertrophy. It plays a major role in cancer as a tumor and metastasis suppressor. Under certain conditions, MKK4 is pro-oncogenic. The MKK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270790 [Multi-domain]  Cd Length: 291  Bit Score: 60.07  E-value: 1.64e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 773 NCIHRDVAARNVLLT-NGHVaKIGDFGLardimndSNYIVKGNARL------PvkWMAPESI--FDCV--YTVQSDVWSY 841
Cdd:cd06616  130 KIIHRDVKPSNILLDrNGNI-KLCDFGI-------SGQLVDSIAKTrdagcrP--YMAPERIdpSASRdgYDVRSDVWSL 199
                         90       100
                 ....*....|....*....|....*..
gi 569026720 842 GILLWEIfSLGLNPYPGIlvNSKFYKL 868
Cdd:cd06616  200 GITLYEV-ATGKFPYPKW--NSVFDQL 223
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
583-902 1.92e-09

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: 59.62  E-value: 1.92e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 583 QFGKTLGAGAFGKVVEATAFGLGKEDAVLKVAVKMLKSTAHADEKEalmsELKIMSHLgQHENIVNLLGACTHGGPVLVI 662
Cdd:cd06626    3 QRGNKIGEGTFGKVYTAVNLDTGELMAMKEIRFQDNDPKTIKEIAD----EMKVLEGL-DHPNLVRYYGVEVHREEVYIF 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 663 TEYCCYGDLLNFLRrkaeamlgpslspgqdpEGGVdyknihLEKKYVRRdsgfssqgvdtyvemrpvstssndsfseqdl 742
Cdd:cd06626   78 MEYCQEGTLEELLR-----------------HGRI------LDEAVIRV------------------------------- 103
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 743 dkedgrplelrdllhFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDIMNDSNYIVKGNARLPV--- 819
Cdd:cd06626  104 ---------------YTLQLLEGLAYLHENGIVHRDIKPANIFLDSNGLIKLGDFGSAVKLKNNTTTMAPGEVNSLVgtp 168
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 820 KWMAPESIFDCVYTVQ---SDVWSYGILLWEIFSlGLNPYPGILVN-SKFYKLVkdgyQMAQPAFAPKNIYS-----IMQ 890
Cdd:cd06626  169 AYMAPEVITGNKGEGHgraADIWSLGCVVLEMAT-GKRPWSELDNEwAIMYHVG----MGHKPPIPDSLQLSpegkdFLS 243
                        330
                 ....*....|..
gi 569026720 891 ACWALEPTHRPT 902
Cdd:cd06626  244 RCLESDPKKRPT 255
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
753-908 2.03e-09

Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK6, also called SSTK, is expressed at the head of elongated sperm. It can phosphorylate histones and associate with heat shock protens HSP90 and HSC70. Male mice deficient in TSSK6 are infertile, showing spermatogenic impairment including reduced sperm counts, impaired DNA condensation, abnormal morphology and decreased motility rates. The TSSK6-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271066 [Multi-domain]  Cd Length: 256  Bit Score: 59.49  E-value: 2.03e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 753 RDLLhfsSQVAQGMAFLASKNCIHRDVAARNVLLT-NGHVAKIGDFGLARDIMN--DSNYIVKGNArlpvKWMAPESIFD 829
Cdd:cd14164  103 RDMF---AQMVGAVNYLHDMNIVHRDLKCENILLSaDDRKIKIADFGFARFVEDypELSTTFCGSR----AYTPPEVILG 175
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 830 CVYTVQS-DVWSYGILLWEIFSlGLNPYPGILVNskFYKLVKDGyqmaqpAFAPKNIySIMQACWAL-------EPTHRP 901
Cdd:cd14164  176 TPYDPKKyDVWSLGVVLYVMVT-GTMPFDETNVR--RLRLQQRG------VLYPSGV-ALEEPCRALirtllqfNPSTRP 245

                 ....*..
gi 569026720 902 TFQQICS 908
Cdd:cd14164  246 SIQQVAG 252
STKc_TGFbR_I cd14056
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta family Type ...
586-848 2.20e-09

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: 59.59  E-value: 2.20e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 586 KTLGAGAFGKVveatAFGLGKEDavlKVAVKMLKSTahadEKEALMSELKIMS-HLGQHENIVNLLGA---CTHGGPVL- 660
Cdd:cd14056    1 KTIGKGRYGEV----WLGKYRGE---KVAVKIFSSR----DEDSWFRETEIYQtVMLRHENILGFIAAdikSTGSWTQLw 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 661 VITEYCCYGDLLNFLRRkaeamlgpslspgqdpeggvdyknihlekkyvrrdsgfssqgvdtyvemRPVSTSsndsfseq 740
Cdd:cd14056   70 LITEYHEHGSLYDYLQR-------------------------------------------------NTLDTE-------- 92
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 741 dldkedgrplelrDLLHFSSQVAQGMAFL-------ASKNCI-HRDVAARNVLLTNGHVAKIGDFGLARDIMNDSNYI-V 811
Cdd:cd14056   93 -------------EALRLAYSAASGLAHLhteivgtQGKPAIaHRDLKSKNILVKRDGTCCIADLGLAVRYDSDTNTIdI 159
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 569026720 812 KGNARLPVK-WMAPESIFDCVYT------VQSDVWSYGILLWEI 848
Cdd:cd14056  160 PPNPRVGTKrYMAPEVLDDSINPksfesfKMADIYSFGLVLWEI 203
PK_GC-C cd14044
Pseudokinase domain of the membrane Guanylate Cyclase receptor, GC-C; The pseudokinase domain ...
697-910 2.67e-09

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: 59.13  E-value: 2.67e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 697 VDYKNihLEKKY--VRRDSGFSsqGVDTYVEMRPVSTSSNDSFSeqdldKEDGRPLELRDLLHFSSQVAQGMAFLASKNC 774
Cdd:cd14044   60 IDYYN--LTKFYgtVKLDTMIF--GVIEYCERGSLRDVLNDKIS-----YPDGTFMDWEFKISVMYDIAKGMSYLHSSKT 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 775 -IHRDVAARNVLLTNGHVAKIGDFGlardimndsnyivkGNARLPVK---WMAPESIFDCVYTVQSDVWSYGILLWEIfs 850
Cdd:cd14044  131 eVHGRLKSTNCVVDSRMVVKITDFG--------------CNSILPPSkdlWTAPEHLRQAGTSQKGDVYSYGIIAQEI-- 194
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 851 lglnpypgILVNSKFY---------KLVKDGYQMAQPAFAP-----------KNIYSIMQACWALEPTHRPTFQQICSFL 910
Cdd:cd14044  195 --------ILRKETFYtaacsdrkeKIYRVQNPKGMKPFRPdlnlesagereREVYGLVKNCWEEDPEKRPDFKKIENTL 266
STKc_BMPR2_AMHR2 cd14054
Catalytic domain of the Serine/Threonine Kinases, Bone Morphogenetic Protein and ...
750-858 2.88e-09

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: 59.30  E-value: 2.88e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 750 LELRDLLHFSSQVAQGMAFLAS--------KNCI-HRDVAARNVLLTNGHVAKIGDFGLARDIMNDSNYIVK----GNAR 816
Cdd:cd14054   90 LDWMSSCRMALSLTRGLAYLHTdlrrgdqyKPAIaHRDLNSRNVLVKADGSCVICDFGLAMVLRGSSLVRGRpgaaENAS 169
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 569026720 817 L----PVKWMAPE------SIFDC-VYTVQSDVWSYGILLWEIFSLGLNPYPG 858
Cdd:cd14054  170 IsevgTLRYMAPEvlegavNLRDCeSALKQVDVYALGLVLWEIAMRCSDLYPG 222
STKc_nPKC_theta_like cd05592
Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and ...
758-858 3.08e-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: 59.71  E-value: 3.08e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 758 FSSQVAQGMAFLASKNCIHRDVAARNVLLT-NGHVaKIGDFGLARDIMNDSNyivKGNA--RLPvKWMAPESIFDCVYTV 834
Cdd:cd05592  101 YGAEIICGLQFLHSRGIIYRDLKLDNVLLDrEGHI-KIADFGMCKENIYGEN---KASTfcGTP-DYIAPEILKGQKYNQ 175
                         90       100
                 ....*....|....*....|....
gi 569026720 835 QSDVWSYGILLWEIFsLGLNPYPG 858
Cdd:cd05592  176 SVDWWSFGVLLYEML-IGQSPFHG 198
STKc_MLCK3 cd14192
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze ...
586-858 3.14e-09

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: 58.82  E-value: 3.14e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 586 KTLGAGAFGKVVEATAFGLGkedavLKVAVKMLKSTAhADEKEALMSELKIMSHLgQHENIVNLLGACTHGGPVLVITEY 665
Cdd:cd14192   10 EVLGGGRFGQVHKCTELSTG-----LTLAAKIIKVKG-AKEREEVKNEINIMNQL-NHVNLIQLYDAFESKTNLTLIMEY 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 666 CcygdllnflrrkaeamlgpslspgqdpEGGVDYKNIhlekkyvrrdsgfssqgvdtyvemrpvstsSNDSFSEQDLDke 745
Cdd:cd14192   83 V---------------------------DGGELFDRI------------------------------TDESYQLTELD-- 103
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 746 dgrplelrdLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTN--GHVAKIGDFGLARDIMNDSNyiVKGNARLPvKWMA 823
Cdd:cd14192  104 ---------AILFTRQICEGVHYLHQHYILHLDLKPENILCVNstGNQIKIIDFGLARRYKPREK--LKVNFGTP-EFLA 171
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 569026720 824 PESI-FDCVyTVQSDVWSYGILLWEIFSlGLNPYPG 858
Cdd:cd14192  172 PEVVnYDFV-SFPTDMWSVGVITYMLLS-GLSPFLG 205
PHA02988 PHA02988
hypothetical protein; Provisional
776-910 3.42e-09

hypothetical protein; Provisional


Pssm-ID: 165291 [Multi-domain]  Cd Length: 283  Bit Score: 58.99  E-value: 3.42e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 776 HRDVAARNVLLTNGHVAKIGDFGLARDIMNDSNYIVKGNARLPVKWMapESIFDcVYTVQSDVWSYGILLWEIFSlGLNP 855
Cdd:PHA02988 146 YKNLTSVSFLVTENYKLKIICHGLEKILSSPPFKNVNFMVYFSYKML--NDIFS-EYTIKDDIYSLGVVLWEIFT-GKIP 221
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 569026720 856 YPGILVNSKFYKLVKDGYQMAQPAFAPKNIYSIMQACWALEPTHRPTFQQICSFL 910
Cdd:PHA02988 222 FENLTTKEIYDLIINKNNSLKLPLDCPLEIKCIVEACTSHDSIKRPNIKEILYNL 276
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
588-906 3.64e-09

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: 58.86  E-value: 3.64e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 588 LGAGAFGKVVEATAFGLGKEDavlKVAVKMLKSTAHA----DEKEALMSELKIMSHLgQHENIVNLLGACTHGGPVLVIT 663
Cdd:cd13994    1 IGKGATSVVRIVTKKNPRSGV---LYAVKEYRRRDDEskrkDYVKRLTSEYIISSKL-HHPNIVKVLDLCQDLHGKWCLV 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 664 -EYCCYGDLLnflrrkaeamlgpslspgqdpeggvdyknihlekkyvrrdsgfssqgvdTYVEMRpvstssnDSFSEQDl 742
Cdd:cd13994   77 mEYCPGGDLF-------------------------------------------------TLIEKA-------DSLSLEE- 99
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 743 dkedgrplelRDLLHFssQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDIMN--DSNYIVKGNARLPVK 820
Cdd:cd13994  100 ----------KDCFFK--QILRGVAYLHSHGIAHRDLKPENILLDEDGVLKLTDFGTAEVFGMpaEKESPMSAGLCGSEP 167
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 821 WMAPEsifdcVYTVQS------DVWSYGILLWEIFslgLNPYPGIL--VNSKFYKLVKDGYQMAQPAFAPKNIYSIMQA- 891
Cdd:cd13994  168 YMAPE-----VFTSGSydgravDVWSCGIVLFALF---TGRFPWRSakKSDSAYKAYEKSGDFTNGPYEPIENLLPSECr 239
                        330       340
                 ....*....|....*....|
gi 569026720 892 --CWAL---EPTHRPTFQQI 906
Cdd:cd13994  240 rlIYRMlhpDPEKRITIDEA 259
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
585-895 3.76e-09

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: 58.46  E-value: 3.76e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 585 GKTLGAGAFGKVVEATAFGLGKedavlKVAVKMLKSTAHADE--KEALMSELKIMSHLgQHENIVNLLGACTHGGPVLVI 662
Cdd:cd14162    5 GKTLGHGSYAVVKKAYSTKHKC-----KVAIKIVSKKKAPEDylQKFLPREIEVIKGL-KHPNLICFYEAIETTSRVYII 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 663 TEYCCYGDLLNFLRRKAeamlgpslspgqdpeggvdykniHLEKKYVRRdsgfssqgvdtyvemrpvstssndsfseqdl 742
Cdd:cd14162   79 MELAENGDLLDYIRKNG-----------------------ALPEPQARR------------------------------- 104
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 743 dkedgrplelrdllhFSSQVAQGMAFLASKNCIHRDVAARNVLLT-NGHVaKIGDFGLARDIMNDSNyivkGNARL---- 817
Cdd:cd14162  105 ---------------WFRQLVAGVEYCHSKGVVHRDLKCENLLLDkNNNL-KITDFGFARGVMKTKD----GKPKLsety 164
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 818 --PVKWMAPESIFDCVYTVQ-SDVWSYGILLWEIFSLGLnPYPgilvNSKFYKLVKdgyQMAQPAFAPKNIySIMQACWA 894
Cdd:cd14162  165 cgSYAYASPEILRGIPYDPFlSDIWSMGVVLYTMVYGRL-PFD----DSNLKVLLK---QVQRRVVFPKNP-TVSEECKD 235

                 .
gi 569026720 895 L 895
Cdd:cd14162  236 L 236
STKc_MEKK3_like_u1 cd06653
Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP) ...
581-850 4.61e-09

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


Pssm-ID: 270819 [Multi-domain]  Cd Length: 264  Bit Score: 58.50  E-value: 4.61e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 581 NLQFGKTLGAGAFGKVVEATAFGLGKEDAVLKVAVKMlKSTAHADEKEALMSELKIMSHLgQHENIVnllgacthggpvl 660
Cdd:cd06653    3 NWRLGKLLGRGAFGEVYLCYDADTGRELAVKQVPFDP-DSQETSKEVNALECEIQLLKNL-RHDRIV------------- 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 661 vitEYccYGDLlnflrrkaeamlgpslspgQDPEggvdyknihlEKKyvrrdsgfssqgVDTYVEMRPVSTSSNDSFSEQ 740
Cdd:cd06653   68 ---QY--YGCL-------------------RDPE----------EKK------------LSIFVEYMPGGSVKDQLKAYG 101
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 741 DLDKEDGRplelrdllHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDIMN--DSNYIVKGNARLP 818
Cdd:cd06653  102 ALTENVTR--------RYTRQILQGVSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRIQTicMSGTGIKSVTGTP 173
                        250       260       270
                 ....*....|....*....|....*....|..
gi 569026720 819 VkWMAPESIFDCVYTVQSDVWSYGILLWEIFS 850
Cdd:cd06653  174 Y-WMSPEVISGEGYGRKADVWSVACTVVEMLT 204
STKc_MELK cd14078
Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; ...
586-908 5.14e-09

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: 58.16  E-value: 5.14e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 586 KTLGAGAFGKVVEATAFGLGKedavlKVAVKMLKSTAHADEKEALMSELKIMSHLgQHENIVNLLGACTHGGPVLVITEY 665
Cdd:cd14078    9 ETIGSGGFAKVKLATHILTGE-----KVAIKIMDKKALGDDLPRVKTEIEALKNL-SHQHICRLYHVIETDNKIFMVLEY 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 666 CCYGDLLNFLrrkaeamlgpslspgqdpeggvdyknihlekkyVRRDSgfssqgvdtyvemrpvstssndsfseqdLDKE 745
Cdd:cd14078   83 CPGGELFDYI---------------------------------VAKDR----------------------------LSED 101
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 746 DGRplelrdllHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLA---RDIMNDSNYIVKGNArlpvKWM 822
Cdd:cd14078  102 EAR--------VFFRQIVSAVAYVHSQGYAHRDLKPENLLLDEDQNLKLIDFGLCakpKGGMDHHLETCCGSP----AYA 169
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 823 APESIFDCVYT-VQSDVWSYGILLWEIFSlGLNPYPGILVnSKFYKLVKDGyQMAQPAFAPKNIYSIMQACWALEPTHRP 901
Cdd:cd14078  170 APELIQGKPYIgSEADVWSMGVLLYALLC-GFLPFDDDNV-MALYRKIQSG-KYEEPEWLSPSSKLLLDQMLQVDPKKRI 246

                 ....*..
gi 569026720 902 TFQQICS 908
Cdd:cd14078  247 TVKELLN 253
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
757-850 6.17e-09

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: 58.07  E-value: 6.17e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 757 HFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLAR----------DIMNDSNYIVKGNARLPVK----WM 822
Cdd:cd14010   98 KFGRDLVRGLHYIHSKGIIYCDLKPSNILLDGNGTLKLSDFGLARregeilkelfGQFSDEGNVNKVSKKQAKRgtpyYM 177
                         90       100
                 ....*....|....*....|....*...
gi 569026720 823 APESIFDCVYTVQSDVWSYGILLWEIFS 850
Cdd:cd14010  178 APELFQGGVHSFASDLWALGCVLYEMFT 205
STKc_CASK cd14094
Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein ...
757-905 6.35e-09

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: 58.32  E-value: 6.35e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 757 HFSSQVAQGMAFLASKNCIHRDVAARNVLLT---NGHVAKIGDFGLARDiMNDSNYIVKGNARLPvKWMAPESIFDCVYT 833
Cdd:cd14094  113 HYMRQILEALRYCHDNNIIHRDVKPHCVLLAskeNSAPVKLGGFGVAIQ-LGESGLVAGGRVGTP-HFMAPEVVKREPYG 190
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 569026720 834 VQSDVWSYGILLWEIFSlGLNPYPGilVNSKFYKLVK------DGYQMAQPAFAPKNIYSIMqacWALEPTHRPTFQQ 905
Cdd:cd14094  191 KPVDVWGCGVILFILLS-GCLPFYG--TKERLFEGIIkgkykmNPRQWSHISESAKDLVRRM---LMLDPAERITVYE 262
STKc_TNIK cd06637
Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs ...
747-916 6.40e-09

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: 58.19  E-value: 6.40e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 747 GRPLELRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDImndSNYIVKGNARLPVK-WMAPE 825
Cdd:cd06637  105 GNTLKEEWIAYICREILRGLSHLHQHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQL---DRTVGRRNTFIGTPyWMAPE 181
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 826 SIF-----DCVYTVQSDVWSYGILLWEIfSLGLNPYPGILVNSKFYKLVKDGYQMAQPAFAPKNIYSIMQACWALEPTHR 900
Cdd:cd06637  182 VIAcdenpDATYDFKSDLWSLGITAIEM-AEGAPPLCDMHPMRALFLIPRNPAPRLKSKKWSKKFQSFIESCLVKNHSQR 260
                        170
                 ....*....|....*...
gi 569026720 901 PTFQQICS--FLQEQAQE 916
Cdd:cd06637  261 PSTEQLMKhpFIRDQPNE 278
STKc_PAK2 cd06655
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the ...
578-856 6.85e-09

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: 58.20  E-value: 6.85e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 578 PRNNLQFGKTLGAGAFGKVVEATAFGLGKEDAVLKVAVKmlkstaHADEKEALMSELKIMSHLgQHENIVNLLGACTHGG 657
Cdd:cd06655   17 PKKKYTRYEKIGQGASGTVFTAIDVATGQEVAIKQINLQ------KQPKKELIINEILVMKEL-KNPNIVNFLDSFLVGD 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 658 PVLVITEYCCYGDLlnflrrkaeamlgpslspgqdpeggvdyknihlekkyvrrdsgfssqgvdtyvemrpvstssNDSF 737
Cdd:cd06655   90 ELFVVMEYLAGGSL--------------------------------------------------------------TDVV 107
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 738 SEQDLDKEDgrplelrdLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDIMNDSNYivKGNARL 817
Cdd:cd06655  108 TETCMDEAQ--------IAAVCRECLQALEFLHANQVIHRDIKSDNVLLGMDGSVKLTDFGFCAQITPEQSK--RSTMVG 177
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 569026720 818 PVKWMAPESIFDCVYTVQSDVWSYGILLWEIFSlGLNPY 856
Cdd:cd06655  178 TPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVE-GEPPY 215
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
579-908 7.34e-09

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: 57.66  E-value: 7.34e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 579 RNNLQFGKTLGAGAFGKVVEAtafglgKEDAVLKVAVKMLKSTAHADEKEAL--MSELKIMSHLgQHENIVNLLGACTHG 656
Cdd:cd14161    2 KHRYEFLETLGKGTYGRVKKA------RDSSGRLVAIKSIRKDRIKDEQDLLhiRREIEIMSSL-NHPHIISVYEVFENS 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 657 GPVLVITEYCCYGDLLNFLRRKaeamlgpslspgqdpeggvdyknihlekkyvrrdsgfssqgvdtyvemrpvstssnds 736
Cdd:cd14161   75 SKIVIVMEYASRGDLYDYISER---------------------------------------------------------- 96
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 737 fseQDLDKEDGRplelrdllHFSSQVAQGMAFLASKNCIHRDVAARNVLL-TNGHVaKIGDFGLArDIMNDSNYIvKGNA 815
Cdd:cd14161   97 ---QRLSELEAR--------HFFRQIVSAVHYCHANGIVHRDLKLENILLdANGNI-KIADFGLS-NLYNQDKFL-QTYC 162
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 816 RLPVkWMAPESIFDCVYT-VQSDVWSYGILLWeIFSLGLNPYPGilvnSKFYKLVKdgyQMAQPAF----APKNIYSIMQ 890
Cdd:cd14161  163 GSPL-YASPEIVNGRPYIgPEVDSWSLGVLLY-ILVHGTMPFDG----HDYKILVK---QISSGAYreptKPSDACGLIR 233
                        330
                 ....*....|....*...
gi 569026720 891 ACWALEPTHRPTFQQICS 908
Cdd:cd14161  234 WLLMVNPERRATLEDVAS 251
STKc_IKK cd13989
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
588-856 7.47e-09

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: 58.23  E-value: 7.47e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 588 LGAGAFGKVVeatafgLGK-EDAVLKVAVKM--LKSTAHADEKEALMSELKIMSHLgQHENIVN-------LLGACTHGG 657
Cdd:cd13989    1 LGSGGFGYVT------LWKhQDTGEYVAIKKcrQELSPSDKNRERWCLEVQIMKKL-NHPNVVSardvppeLEKLSPNDL 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 658 PVLVItEYCCYGDLLNFLRRkaeamlgpslspgqdPEggvdyknihlekkyvrrdsgfSSQGVdtyvemrpvstssndsf 737
Cdd:cd13989   74 PLLAM-EYCSGGDLRKVLNQ---------------PE---------------------NCCGL----------------- 99
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 738 seqdldKEdgrpLELRDLLhfsSQVAQGMAFLASKNCIHRDVAARNVLLTNGH---VAKIGDFGLARDIMNDSNyivkgN 814
Cdd:cd13989  100 ------KE----SEVRTLL---SDISSAISYLHENRIIHRDLKPENIVLQQGGgrvIYKLIDLGYAKELDQGSL-----C 161
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 569026720 815 ARL--PVKWMAPESIFDCVYTVQSDVWSYGILLWEIFSlGLNPY 856
Cdd:cd13989  162 TSFvgTLQYLAPELFESKKYTCTVDYWSFGTLAFECIT-GYRPF 204
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
757-856 7.98e-09

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: 57.61  E-value: 7.98e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 757 HFSSQVAQGMAFLASKNCIHRDVAARNVLLT-NGHVaKIGDFGLAR-DIMNDSNYIVKGNARLPVK------------WM 822
Cdd:cd05579   97 IYIAEIVLALEYLHSHGIIHRDLKPDNILIDaNGHL-KLTDFGLSKvGLVRRQIKLSIQKKSNGAPekedrrivgtpdYL 175
                         90       100       110
                 ....*....|....*....|....*....|....
gi 569026720 823 APESIFDCVYTVQSDVWSYGILLWEiFSLGLNPY 856
Cdd:cd05579  176 APEILLGQGHGKTVDWWSLGVILYE-FLVGIPPF 208
STKc_ACVR1_ALK1 cd14142
Catalytic domain of the Serine/Threonine Kinases, Activin Type I Receptor and Activin ...
749-848 8.55e-09

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


Pssm-ID: 271044 [Multi-domain]  Cd Length: 298  Bit Score: 57.84  E-value: 8.55e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 749 PLELRDLLHFSSQVAQGMAFL-------ASKNCI-HRDVAARNVLLTNGHVAKIGDFGLARDIMNDSNYI-VKGNARLPV 819
Cdd:cd14142   98 TLDHQEMLRLALSAASGLVHLhteifgtQGKPAIaHRDLKSKNILVKSNGQCCIADLGLAVTHSQETNQLdVGNNPRVGT 177
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 569026720 820 K-WMAPE--------SIFDCVYtvQSDVWSYGILLWEI 848
Cdd:cd14142  178 KrYMAPEvldetintDCFESYK--RVDIYAFGLVLWEV 213
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
583-906 8.62e-09

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: 57.41  E-value: 8.62e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 583 QFGKTLGAGAFGKVVEATAFGLGKedavlKVAVKMLKSTAHADEK--EALMSELKIMSHLgQHENIVNL---LGACTHgg 657
Cdd:cd14663    3 ELGRTLGEGTFAKVKFARNTKTGE-----SVAIKIIDKEQVAREGmvEQIKREIAIMKLL-RHPNIVELhevMATKTK-- 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 658 pVLVITEYCCYGDLLNFLrrkaeamlgpslspgqdpeggvdyknihlekkyvrrdsgfssqgvdtyvemrpvstSSNDSF 737
Cdd:cd14663   75 -IFFVMELVTGGELFSKI--------------------------------------------------------AKNGRL 97
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 738 SEqdldkEDGRplelrdllHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLArdIMNDSNyivKGNARL 817
Cdd:cd14663   98 KE-----DKAR--------KYFQQLIDAVDYCHSRGVFHRDLKPENLLLDEDGNLKISDFGLS--ALSEQF---RQDGLL 159
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 818 PVK-----WMAPESIFDCVYT-VQSDVWSYGILLWEIFSlGLNPYPGILVNSKFYKLVKDGYQMaqPAFAPKNIYSIMQA 891
Cdd:cd14663  160 HTTcgtpnYVAPEVLARRGYDgAKADIWSCGVILFVLLA-GYLPFDDENLMALYRKIMKGEFEY--PRWFSPGAKSLIKR 236
                        330
                 ....*....|....*
gi 569026720 892 CWALEPTHRPTFQQI 906
Cdd:cd14663  237 ILDPNPSTRITVEQI 251
PTZ00283 PTZ00283
serine/threonine protein kinase; Provisional
761-902 8.95e-09

serine/threonine protein kinase; Provisional


Pssm-ID: 240344 [Multi-domain]  Cd Length: 496  Bit Score: 59.11  E-value: 8.95e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 761 QVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDIMND-SNYIVKGNARLPVkWMAPESIFDCVYTVQSDVW 839
Cdd:PTZ00283 151 QVLLAVHHVHSKHMIHRDIKSANILLCSNGLVKLGDFGFSKMYAATvSDDVGRTFCGTPY-YVAPEIWRRKPYSKKADMF 229
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 569026720 840 SYGILLWEIFSLGlNPYPGILVNSKFYKLVKDGYQMAQPAFAPKnIYSIMQACWALEPTHRPT 902
Cdd:PTZ00283 230 SLGVLLYELLTLK-RPFDGENMEEVMHKTLAGRYDPLPPSISPE-MQEIVTALLSSDPKRRPS 290
PK_GC-2D cd14043
Pseudokinase domain of the membrane Guanylate Cyclase receptor, GC-2D; The pseudokinase domain ...
764-906 9.68e-09

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: 57.42  E-value: 9.68e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 764 QGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLArDIMNDSNYIVKGNARLPVKWMAPESIFDCVY----TVQSDVW 839
Cdd:cd14043  108 KGMRYLHHRGIVHGRLKSRNCVVDGRFVLKITDYGYN-EILEAQNLPLPEPAPEELLWTAPELLRDPRLerrgTFPGDVF 186
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 569026720 840 SYGILLWEIFS-------LGLNPYPGILVNSKFYKLVKDGYQMAQpafAPKNIYSIMQACWALEPTHRPTFQQI 906
Cdd:cd14043  187 SFAIIMQEVIVrgapycmLGLSPEEIIEKVRSPPPLCRPSVSMDQ---APLECIQLMKQCWSEAPERRPTFDQI 257
STKc_Pho85 cd07836
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; ...
737-858 9.96e-09

Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Pho85 is a multifunctional CDK in yeast. It is regulated by 10 different cyclins (Pcls) and plays a role in G1 progression, cell polarity, phosphate and glycogen metabolism, gene expression, and in signaling changes in the environment. It is not essential for yeast viability and is the functional homolog of mammalian CDK5, which plays a role in central nervous system development. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The Pho85 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143341 [Multi-domain]  Cd Length: 284  Bit Score: 57.49  E-value: 9.96e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 737 FSEQDLDK-----EDGRPLELRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDI---MND-S 807
Cdd:cd07836   79 YMDKDLKKymdthGVRGALDPNTVKSFTYQLLKGIAFCHENRVLHRDLKPQNLLINKRGELKLADFGLARAFgipVNTfS 158
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 569026720 808 NYIVKGNARLPVKWMAPEsifdcVYTVQSDVWSYGILLWEIFSlGLNPYPG 858
Cdd:cd07836  159 NEVVTLWYRAPDVLLGSR-----TYSTSIDIWSVGCIMAEMIT-GRPLFPG 203
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
202-282 1.08e-08

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 433584 [Multi-domain]  Cd Length: 75  Bit Score: 52.59  E-value: 1.08e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720  202 PPALTLVPAELVRIRGEAAQIVCSASSVDVNfDVFLQHNNTKLaipqqSDFHNNRYQKVLTLNLDQVDFQHAGNYSCVAS 281
Cdd:pfam13927   1 KPVITVSPSSVVVVEGETVTLTCEASGSPPP-TITWYKNGGKL-----SSGRTSLVGGNGTLTISNVTREDSGTYTCTAS 74

                  .
gi 569026720  282 N 282
Cdd:pfam13927  75 N 75
STKc_nPKC_eta cd05590
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the ...
586-900 1.20e-08

Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-eta is predominantly expressed in squamous epithelia, where it plays a crucial role in the signaling of cell-type specific differentiation. It is also expressed in pro-B cells and early-stage thymocytes, and acts as a key regulator in early B-cell development. PKC-eta increases glioblastoma multiforme (GBM) proliferation and resistance to radiation, and is being developed as a therapeutic target for the management of GBM. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. The nPKC-eta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270742 [Multi-domain]  Cd Length: 323  Bit Score: 57.61  E-value: 1.20e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 586 KTLGAGAFGKVVEATAfglgKEDAVLkVAVKMLKSTA--HADEKEALMSELKIMSHLGQHENIVNLlgacthggpvlvit 663
Cdd:cd05590    1 RVLGKGSFGKVMLARL----KESGRL-YAVKVLKKDVilQDDDVECTMTEKRILSLARNHPFLTQL-------------- 61
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 664 eYCCYG--DLLNFLrrkAEAMLGPSLSpgqdpeggvdyknIHLEKKyvRRdsgfssqgvdtyvemrpvstssndsfseqd 741
Cdd:cd05590   62 -YCCFQtpDRLFFV---MEFVNGGDLM-------------FHIQKS--RR------------------------------ 92
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 742 LDKEDGRplelrdllHFSSQVAQGMAFLASKNCIHRDVAARNVLLTN-GHvAKIGDFGLARDIMNDSnyIVKGNARLPVK 820
Cdd:cd05590   93 FDEARAR--------FYAAEITSALMFLHDKGIIYRDLKLDNVLLDHeGH-CKLADFGMCKEGIFNG--KTTSTFCGTPD 161
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 821 WMAPESIFDCVYTVQSDVWSYGILLWEIFSlGLNPYPGILVNSKFYKLVKDgyQMAQPAFAPKNIYSIMQACWALEPTHR 900
Cdd:cd05590  162 YIAPEILQEMLYGPSVDWWAMGVLLYEMLC-GHAPFEAENEDDLFEAILND--EVVYPTWLSQDAVDILKAFMTKNPTMR 238
STKc_RIP2 cd14026
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 2; STKs catalyze ...
588-903 1.31e-08

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: 57.24  E-value: 1.31e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 588 LGAGAFGKVVEATafglgKEDAVLKVAVKMLK--STAHADEKEALMSELKIMsHLGQHENIVNLLGACTHGGPVLVITEY 665
Cdd:cd14026    5 LSRGAFGTVSRAR-----HADWRVTVAIKCLKldSPVGDSERNCLLKEAEIL-HKARFSYILPILGICNEPEFLGIVTEY 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 666 CCYGDLLNFLRRKAEamlgpslspgqdpeggvdYKNIhlekkyvrrdsgfssqgvdtyvemrpvstssndsfseqdldke 745
Cdd:cd14026   79 MTNGSLNELLHEKDI------------------YPDV------------------------------------------- 97
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 746 dGRPLELRdLLHfssQVAQGMAFLASKN--CIHRDVAARNVLLTNGHVAKIGDFGLAR-DIMNDSNyiVKGNARLP---- 818
Cdd:cd14026   98 -AWPLRLR-ILY---EIALGVNYLHNMSppLLHHDLKTQNILLDGEFHVKIADFGLSKwRQLSISQ--SRSSKSAPeggt 170
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 819 VKWMAPESIFDCVYT---VQSDVWSYGILLWEI------FSLGLNPYPGILVNSKFYKLV--KDGYQMAQPAFApkNIYS 887
Cdd:cd14026  171 IIYMPPEEYEPSQKRrasVKHDIYSYAIIMWEVlsrkipFEEVTNPLQIMYSVSQGHRPDtgEDSLPVDIPHRA--TLIN 248
                        330
                 ....*....|....*.
gi 569026720 888 IMQACWALEPTHRPTF 903
Cdd:cd14026  249 LIESGWAQNPDERPSF 264
STKc_cPKC cd05587
Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; ...
758-858 1.47e-08

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: 57.40  E-value: 1.47e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 758 FSSQVAQGMAFLASKNCIHRDVAARNVLL-TNGHVaKIGDFGLARDIMNDS----------NYIvkgnarlpvkwmAPES 826
Cdd:cd05587  102 YAAEIAVGLFFLHSKGIIYRDLKLDNVMLdAEGHI-KIADFGMCKEGIFGGkttrtfcgtpDYI------------APEI 168
                         90       100       110
                 ....*....|....*....|....*....|..
gi 569026720 827 IFDCVYTVQSDVWSYGILLWEIFSlGLNPYPG 858
Cdd:cd05587  169 IAYQPYGKSVDWWAYGVLLYEMLA-GQPPFDG 199
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
585-906 1.80e-08

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: 56.49  E-value: 1.80e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 585 GKTLGAGAFGKVVEATAFGLGKedavlKVAVKML-KSTAHADEKEA-LMSELKIMShLGQHENIVNLLGACTHGGPVLVI 662
Cdd:cd14081    6 GKTLGKGQTGLVKLAKHCVTGQ-----KVAIKIVnKEKLSKESVLMkVEREIAIMK-LIEHPNVLKLYDVYENKKYLYLV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 663 TEYCCYGDLLNFLRRKaeamlgpslspgqdpeggvdyknihlekkyvrrdsgfssqgvdtyvemrpvstssndsfseqdl 742
Cdd:cd14081   80 LEYVSGGELFDYLVKK---------------------------------------------------------------- 95
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 743 dkedgRPLELRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDIMNDSnyIVKGNARLPvKWM 822
Cdd:cd14081   96 -----GRLTEKEARKFFRQIISALDYCHSHSICHRDLKPENLLLDEKNNIKIADFGMASLQPEGS--LLETSCGSP-HYA 167
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 823 APESIFDCVYT-VQSDVWSYGILLWEIFSlGLNPYPGILVNSKFYKlVKDG-YQMaqPAFAPKNIYSIMQACWALEPTHR 900
Cdd:cd14081  168 CPEVIKGEKYDgRKADIWSCGVILYALLV-GALPFDDDNLRQLLEK-VKRGvFHI--PHFISPDAQDLLRRMLEVNPEKR 243

                 ....*.
gi 569026720 901 PTFQQI 906
Cdd:cd14081  244 ITIEEI 249
PK_KSR2 cd14153
Pseudokinase domain of Kinase Suppressor of Ras 2; The pseudokinase domain shows similarity to ...
582-912 1.92e-08

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: 56.56  E-value: 1.92e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 582 LQFGKTLGAGAFGKVVEATAFGlgkedavlKVAVKMLKstAHADEKEALMS-ELKIMSHLG-QHENIVNLLGACTHGgPV 659
Cdd:cd14153    2 LEIGELIGKGRFGQVYHGRWHG--------EVAIRLID--IERDNEEQLKAfKREVMAYRQtRHENVVLFMGACMSP-PH 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 660 LVITEYCCYGDLLNFLRRKAEAMLgpslspgqdpeggvdyknihlekkyvrrdsgfssqgvdtyvemrpvstssndsfse 739
Cdd:cd14153   71 LAIITSLCKGRTLYSVVRDAKVVL-------------------------------------------------------- 94
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 740 qDLDKEDgrplelrdllHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAkIGDFGLardiMNDSNYIVKGNA---- 815
Cdd:cd14153   95 -DVNKTR----------QIAQEIVKGMGYLHAKGILHKDLKSKNVFYDNGKVV-ITDFGL----FTISGVLQAGRRedkl 158
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 816 RLPVKW---MAPESIFDCV---------YTVQSDVWSYGILLWEIFSLGLnPYPGILVNSKFYKLVKDGYQMAQPAFAPK 883
Cdd:cd14153  159 RIQSGWlchLAPEIIRQLSpeteedklpFSKHSDVFAFGTIWYELHAREW-PFKTQPAEAIIWQVGSGMKPNLSQIGMGK 237
                        330       340
                 ....*....|....*....|....*....
gi 569026720 884 NIYSIMQACWALEPTHRPTFQQICSFLQE 912
Cdd:cd14153  238 EISDILLFCWAYEQEERPTFSKLMEMLEK 266
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
612-856 1.95e-08

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: 56.60  E-value: 1.95e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 612 KVAVK---MLKSTAHADEkeaLMSELKIMShLGQHENIVNLLGACTHGGPVLVITEYCCYGDLLNFLRRKAeamlgpsls 688
Cdd:cd06610   28 KVAIKridLEKCQTSMDE---LRKEIQAMS-QCNHPNVVSYYTSFVVGDELWLVMPLLSGGSLLDIMKSSY--------- 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 689 pgqdPEGGVDYKNIhlekkyvrrdsgfssqgvdtyvemrpvSTSsndsfseqdldkedgrpleLRDLLhfssqvaQGMAF 768
Cdd:cd06610   95 ----PRGGLDEAII---------------------------ATV-------------------LKEVL-------KGLEY 117
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 769 LASKNCIHRDVAARNVLL-TNGHVaKIGDFGLARDIMndSNYIVKGNARLPVK----WMAPESIF-DCVYTVQSDVWSYG 842
Cdd:cd06610  118 LHSNGQIHRDVKAGNILLgEDGSV-KIADFGVSASLA--TGGDRTRKVRKTFVgtpcWMAPEVMEqVRGYDFKADIWSFG 194
                        250
                 ....*....|....
gi 569026720 843 ILLWEIfSLGLNPY 856
Cdd:cd06610  195 ITAIEL-ATGAAPY 207
STKc_TSSK1_2-like cd14165
Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; ...
585-856 1.99e-08

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: 56.33  E-value: 1.99e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 585 GKTLGAGAFGKVVEATAFGLGKEdavlkVAVKML-KSTAHADEKEA-LMSELKIMSHLgQHENIVNLLGAC-THGGPVLV 661
Cdd:cd14165    6 GINLGEGSYAKVKSAYSERLKCN-----VAIKIIdKKKAPDDFVEKfLPRELEILARL-NHKSIIKTYEIFeTSDGKVYI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 662 ITEYCCYGDLLNFLRRKaeamlgpslspGQDPEggvdykniHLEKKYVRrdsgfssqgvdtyvemrpvstssndsfseqd 741
Cdd:cd14165   80 VMELGVQGDLLEFIKLR-----------GALPE--------DVARKMFH------------------------------- 109
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 742 ldkedgrplelrdllhfssQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDIMNDSNyivkGNARL---- 817
Cdd:cd14165  110 -------------------QLSSAIKYCHELDIVHRDLKCENLLLDKDFNIKLTDFGFSKRCLRDEN----GRIVLsktf 166
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 569026720 818 --PVKWMAPESIFDCVYTVQ-SDVWSYGILLWeIFSLGLNPY 856
Cdd:cd14165  167 cgSAAYAAPEVLQGIPYDPRiYDIWSLGVILY-IMVCGSMPY 207
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
752-906 2.14e-08

Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or General Control Non-derepressible-2; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the overall downregulation of protein synthesis. eIF-2 phosphorylation is induced in response to cellular stresses including virus infection, heat shock, nutrient deficiency, and the accummulation of unfolded proteins, among others. There are four distinct kinases that phosphorylate eIF-2 and control protein synthesis under different stress conditions: GCN2, protein kinase regulated by RNA (PKR), heme-regulated inhibitor kinase (HRI), and PKR-like endoplasmic reticulum kinase (PERK). GCN2 is activated by amino acid or serum starvation and UV irradiation. It induces GCN4, a transcriptional activator of amino acid biosynthetic genes, leading to increased production of amino acids under amino acid-deficient conditions. In serum-starved cells, GCN2 activation induces translation of the stress-responsive transcription factor ATF4, while under UV stress, GCN2 triggers transcriptional rescue via NF-kappaB signaling. GCN2 contains an N-terminal RWD, a degenerate kinase-like (repeat 1), the catalytic kinase (repeat 2), a histidyl-tRNA synthetase (HisRS)-like, and a C-terminal ribosome-binding and dimerization (RB/DD) domains. The degenerate pseudokinase domain of GCN2 may function as a regulatory domain. The GCN2 subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270914 [Multi-domain]  Cd Length: 254  Bit Score: 56.21  E-value: 2.14e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 752 LRDLL------------HFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGH---VAKIGDFGLARDImNDSNYIVKGNAR 816
Cdd:cd14012   91 LSELLdsvgsvpldtarRWTLQLLEALEYLHRNGVVHKSLHAGNVLLDRDAgtgIVKLTDYSLGKTL-LDMCSRGSLDEF 169
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 817 LPVKWMAPESI-FDCVYTVQSDVWSYGILL---------WEIFSlGLNPYPGILVNSK-FYKLVkdgyqmaqpafapkni 885
Cdd:cd14012  170 KQTYWLPPELAqGSKSPTRKTDVWDLGLLFlqmlfgldvLEKYT-SPNPVLVSLDLSAsLQDFL---------------- 232
                        170       180
                 ....*....|....*....|.
gi 569026720 886 ysimQACWALEPTHRPTFQQI 906
Cdd:cd14012  233 ----SKCLSLDPKKRPTALEL 249
PKc_TOPK cd14001
Catalytic domain of the Dual-specificity protein kinase, Lymphokine-activated killer ...
723-911 2.29e-08

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: 56.64  E-value: 2.29e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 723 YVEMRPVSTSSNDSFsEQDLDKEDGrPLELRDLLHFSSQVAQGMAFLAS-KNCIHRDVAARNVLLTNG-HVAKIGDFGLA 800
Cdd:cd14001   82 CLAMEYGGKSLNDLI-EERYEAGLG-PFPAATILKVALSIARALEYLHNeKKILHGDIKSGNVLIKGDfESVKLCDFGVS 159
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 801 RDIMNDSNYIVKGNARL----PvkWMAPESIF-DCVYTVQSDVWSYGILLWEIFSLgLNPYPGILVNSKFY--------K 867
Cdd:cd14001  160 LPLTENLEVDSDPKAQYvgteP--WKAKEALEeGGVITDKADIFAYGLVLWEMMTL-SVPHLNLLDIEDDDedesfdedE 236
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 569026720 868 LVKDGYQMAQPAFAPKNIYSIMQ----------ACWALEPTHRPTFQQICSFLQ 911
Cdd:cd14001  237 EDEEAYYGTLGTRPALNLGELDDsyqkvielfyACTQEDPKDRPSAAHIVEALE 290
STKc_MAP4K4_6_N cd06636
N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase ...
757-848 2.41e-08

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: 56.55  E-value: 2.41e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 757 HFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFG----LARDIMNDSNYIvkGNARlpvkWMAPESIF---- 828
Cdd:cd06636  125 YICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGvsaqLDRTVGRRNTFI--GTPY----WMAPEVIAcden 198
                         90       100
                 ....*....|....*....|.
gi 569026720 829 -DCVYTVQSDVWSYGILLWEI 848
Cdd:cd06636  199 pDATYDYRSDIWSLGITAIEM 219
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
755-906 2.90e-08

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 56.76  E-value: 2.90e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 755 LLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLAR---DIMNDSNYIVKGNArlpvkWMAPESI---- 827
Cdd:PLN00034 170 LADVARQILSGIAYLHRRHIVHRDIKPSNLLINSAKNVKIADFGVSRilaQTMDPCNSSVGTIA-----YMSPERIntdl 244
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 828 FDCVYT-VQSDVWSYGILLWEiFSLGLNPYPgilvnskfykLVKDG--------YQMAQPAFAPKN----IYSIMQACWA 894
Cdd:PLN00034 245 NHGAYDgYAGDIWSLGVSILE-FYLGRFPFG----------VGRQGdwaslmcaICMSQPPEAPATasreFRHFISCCLQ 313
                        170
                 ....*....|..
gi 569026720 895 LEPTHRPTFQQI 906
Cdd:PLN00034 314 REPAKRWSAMQL 325
STKc_PAK_I cd06647
Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze ...
588-856 3.05e-08

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: 55.70  E-value: 3.05e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 588 LGAGAFGKVVEATAFGLGKEdavlkVAVKMLkSTAHADEKEALMSELKIMSHLgQHENIVNLLGACTHGGPVLVITEYCC 667
Cdd:cd06647   15 IGQGASGTVYTAIDVATGQE-----VAIKQM-NLQQQPKKELIINEILVMREN-KNPNIVNYLDSYLVGDELWVVMEYLA 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 668 YGDLlnflrrkaeamlgpslspgqdpeggvdyknihlekkyvrrdsgfssqgvdtyvemrpvstssNDSFSEQDLDkeDG 747
Cdd:cd06647   88 GGSL--------------------------------------------------------------TDVVTETCMD--EG 103
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 748 RplelrdLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDIMNDSNyivKGNARLPVK-WMAPES 826
Cdd:cd06647  104 Q------IAAVCRECLQALEFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQS---KRSTMVGTPyWMAPEV 174
                        250       260       270
                 ....*....|....*....|....*....|
gi 569026720 827 IFDCVYTVQSDVWSYGILLWEIFSlGLNPY 856
Cdd:cd06647  175 VTRKAYGPKVDIWSLGIMAIEMVE-GEPPY 203
STKc_BUR1 cd07866
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), ...
761-849 3.11e-08

Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), Bypass UAS Requirement 1, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BUR1, also called SGV1, is a yeast CDK that is functionally equivalent to mammalian CDK9. It associates with the cyclin BUR2. BUR genes were orginally identified in a genetic screen as factors involved in general transcription. The BUR1/BUR2 complex phosphorylates the C-terminal domain of RNA polymerase II. In addition, this complex regulates histone modification by phosporylating Rad6 and mediating the association of the Paf1 complex with chromatin. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The BUR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270849 [Multi-domain]  Cd Length: 311  Bit Score: 56.17  E-value: 3.11e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 761 QVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDIMNDS---NYIVKGNAR----LPV-KWM-APESIF-DC 830
Cdd:cd07866  123 QLLEGINYLHENHILHRDIKAANILIDNQGILKIADFGLARPYDGPPpnpKGGGGGGTRkytnLVVtRWYrPPELLLgER 202
                         90
                 ....*....|....*....
gi 569026720 831 VYTVQSDVWSYGILLWEIF 849
Cdd:cd07866  203 RYTTAVDIWGIGCVFAEMF 221
PTK_Tyk2_rpt1 cd05076
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; Tyk2 is ...
720-906 3.16e-08

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: 56.07  E-value: 3.16e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 720 VDTYVEMRPVstssnDSFseqdLDKEDGR-PLELRDLLhfSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVA------ 792
Cdd:cd05076   93 VEEFVEHGPL-----DVW----LRKEKGHvPMAWKFVV--ARQLASALSYLENKNLVHGNVCAKNILLARLGLEegtspf 161
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 793 -KIGDFGLARDIMNDSNYIvkgnARLPvkWMAPEsifdCVYTVQS-----DVWSYGILLWEIFSLGLNPYPGILVNSK-- 864
Cdd:cd05076  162 iKLSDPGVGLGVLSREERV----ERIP--WIAPE----CVPGGNSlstaaDKWGFGATLLEICFNGEAPLQSRTPSEKer 231
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 569026720 865 FYKlvkdgYQMAQPAFAPKNIYSIMQACWALEPTHRPTFQQI 906
Cdd:cd05076  232 FYQ-----RQHRLPEPSCPELATLISQCLTYEPTQRPSFRTI 268
STKc_CDK10 cd07845
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs ...
761-849 3.36e-08

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: 56.22  E-value: 3.36e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 761 QVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARdimndsnyivkgNARLPVKWM----------APESIFDC 830
Cdd:cd07845  116 QLLRGLQYLHENFIIHRDLKVSNLLLTDKGCLKIADFGLAR------------TYGLPAKPMtpkvvtlwyrAPELLLGC 183
                         90       100
                 ....*....|....*....|
gi 569026720 831 -VYTVQSDVWSYGILLWEIF 849
Cdd:cd07845  184 tTYTTAIDMWAVGCILAELL 203
STKc_MEKK2 cd06652
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
581-850 3.38e-08

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


Pssm-ID: 270818 [Multi-domain]  Cd Length: 264  Bit Score: 55.82  E-value: 3.38e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 581 NLQFGKTLGAGAFGKVVEATAFGLGKEDAVLKVAVKMlKSTAHADEKEALMSELKIMSHLgQHENIVNLLGacthggpvl 660
Cdd:cd06652    3 NWRLGKLLGQGAFGRVYLCYDADTGRELAVKQVQFDP-ESPETSKEVNALECEIQLLKNL-LHERIVQYYG--------- 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 661 viteyccygdllnFLRRKAEAMLgpSLSPGQDPEGGVdyknihlekkyvrRDSGFSSQGVDTYVEMRpvstssndsfseq 740
Cdd:cd06652   72 -------------CLRDPQERTL--SIFMEYMPGGSI-------------KDQLKSYGALTENVTRK------------- 110
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 741 dldkedgrplelrdllhFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDImndSNYIVKGNARLPVK 820
Cdd:cd06652  111 -----------------YTRQILEGVHYLHSNMIVHRDIKGANILRDSVGNVKLGDFGASKRL---QTICLSGTGMKSVT 170
                        250       260       270
                 ....*....|....*....|....*....|....
gi 569026720 821 ----WMAPESIFDCVYTVQSDVWSYGILLWEIFS 850
Cdd:cd06652  171 gtpyWMSPEVISGEGYGRKADIWSVGCTVVEMLT 204
STKc_PKC cd05570
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer ...
758-858 3.40e-08

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: 56.45  E-value: 3.40e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 758 FSSQVAQGMAFLASKNCIHRDVAARNVLLTN-GHVaKIGDFGLAR-DIMNDS---------NYivkgnarlpvkwMAPES 826
Cdd:cd05570  101 YAAEICLALQFLHERGIIYRDLKLDNVLLDAeGHI-KIADFGMCKeGIWGGNttstfcgtpDY------------IAPEI 167
                         90       100       110
                 ....*....|....*....|....*....|..
gi 569026720 827 IFDCVYTVQSDVWSYGILLWEIFsLGLNPYPG 858
Cdd:cd05570  168 LREQDYGFSVDWWALGVLLYEML-AGQSPFEG 198
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
752-848 3.49e-08

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: 55.69  E-value: 3.49e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 752 LRDLLHFSSQVAQ--------GMAFLASKNCIHRDVAARNVLL-TNGHVaKIGDFGLARDIMNDSN-YIVKGNarlPvKW 821
Cdd:cd05572   84 LRDRGLFDEYTARfytacvvlAFEYLHSRGIIYRDLKPENLLLdSNGYV-KLVDFGFAKKLGSGRKtWTFCGT---P-EY 158
                         90       100
                 ....*....|....*....|....*..
gi 569026720 822 MAPESIFDCVYTVQSDVWSYGILLWEI 848
Cdd:cd05572  159 VAPEIILNKGYDFSVDYWSLGILLYEL 185
STKc_MPK1 cd07857
Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; ...
581-855 3.67e-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: 56.26  E-value: 3.67e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 581 NLQFGKTLGAGAFGKVVEATAFGLGKEDavlKVAVKmlKSTaHADEKEAL----MSELKIMSHLGQHENIVNLlgacthg 656
Cdd:cd07857    1 RYELIKELGQGAYGIVCSARNAETSEEE---TVAIK--KIT-NVFSKKILakraLRELKLLRHFRGHKNITCL------- 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 657 gpvlviteyccygdllnflrrkaeamlgpslspgqdpeggVDYKNIhlekkyvrrdsgFSSQGVDTYVEMRPVstssnds 736
Cdd:cd07857   68 ----------------------------------------YDMDIV------------FPGNFNELYLYEELM------- 88
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 737 fsEQDLDK--EDGRPLELRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDIMND-------- 806
Cdd:cd07857   89 --EADLHQiiRSGQPLTDAHFQSFIYQILCGLKYIHSANVLHRDLKPGNLLVNADCELKICDFGLARGFSENpgenagfm 166
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 569026720 807 SNYIVkgnarlpVKWM-APESIFDCV-YTVQSDVWSYGILLWEIfsLGLNP 855
Cdd:cd07857  167 TEYVA-------TRWYrAPEIMLSFQsYTKAIDVWSVGCILAEL--LGRKP 208
STKc_Titin cd14104
Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the ...
753-858 3.81e-08

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: 55.64  E-value: 3.81e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 753 RDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTN--GHVAKIGDFGLARDIMNDSNYIVKGNArlpVKWMAPESIFDC 830
Cdd:cd14104   97 REIVSYVRQVCEALEFLHSKNIGHFDIRPENIIYCTrrGSYIKIIEFGQSRQLKPGDKFRLQYTS---AEFYAPEVHQHE 173
                         90       100
                 ....*....|....*....|....*...
gi 569026720 831 VYTVQSDVWSYGILLWEIFSlGLNPYPG 858
Cdd:cd14104  174 SVSTATDMWSLGCLVYVLLS-GINPFEA 200
STKc_CDK12 cd07864
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs ...
758-850 4.34e-08

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK12 is also called Cdc2-related protein kinase 7 (CRK7) or Cdc2-related kinase arginine/serine-rich (CrkRS). It is a unique CDK that contains an RS domain, which is predominantly found in splicing factors. CDK12 is widely expressed in tissues. It interacts with cyclins L1 and L2, and plays roles in regulating transcription and alternative splicing. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK12 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270847 [Multi-domain]  Cd Length: 302  Bit Score: 55.96  E-value: 4.34e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 758 FSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDIMNDSNYIVKGnaRLPVKWMAPESIF--DCVYTVQ 835
Cdd:cd07864  121 FMKQLLEGLNYCHKKNFLHRDIKCSNILLNNKGQIKLADFGLARLYNSEESRPYTN--KVITLWYRPPELLlgEERYGPA 198
                         90
                 ....*....|....*
gi 569026720 836 SDVWSYGILLWEIFS 850
Cdd:cd07864  199 IDVWSCGCILGELFT 213
STKc_myosinIIIB_N cd06639
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze ...
570-848 4.39e-08

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: 55.77  E-value: 4.39e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 570 PYN------EKWEFPRNNLQFGKTLGAGAFGKVVEATafglGKEDAVLkVAVKMLKSTAHADEKeaLMSELKIMSHLGQH 643
Cdd:cd06639    6 PYNssmlglESLADPSDTWDIIETIGKGTYGKVYKVT----NKKDGSL-AAVKILDPISDVDEE--IEAEYNILRSLPNH 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 644 ENIVNLLGACTH-----GGPVLVITEYCCYGDLLNFLRrkaeamlgpslspgqdpeggvdyknihlekkyvrrdsGFSSQ 718
Cdd:cd06639   79 PNVVKFYGMFYKadqyvGGQLWLVLELCNGGSVTELVK-------------------------------------GLLKC 121
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 719 GvdtyvemrpvstssndsfseQDLDKEDGRPLELRDLLhfssqvaqGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFG 798
Cdd:cd06639  122 G--------------------QRLDEAMISYILYGALL--------GLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFG 173
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 569026720 799 LARDIMndSNYIVKGNARLPVKWMAPESI-----FDCVYTVQSDVWSYGILLWEI 848
Cdd:cd06639  174 VSAQLT--SARLRRNTSVGTPFWMAPEVIaceqqYDYSYDARCDVWSLGITAIEL 226
STKc_cPKC_alpha cd05615
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs ...
758-900 4.59e-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: 56.16  E-value: 4.59e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 758 FSSQVAQGMAFLASKNCIHRDVAARNVLL-TNGHVaKIGDFGLARDIMNDSnYIVKGNARLPvKWMAPESIFDCVYTVQS 836
Cdd:cd05615  116 YAAEISVGLFFLHKKGIIYRDLKLDNVMLdSEGHI-KIADFGMCKEHMVEG-VTTRTFCGTP-DYIAPEIIAYQPYGRSV 192
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 569026720 837 DVWSYGILLWEIFSlGLNPYPGILVNSKFYKLVKdgYQMAQPAFAPKNIYSIMQACWALEPTHR 900
Cdd:cd05615  193 DWWAYGVLLYEMLA-GQPPFDGEDEDELFQSIME--HNVSYPKSLSKEAVSICKGLMTKHPAKR 253
STKc_LRRK1 cd14067
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze ...
761-913 5.64e-08

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: 55.36  E-value: 5.64e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 761 QVAQGMAFLASKNCIHRDVAARNVLL----TNGHV-AKIGDFGLARDIMNDSNYIVKGNArlpvKWMAPESIFDCVYTVQ 835
Cdd:cd14067  122 QIAAGLAYLHKKNIIFCDLKSDNILVwsldVQEHInIKLSDYGISRQSFHEGALGVEGTP----GYQAPEIRPRIVYDEK 197
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 836 SDVWSYGILLWEIFSlGLNPYPG---ILVNSKFYKLVKDgyQMAQPAFAP-KNIYSIMQACWALEPTHRPtfqQICSFLQ 911
Cdd:cd14067  198 VDMFSYGMVLYELLS-GQRPSLGhhqLQIAKKLSKGIRP--VLGQPEEVQfFRLQALMMECWDTKPEKRP---LACSVVE 271

                 ..
gi 569026720 912 EQ 913
Cdd:cd14067  272 QM 273
STKc_NIM1 cd14075
Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the ...
584-910 5.93e-08

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: 55.04  E-value: 5.93e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 584 FGKTLGAGAFGKVvEATAFGLGKEdavlKVAVKMLKSTaHADEKEALM--SELKIMSHLgQHENIVNLLGACTHGGPVLV 661
Cdd:cd14075    6 IRGELGSGNFSQV-KLGIHQLTKE----KVAIKILDKT-KLDQKTQRLlsREISSMEKL-HHPNIIRLYEVVETLSKLHL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 662 ITEYCCYGDLlnflrrkaeamlgpslspgqdpeggvdYKNIHLEKKyvrrdsgfssqgvdtyvemrpvstssndsfseqd 741
Cdd:cd14075   79 VMEYASGGEL---------------------------YTKISTEGK---------------------------------- 97
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 742 LDKEDGRPLelrdllhFSsQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLardimndSNYIVKGNA------ 815
Cdd:cd14075   98 LSESEAKPL-------FA-QIVSAVKHMHENNIIHRDLKAENVFYASNNCVKVGDFGF-------STHAKRGETlntfcg 162
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 816 RLPvkWMAPESIFDCVYT-VQSDVWSYGILLWeiFSL-GLNPYPGILVnSKFYKLVKDG-YQMaqPAFAPKNIYSIMQAC 892
Cdd:cd14075  163 SPP--YAAPELFKDEHYIgIYVDIWALGVLLY--FMVtGVMPFRAETV-AKLKKCILEGtYTI--PSYVSEPCQELIRGI 235
                        330       340
                 ....*....|....*....|
gi 569026720 893 WALEPTHRPTFQQI--CSFL 910
Cdd:cd14075  236 LQPVPSDRYSIDEIknSEWL 255
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
745-847 6.09e-08

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 411126 [Multi-domain]  Cd Length: 563  Bit Score: 56.34  E-value: 6.09e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 745 EDGRPLELRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDImnDSNYIVKGNARL-PVKWMA 823
Cdd:NF033483  99 REHGPLSPEEAVEIMIQILSALEHAHRNGIVHRDIKPQNILITKDGRVKVTDFGIARAL--SSTTMTQTNSVLgTVHYLS 176
                         90       100
                 ....*....|....*....|....
gi 569026720 824 PESIFDCVYTVQSDVWSYGILLWE 847
Cdd:NF033483 177 PEQARGGTVDARSDIYSLGIVLYE 200
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
21-85 6.77e-08

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 433584 [Multi-domain]  Cd Length: 75  Bit Score: 50.66  E-value: 6.77e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 569026720   21 PVIEPSVPELVVKPGATVTLRCVGNGS----VEW--DGPPSPHWTLYSDGSSSILSTNNATFQNTGTYRCT 85
Cdd:pfam13927   2 PVITVSPSSVVVVEGETVTLTCEASGSppptITWykNGGKLSSGRTSLVGGNGTLTISNVTREDSGTYTCT 72
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
587-858 7.01e-08

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: 54.79  E-value: 7.01e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 587 TLGAGAFGKVVEATAFGLGKEDAVLKVAVKMLKSTAHAdeKEALMSELKIMSHLgQHENIVNLLGACTHGGPVLVITEYC 666
Cdd:cd14098    7 RLGSGTFAEVKKAVEVETGKMRAIKQIVKRKVAGNDKN--LQLFQREINILKSL-EHPGIVRLIDWYEDDQHIYLVMEYV 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 667 CYGDLLNFLrrkaeamlgpslspgqdpeggvdyknihlekkyvrrdsgfssqgvdtyvemrpvstSSNDSFSEQDldked 746
Cdd:cd14098   84 EGGDLMDFI--------------------------------------------------------MAWGAIPEQH----- 102
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 747 GRPLelrdllhfSSQVAQGMAFLASKNCIHRDVAARNVLLTNGH--VAKIGDFGLARDIMNDSnyIVKGNARLPvKWMAP 824
Cdd:cd14098  103 AREL--------TKQILEAMAYTHSMGITHRDLKPENILITQDDpvIVKISDFGLAKVIHTGT--FLVTFCGTM-AYLAP 171
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 569026720 825 ESI------FDCVYTVQSDVWSYGILLWEIFSLGLnPYPG 858
Cdd:cd14098  172 EILmskeqnLQGGYSNLVDMWSVGCLVYVMLTGAL-PFDG 210
STKc_ASK cd06624
Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs ...
588-842 7.02e-08

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: 54.72  E-value: 7.02e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 588 LGAGAFGKVVEATAFglgkeDAVLKVAVKMLKSTaHADEKEALMSELKIMSHLgQHENIVNLLGACTHGGPVLVITEYCC 667
Cdd:cd06624   16 LGKGTFGVVYAARDL-----STQVRIAIKEIPER-DSREVQPLHEEIALHSRL-SHKNIVQYLGSVSEDGFFKIFMEQVP 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 668 YGDLLNFLRRKaeamlgpsLSPGQDPEGGVDYknihlekkyvrrdsgfssqgvdtyvemrpvstssndsfseqdldkedg 747
Cdd:cd06624   89 GGSLSALLRSK--------WGPLKDNENTIGY------------------------------------------------ 112
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 748 rplelrdllhFSSQVAQGMAFLASKNCIHRDVAARNVLL-TNGHVAKIGDFGLARDI--MNDSNYIVKGNarlpVKWMAP 824
Cdd:cd06624  113 ----------YTKQILEGLKYLHDNKIVHRDIKGDNVLVnTYSGVVKISDFGTSKRLagINPCTETFTGT----LQYMAP 178
                        250       260
                 ....*....|....*....|
gi 569026720 825 ESIFDCV--YTVQSDVWSYG 842
Cdd:cd06624  179 EVIDKGQrgYGPPADIWSLG 198
STKc_GRK6 cd05630
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs ...
758-882 7.45e-08

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK6 is widely expressed in many tissues and is expressed as multiple splice variants with different domain architectures. It is post-translationally palmitoylated and localized in the membrane. GRK6 plays important roles in the regulation of dopamine, M3 muscarinic, opioid, and chemokine receptor signaling. It also plays maladaptive roles in addiction and Parkinson's disease. GRK6-deficient mice exhibit altered dopamine receptor regulation, decreased lymphocyte chemotaxis, and increased acute inflammation and neutrophil chemotaxis. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270779 [Multi-domain]  Cd Length: 285  Bit Score: 55.03  E-value: 7.45e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 758 FSSQVAQGMAFLASKNCIHRDVAARNVLLTN-GHVaKIGDFGLARDIMNDSNyiVKGNARlPVKWMAPESIFDCVYTVQS 836
Cdd:cd05630  107 YAAEICCGLEDLHRERIVYRDLKPENILLDDhGHI-RISDLGLAVHVPEGQT--IKGRVG-TVGYMAPEVVKNERYTFSP 182
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 569026720 837 DVWSYGILLWEIFSlGLNPY---PGILVNSKFYKLVKDGYQMAQPAFAP 882
Cdd:cd05630  183 DWWALGCLLYEMIA-GQSPFqqrKKKIKREEVERLVKEVPEEYSEKFSP 230
PKc_MEK1 cd06650
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
759-857 7.83e-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: 55.06  E-value: 7.83e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 759 SSQVAQGMAFLASKNCI-HRDVAARNVLLTNGHVAKIGDFGLARDIMND-SNYIVKGNArlpvkWMAPESIFDCVYTVQS 836
Cdd:cd06650  109 SIAVIKGLTYLREKHKImHRDVKPSNILVNSRGEIKLCDFGVSGQLIDSmANSFVGTRS-----YMSPERLQGTHYSVQS 183
                         90       100
                 ....*....|....*....|.
gi 569026720 837 DVWSYGILLWEIfSLGLNPYP 857
Cdd:cd06650  184 DIWSMGLSLVEM-AVGRYPIP 203
STKc_Kin4 cd14076
Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the ...
585-856 8.92e-08

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: 54.41  E-value: 8.92e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 585 GKTLGAGAFGKVVEATAFGLGKEDAVLKVAVKMLKSTAHADEKEA--LMSELKIMSHLGqHENIVNLLGACTHGGPVLVI 662
Cdd:cd14076    6 GRTLGEGEFGKVKLGWPLPKANHRSGVQVAIKLIRRDTQQENCQTskIMREINILKGLT-HPNIVRLLDVLKTKKYIGIV 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 663 TEYCCYGDLLNFLRRKAeamlgpslspgqdpeggvdykniHLEKKYVRRdsgfssqgvdtyvemrpvstssndsfseqdl 742
Cdd:cd14076   85 LEFVSGGELFDYILARR-----------------------RLKDSVACR------------------------------- 110
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 743 dkedgrplelrdllhFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDIMNDSNYIVKGNARLPVkWM 822
Cdd:cd14076  111 ---------------LFAQLISGVAYLHKKGVVHRDLKLENLLLDKNRNLVITDFGFANTFDHFNGDLMSTSCGSPC-YA 174
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 569026720 823 APESIF-DCVYT-VQSDVWSYGILLWEIFSlGLNPY 856
Cdd:cd14076  175 APELVVsDSMYAgRKADIWSCGVILYAMLA-GYLPF 209
STKc_MARK cd14072
Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; ...
581-906 9.63e-08

Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MARKs, also called Partitioning-defective 1 (Par1) proteins, function as regulators of diverse cellular processes in nematodes, Drosophila, yeast, and vertebrates. They are involved in embryogenesis, epithelial cell polarization, cell signaling, and neuronal differentiation. MARKs phosphorylate tau and related microtubule-associated proteins (MAPs), and regulates microtubule-based intracellular transport. Vertebrates contain four isoforms, namely MARK1 (or Par1c), MARK2 (or Par1b), MARK3 (Par1a), and MARK4 (or MARKL1). Known substrates of MARKs include the cell cycle-regulating phosphatase Cdc25, tyrosine phosphatase PTPH1, MAPK scaffolding protein KSR1, class IIa histone deacetylases, and plakophilin 2. The MARK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270974 [Multi-domain]  Cd Length: 253  Bit Score: 54.06  E-value: 9.63e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 581 NLQFGKTLGAGAFGKVVEATAFGLGKEdavlkVAVKML-KSTAHADEKEALMSELKIMSHLgQHENIVNLLGACTHGGPV 659
Cdd:cd14072    1 NYRLLKTIGKGNFAKVKLARHVLTGRE-----VAIKIIdKTQLNPSSLQKLFREVRIMKIL-NHPNIVKLFEVIETEKTL 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 660 LVITEYCCYGDLLNFLrrkaeamlgpsLSPGQdpeggvdyknihLEKKYVRrdsgfssqgvdtyVEMRpvstssndsfse 739
Cdd:cd14072   75 YLVMEYASGGEVFDYL-----------VAHGR------------MKEKEAR-------------AKFR------------ 106
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 740 qdldkedgrplelrdllhfssQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLardimndSNYIVKGNaRLPV 819
Cdd:cd14072  107 ---------------------QIVSAVQYCHQKRIVHRDLKAENLLLDADMNIKIADFGF-------SNEFTPGN-KLDT 157
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 820 -----KWMAPESIFDCVYT-VQSDVWSYGILLWEIFSLGLnPYPGILVNSKFYKLVKDGYQMaqPAFAPKNIYSIMQACW 893
Cdd:cd14072  158 fcgspPYAAPELFQGKKYDgPEVDVWSLGVILYTLVSGSL-PFDGQNLKELRERVLRGKYRI--PFYMSTDCENLLKKFL 234
                        330
                 ....*....|...
gi 569026720 894 ALEPTHRPTFQQI 906
Cdd:cd14072  235 VLNPSKRGTLEQI 247
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
28-85 1.12e-07

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: 50.20  E-value: 1.12e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 569026720    28 PELVVKPGATVTLRCVGNGS----VEW--DGP----PSPHWTLYSDGSSSILSTNNATFQNTGTYRCT 85
Cdd:smart00410   2 PSVTVKEGESVTLSCEASGSpppeVTWykQGGkllaESGRFSVSRSGSTSTLTISNVTPEDSGTYTCA 69
PKc_MEK2 cd06649
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
759-857 1.17e-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: 54.67  E-value: 1.17e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 759 SSQVAQGMAFLASKNCI-HRDVAARNVLLTNGHVAKIGDFGLARDIMND-SNYIVKGNArlpvkWMAPESIFDCVYTVQS 836
Cdd:cd06649  109 SIAVLRGLAYLREKHQImHRDVKPSNILVNSRGEIKLCDFGVSGQLIDSmANSFVGTRS-----YMSPERLQGTHYSVQS 183
                         90       100
                 ....*....|....*....|.
gi 569026720 837 DVWSYGILLWEIfSLGLNPYP 857
Cdd:cd06649  184 DIWSMGLSLVEL-AIGRYPIP 203
PKc_MKK7 cd06618
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
775-921 1.18e-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: 54.30  E-value: 1.18e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 775 IHRDVAARNVLLTNGHVAKIGDFGLardimndSNYIVKGNARLPVK----WMAPESI----FDcVYTVQSDVWSYGILLW 846
Cdd:cd06618  137 IHRDVKPSNILLDESGNVKLCDFGI-------SGRLVDSKAKTRSAgcaaYMAPERIdppdNP-KYDIRADVWSLGISLV 208
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 569026720 847 EIfSLGLNPYPGilVNSKFYKLVKdgyqmaqpafapkniysIMQACWALEPTHRPTFQQICSFLQEQAQEDRRER 921
Cdd:cd06618  209 EL-ATGQFPYRN--CKTEFEVLTK-----------------ILNEEPPSLPPNEGFSPDFCSFVDLCLTKDHRYR 263
STKc_GRK1 cd05608
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs ...
758-850 1.21e-07

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: 54.50  E-value: 1.21e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 758 FSSQVAQGMAFLASKNCIHRDVAARNVLLTN-GHVaKIGDFGLARDiMNDSNYIVKGNARLPvKWMAPESIFDCVYTVQS 836
Cdd:cd05608  110 YTAQIISGLEHLHQRRIIYRDLKPENVLLDDdGNV-RISDLGLAVE-LKDGQTKTKGYAGTP-GFMAPELLLGEEYDYSV 186
                         90
                 ....*....|....
gi 569026720 837 DVWSYGILLWEIFS 850
Cdd:cd05608  187 DYFTLGVTLYEMIA 200
PK_ILK cd14057
Pseudokinase domain of Integrin Linked Kinase; The pseudokinase domain shows similarity to ...
758-911 1.24e-07

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


Pssm-ID: 270959 [Multi-domain]  Cd Length: 251  Bit Score: 54.03  E-value: 1.24e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 758 FSSQVAQGMAFLAS-KNCIHR-DVAARNVLLTNGHVAKIGdfglardiMNDSNYIVKGNARL--PVkWMAPESIF---DC 830
Cdd:cd14057   99 FALDIARGMAFLHTlEPLIPRhHLNSKHVMIDEDMTARIN--------MADVKFSFQEPGKMynPA-WMAPEALQkkpED 169
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 831 VYTVQSDVWSYGILLWEIFSLGLnPYPGILVNSKFYKLVKDGYQMAQPAFAPKNIYSIMQACWALEPTHRPTFQQICSFL 910
Cdd:cd14057  170 INRRSADMWSFAILLWELVTREV-PFADLSNMEIGMKIALEGLRVTIPPGISPHMCKLMKICMNEDPGKRPKFDMIVPIL 248

                 .
gi 569026720 911 Q 911
Cdd:cd14057  249 E 249
STKc_p38 cd07851
Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs ...
575-847 1.25e-07

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: 54.61  E-value: 1.25e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 575 WEFPR--NNLQFgktLGAGAFGKVVEATAFGLGKedavlKVAVKML----KSTAHAdeKEALmSELKIMSHLgQHENIVN 648
Cdd:cd07851   11 WEVPDryQNLSP---VGSGAYGQVCSAFDTKTGR-----KVAIKKLsrpfQSAIHA--KRTY-RELRLLKHM-KHENVIG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 649 LLGACThggpvlviteyccygdllnflrrkaeamlgpslsPGQdpeggvdykniHLEKkyvrrdsgFSsqgvDTYVEMRP 728
Cdd:cd07851   79 LLDVFT----------------------------------PAS-----------SLED--------FQ----DVYLVTHL 101
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 729 VSTSSNDSFSEQDLDKEdgrplELRDLLHfssQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARdiMNDS- 807
Cdd:cd07851  102 MGADLNNIVKCQKLSDD-----HIQFLVY---QILRGLKYIHSAGIIHRDLKPSNLAVNEDCELKILDFGLAR--HTDDe 171
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 569026720 808 --NYIVkgnarlpVKW-MAPESIFDCV-YTVQSDVWSYGILLWE 847
Cdd:cd07851  172 mtGYVA-------TRWyRAPEIMLNWMhYNQTVDIWSVGCIMAE 208
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
583-850 1.27e-07

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 54.77  E-value: 1.27e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 583 QFGKTLGAGAFGKVVEATAFGLGKEDAVLKVAVKMLKSTAHADEKE--------ALMSELKIMSHLgQHENIVNLLGACT 654
Cdd:PTZ00024  12 QKGAHLGEGTYGKVEKAYDTLTGKIVAIKKVKIIEISNDVTKDRQLvgmcgihfTTLRELKIMNEI-KHENIMGLVDVYV 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 655 HGGPVLVITEYCCYgDLlnflrrkaeamlgpslspgqdpeggvdyknihleKKYVRRDSGFSSQGVDTYVemrpvstssn 734
Cdd:PTZ00024  91 EGDFINLVMDIMAS-DL----------------------------------KKVVDRKIRLTESQVKCIL---------- 125
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 735 dsfseqdldkedgrplelrdllhfsSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLAR----DIMNDSNYI 810
Cdd:PTZ00024 126 -------------------------LQILNGLNVLHKWYFMHRDLSPANIFINSKGICKIADFGLARrygyPPYSDTLSK 180
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 569026720 811 VKGNAR--------LPVKWMAPESIF--DCvYTVQSDVWSYGILLWEIFS 850
Cdd:PTZ00024 181 DETMQRreemtskvVTLWYRAPELLMgaEK-YHFAVDMWSVGCIFAELLT 229
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
761-906 1.28e-07

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 55.41  E-value: 1.28e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 761 QVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDIMNDSNYIVKGNARLPVKWMAPESIFDCVYTVQSDVWS 840
Cdd:PTZ00267 177 QIVLALDEVHSRKMMHRDLKSANIFLMPTGIIKLGDFGFSKQYSDSVSLDVASSFCGTPYYLAPELWERKRYSKKADMWS 256
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 569026720 841 YGILLWEIFSLGlNPYPGILVNSKFYKLVKDGYQmAQPAFAPKNIYSIMQACWALEPTHRPTFQQI 906
Cdd:PTZ00267 257 LGVILYELLTLH-RPFKGPSQREIMQQVLYGKYD-PFPCPVSSGMKALLDPLLSKNPALRPTTQQL 320
STKc_p38alpha cd07877
Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase ...
575-858 1.30e-07

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


Pssm-ID: 143382 [Multi-domain]  Cd Length: 345  Bit Score: 54.66  E-value: 1.30e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 575 WEFPrNNLQFGKTLGAGAFGKVVEATAFGLGkedavLKVAVKML----KSTAHADEKealMSELKIMSHLgQHENIVNLL 650
Cdd:cd07877   13 WEVP-ERYQNLSPVGSGAYGSVCAAFDTKTG-----LRVAVKKLsrpfQSIIHAKRT---YRELRLLKHM-KHENVIGLL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 651 GACThggPVLVITEYccygdllNFLRRKAEAMlgpslspgqdpegGVDYKNIHLEKKYVrrdsgfssqgvDTYVEMrpvs 730
Cdd:cd07877   83 DVFT---PARSLEEF-------NDVYLVTHLM-------------GADLNNIVKCQKLT-----------DDHVQF---- 124
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 731 tssndsfseqdldkedgrplelrdLLHfssQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDIMND-SNY 809
Cdd:cd07877  125 ------------------------LIY---QILRGLKYIHSADIIHRDLKPSNLAVNEDCELKILDFGLARHTDDEmTGY 177
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 569026720 810 IVkgnarlpVKWM-APESIFDCV-YTVQSDVWSYGILLWEIFSlGLNPYPG 858
Cdd:cd07877  178 VA-------TRWYrAPEIMLNWMhYNQTVDIWSVGCIMAELLT-GRTLFPG 220
STKc_Sty1_Hog1 cd07856
Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases ...
748-858 1.38e-07

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: 54.50  E-value: 1.38e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 748 RPLELRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARdiMNDSNYIVKGNARLpvkWMAPESI 827
Cdd:cd07856  103 RPLEKQFIQYFLYQILRGLKYVHSAGVIHRDLKPSNILVNENCDLKICDFGLAR--IQDPQMTGYVSTRY---YRAPEIM 177
                         90       100       110
                 ....*....|....*....|....*....|..
gi 569026720 828 FDC-VYTVQSDVWSYGILLWEIFsLGLNPYPG 858
Cdd:cd07856  178 LTWqKYDVEVDIWSAGCIFAEML-EGKPLFPG 208
STKc_MAP4K5 cd06646
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
738-864 1.43e-07

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: 53.88  E-value: 1.43e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 738 SEQDLDKEDGrPLELRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDImndSNYIVKGNARL 817
Cdd:cd06646   92 SLQDIYHVTG-PLSELQIAYVCRETLQGLAYLHSKGKMHRDIKGANILLTDNGDVKLADFGVAAKI---TATIAKRKSFI 167
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 569026720 818 PVK-WMAPESIF---DCVYTVQSDVWSYGILLWEIFSL-----GLNPYPGILVNSK 864
Cdd:cd06646  168 GTPyWMAPEVAAvekNGGYNQLCDIWAVGITAIELAELqppmfDLHPMRALFLMSK 223
STKc_DRAK1 cd14197
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
753-858 1.76e-07

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: 53.79  E-value: 1.76e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 753 RDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTN----GHVaKIGDFGLARdIMNDSNYI--VKGNArlpvKWMAPES 826
Cdd:cd14197  111 KDVKRLMKQILEGVSFLHNNNVVHLDLKPQNILLTSesplGDI-KIVDFGLSR-ILKNSEELreIMGTP----EYVAPEI 184
                         90       100       110
                 ....*....|....*....|....*....|..
gi 569026720 827 IFDCVYTVQSDVWSYGILLWEIFSlGLNPYPG 858
Cdd:cd14197  185 LSYEPISTATDMWSIGVLAYVMLT-GISPFLG 215
PKc_MEK cd06615
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
762-857 1.93e-07

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: 53.98  E-value: 1.93e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 762 VAQGMAFLASKNCI-HRDVAARNVLLTNGHVAKIGDFGLARDIMND-SNYIVKGNArlpvkWMAPESIFDCVYTVQSDVW 839
Cdd:cd06615  108 VLRGLTYLREKHKImHRDVKPSNILVNSRGEIKLCDFGVSGQLIDSmANSFVGTRS-----YMSPERLQGTHYTVQSDIW 182
                         90
                 ....*....|....*...
gi 569026720 840 SYGILLWEIfSLGLNPYP 857
Cdd:cd06615  183 SLGLSLVEM-AIGRYPIP 199
STKc_RSK_N cd05582
N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; ...
760-858 2.58e-07

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: 53.56  E-value: 2.58e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 760 SQVAQGMAFLASKNCIHRDVAARNVLL-TNGHVaKIGDFGLARDIMNDSN--YIVKGNarlpVKWMAPESIFDCVYTVQS 836
Cdd:cd05582  104 AELALALDHLHSLGIIYRDLKPENILLdEDGHI-KLTDFGLSKESIDHEKkaYSFCGT----VEYMAPEVVNRRGHTQSA 178
                         90       100
                 ....*....|....*....|..
gi 569026720 837 DVWSYGILLWEIFSLGLnPYPG 858
Cdd:cd05582  179 DWWSFGVLMFEMLTGSL-PFQG 199
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
764-856 2.96e-07

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: 53.19  E-value: 2.96e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 764 QGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDIMNDSNYivKGNARLPVKWMAPESIFDCVYTVQSDVWSYGI 843
Cdd:cd06654  127 QALEFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSK--RSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGI 204
                         90
                 ....*....|...
gi 569026720 844 LLWEIFSlGLNPY 856
Cdd:cd06654  205 MAIEMIE-GEPPY 216
PTZ00426 PTZ00426
cAMP-dependent protein kinase catalytic subunit; Provisional
572-856 3.03e-07

cAMP-dependent protein kinase catalytic subunit; Provisional


Pssm-ID: 173616 [Multi-domain]  Cd Length: 340  Bit Score: 53.45  E-value: 3.03e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 572 NEKWEFPRNNLQFGKTLGAGAFGKVVEATAfglgKEDAVLKVAVKMLKSTAHADEKEA--LMSELKIMSHLgQHENIVNL 649
Cdd:PTZ00426  22 KRKNKMKYEDFNFIRTLGTGSFGRVILATY----KNEDFPPVAIKRFEKSKIIKQKQVdhVFSERKILNYI-NHPFCVNL 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 650 LGACTHGGPVLVITEYCCYGDLLNFLRRKaeamlgpslspgqdpeggvdyknihlekKYVRRDSGfssqgvdtyvemrpv 729
Cdd:PTZ00426  97 YGSFKDESYLYLVLEFVIGGEFFTFLRRN----------------------------KRFPNDVG--------------- 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 730 stssndsfseqdldkedgrplelrdlLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARdIMNDSNY 809
Cdd:PTZ00426 134 --------------------------CFYAAQIVLIFEYLQSLNIVYRDLKPENLLLDKDGFIKMTDFGFAK-VVDTRTY 186
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 569026720 810 IVKGNArlpvKWMAPESIFDCVYTVQSDVWSYGILLWEIFsLGLNPY 856
Cdd:PTZ00426 187 TLCGTP----EYIAPEILLNVGHGKAADWWTLGIFIYEIL-VGCPPF 228
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
586-847 3.04e-07

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: 53.14  E-value: 3.04e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 586 KTLGAGAFGKVVEATafglGKEDAVLkVAVKMLKSTAHADEKEALMSELKIMSHLgQHENIVNLLGACTHGGPVLVITEY 665
Cdd:cd14046   12 QVLGKGAFGQVVKVR----NKLDGRY-YAIKKIKLRSESKNNSRILREVMLLSRL-NHQHVVRYYQAWIERANLYIQMEY 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 666 CcygdllnflrrkaeamlgpslspgqdpeggvdyknihlEKKYVRrdsgfssqgvDTYvemrpvstssnDSFSEQDLDke 745
Cdd:cd14046   86 C--------------------------------------EKSTLR----------DLI-----------DSGLFQDTD-- 104
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 746 dgrplelrDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLL-TNGHVaKIGDFGLARDIMN-------------DSNYIV 811
Cdd:cd14046  105 --------RLWRLFRQILEGLAYIHSQGIIHRDLKPVNIFLdSNGNV-KIGDFGLATSNKLnvelatqdinkstSAALGS 175
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 569026720 812 KGNARLPVK---WMAPE--SIFDCVYTVQSDVWSYGILLWE 847
Cdd:cd14046  176 SGDLTGNVGtalYVAPEvqSGTKSTYNEKVDMYSLGIIFFE 216
STKc_MEKK3 cd06651
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
581-906 3.26e-07

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MEKK3 is a MAPK kinase kinase (MAPKKK or MKKK), that phosphorylates and activates the MAPK kinase MEK5 (or MKK5), which in turn phosphorylates and activates ERK5. The ERK5 cascade plays roles in promoting cell proliferation, differentiation, neuronal survival, and neuroprotection. MEKK3 plays an essential role in embryonic angiogenesis and early heart development. In addition, MEKK3 is involved in interleukin-1 receptor and Toll-like receptor 4 signaling. It is also a specific regulator of the proinflammatory cytokines IL-6 and GM-CSF in some immune cells. MEKK3 also regulates calcineurin, which plays a critical role in T cell activation, apoptosis, skeletal myocyte differentiation, and cardiac hypertrophy. The MEKK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270817 [Multi-domain]  Cd Length: 271  Bit Score: 52.78  E-value: 3.26e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 581 NLQFGKTLGAGAFGKVVEATAFGLGKEDAVLKVAVKMlKSTAHADEKEALMSELKIMSHLgQHENIVNLLGAC-THGGPV 659
Cdd:cd06651    8 NWRRGKLLGQGAFGRVYLCYDVDTGRELAAKQVQFDP-ESPETSKEVSALECEIQLLKNL-QHERIVQYYGCLrDRAEKT 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 660 LVI-TEYCCYGDLLNFLrrKAEAMLGPSLSpgqdpeggvdyknihleKKYVRrdsgfssqgvdtyvemrpvstssndsfs 738
Cdd:cd06651   86 LTIfMEYMPGGSVKDQL--KAYGALTESVT-----------------RKYTR---------------------------- 118
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 739 eqdldkedgrplelrdllhfssQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDImndSNYIVKGNARLP 818
Cdd:cd06651  119 ----------------------QILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRL---QTICMSGTGIRS 173
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 819 VK----WMAPESIFDCVYTVQSDVWSYGILLWEIFSLGlNPYPGILVNSKFYKLVKDGYQMAQPAFAPKNIYSIMQaCWA 894
Cdd:cd06651  174 VTgtpyWMSPEVISGEGYGRKADVWSLGCTVVEMLTEK-PPWAEYEAMAAIFKIATQPTNPQLPSHISEHARDFLG-CIF 251
                        330
                 ....*....|..
gi 569026720 895 LEPTHRPTFQQI 906
Cdd:cd06651  252 VEARHRPSAEEL 263
STKc_TDY_MAPK cd07859
Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; ...
758-858 3.32e-07

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: 53.25  E-value: 3.32e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 758 FSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDIMNDSNYIVKGNARLPVKWM-APE--SIFDCVYTV 834
Cdd:cd07859  108 FLYQLLRALKYIHTANVFHRDLKPKNILANADCKLKICDFGLARVAFNDTPTAIFWTDYVATRWYrAPElcGSFFSKYTP 187
                         90       100
                 ....*....|....*....|....
gi 569026720 835 QSDVWSYGILLWEIFsLGLNPYPG 858
Cdd:cd07859  188 AIDIWSIGCIFAEVL-TGKPLFPG 210
STKc_GRK4_like cd05605
Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs ...
758-848 3.58e-07

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: 52.74  E-value: 3.58e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 758 FSSQVAQGMAFLASKNCIHRDVAARNVLLTN-GHVaKIGDFGLARDImnDSNYIVKGnaRL-PVKWMAPESIFDCVYTVQ 835
Cdd:cd05605  107 YAAEITCGLEHLHSERIVYRDLKPENILLDDhGHV-RISDLGLAVEI--PEGETIRG--RVgTVGYMAPEVVKNERYTFS 181
                         90
                 ....*....|...
gi 569026720 836 SDVWSYGILLWEI 848
Cdd:cd05605  182 PDWWGLGCLIYEM 194
STKc_CDK5 cd07839
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs ...
758-870 4.18e-07

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


Pssm-ID: 143344 [Multi-domain]  Cd Length: 284  Bit Score: 52.82  E-value: 4.18e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 758 FSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARdimndsnyivkgNARLPVK----------WMAPESI 827
Cdd:cd07839  104 FMFQLLKGLAFCHSHNVLHRDLKPQNLLINKNGELKLADFGLAR------------AFGIPVRcysaevvtlwYRPPDVL 171
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 569026720 828 FDC-VYTVQSDVWSYGILLWEIFSLGLNPYPGILVNSKFYKLVK 870
Cdd:cd07839  172 FGAkLYSTSIDMWSAGCIFAELANAGRPLFPGNDVDDQLKRIFR 215
STKc_DAPK3 cd14195
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs ...
583-858 4.73e-07

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: 52.31  E-value: 4.73e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 583 QFGKTLGAGAFGKVVEATAFGLGKEDAVLKVAVKMLKSTAHADEKEALMSELKIMSHLgQHENIVNLLGACTHGGPVLVI 662
Cdd:cd14195    8 EMGEELGSGQFAIVRKCREKGTGKEYAAKFIKKRRLSSSRRGVSREEIEREVNILREI-QHPNIITLHDIFENKTDVVLI 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 663 TEYCCYGDLLNFLRRKaeamlgpslspgqdpeggvdyknihlekkyvrrdsgfssqgvdtyvemrpvstssnDSFSEQDL 742
Cdd:cd14195   87 LELVSGGELFDFLAEK--------------------------------------------------------ESLTEEEA 110
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 743 DKedgrplelrdllhFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVA----KIGDFGLARDIMNDSNYivkGNARLP 818
Cdd:cd14195  111 TQ-------------FLKQILDGVHYLHSKRIAHFDLKPENIMLLDKNVPnpriKLIDFGIAHKIEAGNEF---KNIFGT 174
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 569026720 819 VKWMAPESIFDCVYTVQSDVWSYGILLWEIFSlGLNPYPG 858
Cdd:cd14195  175 PEFVAPEIVNYEPLGLEADMWSIGVITYILLS-GASPFLG 213
STKc_PAK5 cd06658
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the ...
762-856 4.88e-07

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: 52.35  E-value: 4.88e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 762 VAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDImndSNYIVKGNARLPVK-WMAPESIFDCVYTVQSDVWS 840
Cdd:cd06658  127 VLRALSYLHNQGVIHRDIKSDSILLTSDGRIKLSDFGFCAQV---SKEVPKRKSLVGTPyWMAPEVISRLPYGTEVDIWS 203
                         90
                 ....*....|....*.
gi 569026720 841 YGILLWEIFSlGLNPY 856
Cdd:cd06658  204 LGIMVIEMID-GEPPY 218
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
764-856 5.12e-07

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: 52.42  E-value: 5.12e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 764 QGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDIMNDSNYivKGNARLPVKWMAPESIFDCVYTVQSDVWSYGI 843
Cdd:cd06656  126 QALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSK--RSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGI 203
                         90
                 ....*....|...
gi 569026720 844 LLWEIFSlGLNPY 856
Cdd:cd06656  204 MAIEMVE-GEPPY 215
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
758-856 5.14e-07

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: 52.10  E-value: 5.14e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 758 FSSQVAQGMAFLASKNCIHRDVAARNVLLTN-GHVaKIGDFGLARdimndSNYIVKGNARL---PvKWMAPESIFDCVYT 833
Cdd:cd05611  102 YIAEVVLGVEDLHQRGIIHRDIKPENLLIDQtGHL-KLTDFGLSR-----NGLEKRHNKKFvgtP-DYLAPETILGVGDD 174
                         90       100
                 ....*....|....*....|...
gi 569026720 834 VQSDVWSYGILLWEiFSLGLNPY 856
Cdd:cd05611  175 KMSDWWSLGCVIFE-FLFGYPPF 196
STKc_GRK7 cd05607
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; ...
748-856 5.14e-07

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: 52.21  E-value: 5.14e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 748 RPLELRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDIMNDSNYIVKGNARlpvKWMAPESI 827
Cdd:cd05607   99 RGIEMERVIFYSAQITCGILHLHSLKIVYRDMKPENVLLDDNGNCRLSDLGLAVEVKEGKPITQRAGTN---GYMAPEIL 175
                         90       100
                 ....*....|....*....|....*....
gi 569026720 828 FDCVYTVQSDVWSYGILLWEIFSlGLNPY 856
Cdd:cd05607  176 KEESYSYPVDWFAMGCSIYEMVA-GRTPF 203
STKc_MAPK15-like cd07852
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and ...
761-849 5.50e-07

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


Pssm-ID: 270841 [Multi-domain]  Cd Length: 337  Bit Score: 52.56  E-value: 5.50e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 761 QVAQGMAFLASKNCIHRDVAARNVLL-TNGHVaKIGDFGLARDIMNDSNYIvkGNARL----PVKWM-APESIFDCV-YT 833
Cdd:cd07852  115 QLLKALKYLHSGGVIHRDLKPSNILLnSDCRV-KLADFGLARSLSQLEEDD--ENPVLtdyvATRWYrAPEILLGSTrYT 191
                         90
                 ....*....|....*.
gi 569026720 834 VQSDVWSYGILLWEIF 849
Cdd:cd07852  192 KGVDMWSVGCILGEML 207
STKc_ERK1_2_like cd07849
Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine ...
757-850 5.56e-07

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: 52.69  E-value: 5.56e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 757 HFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDIMNDSNYIVKGNARLPVKWM-APESIFDC-VYTV 834
Cdd:cd07849  110 YFLYQILRGLKYIHSANVLHRDLKPSNLLLNTNCDLKICDFGLARIADPEHDHTGFLTEYVATRWYrAPEIMLNSkGYTK 189
                         90
                 ....*....|....*.
gi 569026720 835 QSDVWSYGILLWEIFS 850
Cdd:cd07849  190 AIDIWSVGCILAEMLS 205
STKc_CDK2_3 cd07860
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; ...
737-848 6.02e-07

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: 52.12  E-value: 6.02e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 737 FSEQDLDK-EDGRP---LELRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLL-TNGHVaKIGDFGLARDImndsnyiv 811
Cdd:cd07860   80 FLHQDLKKfMDASAltgIPLPLIKSYLFQLLQGLAFCHSHRVLHRDLKPQNLLInTEGAI-KLADFGLARAF-------- 150
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 569026720 812 kgnaRLPVK----------WMAPESIFDC-VYTVQSDVWSYGILLWEI 848
Cdd:cd07860  151 ----GVPVRtythevvtlwYRAPEILLGCkYYSTAVDIWSLGCIFAEM 194
STKc_PKB_beta cd05595
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); ...
758-848 6.65e-07

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: 52.32  E-value: 6.65e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 758 FSSQVAQGMAFLASKNCIHRDVAARNVLLTN-GHVaKIGDFGLARDIMNDSNyIVKGNARLPvKWMAPESIFDCVYTVQS 836
Cdd:cd05595  100 YGAEIVSALEYLHSRDVVYRDIKLENLMLDKdGHI-KITDFGLCKEGITDGA-TMKTFCGTP-EYLAPEVLEDNDYGRAV 176
                         90
                 ....*....|..
gi 569026720 837 DVWSYGILLWEI 848
Cdd:cd05595  177 DWWGLGVVMYEM 188
STKc_SPEG_rpt2 cd14111
Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle ...
754-856 6.91e-07

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: 51.75  E-value: 6.91e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 754 DLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDiMNDSNYIVKGNARLPVKWMAPESIFDCVYT 833
Cdd:cd14111  100 DVVGYLVQILQGLEYLHGRRVLHLDIKPDNIMVTNLNAIKIVDFGSAQS-FNPLSLRQLGRRTGTLEYMAPEMVKGEPVG 178
                         90       100
                 ....*....|....*....|...
gi 569026720 834 VQSDVWSYGILLWEIFSlGLNPY 856
Cdd:cd14111  179 PPADIWSIGVLTYIMLS-GRSPF 200
STKc_GRK5 cd05632
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs ...
747-858 7.06e-07

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: 52.28  E-value: 7.06e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 747 GRP-LELRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTN-GHVaKIGDFGLARDIMNDSnyIVKGNARlPVKWMAP 824
Cdd:cd05632   97 GNPgFEEERALFYAAEILCGLEDLHRENTVYRDLKPENILLDDyGHI-RISDLGLAVKIPEGE--SIRGRVG-TVGYMAP 172
                         90       100       110
                 ....*....|....*....|....*....|....
gi 569026720 825 ESIFDCVYTVQSDVWSYGILLWEIFSlGLNPYPG 858
Cdd:cd05632  173 EVLNNQRYTLSPDYWGLGCLIYEMIE-GQSPFRG 205
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
740-858 7.29e-07

Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related Apoptosis-inducing protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DRAKs, also called STK17, were named based on their similarity (around 50% identity) to the kinase domain of DAPKs. They contain an N-terminal kinase domain and a C-terminal regulatory domain. Vertebrates contain two subfamily members, DRAK1 and DRAK2. Both DRAKs are localized to the nucleus, autophosphorylate themselves, and phosphorylate myosin light chain as a substrate. They may play a role in apoptotic signaling. The DRAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271008 [Multi-domain]  Cd Length: 268  Bit Score: 51.58  E-value: 7.29e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 740 QDLDKEDGRPLElRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLT----NGHVaKIGDFGLA---------RDIMND 806
Cdd:cd14106   96 QTLLDEEECLTE-ADVRRLMRQILEGVQYLHERNIVHLDLKPQNILLTsefpLGDI-KLCDFGISrvigegeeiREILGT 173
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 569026720 807 SNYIvkgnarlpvkwmAPESIFDCVYTVQSDVWSYGILLWEIFSlGLNPYPG 858
Cdd:cd14106  174 PDYV------------APEILSYEPISLATDMWSIGVLTYVLLT-GHSPFGG 212
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
741-913 7.57e-07

Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK16 is associated with many names including Myristylated and Palmitylated Serine/threonine Kinase 1 (MPSK1), Kinase related to cerevisiae and thaliana (Krct), and Protein Kinase expressed in day 12 fetal liver (PKL12). It is widely expressed in mammals with highest levels found in liver, testis, and kidney. It is localized in the Golgi but is translocated to the nucleus upon disorganization of the Golgi. STK16 is constitutively active and is capable of phosphorylating itself and other substrates. It may be involved in regulating stromal-epithelial interactions during mammary gland ductal morphogenesis. It may also function as a transcriptional co-activator of type-C natriuretic peptide and VEGF. The STK16 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270888 [Multi-domain]  Cd Length: 282  Bit Score: 51.91  E-value: 7.57e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 741 DLDKEDGRPLELRDLLHFSSQVAQG---MAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGlardIMNDSNYIVKGNA-- 815
Cdd:cd13986   94 ERRLVKGTFFPEDRILHIFLGICRGlkaMHEPELVPYAHRDIKPGNVLLSEDDEPILMDLG----SMNPARIEIEGRRea 169
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 816 ---------RLPVKWMAPEsIFD----CVYTVQSDVWSYGILLWEIFsLGLNPYPGIL---------VNSKFYKlvkdgy 873
Cdd:cd13986  170 lalqdwaaeHCTMPYRAPE-LFDvkshCTIDEKTDIWSLGCTLYALM-YGESPFERIFqkgdslalaVLSGNYS------ 241
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 569026720 874 qmaqpaFAPKNIYS-----IMQACWALEPTHRPTFQQICSFLQEQ 913
Cdd:cd13986  242 ------FPDNSRYSeelhqLVKSMLVVNPAERPSIDDLLSRVHDL 280
STKc_EIF2AK1_HRI cd14049
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
734-849 7.59e-07

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: 51.74  E-value: 7.59e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 734 NDSFSEQDLDKEDGRPLELRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLT-NGHVAKIGDFGLA-RDIMNDSNYIV 811
Cdd:cd14049  101 NKRPCEEEFKSAPYTPVDVDVTTKILQQLLEGVTYIHSMGIVHRDLKPRNIFLHgSDIHVRIGDFGLAcPDILQDGNDST 180
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 569026720 812 KGNARL---------PVKWMAPESIFDCVYTVQSDVWSYGILLWEIF 849
Cdd:cd14049  181 TMSRLNglthtsgvgTCLYAAPEQLEGSHYDFKSDMYSIGVILLELF 227
STKc_MOK cd07831
Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs ...
748-858 7.69e-07

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: 51.89  E-value: 7.69e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 748 RPLELRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVaKIGDFGLARDIMND---SNYIvkgnarlPVKWM-A 823
Cdd:cd07831   95 RPLPEKRVKNYMYQLLKSLDHMHRNGIFHRDIKPENILIKDDIL-KLADFGSCRGIYSKppyTEYI-------STRWYrA 166
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 569026720 824 PESIF-DCVYTVQSDVWSYGILLWEIFSlgLNP-YPG 858
Cdd:cd07831  167 PECLLtDGYYGPKMDIWAVGCVFFEILS--LFPlFPG 201
STKc_p38beta cd07878
Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase ...
575-858 7.72e-07

Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase (also called MAPK11); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38beta/MAPK11 is widely expressed in tissues and shows more similarity with p38alpha than with the other isoforms. Both are sensitive to pyridinylimidazoles and share some common substrates such as MAPK activated protein kinase 2 (MK2) and the transcription factors ATF2, c-Fos and, ELK-1. p38beta is involved in regulating the activation of the cyclooxygenase-2 promoter and the expression of TGFbeta-induced alpha-smooth muscle cell actin. p38 kinases are mitogen-activated protein kinases (MAPKs), serving as important mediators of cellular responses to extracellular signals. They are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. The p38beta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143383 [Multi-domain]  Cd Length: 343  Bit Score: 52.36  E-value: 7.72e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 575 WEFPRNnLQFGKTLGAGAFGKVVEATAFGLGKEDAVLKVAvKMLKSTAHADEKealMSELKIMSHLgQHENIVNLLGACT 654
Cdd:cd07878   11 WEVPER-YQNLTPVGSGAYGSVCSAYDTRLRQKVAVKKLS-RPFQSLIHARRT---YRELRLLKHM-KHENVIGLLDVFT 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 655 hggPVLVITEYccygdllnflrrkAEAMLGPSLSpgqdpegGVDYKNIHLEKKYVrrdsgfssqgvDTYVEMrpvstssn 734
Cdd:cd07878   85 ---PATSIENF-------------NEVYLVTNLM-------GADLNNIVKCQKLS-----------DEHVQF-------- 122
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 735 dsfseqdldkedgrplelrdLLHfssQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDIMND-SNYIVkg 813
Cdd:cd07878  123 --------------------LIY---QLLRGLKYIHSAGIIHRDLKPSNVAVNEDCELRILDFGLARQADDEmTGYVA-- 177
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 569026720 814 narlpVKWM-APESIFDCVYTVQS-DVWSYGILLWEIFSlGLNPYPG 858
Cdd:cd07878  178 -----TRWYrAPEIMLNWMHYNQTvDIWSVGCIMAELLK-GKALFPG 218
STKc_MAP4K3 cd06645
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
738-851 8.49e-07

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: 51.58  E-value: 8.49e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 738 SEQDLDKEDGrPLELRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLT-NGHVaKIGDFGLARDImndSNYIVKGNAR 816
Cdd:cd06645   94 SLQDIYHVTG-PLSESQIAYVSRETLQGLYYLHSKGKMHRDIKGANILLTdNGHV-KLADFGVSAQI---TATIAKRKSF 168
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 569026720 817 LPVK-WMAPESIF---DCVYTVQSDVWSYGILLWEIFSL 851
Cdd:cd06645  169 IGTPyWMAPEVAAverKGGYNQLCDIWAVGITAIELAEL 207
PTZ00036 PTZ00036
glycogen synthase kinase; Provisional
749-870 8.59e-07

glycogen synthase kinase; Provisional


Pssm-ID: 173333 [Multi-domain]  Cd Length: 440  Bit Score: 52.35  E-value: 8.59e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 749 PLELRDLlhFSSQVAQGMAFLASKNCIHRDVAARNVLLT-NGHVAKIGDFGLARDIMNDSNYIVKGNARLpvkWMAPESI 827
Cdd:PTZ00036 168 PLFLVKL--YSYQLCRALAYIHSKFICHRDLKPQNLLIDpNTHTLKLCDFGSAKNLLAGQRSVSYICSRF---YRAPELM 242
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 569026720 828 FDCV-YTVQSDVWSYGILLWEIFsLGlnpYPGILVNSKFYKLVK 870
Cdd:PTZ00036 243 LGATnYTTHIDLWSLGCIIAEMI-LG---YPIFSGQSSVDQLVR 282
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
570-856 9.39e-07

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 51.74  E-value: 9.39e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 570 PYNEKWEFprNNLQFGKTLGAGAFGKVVEATAFGLGKedavlKVAVKMLKSTA--HADEKEALMSELKIMSHLgQHENIV 647
Cdd:PTZ00263  10 PDTSSWKL--SDFEMGETLGTGSFGRVRIAKHKGTGE-----YYAIKCLKKREilKMKQVQHVAQEKSILMEL-SHPFIV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 648 NLLGACTHGGPVLVITEYCCYGDLLNFLRrkaeamlgpslSPGQDPeggvdyknihlekkyvrrdsgfssqgvdtyvemr 727
Cdd:PTZ00263  82 NMMCSFQDENRVYFLLEFVVGGELFTHLR-----------KAGRFP---------------------------------- 116
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 728 pvstssndsfseQDLDKedgrplelrdllHFSSQVAQGMAFLASKNCIHRDVAARNVLLTN-GHVaKIGDFGLARDImND 806
Cdd:PTZ00263 117 ------------NDVAK------------FYHAELVLAFEYLHSKDIIYRDLKPENLLLDNkGHV-KVTDFGFAKKV-PD 170
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 569026720 807 SNYIVKGNArlpvKWMAPESIFDCVYTVQSDVWSYGILLWEiFSLGLNPY 856
Cdd:PTZ00263 171 RTFTLCGTP----EYLAPEVIQSKGHGKAVDWWTMGVLLYE-FIAGYPPF 215
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
761-870 9.60e-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: 51.65  E-value: 9.60e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 761 QVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDIMND----SNYIVkgnarlpVKWM-APESIF-DCVYTV 834
Cdd:cd07846  108 QILRGIDFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAAPgevyTDYVA-------TRWYrAPELLVgDTKYGK 180
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 569026720 835 QSDVWSYGILLWEIFSlgLNPY-PGILVNSKFYKLVK 870
Cdd:cd07846  181 AVDVWAVGCLVTEMLT--GEPLfPGDSDIDQLYHIIK 215
STKc_BMPR1 cd14144
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type I Receptor; ...
750-848 9.64e-07

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


Pssm-ID: 271046 [Multi-domain]  Cd Length: 287  Bit Score: 51.71  E-value: 9.64e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 750 LELRDLLHFSSQVAQGMAFLASKNC--------IHRDVAARNVLLTNGHVAKIGDFGLARDIMNDSNYI-VKGNARLPVK 820
Cdd:cd14144   89 LDTQSMLKLAYSAACGLAHLHTEIFgtqgkpaiAHRDIKSKNILVKKNGTCCIADLGLAVKFISETNEVdLPPNTRVGTK 168
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 569026720 821 -WMAPESI--------FDCVytVQSDVWSYGILLWEI 848
Cdd:cd14144  169 rYMAPEVLdeslnrnhFDAY--KMADMYSFGLVLWEI 203
STKc_p38delta cd07879
Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase ...
575-850 9.72e-07

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


Pssm-ID: 143384 [Multi-domain]  Cd Length: 342  Bit Score: 51.83  E-value: 9.72e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 575 WEFPRNNLQFgKTLGAGAFGKVVEATAFGLGKedavlKVAVKMLKSTAHAD--EKEALmSELKIMSHLgQHENIVNLLGa 652
Cdd:cd07879   11 WELPERYTSL-KQVGSGAYGSVCSAIDKRTGE-----KVAIKKLSRPFQSEifAKRAY-RELTLLKHM-QHENVIGLLD- 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 653 cthggpvlVITEYCCYGDLLNFlrrkaeamlgpslspgqdpeggvdyknihlekkyvrrdsgfssqgvdtYVEMrpvsts 732
Cdd:cd07879   82 --------VFTSAVSGDEFQDF------------------------------------------------YLVM------ 99
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 733 sndSFSEQDLDKEDGRPLELRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDIMND-SNYIV 811
Cdd:cd07879  100 ---PYMQTDLQKIMGHPLSEDKVQYLVYQMLCGLKYIHSAGIIHRDLKPGNLAVNEDCELKILDFGLARHADAEmTGYVV 176
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 569026720 812 kgnarlpVKWM-APESIFDCV-YTVQSDVWSYGILLWEIFS 850
Cdd:cd07879  177 -------TRWYrAPEVILNWMhYNQTVDIWSVGCIMAEMLT 210
STKc_MLCK1 cd14191
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze ...
750-858 1.02e-06

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: 51.16  E-value: 1.02e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 750 LELRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTN--GHVAKIGDFGLARDIMN-DSNYIVKGNArlpvKWMAPES 826
Cdd:cd14191   97 LTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNktGTKIKLIDFGLARRLENaGSLKVLFGTP----EFVAPEV 172
                         90       100       110
                 ....*....|....*....|....*....|..
gi 569026720 827 IFDCVYTVQSDVWSYGILLWEIFSlGLNPYPG 858
Cdd:cd14191  173 INYEPIGYATDMWSIGVICYILVS-GLSPFMG 203
STKc_PLK3 cd14189
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the ...
757-906 1.09e-06

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: 51.08  E-value: 1.09e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 757 HFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLA----------RDIMNDSNYIvkgnarlpvkwmAPES 826
Cdd:cd14189  105 YYLKQIISGLKYLHLKGILHRDLKLGNFFINENMELKVGDFGLAarleppeqrkKTICGTPNYL------------APEV 172
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 827 IFDCVYTVQSDVWSYGILLWEIfsLGLNPYPGILVNSKFYKLVKDgYQMAQPAF----APKNIYSIMQAcwalEPTHRPT 902
Cdd:cd14189  173 LLRQGHGPESDVWSLGCVMYTL--LCGNPPFETLDLKETYRCIKQ-VKYTLPASlslpARHLLAGILKR----NPGDRLT 245

                 ....
gi 569026720 903 FQQI 906
Cdd:cd14189  246 LDQI 249
STKc_IKK_alpha cd14039
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
588-912 1.28e-06

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: 51.07  E-value: 1.28e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 588 LGAGAFGKVVEATafglgKEDAVLKVAVKMLKSTAHADEKEALMSELKIMSHLgQHENIVNllgAC---------THGGP 658
Cdd:cd14039    1 LGTGGFGNVCLYQ-----NQETGEKIAIKSCRLELSVKNKDRWCHEIQIMKKL-NHPNVVK---ACdvpeemnflVNDVP 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 659 VLVItEYCCYGDLLNFLRRkaeamlgpslspgqdPEGGVDYKnihlekkyvrrdsgfSSQgvdtyvemrpvstssndsfs 738
Cdd:cd14039   72 LLAM-EYCSGGDLRKLLNK---------------PENCCGLK---------------ESQ-------------------- 100
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 739 eqdldkedgrplelrdLLHFSSQVAQGMAFLASKNCIHRDVAARNVLL--TNGH-VAKIGDFGLARDIMNDS---NYIVK 812
Cdd:cd14039  101 ----------------VLSLLSDIGSGIQYLHENKIIHRDLKPENIVLqeINGKiVHKIIDLGYAKDLDQGSlctSFVGT 164
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 813 gnarlpVKWMAPESIFDCVYTVQSDVWSYGILLWEIFSlGLNPYPGILVNSKFYKLVKDGyqmaqpafAPKNIYSIMQAC 892
Cdd:cd14039  165 ------LQYLAPELFENKSYTVTVDYWSFGTMVFECIA-GFRPFLHNLQPFTWHEKIKKK--------DPKHIFAVEEMN 229
                        330       340
                 ....*....|....*....|.
gi 569026720 893 WALE-PTHRPTFQQICSFLQE 912
Cdd:cd14039  230 GEVRfSTHLPQPNNLCSLIVE 250
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
756-856 1.49e-06

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: 50.90  E-value: 1.49e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 756 LHFSSQVAQGMAFLASKNCIHRDVAARNVLLT-NGHVaKIGDFGLARDIMnDSNYIVKGNArlpvKWMAPESIFDCVYTV 834
Cdd:cd05612  104 LFYASEIVCALEYLHSKEIVYRDLKPENILLDkEGHI-KLTDFGFAKKLR-DRTWTLCGTP----EYLAPEVIQSKGHNK 177
                         90       100
                 ....*....|....*....|..
gi 569026720 835 QSDVWSYGILLWEIFSlGLNPY 856
Cdd:cd05612  178 AVDWWALGILIYEMLV-GYPPF 198
STKc_CDKL5 cd07848
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs ...
761-858 1.62e-06

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: 50.76  E-value: 1.62e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 761 QVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDIM--NDSNYivkgNARLPVKWM-APESIFDCVYTVQSD 837
Cdd:cd07848  108 QLIKAIHWCHKNDIVHRDIKPENLLISHNDVLKLCDFGFARNLSegSNANY----TEYVATRWYrSPELLLGAPYGKAVD 183
                         90       100
                 ....*....|....*....|.
gi 569026720 838 VWSYGILLWEIfSLGLNPYPG 858
Cdd:cd07848  184 MWSVGCILGEL-SDGQPLFPG 203
STKc_PAK4 cd06657
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the ...
762-856 1.73e-06

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: 50.79  E-value: 1.73e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 762 VAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDIMNDSNYiVKGNARLPVkWMAPESIFDCVYTVQSDVWSY 841
Cdd:cd06657  125 VLKALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVPR-RKSLVGTPY-WMAPELISRLPYGPEVDIWSL 202
                         90
                 ....*....|....*
gi 569026720 842 GILLWEIFSlGLNPY 856
Cdd:cd06657  203 GIMVIEMVD-GEPPY 216
STKc_MAP3K8 cd13995
Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) ...
749-914 1.74e-06

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


Pssm-ID: 270897 [Multi-domain]  Cd Length: 256  Bit Score: 50.39  E-value: 1.74e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 749 PLELRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHvAKIGDFGLARDiMNDSNYIVKgNARLPVKWMAPESIF 828
Cdd:cd13995   92 PMREFEIIWVTKHVLKGLDFLHSKNIIHHDIKPSNIVFMSTK-AVLVDFGLSVQ-MTEDVYVPK-DLRGTEIYMSPEVIL 168
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 829 DCVYTVQSDVWSYGILLWEIFSlGLNP----YPGILVNSKFYKLVKDGYQMAQ-PAFAPKNIYSIMQACWALEPTHRPTF 903
Cdd:cd13995  169 CRGHNTKADIYSLGATIIHMQT-GSPPwvrrYPRSAYPSYLYIIHKQAPPLEDiAQDCSPAMRELLEAALERNPNHRSSA 247
                        170
                 ....*....|.
gi 569026720 904 QQIcsfLQEQA 914
Cdd:cd13995  248 AEL---LKHEA 255
STKc_CDC2L1 cd07843
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze ...
751-850 2.05e-06

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: 50.69  E-value: 2.05e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 751 ELRDLLHfssQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDI-MNDSNYivkgnARLPVK-WM-APESI 827
Cdd:cd07843  107 EVKCLML---QLLSGVAHLHDNWILHRDLKTSNLLLNNRGILKICDFGLAREYgSPLKPY-----TQLVVTlWYrAPELL 178
                         90       100
                 ....*....|....*....|....
gi 569026720 828 FDC-VYTVQSDVWSYGILLWEIFS 850
Cdd:cd07843  179 LGAkEYSTAIDMWSVGCIFAELLT 202
STKc_DCKL1 cd14183
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called ...
753-858 2.07e-06

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: 50.38  E-value: 2.07e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 753 RDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLL----TNGHVAKIGDFGLArDIMNDSNYIVKGNArlpvKWMAPESIF 828
Cdd:cd14183  104 RDASGMLYNLASAIKYLHSLNIVHRDIKPENLLVyehqDGSKSLKLGDFGLA-TVVDGPLYTVCGTP----TYVAPEIIA 178
                         90       100       110
                 ....*....|....*....|....*....|
gi 569026720 829 DCVYTVQSDVWSYGILLWeIFSLGLNPYPG 858
Cdd:cd14183  179 ETGYGLKVDIWAAGVITY-ILLCGFPPFRG 207
STKc_CaMKK1 cd14200
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; ...
738-856 2.22e-06

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: 50.33  E-value: 2.22e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 738 SEQDLDKEDGRpLELRDllhfssqVAQGMAFLASKNCIHRDVAARNVLL-TNGHVaKIGDFGLARDIM-NDSnyIVKGNA 815
Cdd:cd14200  117 SDKPFSEDQAR-LYFRD-------IVLGIEYLHYQKIVHRDIKPSNLLLgDDGHV-KIADFGVSNQFEgNDA--LLSSTA 185
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 569026720 816 RLPVkWMAPESIFDcvyTVQS------DVWSYGILLWeIFSLGLNPY 856
Cdd:cd14200  186 GTPA-FMAPETLSD---SGQSfsgkalDVWAMGVTLY-CFVYGKCPF 227
STKc_BMPR1b cd14219
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IB; STKs ...
755-902 2.37e-06

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: 50.43  E-value: 2.37e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 755 LLHFSSQV--AQGMAFLAsknciHRDVAARNVLLTNGHVAKIGDFGLARDIMNDSNYI-VKGNARLPVK-WMAPESIFDC 830
Cdd:cd14219  115 LCHLHTEIfsTQGKPAIA-----HRDLKSKNILVKKNGTCCIADLGLAVKFISDTNEVdIPPNTRVGTKrYMPPEVLDES 189
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 831 VYT------VQSDVWSYGILLWEIFSLGLN---------PYPGILVNSKFYKLVKD--GYQMAQPAFAP--------KNI 885
Cdd:cd14219  190 LNRnhfqsyIMADMYSFGLILWEVARRCVSggiveeyqlPYHDLVPSDPSYEDMREivCIKRLRPSFPNrwssdeclRQM 269
                        170
                 ....*....|....*..
gi 569026720 886 YSIMQACWALEPTHRPT 902
Cdd:cd14219  270 GKLMTECWAHNPASRLT 286
STKc_SGK2 cd05603
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; ...
758-921 2.38e-06

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: 50.74  E-value: 2.38e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 758 FSSQVAQGMAFLASKNCIHRDVAARNVLL-TNGHVAkIGDFGLARDIM--NDSNYIVKGNArlpvKWMAPESIFDCVYTV 834
Cdd:cd05603  101 YAAEVASAIGYLHSLNIIYRDLKPENILLdCQGHVV-LTDFGLCKEGMepEETTSTFCGTP----EYLAPEVLRKEPYDR 175
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 835 QSDVWSYGILLWEIFsLGLNPypgilvnskFYKlvKDGYQMAQpafapkNIYSimqacwalEPTHRPTFQQI--CSFLQE 912
Cdd:cd05603  176 TVDWWCLGAVLYEML-YGLPP---------FYS--RDVSQMYD------NILH--------KPLHLPGGKTVaaCDLLQG 229

                 ....*....
gi 569026720 913 QAQEDRRER 921
Cdd:cd05603  230 LLHKDQRRR 238
STKc_YPK1_like cd05585
Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the ...
758-871 2.46e-06

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: 50.65  E-value: 2.46e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 758 FSSQVAQGMAFLASKNCIHRDVAARNVLLT-NGHVAkIGDFGLARDIMNDSNyivKGNARLPV-KWMAPESIFDCVYTVQ 835
Cdd:cd05585   99 YTAELLCALECLHKFNVIYRDLKPENILLDyTGHIA-LCDFGLCKLNMKDDD---KTNTFCGTpEYLAPELLLGHGYTKA 174
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 569026720 836 SDVWSYGILLWEIFSlGLNPYPGILVNSKFYKLVKD 871
Cdd:cd05585  175 VDWWTLGVLLYEMLT-GLPPFYDENTNEMYRKILQE 209
STKc_PCTAIRE1 cd07873
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer ...
739-870 2.63e-06

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: 50.39  E-value: 2.63e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 739 EQDLDkEDGRPLELRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLAR----DIMNDSNYIVkgn 814
Cdd:cd07873   87 KQYLD-DCGNSINMHNVKLFLFQLLRGLAYCHRRKVLHRDLKPQNLLINERGELKLADFGLARaksiPTKTYSNEVV--- 162
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 569026720 815 arlpVKWMAPESIF--DCVYTVQSDVWSYGILLWEIfSLGLNPYPGILVNSKFYKLVK 870
Cdd:cd07873  163 ----TLWYRPPDILlgSTDYSTQIDMWGVGCIFYEM-STGRPLFPGSTVEEQLHFIFR 215
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
209-290 2.73e-06

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: 46.34  E-value: 2.73e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720   209 PAELVRIRGEAAQIVCSASSvDVNFDVFLQHNNTKLaIPQQSDFHNNRYQKVLTLNLDQVDFQHAGNYSCVASNVQGKHS 288
Cdd:smart00410   1 PPSVTVKEGESVTLSCEASG-SPPPEVTWYKQGGKL-LAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSAS 78

                   ..
gi 569026720   289 TS 290
Cdd:smart00410  79 SG 80
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
746-856 2.98e-06

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: 49.83  E-value: 2.98e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 746 DGRPLELRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTN-GHVaKIGDFGLARDIMNDSNyiVKGNARLPvKWMAP 824
Cdd:cd05577   88 GTRGFSEARAIFYAAEIICGLEHLHNRFIVYRDLKPENILLDDhGHV-RISDLGLAVEFKGGKK--IKGRVGTH-GYMAP 163
                         90       100       110
                 ....*....|....*....|....*....|...
gi 569026720 825 ESIFDCV-YTVQSDVWSYGILLWEIFSlGLNPY 856
Cdd:cd05577  164 EVLQKEVaYDFSVDWFALGCMLYEMIA-GRSPF 195
STKc_WNK cd13983
Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze ...
750-906 2.99e-06

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: 49.92  E-value: 2.99e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 750 LELRDLLHFSSQVAQGMAFLASKN--CIHRDVAARNVLL--TNGHVaKIGDFGLARDIMNDSNYIVKGNarlPvKWMAPE 825
Cdd:cd13983   99 LKLKVIKSWCRQILEGLNYLHTRDppIIHRDLKCDNIFIngNTGEV-KIGDLGLATLLRQSFAKSVIGT---P-EFMAPE 173
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 826 sIFDCVYTVQSDVWSYGILLWEIFSlGLNPYPGILVNSKFYKLVKDGYqmaQPA----FAPKNIYSIMQACWAlEPTHRP 901
Cdd:cd13983  174 -MYEEHYDEKVDIYAFGMCLLEMAT-GEYPYSECTNAAQIYKKVTSGI---KPEslskVKDPELKDFIEKCLK-PPDERP 247

                 ....*
gi 569026720 902 TFQQI 906
Cdd:cd13983  248 SAREL 252
STKc_IRAK1 cd14159
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 1; ...
588-850 3.04e-06

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: 50.21  E-value: 3.04e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 588 LGAGAFGKVVEATAFGLgkedavlKVAVKMLKSTAHAD---EKEALMSELKIMSHLgQHENIVNLLGACTHGGpvlvitE 664
Cdd:cd14159    1 IGEGGFGCVYQAVMRNT-------EYAVKRLKEDSELDwsvVKNSFLTEVEKLSRF-RHPNIVDLAGYSAQQG------N 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 665 YC-CYGDLlnflrrkaeamlgpslspgqdPEGGVDyKNIHLEKKYVrrdsgfssqgvdtyvemrpvstssndsfseqdld 743
Cdd:cd14159   67 YClIYVYL---------------------PNGSLE-DRLHCQVSCP---------------------------------- 90
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 744 kedgrPLELRDLLHFSSQVAQGMAFL--ASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDIMNDSN----------YIV 811
Cdd:cd14159   91 -----CLSWSQRLHVLLGTARAIQYLhsDSPSLIHGDVKSSNILLDAALNPKLGDFGLARFSRRPKQpgmsstlartQTV 165
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 569026720 812 KGN-ARLPvkwmaPESIFDCVYTVQSDVWSYGILLWEIFS 850
Cdd:cd14159  166 RGTlAYLP-----EEYVKTGTLSVEIDVYSFGVVLLELLT 200
STKc_PDIK1L cd13977
Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs ...
758-846 3.10e-06

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


Pssm-ID: 270879 [Multi-domain]  Cd Length: 322  Bit Score: 50.25  E-value: 3.10e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 758 FSSQVAQGMAFLASKNCIHRDVAARNVLLTNGH---VAKIGDFGLARdIMNDSNYIVKGNARLPVKW----------MAP 824
Cdd:cd13977  139 FMLQLSSALAFLHRNQIVHRDLKPDNILISHKRgepILKVADFGLSK-VCSGSGLNPEEPANVNKHFlssacgsdfyMAP 217
                         90       100
                 ....*....|....*....|..
gi 569026720 825 EsIFDCVYTVQSDVWSYGILLW 846
Cdd:cd13977  218 E-VWEGHYTAKADIFALGIIIW 238
STKc_GRK4 cd05631
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs ...
758-856 3.79e-06

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK4 has a limited tissue distribution. It is mainly found in the testis, but is also present in the cerebellum and kidney. It is expressed as multiple splice variants with different domain architectures and is post-translationally palmitoylated and localized in the membrane. GRK4 polymorphisms are associated with hypertension and salt sensitivity, as they cause hyperphosphorylation, desensitization, and internalization of the dopamine 1 (D1) receptor while increasing the expression of the angiotensin II type 1 receptor. GRK4 plays a crucial role in the D1 receptor regulation of sodium excretion and blood pressure. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173720 [Multi-domain]  Cd Length: 285  Bit Score: 49.61  E-value: 3.79e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 758 FSSQVAQGMAFLASKNCIHRDVAARNVLLTN-GHVaKIGDFGLARDIMNDSNyiVKGNARlPVKWMAPESIFDCVYTVQS 836
Cdd:cd05631  107 YAAELCCGLEDLQRERIVYRDLKPENILLDDrGHI-RISDLGLAVQIPEGET--VRGRVG-TVGYMAPEVINNEKYTFSP 182
                         90       100
                 ....*....|....*....|
gi 569026720 837 DVWSYGILLWEIFSlGLNPY 856
Cdd:cd05631  183 DWWGLGCLIYEMIQ-GQSPF 201
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
581-846 3.95e-06

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: 49.37  E-value: 3.95e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 581 NLQFGKTLGAGAFGKVVEATAFGLGKedavlKVAVKMLKSTAHADEKEALMSELK-------------IMSHLGQHENIV 647
Cdd:cd14077    2 NWEFVKTIGAGSMGKVKLAKHIRTGE-----KCAIKIIPRASNAGLKKEREKRLEkeisrdirtireaALSSLLNHPHIC 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 648 NLLGACTHGGPVLVITEYCCYGDLLNFLrrkaeamlgpsLSPGQDPEggvdykniHLEKKYVRrdsgfssqgvdtyvemr 727
Cdd:cd14077   77 RLRDFLRTPNHYYMLFEYVDGGQLLDYI-----------ISHGKLKE--------KQARKFAR----------------- 120
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 728 pvstssndsfseqdldkedgrplelrdllhfssQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLardimndS 807
Cdd:cd14077  121 ---------------------------------QIASALDYLHRNSIVHRDLKIENILISKSGNIKIIDFGL-------S 160
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 569026720 808 NyIVKGNARL-----PVKWMAPESIFDCVYT-VQSDVWSYGILLW 846
Cdd:cd14077  161 N-LYDPRRLLrtfcgSLYFAAPELLQAQPYTgPEVDVWSFGVVLY 204
STKc_BMPR1a cd14220
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IA Receptor; ...
750-906 4.10e-06

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: 49.65  E-value: 4.10e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 750 LELRDLLHFSSQVAQGMAFLAS-------KNCI-HRDVAARNVLLTNGHVAKIGDFGLARDIMNDSNYI-VKGNARLPVK 820
Cdd:cd14220   89 LDTRALLKLAYSAACGLCHLHTeiygtqgKPAIaHRDLKSKNILIKKNGTCCIADLGLAVKFNSDTNEVdVPLNTRVGTK 168
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 821 -WMAPESIFDCVYT------VQSDVWSYGILLWEIFSLGLN---------PYPGILVNSKFYKLVKDGYQMA--QPAFAP 882
Cdd:cd14220  169 rYMAPEVLDESLNKnhfqayIMADIYSFGLIIWEMARRCVTggiveeyqlPYYDMVPSDPSYEDMREVVCVKrlRPTVSN 248
                        170       180       190
                 ....*....|....*....|....*....|..
gi 569026720 883 --------KNIYSIMQACWALEPTHRPTFQQI 906
Cdd:cd14220  249 rwnsdeclRAVLKLMSECWAHNPASRLTALRI 280
STKc_Aurora-B_like cd14117
Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs ...
576-906 4.13e-06

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: 49.48  E-value: 4.13e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 576 EFPRNNLQFGKTLGAGAFGKVVEATAfglgKEDAVLkVAVKML-KSTAHADEKE-ALMSELKIMSHLgQHENIVNLLGAC 653
Cdd:cd14117    2 KFTIDDFDIGRPLGKGKFGNVYLARE----KQSKFI-VALKVLfKSQIEKEGVEhQLRREIEIQSHL-RHPNILRLYNYF 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 654 THGGPVLVITEYCCYGDLlnflrrkaeamlgpslspgqdpeggvdYKNIhleKKYVRrdsgFSSQGVDTYVEmrpvstss 733
Cdd:cd14117   76 HDRKRIYLILEYAPRGEL---------------------------YKEL---QKHGR----FDEQRTATFME-------- 113
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 734 ndsfseqdldkedgrplELRDLLHFSSqvaqgmaflaSKNCIHRDVAARNVLLTNGHVAKIGDFG-------LARDIMND 806
Cdd:cd14117  114 -----------------ELADALHYCH----------EKKVIHRDIKPENLLMGYKGELKIADFGwsvhapsLRRRTMCG 166
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 807 SnyivkgnarlpVKWMAPESIFDCVYTVQSDVWSYGILLWEIFsLGLNPYPGILVNSKFYKLVKDGYQMaqPAFAPKNIY 886
Cdd:cd14117  167 T-----------LDYLPPEMIEGRTHDEKVDLWCIGVLCYELL-VGMPPFESASHTETYRRIVKVDLKF--PPFLSDGSR 232
                        330       340
                 ....*....|....*....|
gi 569026720 887 SIMQACWALEPTHRPTFQQI 906
Cdd:cd14117  233 DLISKLLRYHPSERLPLKGV 252
PKc_YAK1 cd14212
Catalytic domain of the Dual-specificity protein kinase, YAK1; Dual-specificity PKs catalyze ...
748-870 4.61e-06

Catalytic domain of the Dual-specificity protein kinase, YAK1; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. This subfamily is composed of proteins with similarity to Saccharomyces cerevisiae YAK1 (or Yak1p), a dual-specificity kinase that autophosphorylates at tyrosine residues and phosphorylates substrates on S/T residues. YAK1 phosphorylates and activates the transcription factors Hsf1 and Msn2, which play important roles in cellular homeostasis during stress conditions including heat shock, oxidative stress, and nutrient deficiency. It also phosphorylates the protein POP2, a component of a complex that regulates transcription, under glucose-deprived conditions. It functions as a part of a glucose-sensing system that is involved in controlling growth in yeast. The YAK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271114 [Multi-domain]  Cd Length: 330  Bit Score: 49.56  E-value: 4.61e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 748 RPLELRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVA--KIGDFGLArdIMNDS---NYIVKGNARlpvkwm 822
Cdd:cd14212   98 RGLSLQLIRKFLQQLLDALSVLKDARIIHCDLKPENILLVNLDSPeiKLIDFGSA--CFENYtlyTYIQSRFYR------ 169
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 569026720 823 APESIFDCVYTVQSDVWSYGILLWEIFsLGLNPYPGilvNSKFYKLVK 870
Cdd:cd14212  170 SPEVLLGLPYSTAIDMWSLGCIAAELF-LGLPLFPG---NSEYNQLSR 213
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
772-908 4.87e-06

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: 49.04  E-value: 4.87e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 772 KNCIHRDVAARNVLLTNGHVAKIGDFGLARDIMNDSNYI--VKGNarlpVKWMAPESIFDCVYTVQSDVWSYGILLWEIF 849
Cdd:cd08528  133 KQIVHRDLKPNNIMLGEDDKVTITDFGLAKQKGPESSKMtsVVGT----ILYSCPEIVQNEPYGEKADIWALGCILYQMC 208
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 569026720 850 SLGlNPYPGILVNSKFYKLVKDGYqmaQPafAPKNIYS-----IMQACWALEPTHRPTFQQICS 908
Cdd:cd08528  209 TLQ-PPFYSTNMLTLATKIVEAEY---EP--LPEGMYSdditfVIRSCLTPDPEARPDIVEVSS 266
STKc_MSK1_N cd05613
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
581-856 4.95e-06

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: 49.23  E-value: 4.95e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 581 NLQFGKTLGAGAFGKVVEATAfgLGKEDAVLKVAVKMLKSTA---HADEKEALMSELKIMSHLGQhenivnllgacthgG 657
Cdd:cd05613    1 NFELLKVLGTGAYGKVFLVRK--VSGHDAGKLYAMKVLKKATivqKAKTAEHTRTERQVLEHIRQ--------------S 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 658 PVLVITEYCCYGDllnflrrkaeamlgpslspgqdpeggvdyKNIHLEKKYVRRDSGFssqgvdTYVEMRpvstssnDSF 737
Cdd:cd05613   65 PFLVTLHYAFQTD-----------------------------TKLHLILDYINGGELF------THLSQR-------ERF 102
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 738 SEQDLdkedgrplelrdlLHFSSQVAQGMAFLASKNCIHRDVAARNVLL-TNGHVAkIGDFGLARDIMNDSN---YIVKG 813
Cdd:cd05613  103 TENEV-------------QIYIGEIVLALEHLHKLGIIYRDIKLENILLdSSGHVV-LTDFGLSKEFLLDENeraYSFCG 168
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 569026720 814 NarlpVKWMAPESIF--DCVYTVQSDVWSYGILLWEIFSlGLNPY 856
Cdd:cd05613  169 T----IEYMAPEIVRggDSGHDKAVDWWSLGVLMYELLT-GASPF 208
STKc_MAST cd05609
Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine ...
768-871 5.05e-06

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: 49.33  E-value: 5.05e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 768 FLASKNCIHRDVAARNVLLTN-GHVaKIGDFGLAR-DIMNDSNYIVKGNARLPVK------------WMAPESIFDCVYT 833
Cdd:cd05609  115 YLHSYGIVHRDLKPDNLLITSmGHI-KLTDFGLSKiGLMSLTTNLYEGHIEKDTRefldkqvcgtpeYIAPEVILRQGYG 193
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 569026720 834 VQSDVWSYGILLWEiFSLGLNPYPGILVNSKFYKLVKD 871
Cdd:cd05609  194 KPVDWWAMGIILYE-FLVGCVPFFGDTPEELFGQVISD 230
STKc_MLCK4 cd14193
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze ...
581-858 5.56e-06

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: 49.14  E-value: 5.56e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 581 NLQFGKTLGAGAFGKV--VEATAFGLgkedavlKVAVKMLKSTAHaDEKEALMSELKIMSHLgQHENIVNLLGACTHGGP 658
Cdd:cd14193    5 NVNKEEILGGGRFGQVhkCEEKSSGL-------KLAAKIIKARSQ-KEKEEVKNEIEVMNQL-NHANLIQLYDAFESRND 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 659 VLVITEYCCYGDLLNflrrkaeamlgpslspgqdpeggvdyknihlekkyvrrdsgfssqgvdtyvemRPVSTSSNdsfs 738
Cdd:cd14193   76 IVLVMEYVDGGELFD-----------------------------------------------------RIIDENYN---- 98
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 739 eqdldkedgrpLELRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTN--GHVAKIGDFGLARDIMNDSNyiVKGNAR 816
Cdd:cd14193   99 -----------LTELDTILFIKQICEGIQYMHQMYILHLDLKPENILCVSreANQVKIIDFGLARRYKPREK--LRVNFG 165
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 569026720 817 LPvKWMAPESI-FDCVyTVQSDVWSYGILLWEIFSlGLNPYPG 858
Cdd:cd14193  166 TP-EFLAPEVVnYEFV-SFPTDMWSLGVIAYMLLS-GLSPFLG 205
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
401-489 6.68e-06

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 433584 [Multi-domain]  Cd Length: 75  Bit Score: 44.88  E-value: 6.68e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720  401 PPEVSV----IWTFINGSGTLLCAASGYPQPNVTWLQCSghtdrcdeaqvlqvwddpypEVLSQEPFHKVTVQSLLTVE- 475
Cdd:pfam13927   1 KPVITVspssVVVVEGETVTLTCEASGSPPPTITWYKNG--------------------GKLSSGRTSLVGGNGTLTISn 60
                          90
                  ....*....|....*
gi 569026720  476 -TLEHNQTYECRAHN 489
Cdd:pfam13927  61 vTREDSGTYTCTASN 75
STKc_TGFbR1_ACVR1b_ACVR1c cd14143
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta Type I ...
749-848 6.90e-06

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: 48.98  E-value: 6.90e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 749 PLELRDLLHFSSQVAQGMAFL-------ASKNCI-HRDVAARNVLLTNGHVAKIGDFGLARDIMNDSNYI-VKGNARLPV 819
Cdd:cd14143   88 TVTVEGMIKLALSIASGLAHLhmeivgtQGKPAIaHRDLKSKNILVKKNGTCCIADLGLAVRHDSATDTIdIAPNHRVGT 167
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 569026720 820 K-WMAPESIFDCVYTV------QSDVWSYGILLWEI 848
Cdd:cd14143  168 KrYMAPEVLDDTINMKhfesfkRADIYALGLVFWEI 203
STKc_IKK_beta cd14038
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
760-856 7.53e-06

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: 48.81  E-value: 7.53e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 760 SQVAQGMAFLASKNCIHRDVAARNVLLTNGH---VAKIGDFGLARDiMNDSNYIVKGNARLpvKWMAPESIFDCVYTVQS 836
Cdd:cd14038  108 SDISSALRYLHENRIIHRDLKPENIVLQQGEqrlIHKIIDLGYAKE-LDQGSLCTSFVGTL--QYLAPELLEQQKYTVTV 184
                         90       100
                 ....*....|....*....|
gi 569026720 837 DVWSYGILLWEIFSlGLNPY 856
Cdd:cd14038  185 DYWSFGTLAFECIT-GFRPF 203
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
754-856 7.76e-06

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type II; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. There are several types of CaMKs including CaMKI, CaMKII, and CaMKIV. CaMKs contain an N-terminal catalytic domain followed by a regulatory domain that harbors a CaM binding site. In addition, CaMKII contains a C-terminal association domain that facilitates oligomerization. There are four CaMKII proteins (alpha, beta, gamma, delta) encoded by different genes; each gene undergoes alternative splicing to produce more than 30 isoforms. CaMKII-alpha and -beta are enriched in neurons while CaMKII-gamma and -delta are predominant in myocardium. CaMKII is a signaling molecule that translates upstream calcium and reactive oxygen species (ROS) signals into downstream responses that play important roles in synaptic function and cardiovascular physiology. It is a major component of the postsynaptic density and is critical in regulating synaptic plasticity including long-term potentiation. It is critical in regulating ion channels and proteins involved in myocardial excitation-contraction and excitation-transcription coupling. Excessive CaMKII activity promotes processes that contribute to heart failure and arrhythmias. The CaMKII subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270988 [Multi-domain]  Cd Length: 292  Bit Score: 48.96  E-value: 7.76e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 754 DLLHFSSQVAQGMAFLASKNCIHRDVAARNVLL---TNGHVAKIGDFGLARDIMNDSNYIVkGNARLPVkWMAPESIFDC 830
Cdd:cd14086  101 DASHCIQQILESVNHCHQNGIVHRDLKPENLLLaskSKGAAVKLADFGLAIEVQGDQQAWF-GFAGTPG-YLSPEVLRKD 178
                         90       100
                 ....*....|....*....|....*.
gi 569026720 831 VYTVQSDVWSYGILLWeIFSLGLNPY 856
Cdd:cd14086  179 PYGKPVDIWACGVILY-ILLVGYPPF 203
PK_Unc-89_rpt1 cd14109
Pseudokinase domain, first repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein ...
753-859 8.21e-06

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: 48.28  E-value: 8.21e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 753 RDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVaKIGDFGLARDIMNDSnyiVKGNARLPVKWMAPESIFDCVY 832
Cdd:cd14109   99 RQVAVFVRQLLLALKHMHDLGIAHLDLRPEDILLQDDKL-KLADFGQSRRLLRGK---LTTLIYGSPEFVSPEIVNSYPV 174
                         90       100
                 ....*....|....*....|....*..
gi 569026720 833 TVQSDVWSYGILLWEIFSlGLNPYPGI 859
Cdd:cd14109  175 TLATDMWSVGVLTYVLLG-GISPFLGD 200
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
761-845 8.27e-06

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: 48.47  E-value: 8.27e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 761 QVAQGMAFLASKNCIHRDVAARNVLLTNGH--VAKIGDFGLARDImnDSnyIVKGNAR-LPvkWMAPEsIFDCV----YT 833
Cdd:cd13987   99 QLASALDFMHSKNLVHRDIKPENVLLFDKDcrRVKLCDFGLTRRV--GS--TVKRVSGtIP--YTAPE-VCEAKknegFV 171
                         90
                 ....*....|....
gi 569026720 834 VQ--SDVWSYGILL 845
Cdd:cd13987  172 VDpsIDVWAFGVLL 185
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
416-492 9.37e-06

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: 44.24  E-value: 9.37e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 569026720 416 TLLCAASGYPQPNVTWLqcsghtdrcdeaqvlqvWDDPYPEVLSQEPFHKVTVQSLLTVE--TLEHNQTYECRAHNSVG 492
Cdd:cd00096    2 TLTCSASGNPPPTITWY-----------------KNGKPLPPSSRDSRRSELGNGTLTISnvTLEDSGTYTCVASNSAG 63
STKc_PCTAIRE2 cd07872
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer ...
747-866 9.39e-06

Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PCTAIRE-2 is specifically expressed in neurons in the central nervous system, mainly in terminally differentiated neurons. It associates with Trap (Tudor repeat associator with PCTAIRE-2) and could play a role in regulating mitochondrial function in neurons. PCTAIRE-2 shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PCTAIRE-2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143377 [Multi-domain]  Cd Length: 309  Bit Score: 48.83  E-value: 9.39e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 747 GRPLELRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLAR----DIMNDSNYIVkgnarlpVKWM 822
Cdd:cd07872   98 GNIMSMHNVKIFLYQILRGLAYCHRRKVLHRDLKPQNLLINERGELKLADFGLARaksvPTKTYSNEVV-------TLWY 170
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 569026720 823 APESIF--DCVYTVQSDVWSYGILLWEIFSlGLNPYPGILVNSKFY 866
Cdd:cd07872  171 RPPDVLlgSSEYSTQIDMWGVGCIFFEMAS-GRPLFPGSTVEDELH 215
PHA03212 PHA03212
serine/threonine kinase US3; Provisional
746-848 9.76e-06

serine/threonine kinase US3; Provisional


Pssm-ID: 165478 [Multi-domain]  Cd Length: 391  Bit Score: 48.84  E-value: 9.76e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 746 DGRPLELRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLA---RDIMNDSNYIVKGNarlpVKWM 822
Cdd:PHA03212 175 AKRNIAICDILAIERSVLRAIQYLHENRIIHRDIKAENIFINHPGDVCLGDFGAAcfpVDINANKYYGWAGT----IATN 250
                         90       100
                 ....*....|....*....|....*.
gi 569026720 823 APESIFDCVYTVQSDVWSYGILLWEI 848
Cdd:PHA03212 251 APELLARDPYGPAVDIWSAGIVLFEM 276
STKc_DCKL2 cd14184
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called ...
762-856 1.11e-05

Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called Doublecortin-like and CAM kinase-like 2); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DCKL2 (or DCAMKL2) belongs to the doublecortin (DCX) family of proteins which are involved in neuronal migration, neurogenesis, and eye receptor development, among others. Family members typically contain tandem doublecortin (DCX) domains at the N-terminus; DCX domains can bind microtubules and serve as protein-interaction platforms. In addition, DCKL2 contains a serine, threonine, and proline rich domain (SP) and a C-terminal kinase domain with similarity to CAMKs. DCKL2 has been shown to interact with tubulin, JIP1/2, JNK, neurabin 2, and actin. It is associated with the terminal segments of axons and dendrites, and may function as a phosphorylation-dependent switch to control microtubule dynamics in neuronal growth cones. The DCKL2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271086 [Multi-domain]  Cd Length: 259  Bit Score: 48.10  E-value: 1.11e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 762 VAQGMAFLASKNCIHRDVAARNVLL---TNGHVA-KIGDFGLArDIMNDSNYIVKGNArlpvKWMAPESIFDCVYTVQSD 837
Cdd:cd14184  108 LASALKYLHGLCIVHRDIKPENLLVceyPDGTKSlKLGDFGLA-TVVEGPLYTVCGTP----TYVAPEIIAETGYGLKVD 182
                         90
                 ....*....|....*....
gi 569026720 838 VWSYGILLWeIFSLGLNPY 856
Cdd:cd14184  183 IWAAGVITY-ILLCGFPPF 200
STKc_NLK cd07853
Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer ...
758-850 1.15e-05

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


Pssm-ID: 173748 [Multi-domain]  Cd Length: 372  Bit Score: 48.59  E-value: 1.15e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 758 FSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLAR-DIMNDSNY----IVKGNARlpvkwmAPESIFDCV- 831
Cdd:cd07853  108 FLYQILRGLKYLHSAGILHRDIKPGNLLVNSNCVLKICDFGLARvEEPDESKHmtqeVVTQYYR------APEILMGSRh 181
                         90
                 ....*....|....*....
gi 569026720 832 YTVQSDVWSYGILLWEIFS 850
Cdd:cd07853  182 YTSAVDIWSVGCIFAELLG 200
STKc_CaMKK2 cd14199
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; ...
745-856 1.15e-05

Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKKs are upstream kinases of the CaM kinase cascade that phosphorylate and activate CaMKI and CamKIV. They may also phosphorylate other substrates including PKB and AMP-activated protein kinase (AMPK). CaMKK2, also called CaMKK beta, is one of the most versatile CaMKs. It is involved in regulating energy balance, glucose metabolism, adiposity, hematopoiesis, inflammation, and cancer. CaMKK2 contains unique N- and C-terminal domains and a central catalytic kinase domain that is followed by a regulatory domain that bears overlapping autoinhibitory and CaM-binding regions. It can be activated by signaling through G-coupled receptors, IP3 receptors, plasma membrane ion channels, and Toll-like receptors. Thus, CaMKK2 acts as a molecular hub that is capable of receiving and decoding signals from diverse pathways. The CaMKK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271101 [Multi-domain]  Cd Length: 286  Bit Score: 48.04  E-value: 1.15e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 745 EDGRPLELRDLLhfssqvaQGMAFLASKNCIHRDVAARNVLL-TNGHVaKIGDFGLARDiMNDSNYIVKGNARLPVkWMA 823
Cdd:cd14199  125 EDQARFYFQDLI-------KGIEYLHYQKIIHRDVKPSNLLVgEDGHI-KIADFGVSNE-FEGSDALLTNTVGTPA-FMA 194
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 569026720 824 PESIFDC--VYTVQS-DVWSYGILLWeIFSLGLNPY 856
Cdd:cd14199  195 PETLSETrkIFSGKAlDVWAMGVTLY-CFVFGQCPF 229
STKc_GAK cd14036
Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs ...
582-914 1.16e-05

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


Pssm-ID: 270938 [Multi-domain]  Cd Length: 282  Bit Score: 48.27  E-value: 1.16e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 582 LQFGKTLGAGAFGKVVEATAFGLGKEdavlkVAVKMLksTAHADEK-EALMSELKIMSHLGQHENIVNLLGACTHG---- 656
Cdd:cd14036    2 LRIKRVIAEGGFAFVYEAQDVGTGKE-----YALKRL--LSNEEEKnKAIIQEINFMKKLSGHPNIVQFCSAASIGkees 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 657 ----GPVLVITEYcCYGDLLNFLRRkaeamlgpslspgqdpeggvdyknihlekkyvrrdsgfssqgvdtyvemrpvsts 732
Cdd:cd14036   75 dqgqAEYLLLTEL-CKGQLVDFVKK------------------------------------------------------- 98
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 733 sndsfseqdldKEDGRPLELRDLLHFSSQVAQGMAFLASKN--CIHRDVAARNVLLTNGHVAKIGDFGLARDIMNDSNYI 810
Cdd:cd14036   99 -----------VEAPGPFSPDTVLKIFYQTCRAVQHMHKQSppIIHRDLKIENLLIGNQGQIKLCDFGSATTEAHYPDYS 167
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 811 VKGNARLPVK----------WMAPESI---FDCVYTVQSDVWSYGILLweiFSLGLNPYPgiLVNSKFYKLVKDGYQMAQ 877
Cdd:cd14036  168 WSAQKRSLVEdeitrnttpmYRTPEMIdlySNYPIGEKQDIWALGCIL---YLLCFRKHP--FEDGAKLRIINAKYTIPP 242
                        330       340       350
                 ....*....|....*....|....*....|....*..
gi 569026720 878 PAFAPKNIYSIMQACWALEPTHRPTFQQICSFLQEQA 914
Cdd:cd14036  243 NDTQYTVFHDLIRSTLKVNPEERLSITEIVEQLQELA 279
STKc_PASK cd14004
Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs ...
761-906 1.31e-05

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: 47.77  E-value: 1.31e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 761 QVAQGMAFLASKNCIHRDVAARNVLL-TNGHVaKIGDFGLARDIMNDSNYIVKGNarlpVKWMAPESIFDCVYTVQS-DV 838
Cdd:cd14004  117 QVADAVKHLHDQGIVHRDIKDENVILdGNGTI-KLIDFGSAAYIKSGPFDTFVGT----IDYAAPEVLRGNPYGGKEqDI 191
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 569026720 839 WSYGILLWEIFsLGLNPYPGIL----VNSKFYKLVKdgyqmaqpafapKNIYSIMQACWALEPTHRPTFQQI 906
Cdd:cd14004  192 WALGVLLYTLV-FKENPFYNIEeileADLRIPYAVS------------EDLIDLISRMLNRDVGDRPTIEEL 250
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
25-85 1.83e-05

Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of proteins of different functions. Examples include antibodies, the giant muscle kinase titin and receptor tyrosine kinases. Immunoglobulin-like domains may be involved in protein-protein and protein-ligand interactions.


Pssm-ID: 395002  Cd Length: 86  Bit Score: 44.11  E-value: 1.83e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 569026720   25 PSVPELVVKPGATVTLRC-----VGNGSVEW----DGPPSPHWTLYSDGSSSI--LSTNNATFQNTGTYRCT 85
Cdd:pfam00047   1 SAPPTVTVLEGDSATLTCsastgSPGPDVTWskegGTLIESLKVKHDNGRTTQssLLISNVTKEDAGTYTCV 72
STKc_ACVR2a cd14141
Catalytic domain of the Serine/Threonine Kinase, Activin Type IIA Receptor; STKs catalyze the ...
754-850 2.06e-05

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


Pssm-ID: 271043 [Multi-domain]  Cd Length: 290  Bit Score: 47.34  E-value: 2.06e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 754 DLLHFSSQVAQGMAFLAS---------KNCI-HRDVAARNVLLTNGHVAKIGDFGLARDIMNDSNyivKGNARLPV---K 820
Cdd:cd14141   93 ELCHIAQTMARGLAYLHEdipglkdghKPAIaHRDIKSKNVLLKNNLTACIADFGLALKFEAGKS---AGDTHGQVgtrR 169
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 569026720 821 WMAPESI-----FDCVYTVQSDVWSYGILLWEIFS 850
Cdd:cd14141  170 YMAPEVLegainFQRDAFLRIDMYAMGLVLWELAS 204
STKc_NIK cd13991
Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs ...
742-840 2.21e-05

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


Pssm-ID: 270893 [Multi-domain]  Cd Length: 268  Bit Score: 47.12  E-value: 2.21e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 742 LDKEDGRPLELRDLlHFSSQVAQGMAFLASKNCIHRDVAARNVLLT-NGHVAKIGDFGLARDIMND--SNYIVKGNArLP 818
Cdd:cd13991   88 LIKEQGCLPEDRAL-HYLGQALEGLEYLHSRKILHGDVKADNVLLSsDGSDAFLCDFGHAECLDPDglGKSLFTGDY-IP 165
                         90       100
                 ....*....|....*....|....
gi 569026720 819 --VKWMAPESIFDCVYTVQSDVWS 840
Cdd:cd13991  166 gtETHMAPEVVLGKPCDAKVDVWS 189
PKc_DYRK_like cd14133
Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like ...
586-850 2.33e-05

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: 46.88  E-value: 2.33e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 586 KTLGAGAFGKVVEATAFGLGKEdavlkVAVKMLK-STAHADEKealMSELKIMSHLGQH-----ENIVNLLGACTHGGPV 659
Cdd:cd14133    5 EVLGKGTFGQVVKCYDLLTGEE-----VALKIIKnNKDYLDQS---LDEIRLLELLNKKdkadkYHIVRLKDVFYFKNHL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 660 LVITEyccygdllnflrrkaeaMLGPSLspgqdpeggvdyknihlekkyvrrdsgfssqgvdtYvemrpvstssndSFSE 739
Cdd:cd14133   77 CIVFE-----------------LLSQNL-----------------------------------Y------------EFLK 92
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 740 QDLDkedgRPLELRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVA--KIGDFGLARDIMNDSNYIVKGNArl 817
Cdd:cd14133   93 QNKF----QYLSLPRIRKIAQQILEALVFLHSLGLIHCDLKPENILLASYSRCqiKIIDFGSSCFLTQRLYSYIQSRY-- 166
                        250       260       270
                 ....*....|....*....|....*....|...
gi 569026720 818 pvkWMAPESIFDCVYTVQSDVWSYGILLWEIFS 850
Cdd:cd14133  167 ---YRAPEVILGLPYDEKIDMWSLGCILAELYT 196
STKc_PLK2 cd14188
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the ...
757-906 2.51e-05

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: 46.93  E-value: 2.51e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 757 HFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLA----------RDIMNDSNYivkgnarlpvkwMAPES 826
Cdd:cd14188  105 YYLRQIVSGLKYLHEQEILHRDLKLGNFFINENMELKVGDFGLAarleplehrrRTICGTPNY------------LSPEV 172
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 827 IFDCVYTVQSDVWSYGILLWEIFsLGLNPYPGILVNSKFYKLVKDGYQMAQPAFAPKNiySIMQACWALEPTHRPTFQQI 906
Cdd:cd14188  173 LNKQGHGCESDIWALGCVMYTML-LGRPPFETTNLKETYRCIREARYSLPSSLLAPAK--HLIASMLSKNPEDRPSLDEI 249
STKc_p38gamma cd07880
Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase ...
761-850 2.51e-05

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


Pssm-ID: 143385 [Multi-domain]  Cd Length: 343  Bit Score: 47.64  E-value: 2.51e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 761 QVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDIMND-SNYIVkgnarlpVKWM-APESIFDCV-YTVQSD 837
Cdd:cd07880  126 QMLKGLKYIHAAGIIHRDLKPGNLAVNEDCELKILDFGLARQTDSEmTGYVV-------TRWYrAPEVILNWMhYTQTVD 198
                         90
                 ....*....|...
gi 569026720 838 VWSYGILLWEIFS 850
Cdd:cd07880  199 IWSVGCIMAEMLT 211
STKc_CDK1_CdkB_like cd07835
Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of ...
737-842 2.51e-05

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: 47.28  E-value: 2.51e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 737 FSEQDL----DKEDGRPLELRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDImndsnyivk 812
Cdd:cd07835   79 FLDLDLkkymDSSPLTGLDPPLIKSYLYQLLQGIAFCHSHRVLHRDLKPQNLLIDTEGALKLADFGLARAF--------- 149
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 569026720 813 gnaRLPVK---------WM-APESIFDC-VYTVQSDVWSYG 842
Cdd:cd07835  150 ---GVPVRtythevvtlWYrAPEILLGSkHYSTPVDIWSVG 187
STKc_ACVR2b cd14140
Catalytic domain of the Serine/Threonine Kinase, Activin Type IIB Receptor; STKs catalyze the ...
743-850 2.66e-05

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


Pssm-ID: 271042 [Multi-domain]  Cd Length: 291  Bit Score: 46.95  E-value: 2.66e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 743 DKEDGRPLELRDLLHFSSQVAQGMAFL----------ASKNCI-HRDVAARNVLLTNGHVAKIGDFGLARDIM-----ND 806
Cdd:cd14140   82 DYLKGNIVSWNELCHIAETMARGLSYLhedvprckgeGHKPAIaHRDFKSKNVLLKNDLTAVLADFGLAVRFEpgkppGD 161
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 569026720 807 SNYIVkGNARlpvkWMAPESI-----FDCVYTVQSDVWSYGILLWEIFS 850
Cdd:cd14140  162 THGQV-GTRR----YMAPEVLegainFQRDSFLRIDMYAMGLVLWELVS 205
STKc_p70S6K cd05584
Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs ...
586-858 2.83e-05

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: 47.40  E-value: 2.83e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 586 KTLGAGAFGKVVEA---TAFGLGKEDA--VLKVA--VKMLKSTAHADekealmSELKIMSHLgQHENIVNLLGACTHGGP 658
Cdd:cd05584    2 KVLGKGGYGKVFQVrktTGSDKGKIFAmkVLKKAsiVRNQKDTAHTK------AERNILEAV-KHPFIVDLHYAFQTGGK 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 659 VLVITEYCCYGDLLNFLRRkaeamlgpslspgqdpEGgvdyknIHLEkkyvrrdsgfssqgvDTYvemrpvstssndSFs 738
Cdd:cd05584   75 LYLILEYLSGGELFMHLER----------------EG------IFME---------------DTA------------CF- 104
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 739 eqdldkedgrplelrdllhFSSQVAQGMAFLASKNCIHRDVAARNVLL-TNGHVaKIGDFGLARD-IMNDS-NYIVKGNa 815
Cdd:cd05584  105 -------------------YLAEITLALGHLHSLGIIYRDLKPENILLdAQGHV-KLTDFGLCKEsIHDGTvTHTFCGT- 163
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 569026720 816 rlpVKWMAPESIFDCVYTVQSDVWSYGILLWEIFSlGLNPYPG 858
Cdd:cd05584  164 ---IEYMAPEILTRSGHGKAVDWWSLGALMYDMLT-GAPPFTA 202
STKc_RSK1_C cd14175
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called ...
611-856 3.18e-05

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: 46.94  E-value: 3.18e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 611 LKVAVKMLKSTAHaDEKEalmsELKIMSHLGQHENIVNLLGACTHGGPVLVITEYCCYGDLLNFLrrkaeamlgpslspg 690
Cdd:cd14175   27 MEYAVKVIDKSKR-DPSE----EIEILLRYGQHPNIITLKDVYDDGKHVYLVTELMRGGELLDKI--------------- 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 691 qdpeggvdyknihLEKKYvrrdsgfssqgvdtyvemrpvstssndsFSEQdldkedgrplELRDLLHfssQVAQGMAFLA 770
Cdd:cd14175   87 -------------LRQKF----------------------------FSER----------EASSVLH---TICKTVEYLH 112
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 771 SKNCIHRDVAARNVLLT----NGHVAKIGDFGLARDIMNDSNYIVkgNARLPVKWMAPESIFDCVYTVQSDVWSYGILLW 846
Cdd:cd14175  113 SQGVVHRDLKPSNILYVdesgNPESLRICDFGFAKQLRAENGLLM--TPCYTANFVAPEVLKRQGYDEGCDIWSLGILLY 190
                        250
                 ....*....|
gi 569026720 847 EIFSlGLNPY 856
Cdd:cd14175  191 TMLA-GYTPF 199
STKc_PCTAIRE3 cd07871
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer ...
735-866 3.26e-05

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: 46.93  E-value: 3.26e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 735 DSFSEQDLDkEDGRPLELRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLAR----DIMNDSNYI 810
Cdd:cd07871   86 DSDLKQYLD-NCGNLMSMHNVKIFMFQLLRGLSYCHKRKILHRDLKPQNLLINEKGELKLADFGLARaksvPTKTYSNEV 164
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 569026720 811 VkgnarlpVKWMAPESIF--DCVYTVQSDVWSYGILLWEIFSlGLNPYPGILVNSKFY 866
Cdd:cd07871  165 V-------TLWYRPPDVLlgSTEYSTPIDMWGVGCILYEMAT-GRPMFPGSTVKEELH 214
Ig1_FcgammaR_like cd05752
First immunoglobulin (Ig)-like domain of Fcgamma-receptors (FcgammaRs), and similar domains; ...
35-101 3.30e-05

First immunoglobulin (Ig)-like domain of Fcgamma-receptors (FcgammaRs), and similar domains; The members here are composed of the first immunoglobulin (Ig)-like domain of Fcgamma-receptors (FcgammaRs). Interactions between IgG and FcgammaR are important to the initiation of cellular and humoral response. IgG binding to FcgammaR leads to a cascade of signals and ultimately to functions such as antibody-dependent-cellular-cytotoxicity (ADCC), endocytosis, phagocytosis, release of inflammatory mediators, etc. FcgammaR has two Ig-like domains. This group also contains FcepsilonRI which binds IgE with high affinity.


Pssm-ID: 409410 [Multi-domain]  Cd Length: 79  Bit Score: 43.12  E-value: 3.30e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 569026720  35 GATVTLRCVGNGSVEwdgPPSPHW----TLYSDGSSSIlSTNNATFQNTGTYRCTEPGDPLggSAAIHLYV 101
Cdd:cd05752   15 GEKVTLTCQGFYSPE---QNSTQWyhngTLISSTSSSY-RIVAATVNDSGEYRCQTQGSSL--SDPVHLEV 79
STKc_CDK8_like cd07842
Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs ...
752-851 3.50e-05

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: 46.89  E-value: 3.50e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 752 LRDLLHfssQVAQGMAFLASKNCIHRDVAARNVLLT----NGHVAKIGDFGLARDIMNDSNYIVKGNARLPVKWM-APES 826
Cdd:cd07842  110 VKSLLW---QILNGIHYLHSNWVLHRDLKPANILVMgegpERGVVKIGDLGLARLFNAPLKPLADLDPVVVTIWYrAPEL 186
                         90       100
                 ....*....|....*....|....*.
gi 569026720 827 IFDCV-YTVQSDVWSYGILLWEIFSL 851
Cdd:cd07842  187 LLGARhYTKAIDIWAIGCIFAELLTL 212
STKc_CAMKK cd14118
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; ...
752-846 3.57e-05

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: 46.58  E-value: 3.57e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 752 LRDLLhfssqvaQGMAFLASKNCIHRDVAARNVLLT-NGHVaKIGDFGLArDIMNDSNYIVKGNARLPVkWMAPESIFDC 830
Cdd:cd14118  121 FRDIV-------LGIEYLHYQKIIHRDIKPSNLLLGdDGHV-KIADFGVS-NEFEGDDALLSSTAGTPA-FMAPEALSES 190
                         90
                 ....*....|....*....
gi 569026720 831 VYTVQS---DVWSYGILLW 846
Cdd:cd14118  191 RKKFSGkalDIWAMGVTLY 209
STKc_SGK1 cd05602
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
758-856 3.61e-05

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: 46.93  E-value: 3.61e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 758 FSSQVAQGMAFLASKNCIHRDVAARNVLL-TNGHVAkIGDFGLARDIMnDSNYIVKGNARLPvKWMAPESIFDCVYTVQS 836
Cdd:cd05602  113 YAAEIASALGYLHSLNIVYRDLKPENILLdSQGHIV-LTDFGLCKENI-EPNGTTSTFCGTP-EYLAPEVLHKQPYDRTV 189
                         90       100
                 ....*....|....*....|
gi 569026720 837 DVWSYGILLWEIFsLGLNPY 856
Cdd:cd05602  190 DWWCLGAVLYEML-YGLPPF 208
STKc_JNK cd07850
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the ...
761-848 4.21e-05

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: 46.64  E-value: 4.21e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 761 QVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDIMND---SNYIVKGNARlpvkwmAPESIFDCVYTVQSD 837
Cdd:cd07850  110 QMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLARTAGTSfmmTPYVVTRYYR------APEVILGMGYKENVD 183
                         90
                 ....*....|.
gi 569026720 838 VWSYGILLWEI 848
Cdd:cd07850  184 IWSVGCIMGEM 194
PHA03207 PHA03207
serine/threonine kinase US3; Provisional
749-848 4.25e-05

serine/threonine kinase US3; Provisional


Pssm-ID: 165473 [Multi-domain]  Cd Length: 392  Bit Score: 46.76  E-value: 4.25e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 749 PLELRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDiMNDSNYIVKGNArlpvkWM------ 822
Cdd:PHA03207 181 PLPLEQAITIQRRLLEALAYLHGRGIIHRDVKTENIFLDEPENAVLGDFGAACK-LDAHPDTPQCYG-----WSgtletn 254
                         90       100
                 ....*....|....*....|....*.
gi 569026720 823 APESIFDCVYTVQSDVWSYGILLWEI 848
Cdd:PHA03207 255 SPELLALDPYCAKTDIWSAGLVLFEM 280
STKc_PIM2 cd14101
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
758-906 4.31e-05

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: 46.38  E-value: 4.31e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 758 FSSQVAQGMAFLASKNCIHRDVAARNVLL-TNGHVAKIGDFGlARDIMNDSNYIVKGNARL--PVKWMAPESifdcVYTV 834
Cdd:cd14101  113 FFKQVVEAVQHCHSKGVVHRDIKDENILVdLRTGDIKLIDFG-SGATLKDSMYTDFDGTRVysPPEWILYHQ----YHAL 187
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 569026720 835 QSDVWSYGILLWEIFSlGLNPYpgilvnSKFYKLVKdgyqmAQPAFaPKNIY----SIMQACWALEPTHRPTFQQI 906
Cdd:cd14101  188 PATVWSLGILLYDMVC-GDIPF------ERDTDILK-----AKPSF-NKRVSndcrSLIRSCLAYNPSDRPSLEQI 250
STKc_HIPK3 cd14229
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 3; ...
749-860 4.40e-05

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: 46.56  E-value: 4.40e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 749 PLELRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTN----GHVAKIGDFGLARDIMND--SNYIVKGNARlpvkwm 822
Cdd:cd14229   98 PLPLKVIRPILQQVATALKKLKSLGLIHADLKPENIMLVDpvrqPYRVKVIDFGSASHVSKTvcSTYLQSRYYR------ 171
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 569026720 823 APESIFDCVYTVQSDVWSYGILLWEIFsLGLNPYPGIL 860
Cdd:cd14229  172 APEIILGLPFCEAIDMWSLGCVIAELF-LGWPLYPGAL 208
STKc_PKA cd14209
Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze ...
758-856 4.42e-05

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: 46.24  E-value: 4.42e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 758 FSSQVAQGMAFLASKNCIHRDVAARNVLL-TNGHVaKIGDFGLARDImNDSNYIVKGNArlpvKWMAPESIFDCVYTVQS 836
Cdd:cd14209  106 YAAQIVLAFEYLHSLDLIYRDLKPENLLIdQQGYI-KVTDFGFAKRV-KGRTWTLCGTP----EYLAPEIILSKGYNKAV 179
                         90       100
                 ....*....|....*....|
gi 569026720 837 DVWSYGILLWEiFSLGLNPY 856
Cdd:cd14209  180 DWWALGVLIYE-MAAGYPPF 198
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
583-856 4.53e-05

Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called Doublecortin-like and CAM kinase-like); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DCKL (or DCAMKL) proteins belong to the doublecortin (DCX) family of proteins which are involved in neuronal migration, neurogenesis, and eye receptor development, among others. Family members typically contain tandem doublecortin (DCX) domains at the N-terminus; DCX domains can bind microtubules and serve as protein-interaction platforms. In addition, DCKL proteins contain a C-terminal kinase domain with similarity to CAMKs. They are involved in the regulation of cAMP signaling. Vertebrates contain three DCKL proteins (DCKL1-3); DCKL1 and 2 also contain a serine, threonine, and proline rich domain (SP), while DCKL3 contains only a single DCX domain instead of tandem domains. The DCKL subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270997 [Multi-domain]  Cd Length: 258  Bit Score: 46.16  E-value: 4.53e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 583 QFGKTLGAGAFGKVVEATAFGLGKEDAvLKVAVKM-LKSTAHADEkealmSELKIMSHLgQHENIVNLLGACTHGGPVLV 661
Cdd:cd14095    3 DIGRVIGDGNFAVVKECRDKATDKEYA-LKIIDKAkCKGKEHMIE-----NEVAILRRV-KHPNIVQLIEEYDTDTELYL 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 662 ITEYCCYGDLLNflrrkaeamlgpslspgqdpeggvdykNIHLEKKYVRRDSgfssqgvdtyVEMrpvstssndsfseqd 741
Cdd:cd14095   76 VMELVKGGDLFD---------------------------AITSSTKFTERDA----------SRM--------------- 103
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 742 ldkedgrpleLRDLlhfssqvAQGMAFLASKNCIHRDVAARNVLL---TNGHVA-KIGDFGLARdIMNDSNYIVKGNarl 817
Cdd:cd14095  104 ----------VTDL-------AQALKYLHSLSIVHRDIKPENLLVvehEDGSKSlKLADFGLAT-EVKEPLFTVCGT--- 162
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 569026720 818 PVkWMAPESIFDCVYTVQSDVWSYGILLWeIFSLGLNPY 856
Cdd:cd14095  163 PT-YVAPEILAETGYGLKVDIWAAGVITY-ILLCGFPPF 199
STKc_DRAK2 cd14198
The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
754-858 4.54e-05

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: 46.07  E-value: 4.54e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 754 DLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTN----GHVaKIGDFGLARDIMNDSNYI-VKGNArlpvKWMAPESI- 827
Cdd:cd14198  111 DIIRLIRQILEGVYYLHQNNIVHLDLKPQNILLSSiyplGDI-KIVDFGMSRKIGHACELReIMGTP----EYLAPEILn 185
                         90       100       110
                 ....*....|....*....|....*....|.
gi 569026720 828 FDCVyTVQSDVWSYGILLWEIFSlGLNPYPG 858
Cdd:cd14198  186 YDPI-TTATDMWNIGVIAYMLLT-HESPFVG 214
STKc_TGFbR2_like cd14055
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Type II ...
747-850 4.96e-05

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: 46.22  E-value: 4.96e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 747 GRPLELRDLLHFSSQVAQGMAFLAS--------KNCI-HRDVAARNVLLTNGHVAKIGDFGLA--------RDIMNDSNY 809
Cdd:cd14055   92 RHILSWEDLCKMAGSLARGLAHLHSdrtpcgrpKIPIaHRDLKSSNILVKNDGTCVLADFGLAlrldpslsVDELANSGQ 171
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 569026720 810 IvkGNARlpvkWMAPEsIFDCVYTV-------QSDVWSYGILLWEIFS 850
Cdd:cd14055  172 V--GTAR----YMAPE-ALESRVNLedlesfkQIDVYSMALVLWEMAS 212
STKc_Mnk2 cd14173
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
757-858 5.02e-05

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


Pssm-ID: 271075 [Multi-domain]  Cd Length: 288  Bit Score: 46.17  E-value: 5.02e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 757 HFSSQ--------VAQGMAFLASKNCIHRDVAARNVLLTNGHV---AKIGDFGLARDIM--NDSNYIVKGNARLP---VK 820
Cdd:cd14173   96 HFNELeasvvvqdIASALDFLHNKGIAHRDLKPENILCEHPNQvspVKICDFDLGSGIKlnSDCSPISTPELLTPcgsAE 175
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 569026720 821 WMAPESI--FD---CVYTVQSDVWSYGILLWEIFSlGLNPYPG 858
Cdd:cd14173  176 YMAPEVVeaFNeeaSIYDKRCDLWSLGVILYIMLS-GYPPFVG 217
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
579-878 5.15e-05

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: 46.17  E-value: 5.15e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 579 RNNLQFGKTLGAGAFGKVVeatafgLGKEDAVLK-VAVKMLKSTAHADEKEALMSELKIMsHLGQHENIVNLLGACTHGG 657
Cdd:cd14167    2 RDIYDFREVLGTGAFSEVV------LAEEKRTQKlVAIKCIAKKALEGKETSIENEIAVL-HKIKHPNIVALDDIYESGG 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 658 PVLVITEYCCYGDLLNFLRRKaeamlgpslspgqdpeggvdyknihlekkyvrrdsGFssqgvdtyvemrpvstssndsF 737
Cdd:cd14167   75 HLYLIMQLVSGGELFDRIVEK-----------------------------------GF---------------------Y 98
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 738 SEQDLDKedgrplelrdllhFSSQVAQGMAFLASKNCIHRDVAARNVL---LTNGHVAKIGDFGLARdiMNDSNYIVKGN 814
Cdd:cd14167   99 TERDASK-------------LIFQILDAVKYLHDMGIVHRDLKPENLLyysLDEDSKIMISDFGLSK--IEGSGSVMSTA 163
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 569026720 815 ARLPvKWMAPESIFDCVYTVQSDVWSYGILLWeIFSLGLNPYPGILVNSKFYKLVKDGYQMAQP 878
Cdd:cd14167  164 CGTP-GYVAPEVLAQKPYSKAVDCWSIGVIAY-ILLCGYPPFYDENDAKLFEQILKAEYEFDSP 225
STKc_CDK1_euk cd07861
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher ...
761-848 5.23e-05

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: 46.26  E-value: 5.23e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 761 QVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDImndsnyivkgnaRLPVK----------WMAPESIFDC 830
Cdd:cd07861  109 QILQGILFCHSRRVLHRDLKPQNLLIDNKGVIKLADFGLARAF------------GIPVRvythevvtlwYRAPEVLLGS 176
                         90
                 ....*....|....*....
gi 569026720 831 V-YTVQSDVWSYGILLWEI 848
Cdd:cd07861  177 PrYSTPVDIWSIGTIFAEM 195
STKc_SGK3 cd05604
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
756-856 5.27e-05

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: 46.49  E-value: 5.27e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 756 LHFSSQVAQGMAFLASKNCIHRDVAARNVLL-TNGHVAkIGDFGLARDIMNDSNYIVK--GNArlpvKWMAPESIFDCVY 832
Cdd:cd05604  100 RFYAAEIASALGYLHSINIVYRDLKPENILLdSQGHIV-LTDFGLCKEGISNSDTTTTfcGTP----EYLAPEVIRKQPY 174
                         90       100
                 ....*....|....*....|....
gi 569026720 833 TVQSDVWSYGILLWEIFSlGLNPY 856
Cdd:cd05604  175 DNTVDWWCLGSVLYEMLY-GLPPF 197
STKc_PKB_gamma cd05593
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); ...
758-848 5.50e-05

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: 46.61  E-value: 5.50e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 758 FSSQVAQGMAFLASKNCIHRDVAARNVLL-TNGHVaKIGDFGLARDIMNDSNyIVKGNARLPvKWMAPESIFDCVYTVQS 836
Cdd:cd05593  120 YGAEIVSALDYLHSGKIVYRDLKLENLMLdKDGHI-KITDFGLCKEGITDAA-TMKTFCGTP-EYLAPEVLEDNDYGRAV 196
                         90
                 ....*....|..
gi 569026720 837 DVWSYGILLWEI 848
Cdd:cd05593  197 DWWGLGVVMYEM 208
Ig_2 pfam13895
Immunoglobulin domain; This domain contains immunoglobulin-like domains.
21-85 5.63e-05

Immunoglobulin domain; This domain contains immunoglobulin-like domains.


Pssm-ID: 433563 [Multi-domain]  Cd Length: 76  Bit Score: 42.39  E-value: 5.63e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 569026720   21 PVIEPSVPELVVkpGATVTLRCvgngsvEWDGPPSPHWTLYSDG----SSSILSTNNATFQNTGTYRCT 85
Cdd:pfam13895   2 PVLTPSPTVVTE--GEPVTLTC------SAPGNPPASYTWYKGGealnSSPNFFILAVSAEDSGTYTCV 62
STKc_MSK2_N cd05614
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
581-856 5.64e-05

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: 46.45  E-value: 5.64e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 581 NLQFGKTLGAGAFGKVVEATAfgLGKEDAVLKVAVKMLKstahadeKEALMSELKIMSHLGQHENIVNLLgactHGGPVL 660
Cdd:cd05614    1 NFELLKVLGTGAYGKVFLVRK--VSGHDANKLYAMKVLR-------KAALVQKAKTVEHTRTERNVLEHV----RQSPFL 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 661 VITEYCCYGDllnflrrkaeamlgpslspgqdpeggvdyKNIHLEKKYVRRDSGFssqgvdTYVEMRpvstssnDSFSEQ 740
Cdd:cd05614   68 VTLHYAFQTD-----------------------------AKLHLILDYVSGGELF------THLYQR-------DHFSED 105
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 741 dldkedgrplELRdllHFSSQVAQGMAFLASKNCIHRDVAARNVLL-TNGHVAkIGDFGLARDIMNDS---NYIVKGNar 816
Cdd:cd05614  106 ----------EVR---FYSGEIILALEHLHKLGIVYRDIKLENILLdSEGHVV-LTDFGLSKEFLTEEkerTYSFCGT-- 169
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 569026720 817 lpVKWMAPESIFDCVYTVQS-DVWSYGILLWEIFSlGLNPY 856
Cdd:cd05614  170 --IEYMAPEIIRGKSGHGKAvDWWSLGILMFELLT-GASPF 207
STKc_Mnk cd14090
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase ...
585-858 6.52e-05

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


Pssm-ID: 270992 [Multi-domain]  Cd Length: 289  Bit Score: 45.87  E-value: 6.52e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 585 GKTLGAGAFGKVVEATAFGLGKEdavlkVAVKML-KSTAHADEKeaLMSELKIMSHLGQHENIVNLLgacthggpvlvit 663
Cdd:cd14090    7 GELLGEGAYASVQTCINLYTGKE-----YAVKIIeKHPGHSRSR--VFREVETLHQCQGHPNILQLI------------- 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 664 EYCCYGDLLNFLRRKAEAmlGPSLSpgqdpeggvdykniHLEKKyvrrdsgfssqgvdtyvemrpvstssnDSFSEQDLD 743
Cdd:cd14090   67 EYFEDDERFYLVFEKMRG--GPLLS--------------HIEKR---------------------------VHFTEQEAS 103
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 744 kedgrpLELRDllhfssqVAQGMAFLASKNCIHRDVAARNVLL-TNGHVA--KIGDFGLA---RDIMNDSNYIVKGNARL 817
Cdd:cd14090  104 ------LVVRD-------IASALDFLHDKGIAHRDLKPENILCeSMDKVSpvKICDFDLGsgiKLSSTSMTPVTTPELLT 170
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 569026720 818 PV---KWMAPEsIFDC------VYTVQSDVWSYGILLWeIFSLGLNPYPG 858
Cdd:cd14090  171 PVgsaEYMAPE-VVDAfvgealSYDKRCDLWSLGVILY-IMLCGYPPFYG 218
STKc_JNK2 cd07876
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the ...
761-848 7.32e-05

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: 46.17  E-value: 7.32e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 761 QVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDIMND---SNYIVKGNARlpvkwmAPESIFDCVYTVQSD 837
Cdd:cd07876  131 QMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLARTACTNfmmTPYVVTRYYR------APEVILGMGYKENVD 204
                         90
                 ....*....|.
gi 569026720 838 VWSYGILLWEI 848
Cdd:cd07876  205 IWSVGCIMGEL 215
STKc_PFTAIRE2 cd07870
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer ...
758-870 7.49e-05

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: 45.72  E-value: 7.49e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 758 FSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLAR-DIMNDSNYivkgNARLPVKWMAPESIF--DCVYTV 834
Cdd:cd07870  103 FMFQLLRGLAYIHGQHILHRDLKPQNLLISYLGELKLADFGLARaKSIPSQTY----SSEVVTLWYRPPDVLlgATDYSS 178
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 569026720 835 QSDVWSYGILLWEIFSlGLNPYPGilVNSKFYKLVK 870
Cdd:cd07870  179 ALDIWGAGCIFIEMLQ-GQPAFPG--VSDVFEQLEK 211
STKc_MAPKAPK2 cd14170
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
762-905 1.03e-04

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


Pssm-ID: 271072 [Multi-domain]  Cd Length: 303  Bit Score: 45.41  E-value: 1.03e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 762 VAQGMAFLASKNCIHRDVAARNVLLTNGH---VAKIGDFGLARDIMNDSNYIVKgnARLPVkWMAPESIFDCVYTVQSDV 838
Cdd:cd14170  110 IGEAIQYLHSINIAHRDVKPENLLYTSKRpnaILKLTDFGFAKETTSHNSLTTP--CYTPY-YVAPEVLGPEKYDKSCDM 186
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 569026720 839 WSYGILLWeIFSLGLNPY---PGILVNSKFYKLVKDG-YQMAQPAFA--PKNIYSIMQACWALEPTHRPTFQQ 905
Cdd:cd14170  187 WSLGVIMY-ILLCGYPPFysnHGLAISPGMKTRIRMGqYEFPNPEWSevSEEVKMLIRNLLKTEPTQRMTITE 258
pknD PRK13184
serine/threonine-protein kinase PknD;
761-869 1.07e-04

serine/threonine-protein kinase PknD;


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 46.30  E-value: 1.07e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 761 QVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLA------RDIMNDSNYIVKG----NARLPVK------WMAP 824
Cdd:PRK13184 121 KICATIEYVHSKGVLHRDLKPDNILLGLFGEVVILDWGAAifkkleEEDLLDIDVDERNicysSMTIPGKivgtpdYMAP 200
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 569026720 825 ESIFDCVYTVQSDVWSYGILLWEIFSLGlNPYPgilvNSKFYKLV 869
Cdd:PRK13184 201 ERLLGVPASESTDIYALGVILYQMLTLS-FPYR----RKKGRKIS 240
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
774-849 1.10e-04

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: 45.35  E-value: 1.10e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 774 CIHRDVAARNVLLT-NGHVaKIGDFGLA------RDIMNDSNYIVKGNARLPVK---------------------WMAPE 825
Cdd:cd05573  122 FIHRDIKPDNILLDaDGHI-KLADFGLCtkmnksGDRESYLNDSVNTLFQDNVLarrrphkqrrvraysavgtpdYIAPE 200
                         90       100
                 ....*....|....*....|....
gi 569026720 826 SIFDCVYTVQSDVWSYGILLWEIF 849
Cdd:cd05573  201 VLRGTGYGPECDWWSLGVILYEML 224
STKc_RSK3_C cd14178
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called ...
762-856 1.11e-04

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: 45.39  E-value: 1.11e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 762 VAQGMAFLASKNCIHRDVAARNVLLT----NGHVAKIGDFGLARDIMNDSNYIVkgNARLPVKWMAPESIFDCVYTVQSD 837
Cdd:cd14178  106 ITKTVEYLHSQGVVHRDLKPSNILYMdesgNPESIRICDFGFAKQLRAENGLLM--TPCYTANFVAPEVLKRQGYDAACD 183
                         90
                 ....*....|....*....
gi 569026720 838 VWSYGILLWEIFSlGLNPY 856
Cdd:cd14178  184 IWSLGILLYTMLA-GFTPF 201
STKc_CRIK cd05601
Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze ...
775-847 1.13e-04

Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CRIK (also called citron kinase) is an effector of the small GTPase Rho. It plays an important function during cytokinesis and affects its contractile process. CRIK-deficient mice show severe ataxia and epilepsy as a result of abnormal cytokinesis and massive apoptosis in neuronal precursors. A Down syndrome critical region protein TTC3 interacts with CRIK and inhibits CRIK-dependent neuronal differentiation and neurite extension. CRIK contains a catalytic domain, a central coiled-coil domain, and a C-terminal region containing a Rho-binding domain (RBD), a zinc finger, and a pleckstrin homology (PH) domain, in addition to other motifs. The CRIK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270752 [Multi-domain]  Cd Length: 328  Bit Score: 45.38  E-value: 1.13e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 775 IHRDVAARNVLL-TNGHVaKIGDFGLARDImnDSNYIVkgNARLPV---KWMAPE------SIFDCVYTVQSDVWSYGIL 844
Cdd:cd05601  124 VHRDIKPENILIdRTGHI-KLADFGSAAKL--SSDKTV--TSKMPVgtpDYIAPEvltsmnGGSKGTYGVECDWWSLGIV 198

                 ...
gi 569026720 845 LWE 847
Cdd:cd05601  199 AYE 201
STKc_RSK2_C cd14176
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called ...
579-856 1.19e-04

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: 45.40  E-value: 1.19e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 579 RNNLQF------GKTLGAGAFGKVVEATAFGLGKEdavlkVAVKMLKStahadEKEALMSELKIMSHLGQHENIVNLLGA 652
Cdd:cd14176   12 RNSIQFtdgyevKEDIGVGSYSVCKRCIHKATNME-----FAVKIIDK-----SKRDPTEEIEILLRYGQHPNIITLKDV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 653 CTHGGPVLVITEYCCYGDLLN-FLRRKAeamlgpslspgqdpeggvdyknihlekkyvrrdsgfssqgvdtyvemrpvst 731
Cdd:cd14176   82 YDDGKYVYVVTELMKGGELLDkILRQKF---------------------------------------------------- 109
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 732 ssndsFSEQdldkedgrplELRDLLHFSSQVAQgmaFLASKNCIHRDVAARNVLLT----NGHVAKIGDFGLARDIMNDS 807
Cdd:cd14176  110 -----FSER----------EASAVLFTITKTVE---YLHAQGVVHRDLKPSNILYVdesgNPESIRICDFGFAKQLRAEN 171
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 569026720 808 NYIVkgNARLPVKWMAPESIFDCVYTVQSDVWSYGILLWEIFSlGLNPY 856
Cdd:cd14176  172 GLLM--TPCYTANFVAPEVLERQGYDAACDIWSLGVLLYTMLT-GYTPF 217
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
586-906 1.30e-04

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: 44.69  E-value: 1.30e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 586 KTLGAGAFGKVveatAFGLGKEDAVlKVAVKMLK-------STAHADEKEALMSELKIMSHLgQHENIVNLLGACTHGGP 658
Cdd:cd14084   12 RTLGSGACGEV----KLAYDKSTCK-KVAIKIINkrkftigSRREINKPRNIETEIEILKKL-SHPCIIKIEDFFDAEDD 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 659 VLVITEYCCYGDLLNFLRrkaeamlgpslspgqdpeggvdyKNIHLekkyvrrdsgfssqgvdtyvemrpvstssndsfs 738
Cdd:cd14084   86 YYIVLELMEGGELFDRVV-----------------------SNKRL---------------------------------- 108
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 739 eqdldKEDGRPLELRDLLHfssqvaqGMAFLASKNCIHRDVAARNVLLTNGH---VAKIGDFGLARDIMNDSnyIVKGNA 815
Cdd:cd14084  109 -----KEAICKLYFYQMLL-------AVKYLHSNGIIHRDLKPENVLLSSQEeecLIKITDFGLSKILGETS--LMKTLC 174
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 816 RLPVkWMAPESI--FDCV-YTVQSDVWSYGILLWEIFSlGLNPYPGILVNSKFYKLVKDG-YQMAQPAFapKNI----YS 887
Cdd:cd14084  175 GTPT-YLAPEVLrsFGTEgYTRAVDCWSLGVILFICLS-GYPPFSEEYTQMSLKEQILSGkYTFIPKAW--KNVseeaKD 250
                        330
                 ....*....|....*....
gi 569026720 888 IMQACWALEPTHRPTFQQI 906
Cdd:cd14084  251 LVKKMLVVDPSRRPSIEEA 269
STKc_CDK9 cd07865
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs ...
761-801 1.37e-04

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


Pssm-ID: 270848 [Multi-domain]  Cd Length: 310  Bit Score: 45.05  E-value: 1.37e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 569026720 761 QVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLAR 801
Cdd:cd07865  127 MLLNGLYYIHRNKILHRDMKAANILITKDGVLKLADFGLAR 167
STKc_PSKH1 cd14087
Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the ...
753-856 1.39e-04

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


Pssm-ID: 270989 [Multi-domain]  Cd Length: 259  Bit Score: 44.83  E-value: 1.39e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 753 RDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTN-GHVAK--IGDFGLARDIMNDSNYIVKGNARLPvKWMAPESIFD 829
Cdd:cd14087   97 RDATRVLQMVLDGVKYLHGLGITHRDLKPENLLYYHpGPDSKimITDFGLASTRKKGPNCLMKTTCGTP-EYIAPEILLR 175
                         90       100
                 ....*....|....*....|....*..
gi 569026720 830 CVYTVQSDVWSYGILLWEIFSlGLNPY 856
Cdd:cd14087  176 KPYTQSVDMWAVGVIAYILLS-GTMPF 201
STKc_RSK4_C cd14177
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called ...
762-906 1.40e-04

C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called Ribosomal protein S6 kinase alpha-6 or 90kDa ribosomal protein S6 kinase 6); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSK4 is also called S6K-alpha-6, RPS6KA6, p90RSK6 or pp90RSK4. RSK4 is a substrate of ERK and is a modulator of p53-dependent proliferation arrest in human cells. Deletion of the RSK4 gene, RPS6KA6, frequently occurs in patients of X-linked deafness type 3, mental retardation and choroideremia. Studies of RSK4 in cancer cells and tissues suggest that it may be oncogenic or tumor suppressive depending on many factors. RSK4 is one of four RSK isoforms (RSK1-4) from distinct genes present in vertebrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. The RSK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271079 [Multi-domain]  Cd Length: 295  Bit Score: 45.01  E-value: 1.40e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 762 VAQGMAFLASKNCIHRDVAARNVLL----TNGHVAKIGDFGLARDIMNDSNYIVkgNARLPVKWMAPESIFDCVYTVQSD 837
Cdd:cd14177  107 ITKTVDYLHCQGVVHRDLKPSNILYmddsANADSIRICDFGFAKQLRGENGLLL--TPCYTANFVAPEVLMRQGYDAACD 184
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 569026720 838 VWSYGILLWEI------FSLGLNPYP-GILVNSKFYKLVKDGYQMAQPAFAPKNIYSIMqacWALEPTHRPTFQQI 906
Cdd:cd14177  185 IWSLGVLLYTMlagytpFANGPNDTPeEILLRIGSGKFSLSGGNWDTVSDAAKDLLSHM---LHVDPHQRYTAEQV 257
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
761-846 1.50e-04

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: 44.65  E-value: 1.50e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 761 QVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDImnDSNYIVKGNARLPvKWMAPE----SIFDCV--YTV 834
Cdd:cd14093  117 QLFEAVEFLHSLNIVHRDLKPENILLDDNLNVKISDFGFATRL--DEGEKLRELCGTP-GYLAPEvlkcSMYDNApgYGK 193
                         90
                 ....*....|..
gi 569026720 835 QSDVWSYGILLW 846
Cdd:cd14093  194 EVDMWACGVIMY 205
STKc_PKB_alpha cd05594
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); ...
758-848 1.71e-04

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: 45.02  E-value: 1.71e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 758 FSSQVAQGMAFL-ASKNCIHRDVAARNVLL-TNGHVaKIGDFGLARDIMNDSNyIVKGNARLPvKWMAPESIFDCVYTVQ 835
Cdd:cd05594  130 YGAEIVSALDYLhSEKNVVYRDLKLENLMLdKDGHI-KITDFGLCKEGIKDGA-TMKTFCGTP-EYLAPEVLEDNDYGRA 206
                         90
                 ....*....|...
gi 569026720 836 SDVWSYGILLWEI 848
Cdd:cd05594  207 VDWWGLGVVMYEM 219
STKc_Unc-89_rpt2 cd14112
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Uncoordinated ...
732-858 1.86e-04

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


Pssm-ID: 271014 [Multi-domain]  Cd Length: 259  Bit Score: 44.44  E-value: 1.86e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 732 SSNDSFSEQDLDKedgrplelrdllhFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGH--VAKIGDFGLARDIMNDSNY 809
Cdd:cd14112   91 SSNDYYSEEQVAT-------------TVRQILDALHYLHFKGIAHLDVQPDNIMFQSVRswQVKLVDFGRAQKVSKLGKV 157
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 569026720 810 IVKGNarlpVKWMAPESIFD-CVYTVQSDVWSYGILLWEIFSlGLNPYPG 858
Cdd:cd14112  158 PVDGD----TDWASPEFHNPeTPITVQSDIWGLGVLTFCLLS-GFHPFTS 202
PHA03211 PHA03211
serine/threonine kinase US3; Provisional
748-847 1.96e-04

serine/threonine kinase US3; Provisional


Pssm-ID: 223009 [Multi-domain]  Cd Length: 461  Bit Score: 44.88  E-value: 1.96e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 748 RPLELRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLArdimndsnYIVKGNARLPVKW------ 821
Cdd:PHA03211 255 RPLGLAQVTAVARQLLSAIDYIHGEGIIHRDIKTENVLVNGPEDICLGDFGAA--------CFARGSWSTPFHYgiagtv 326
                         90       100
                 ....*....|....*....|....*...
gi 569026720 822 --MAPESIFDCVYTVQSDVWSYGILLWE 847
Cdd:PHA03211 327 dtNAPEVLAGDPYTPSVDIWSAGLVIFE 354
IgI_SALM5_like cd05764
Immunoglobulin domain of human Synaptic Adhesion-Like Molecule 5 (SALM5) and similar proteins; ...
21-101 2.12e-04

Immunoglobulin domain of human Synaptic Adhesion-Like Molecule 5 (SALM5) and similar proteins; member of the I-set of IgSF domains; This group contains the immunoglobulin domain of human Synaptic Adhesion-Like Molecule 5 (SALM5) and similar proteins. The SALM (for synaptic adhesion-like molecules; also known as Lrfn for leucine-rich repeat and fibronectin type III domain containing) family of adhesion molecules consists of five known members: SALM1/Lrfn2, SALM2/Lrfn1, SALM3/Lrfn4, SALM4/Lrfn3, and SALM5/Lrfn5. SALMs share a similar domain structure, containing leucine-rich repeats (LRRs), an immunoglobulin (Ig) domain, and a fibronectin III (FNIII) domain, followed by a transmembrane domain and a C-terminal PDZ-binding motif. SALM5 is implicated in autism spectrum disorders (ASDs) and schizophrenia, induces presynaptic differentiation in contacting axons. SALM5 interacts with the Ig domains of LAR (Leukocyte common Antigen-Related) family receptor protein tyrosine phosphatases (LAR-RPTPs; LAR, PTPdelta, and PTPsigma). In addition, PTPdelta is implicated in ASDs, ADHD, bipolar disorder, and restless leg syndrome. Studies have shown that LAR-RPTPs are novel and splicing-dependent presynaptic ligands for SALM5, and that they mediate SALM5-dependent presynaptic differentiation. Furthermore, SALM5 maintains AMPA receptor (AMPAR)-mediated excitatory synaptic transmission through mechanisms involving the interaction of SALM5 with LAR-RPTPs. This group belongs to the I-set of immunoglobulin superfamily (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: 409421 [Multi-domain]  Cd Length: 88  Bit Score: 40.92  E-value: 2.12e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720  21 PVIEPSVPELVVKPGATVTLRCVGNGsvewDGPPSPHW--------------TLYSDGSSSILSTnnaTFQNTGTYRCTE 86
Cdd:cd05764    1 PLITRHTHELRVLEGQRATLRCKARG----DPEPAIHWispegklisnssrtLVYDNGTLDILIT---TVKDTGAFTCIA 73
                         90
                 ....*....|....*.
gi 569026720  87 pGDPLGGS-AAIHLYV 101
Cdd:cd05764   74 -SNPAGEAtARVELHI 88
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
220-292 2.54e-04

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: 40.39  E-value: 2.54e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 569026720 220 AQIVCSASSvDVNFDVFLQHNNTKlaIPQQSDFHNNRYQKVLTLNLDQVDFQHAGNYSCVASNVQGKHSTSMF 292
Cdd:cd00096    1 VTLTCSASG-NPPPTITWYKNGKP--LPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAGGSASASV 70
STKc_obscurin_rpt2 cd14110
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
751-850 2.77e-04

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: 43.75  E-value: 2.77e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 751 ELRDLLHfssQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDiMNDSNYIVKGNARLPVKWMAPESIFDC 830
Cdd:cd14110  100 EVTDYLW---QILSAVDYLHSRRILHLDLRSENMIITEKNLLKIVDLGNAQP-FNQGKVLMTDKKGDYVETMAPELLEGQ 175
                         90       100
                 ....*....|....*....|
gi 569026720 831 VYTVQSDVWSYGILLWEIFS 850
Cdd:cd14110  176 GAGPQTDIWAIGVTAFIMLS 195
STKc_JNK3 cd07874
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the ...
761-848 3.06e-04

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: 43.92  E-value: 3.06e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 761 QVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDIMND---SNYIVKGNARlpvkwmAPESIFDCVYTVQSD 837
Cdd:cd07874  127 QMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLARTAGTSfmmTPYVVTRYYR------APEVILGMGYKENVD 200
                         90
                 ....*....|.
gi 569026720 838 VWSYGILLWEI 848
Cdd:cd07874  201 IWSVGCIMGEM 211
PKc_CLK1_4 cd14213
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases 1 and 4; ...
587-857 3.23e-04

Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases 1 and 4; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. CLK1 plays a role in neuronal differentiation. CLKs are involved in the phosphorylation and regulation of serine/arginine-rich (SR) proteins, which play a crucial role in pre-mRNA splicing by directing splice site selection. SR proteins are phosphorylated first by SR protein kinases (SRPKs) at the N-terminus, which leads to its assembly into nuclear speckles where splicing factors are stored. CLKs phosphorylate the C-terminal part of SR proteins, causing the nuclear speckles to dissolve and splicing factors to be recruited at sites of active transcription. Based on a conserved "EHLAMMERILG" signature motif which may be crucial for substrate specificity, CLKs are also referred to as LAMMER kinases. CLKs autophosphorylate at tyrosine residues and phosphorylate their substrates exclusively on serine/threonine residues. The CLK1/4 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: 271115 [Multi-domain]  Cd Length: 330  Bit Score: 44.07  E-value: 3.23e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 587 TLGAGAFGKVVEATAFGLGKedavLKVAVKMLKSTAHAdeKEALMSELKIMSHLGQHE-----NIVNLLGACTHGGPVLV 661
Cdd:cd14213   19 TLGEGAFGKVVECIDHKMGG----MHVAVKIVKNVDRY--REAARSEIQVLEHLNTTDpnstfRCVQMLEWFDHHGHVCI 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 662 ITEyccygdLLnflrrkaeamlgpslspgqdpeggvdyknihlekkyvrrdsgfssqGVDTYvemrpvstssndsfseqD 741
Cdd:cd14213   93 VFE------LL----------------------------------------------GLSTY-----------------D 103
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 742 LDKEDG-RPLELRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVL--------------------LTNGHVaKIGDFGLA 800
Cdd:cd14213  104 FIKENSfLPFPIDHIRNMAYQICKSVNFLHHNKLTHTDLKPENILfvqsdyvvkynpkmkrdertLKNPDI-KVVDFGSA 182
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 569026720 801 rdIMNDSNYIVKGNARlpvKWMAPESIFDCVYTVQSDVWSYGILLWEIFsLGLNPYP 857
Cdd:cd14213  183 --TYDDEHHSTLVSTR---HYRAPEVILALGWSQPCDVWSIGCILIEYY-LGFTVFQ 233
STKc_PFTAIRE1 cd07869
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer ...
740-859 3.36e-04

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: 43.91  E-value: 3.36e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 740 QDLDKEDGrPLELRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDIMNDSNyiVKGNARLPV 819
Cdd:cd07869   91 QYMDKHPG-GLHPENVKLFLFQLLRGLSYIHQRYILHRDLKPQNLLISDTGELKLADFGLARAKSVPSH--TYSNEVVTL 167
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 569026720 820 KWMAPESIFDCV-YTVQSDVWSYGILLWEIFSlGLNPYPGI 859
Cdd:cd07869  168 WYRPPDVLLGSTeYSTCLDMWGVGCIFVEMIQ-GVAAFPGM 207
STKc_MSK_N cd05583
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
769-856 3.49e-04

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: 43.54  E-value: 3.49e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 769 LASKNCIHRDVAARNVLL-TNGHVaKIGDFGLARDIMNDSN---YIVKGNarlpVKWMAPESIF--DCVYTVQSDVWSYG 842
Cdd:cd05583  115 LHKLGIIYRDIKLENILLdSEGHV-VLTDFGLSKEFLPGENdraYSFCGT----IEYMAPEVVRggSDGHDKAVDWWSLG 189
                         90
                 ....*....|....
gi 569026720 843 ILLWEIFSlGLNPY 856
Cdd:cd05583  190 VLTYELLT-GASPF 202
STKc_CaMKIV cd14085
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
753-856 3.73e-04

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type IV; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. There are several types of CaMKs including CaMKI, CaMKII, and CaMKIV. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKIV is found predominantly in neurons and immune cells. It is activated by the binding of calcium/CaM and phosphorylation by CaMKK (alpha or beta). The CaMKK-CaMKIV cascade participates in regulating several transcription factors like CREB, MEF2, and retinoid orphan receptors. It also is implicated in T-cell development and signaling, cytokine secretion, and signaling through Toll-like receptors, and is thus, pivotal in immune response and inflammation. The CaMKIV subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270987 [Multi-domain]  Cd Length: 294  Bit Score: 43.66  E-value: 3.73e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 753 RDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTN---GHVAKIGDFGLARDImnDSNYIVKGNARLPvKWMAPESIFD 829
Cdd:cd14085   98 RDAADAVKQILEAVAYLHENGIVHRDLKPENLLYATpapDAPLKIADFGLSKIV--DQQVTMKTVCGTP-GYCAPEILRG 174
                         90       100
                 ....*....|....*....|....*..
gi 569026720 830 CVYTVQSDVWSYGILLWeIFSLGLNPY 856
Cdd:cd14085  175 CAYGPEVDMWSVGVITY-ILLCGFEPF 200
STKc_JNK1 cd07875
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the ...
761-858 3.74e-04

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


Pssm-ID: 143380 [Multi-domain]  Cd Length: 364  Bit Score: 43.88  E-value: 3.74e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 761 QVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDIMND---SNYIVKGNARlpvkwmAPESIFDCVYTVQSD 837
Cdd:cd07875  134 QMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLARTAGTSfmmTPYVVTRYYR------APEVILGMGYKENVD 207
                         90       100
                 ....*....|....*....|.
gi 569026720 838 VWSYGILLWEIFSLGLnPYPG 858
Cdd:cd07875  208 IWSVGCIMGEMIKGGV-LFPG 227
STKc_KIS cd14020
Catalytic domain of the Serine/Threonine Kinase, Kinase Interacting with Stathmin (also called ...
757-850 3.80e-04

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: 43.38  E-value: 3.80e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 757 HFSSQVAQGMAFLASKNCIHRDVAARNVLLT-NGHVAKIGDFGLA-RDIMNDSNYIVKGNARLP-------VKWMAPESI 827
Cdd:cd14020  114 HCARDVLEALAFLHHEGYVHADLKPRNILWSaEDECFKLIDFGLSfKEGNQDVKYIQTDGYRAPeaelqncLAQAGLQSE 193
                         90       100
                 ....*....|....*....|...
gi 569026720 828 FDCVYTVqsDVWSYGILLWEIFS 850
Cdd:cd14020  194 TECTSAV--DLWSLGIVLLEMFS 214
STKc_MAPKAPK3 cd14172
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
765-905 3.86e-04

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: 43.44  E-value: 3.86e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 765 GMA--FLASKNCIHRDVAARNVLLTNGH---VAKIGDFGLARDIMndsnyiVKGNARLPVK---WMAPESIFDCVYTVQS 836
Cdd:cd14172  113 GTAiqYLHSMNIAHRDVKPENLLYTSKEkdaVLKLTDFGFAKETT------VQNALQTPCYtpyYVAPEVLGPEKYDKSC 186
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 569026720 837 DVWSYGILLWeIFSLGLNPY---PGILVNSKFYKLVKDG-YQMAQPAFA--PKNIYSIMQACWALEPTHRPTFQQ 905
Cdd:cd14172  187 DMWSLGVIMY-ILLCGFPPFysnTGQAISPGMKRRIRMGqYGFPNPEWAevSEEAKQLIRHLLKTDPTERMTITQ 260
STKc_TLK cd13990
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the ...
761-848 5.13e-04

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: 43.08  E-value: 5.13e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 761 QVAQGMAFLASKN--CIHRDVAARNVLLTNGHVA---KIGDFGLARdIMNDSNYIVkGNARLPVK-----WMAPESIFDC 830
Cdd:cd13990  113 QVVSALKYLNEIKppIIHYDLKPGNILLHSGNVSgeiKITDFGLSK-IMDDESYNS-DGMELTSQgagtyWYLPPECFVV 190
                         90       100
                 ....*....|....*....|...
gi 569026720 831 VYTVQS-----DVWSYGILLWEI 848
Cdd:cd13990  191 GKTPPKisskvDVWSVGVIFYQM 213
STKc_DCKL3 cd14185
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called ...
583-856 5.35e-04

Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called Doublecortin-like and CAM kinase-like 3); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DCKL3 (or DCAMKL3) belongs to the doublecortin (DCX) family of proteins which are involved in neuronal migration, neurogenesis, and eye receptor development, among others. Family members typically contain tandem doublecortin (DCX) domains at the N-terminus; DCX domains can bind microtubules and serve as protein-interaction platforms. DCKL3 contains a single DCX domain (instead of a tandem) and a C-terminal kinase domain with similarity to CAMKs. It has been shown to interact with tubulin and JIP1/2. The DCKL3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271087 [Multi-domain]  Cd Length: 258  Bit Score: 43.01  E-value: 5.35e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 583 QFGKTLGAGAFGKVVEATAFGLGKEdavlkVAVKMLKSTAHADEKEALMSELKIMSHLgQHENIVNLLGACTHGGPVLVI 662
Cdd:cd14185    3 EIGRTIGDGNFAVVKECRHWNENQE-----YAMKIIDKSKLKGKEDMIESEILIIKSL-SHPNIVKLFEVYETEKEIYLI 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 663 TEYCCYGDLLnflrrkaeamlgpslspgqdpeggvdyknihlekkyvrrdsgfssqgvDTYVEmrpvstssNDSFSEQDl 742
Cdd:cd14185   77 LEYVRGGDLF------------------------------------------------DAIIE--------SVKFTEHD- 99
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 743 dkedgRPLELRDLlhfssqvAQGMAFLASKNCIHRDVAARNVLLTNGH----VAKIGDFGLARDIMNDSnYIVKGNArlp 818
Cdd:cd14185  100 -----AALMIIDL-------CEALVYIHSKHIVHRDLKPENLLVQHNPdkstTLKLADFGLAKYVTGPI-FTVCGTP--- 163
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 569026720 819 vKWMAPESIFDCVYTVQSDVWSYGILLWeIFSLGLNPY 856
Cdd:cd14185  164 -TYVAPEILSEKGYGLEVDMWAAGVILY-ILLCGFPPF 199
STKc_nPKC_epsilon cd05591
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze ...
758-850 6.62e-04

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


Pssm-ID: 270743 [Multi-domain]  Cd Length: 321  Bit Score: 42.86  E-value: 6.62e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 758 FSSQVAQGMAFLASKNCIHRDVAARNVLL-TNGHVaKIGDFGLARDIMNDsNYIVKGNARLPvKWMAPESIFDCVYTVQS 836
Cdd:cd05591  101 YAAEVTLALMFLHRHGVIYRDLKLDNILLdAEGHC-KLADFGMCKEGILN-GKTTTTFCGTP-DYIAPEILQELEYGPSV 177
                         90
                 ....*....|....
gi 569026720 837 DVWSYGILLWEIFS 850
Cdd:cd05591  178 DWWALGVLMYEMMA 191
IgI_1_MuSK cd20970
agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of ...
416-492 7.57e-04

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: 39.41  E-value: 7.57e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 569026720 416 TLLCAASGYPQPNVTWLQCSGHTDRCDEAQVLQVWDDpypevlsqepfhkvtvqsLLTVETLE--HNQTYECRAHNSVG 492
Cdd:cd20970   21 TFMCRAEGSPEPEISWTRNGNLIIEFNTRYIVRENGT------------------TLTIRNIRrsDMGIYLCIASNGVP 81
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
775-856 8.22e-04

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 43.19  E-value: 8.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720  775 IHRDVAARNVLLTNG--HV---------------AKIGDFGLARDIMNDSnyIVKGNARLPVKWmAPESIFDCV--YTVQ 835
Cdd:PTZ00266  147 LHRDLKPQNIFLSTGirHIgkitaqannlngrpiAKIGDFGLSKNIGIES--MAHSCVGTPYYW-SPELLLHETksYDDK 223
                          90       100
                  ....*....|....*....|.
gi 569026720  836 SDVWSYGILLWEIFSlGLNPY 856
Cdd:PTZ00266  224 SDMWALGCIIYELCS-GKTPF 243
STKc_HIPK1 cd14228
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 1; ...
749-858 8.41e-04

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: 42.77  E-value: 8.41e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 749 PLELRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTN----GHVAKIGDFGLARDIMND--SNYIVKGNARlpvkwm 822
Cdd:cd14228  113 PLPLKYIRPILQQVATALMKLKSLGLIHADLKPENIMLVDpvrqPYRVKVIDFGSASHVSKAvcSTYLQSRYYR------ 186
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 569026720 823 APESIFDCVYTVQSDVWSYGILLWEIFsLGLNPYPG 858
Cdd:cd14228  187 APEIILGLPFCEAIDMWSLGCVIAELF-LGWPLYPG 221
STKc_aPKC_zeta cd05617
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze ...
758-862 8.70e-04

Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-zeta plays a critical role in activating the glucose transport response. It is activated by glucose, insulin, and exercise through diverse pathways. PKC-zeta also plays a central role in maintaining cell polarity in yeast and mammalian cells. In addition, it affects actin remodeling in muscle cells. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. aPKCs only require phosphatidylserine (PS) for activation. The aPKC-zeta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270768 [Multi-domain]  Cd Length: 357  Bit Score: 42.70  E-value: 8.70e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 758 FSSQVAQGMAFLASKNCIHRDVAARNVLL-TNGHVaKIGDFGLARDIM--NDSNYIVKGNArlpvKWMAPESIFDCVYTV 834
Cdd:cd05617  121 YAAEICIALNFLHERGIIYRDLKLDNVLLdADGHI-KLTDYGMCKEGLgpGDTTSTFCGTP----NYIAPEILRGEEYGF 195
                         90       100
                 ....*....|....*....|....*...
gi 569026720 835 QSDVWSYGILLWEIFSlGLNPYPGILVN 862
Cdd:cd05617  196 SVDWWALGVLMFEMMA-GRSPFDIITDN 222
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
761-878 8.85e-04

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: 42.29  E-value: 8.85e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 761 QVAQGMAFLASKNCIHRDVAARNVL-LTNGHVAKI--GDFGLARdiMNDsNYIVKGNARLPvKWMAPESIFDCVYTVQSD 837
Cdd:cd14166  108 QVLSAVKYLHENGIVHRDLKPENLLyLTPDENSKImiTDFGLSK--MEQ-NGIMSTACGTP-GYVAPEVLAQKPYSKAVD 183
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 569026720 838 VWSYGILLWeIFSLGLNPYPGILVNSKFYKLVKDGYQMAQP 878
Cdd:cd14166  184 CWSIGVITY-ILLCGYPPFYEETESRLFEKIKEGYYEFESP 223
STKc_HIPK2 cd14227
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 2; ...
749-858 9.33e-04

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: 42.38  E-value: 9.33e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 749 PLELRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTN----GHVAKIGDFGLARDIMND--SNYIVKGNARlpvkwm 822
Cdd:cd14227  113 PLPLKYIRPILQQVATALMKLKSLGLIHADLKPENIMLVDpsrqPYRVKVIDFGSASHVSKAvcSTYLQSRYYR------ 186
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 569026720 823 APESIFDCVYTVQSDVWSYGILLWEIFsLGLNPYPG 858
Cdd:cd14227  187 APEIILGLPFCEAIDMWSLGCVIAELF-LGWPLYPG 221
STKc_PINK1 cd14018
Catalytic domain of the Serine/Threonine protein kinase, Pten INduced Kinase 1; STKs catalyze ...
761-902 9.39e-04

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: 42.48  E-value: 9.39e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 761 QVAQGMAFLASKNCIHRDVAARNVLL----TNGHVAKIGDFG--LARDIMN-----DSNYIVK-GNARLpvkwMAPEsIF 828
Cdd:cd14018  146 QLLEGVDHLVRHGIAHRDLKSDNILLeldfDGCPWLVIADFGccLADDSIGlqlpfSSWYVDRgGNACL----MAPE-VS 220
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 829 DCV---YTV----QSDVWSYGILLWEIFSLGlNPypgilvnskFYKLVKDG-----YQMAQ----PAFAPKNIYSIMQAC 892
Cdd:cd14018  221 TAVpgpGVVinysKADAWAVGAIAYEIFGLS-NP---------FYGLGDTMlesrsYQESQlpalPSAVPPDVRQVVKDL 290
                        170
                 ....*....|
gi 569026720 893 WALEPTHRPT 902
Cdd:cd14018  291 LQRDPNKRVS 300
PHA03210 PHA03210
serine/threonine kinase US3; Provisional
739-858 9.61e-04

serine/threonine kinase US3; Provisional


Pssm-ID: 165476 [Multi-domain]  Cd Length: 501  Bit Score: 42.76  E-value: 9.61e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 739 EQDLDKEDgRPLeLRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDIMNDsnyivkgnaRLP 818
Cdd:PHA03210 255 DEAFDWKD-RPL-LKQTRAIMKQLLCAVEYIHDKKLIHRDIKLENIFLNCDGKIVLGDFGTAMPFEKE---------REA 323
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 569026720 819 VK--WM------APESIFDCVYTVQSDVWSYGILLWEIFSLGLNPYPG 858
Cdd:PHA03210 324 FDygWVgtvatnSPEILAGDGYCEITDIWSCGLILLDMLSHDFCPIGD 371
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
401-495 1.12e-03

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: 38.64  E-value: 1.12e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720   401 PPEVSViwtFINGSGTLLCAASGYPQPNVTWLQcsghtdrcdeaqvlqvwddPYPEVLSQEPFHKVTVQSL---LTVE-- 475
Cdd:smart00410   1 PPSVTV---KEGESVTLSCEASGSPPPEVTWYK-------------------QGGKLLAESGRFSVSRSGStstLTISnv 58
                           90       100
                   ....*....|....*....|
gi 569026720   476 TLEHNQTYECRAHNSVGSGS 495
Cdd:smart00410  59 TPEDSGTYTCAATNSSGSAS 78
STKc_PIM cd14005
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
757-848 1.21e-03

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


Pssm-ID: 270907 [Multi-domain]  Cd Length: 255  Bit Score: 41.84  E-value: 1.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 757 HFSSQVAQGMAFLASKNCIHRDVAARNVLLT-NGHVAKIGDFGLArDIMNDSNYIVKGNARLpvkWMAPESIFDCVYTVQ 835
Cdd:cd14005  111 IIFRQVVEAVRHCHQRGVLHRDIKDENLLINlRTGEVKLIDFGCG-ALLKDSVYTDFDGTRV---YSPPEWIRHGRYHGR 186
                         90
                 ....*....|....
gi 569026720 836 S-DVWSYGILLWEI 848
Cdd:cd14005  187 PaTVWSLGILLYDM 200
STKc_PhKG1 cd14182
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs ...
751-856 1.34e-03

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: 41.82  E-value: 1.34e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 751 ELRDLLHFSSQVAQgmaFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDImnDSNYIVKGNARLPvKWMAPEsIFDC 830
Cdd:cd14182  111 ETRKIMRALLEVIC---ALHKLNIVHRDLKPENILLDDDMNIKLTDFGFSCQL--DPGEKLREVCGTP-GYLAPE-IIEC 183
                         90       100       110
                 ....*....|....*....|....*....|...
gi 569026720 831 V-------YTVQSDVWSYGILLWEIFSlGLNPY 856
Cdd:cd14182  184 SmddnhpgYGKEVDMWSTGVIMYTLLA-GSPPF 215
STKc_LATS cd05598
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the ...
775-847 1.50e-03

Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LATS was originally identified in Drosophila using a screen for genes whose inactivation led to overproliferation of cells. In tetrapods, there are two LATS isoforms, LATS1 and LATS2. Inactivation of LATS1 in mice results in the development of various tumors, including sarcomas and ovarian cancer. LATS functions as a tumor suppressor and is implicated in cell cycle regulation. The LATS subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270749 [Multi-domain]  Cd Length: 333  Bit Score: 41.92  E-value: 1.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 775 IHRDVAARNVLL-TNGHVaKIGDFGL--------------ARDIMNDSNYIvkgnarlpvkwmAPESIFDCVYTVQSDVW 839
Cdd:cd05598  123 IHRDIKPDNILIdRDGHI-KLTDFGLctgfrwthdskyylAHSLVGTPNYI------------APEVLLRTGYTQLCDWW 189

                 ....*...
gi 569026720 840 SYGILLWE 847
Cdd:cd05598  190 SVGVILYE 197
STKc_CK1_delta_epsilon cd14125
Catalytic domain of the Serine/Threonine protein kinases, Casein Kinase 1 delta and epsilon; ...
738-801 1.52e-03

Catalytic domain of the Serine/Threonine protein kinases, Casein Kinase 1 delta and epsilon; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CK1 phosphorylates a variety of substrates including enzymes, transcription and splice factors, cytoskeletal proteins, viral oncogenes, receptors, and membrane-associated proteins. There are mutliple isoforms of CK1 and in mammals, seven isoforms (alpha, beta, gamma1-3, delta, and epsilon) have been characterized. These isoforms differ mainly in the length and structure of their C-terminal non-catalytic region. The delta and epsilon isoforms of CK1 play important roles in circadian rhythm and cell growth. They phosphorylate PERIOD proteins (PER1-3), which are circadian clock proteins that fulfill negative regulatory functions. PER phosphorylation leads to its degradation. However, CRY proteins form a complex with PER and CK1delta/epsilon that protects PER from degradation and leads to nuclear accummulation of the complex, which inhibits BMAL1-CLOCK dependent transcription activation. CK1delta/epsilon also phosphorylate the tumor suppressor p53 and the cellular oncogene Mdm2, which are key regulators of cell growth, genome integrity, and the development of cancer. This subfamily also includes the CK1 fungal proteins Saccharomyces cerevisiae HRR25 and Schizosaccharomyces pombe HHP1. These fungal proteins are involved in DNA repair. The CK1 delta/epsilon subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271027 [Multi-domain]  Cd Length: 275  Bit Score: 41.58  E-value: 1.52e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 569026720 738 SEQDLDKEDGRPLELRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLL---TNGHVAKIGDFGLAR 801
Cdd:cd14125   81 SLEDLFNFCSRKFSLKTVLMLADQMISRIEYVHSKNFIHRDIKPDNFLMglgKKGNLVYIIDFGLAK 147
STKc_PKB cd05571
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer ...
758-848 1.59e-03

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


Pssm-ID: 270723 [Multi-domain]  Cd Length: 322  Bit Score: 41.57  E-value: 1.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 758 FSSQVAQGMAFLASKNCIHRDVAARNVLL-TNGHVaKIGDFGLARDIMNDSNyIVKGNARLPvKWMAPESIFDCVYTVQS 836
Cdd:cd05571  100 YGAEIVLALGYLHSQGIVYRDLKLENLLLdKDGHI-KITDFGLCKEEISYGA-TTKTFCGTP-EYLAPEVLEDNDYGRAV 176
                         90
                 ....*....|..
gi 569026720 837 DVWSYGILLWEI 848
Cdd:cd05571  177 DWWGLGVVMYEM 188
STKc_MSK2_C cd14180
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
766-850 1.59e-03

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


Pssm-ID: 271082 [Multi-domain]  Cd Length: 309  Bit Score: 41.78  E-value: 1.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 766 MAFLASKNCIHRDVAARNVLL---TNGHVAKIGDFGLARdiMNDSNYIVKGNARLPVKWMAPESIFDCVYTVQSDVWSYG 842
Cdd:cd14180  114 VSFMHEAGVVHRDLKPENILYadeSDGAVLKVIDFGFAR--LRPQGSRPLQTPCFTLQYAAPELFSNQGYDESCDLWSLG 191

                 ....*...
gi 569026720 843 ILLWEIFS 850
Cdd:cd14180  192 VILYTMLS 199
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
584-845 1.72e-03

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: 41.20  E-value: 1.72e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 584 FGKTLGAGAFGKVVEATAFGLGKedavlKVAVKMLKSTAHADEKEALMSELKIMSHLgQHENIVNLLGACTHGGPVLVIT 663
Cdd:cd14083    7 FKEVLGTGAFSEVVLAEDKATGK-----LVAIKCIDKKALKGKEDSLENEIAVLRKI-KHPNIVQLLDIYESKSHLYLVM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 664 EYCCYGDLLNflrrkaeamlgpslspgqdpeggvdyknihlekKYVRRDSgfssqgvdtYVEmrpvstssndsfseqdld 743
Cdd:cd14083   81 ELVTGGELFD---------------------------------RIVEKGS---------YTE------------------ 100
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 744 kedgrplelRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVL-LTNGHVAKI--GDFGLARdiMNDSNyiVKGNARLPVK 820
Cdd:cd14083  101 ---------KDASHLIRQVLEAVDYLHSLGIVHRDLKPENLLyYSPDEDSKImiSDFGLSK--MEDSG--VMSTACGTPG 167
                        250       260
                 ....*....|....*....|....*....
gi 569026720 821 WMAPESIFDCVYTVQSDVWSYG----ILL 845
Cdd:cd14083  168 YVAPEVLAQKPYGKAVDCWSIGvisyILL 196
STKc_CdkB_plant cd07837
Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; ...
744-848 1.72e-03

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: 41.36  E-value: 1.72e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 744 KEDGRPLELRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGH-VAKIGDFGLARDImndsnyivkgnaRLPVK-- 820
Cdd:cd07837  100 RGPHNPLPAKTIQSFMYQLCKGVAHCHSHGVMHRDLKPQNLLVDKQKgLLKIADLGLGRAF------------TIPIKsy 167
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 569026720 821 --------WMAPESIFDCV-YTVQSDVWSYGILLWEI 848
Cdd:cd07837  168 theivtlwYRAPEVLLGSThYSTPVDMWSVGCIFAEM 204
PK_STRAD cd08216
Pseudokinase domain of STE20-related kinase adapter protein; The pseudokinase domain shows ...
613-843 1.85e-03

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


Pssm-ID: 270856 [Multi-domain]  Cd Length: 315  Bit Score: 41.51  E-value: 1.85e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 613 VAVKM--LKSTAHADEKEaLMSELKIMSHLgQHENIVNLLGACTHGGPVLVITEYCCYGDLLNFLRRkaeamlgpslspg 690
Cdd:cd08216   28 VAVKKinLESDSKEDLKF-LQQEILTSRQL-QHPNILPYVTSFVVDNDLYVVTPLMAYGSCRDLLKT------------- 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 691 qdpeggvdykniHLEkkyvrrdSGFssqgvdtyvemrpvstssndsfseqdldKEDGRPLELRDLLHfssqvaqGMAFLA 770
Cdd:cd08216   93 ------------HFP-------EGL----------------------------PELAIAFILRDVLN-------ALEYIH 118
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 771 SKNCIHRDVAARNVLLT-NGHVaKIGDFGLARDIMNdsnyivKGNARLPV-----------KWMAPESIFDCV--YTVQS 836
Cdd:cd08216  119 SKGYIHRSVKASHILISgDGKV-VLSGLRYAYSMVK------HGKRQRVVhdfpksseknlPWLSPEVLQQNLlgYNEKS 191

                 ....*..
gi 569026720 837 DVWSYGI 843
Cdd:cd08216  192 DIYSVGI 198
STKc_RSK_C cd14091
C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs ...
587-678 1.88e-03

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


Pssm-ID: 270993 [Multi-domain]  Cd Length: 291  Bit Score: 41.46  E-value: 1.88e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 587 TLGAGAFGKVVEATAFGLGKEdavlkVAVKML-KSTAHADEkealmsELKIMSHLGQHENIVNLLGACTHGGPVLVITEY 665
Cdd:cd14091    7 EIGKGSYSVCKRCIHKATGKE-----YAVKIIdKSKRDPSE------EIEILLRYGQHPNIITLRDVYDDGNSVYLVTEL 75
                         90
                 ....*....|....
gi 569026720 666 CCYGDLLN-FLRRK 678
Cdd:cd14091   76 LRGGELLDrILRQK 89
STKc_HUNK cd14070
Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase ...
585-908 1.88e-03

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: 41.34  E-value: 1.88e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 585 GKTLGAGAFGKVVEATAFGLGKedavlKVAVKML-KSTAHADE--KEALMSELKIMSHLgQHENIVNLLGACTHGGPVLV 661
Cdd:cd14070    7 GRKLGEGSFAKVREGLHAVTGE-----KVAIKVIdKKKAKKDSyvTKNLRREGRIQQMI-RHPNITQLLDILETENSYYL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 662 ITEYCCYGDLLNFLrrkaeamlgpslspgqdpeggvdYKNIHLEKKYVRRdsgfssqgvdtyvemrpvstssndsfseqd 741
Cdd:cd14070   81 VMELCPGGNLMHRI-----------------------YDKKRLEEREARR------------------------------ 107
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 742 ldkedgrplelrdllhFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDI----MNDSNYIVKGNArl 817
Cdd:cd14070  108 ----------------YIRQLVSAVEHLHRAGVVHRDLKIENLLLDENDNIKLIDFGLSNCAgilgYSDPFSTQCGSP-- 169
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 818 pvKWMAPESIFDCVYTVQSDVWSYGILLWEIFSlGLNPYPGILVNSK-FYKLVKDGYQMAQPAFAPKNIYSIMQACWALE 896
Cdd:cd14070  170 --AYAAPELLARKKYGPKVDVWSIGVNMYAMLT-GTLPFTVEPFSLRaLHQKMVDKEMNPLPTDLSPGAISFLRSLLEPD 246
                        330
                 ....*....|..
gi 569026720 897 PTHRPTFQQICS 908
Cdd:cd14070  247 PLKRPNIKQALA 258
STKc_SGK cd05575
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; ...
758-921 2.06e-03

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


Pssm-ID: 270727 [Multi-domain]  Cd Length: 323  Bit Score: 41.53  E-value: 2.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 758 FSSQVAQGMAFLASKNCIHRDVAARNVLL-TNGHVaKIGDFGLARDIMNDSNYIVK--GNArlpvKWMAPESIFDCVYTV 834
Cdd:cd05575  101 YAAEIASALGYLHSLNIIYRDLKPENILLdSQGHV-VLTDFGLCKEGIEPSDTTSTfcGTP----EYLAPEVLRKQPYDR 175
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 835 QSDVWSYGILLWEIFSlGLNPypgilvnskFYKlvKDGYQM-----AQPAFAPKNIYSIMqacwalepthrptfqqiCSF 909
Cdd:cd05575  176 TVDWWCLGAVLYEMLY-GLPP---------FYS--RDTAEMydnilHKPLRLRTNVSPSA-----------------RDL 226
                        170
                 ....*....|..
gi 569026720 910 LQEQAQEDRRER 921
Cdd:cd05575  227 LEGLLQKDRTKR 238
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
38-85 2.08e-03

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: 37.69  E-value: 2.08e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 569026720  38 VTLRCVGNG----SVEW-----DGPPSPHWTLYSDGSSSILSTNNATFQNTGTYRCT 85
Cdd:cd00096    1 VTLTCSASGnpppTITWykngkPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCV 57
IgI_6_Dscam cd20959
Sixth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
217-288 2.51e-03

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: 38.24  E-value: 2.51e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 569026720 217 GEAAQIVCSASSVDVNFDVFLQHNNTklAIPQQSDFHN---NRYQKVLTLnlDQVDFQHAGNYSCVASNVQGKHS 288
Cdd:cd20959   17 GMRAQLHCGVPGGDLPLNIRWTLDGQ--PISDDLGITVsrlGRRSSILSI--DSLEASHAGNYTCHARNSAGSAS 87
STKc_HIPK cd14211
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase; STKs ...
748-858 3.37e-03

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


Pssm-ID: 271113 [Multi-domain]  Cd Length: 329  Bit Score: 40.51  E-value: 3.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 748 RPLELRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNG----HVAKIGDFGLARDIMND--SNYIVKGNARlpvkw 821
Cdd:cd14211   96 SPLPLKYIRPILQQVLTALLKLKSLGLIHADLKPENIMLVDPvrqpYRVKVIDFGSASHVSKAvcSTYLQSRYYR----- 170
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 569026720 822 mAPESIFDCVYTVQSDVWSYGILLWEIFsLGLNPYPG 858
Cdd:cd14211  171 -APEIILGLPFCEAIDMWSLGCVIAELF-LGWPLYPG 205
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
758-850 3.75e-03

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 40.57  E-value: 3.75e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 758 FSSQVAQGMAFLASKNCIHRDVAARNVLL---TNghVAKIGDFGLARDImndsnyivkgnaRLPVK----------WMAP 824
Cdd:PLN00009 107 YLYQILRGIAYCHSHRVLHRDLKPQNLLIdrrTN--ALKLADFGLARAF------------GIPVRtfthevvtlwYRAP 172
                         90       100
                 ....*....|....*....|....*..
gi 569026720 825 ESIF-DCVYTVQSDVWSYGILLWEIFS 850
Cdd:PLN00009 173 EILLgSRHYSTPVDIWSVGCIFAEMVN 199
STKc_PRP4 cd14135
Catalytic domain of the Serine/Threonine Kinase, Pre-mRNA-Processing factor 4; STKs catalyze ...
772-850 3.83e-03

Catalytic domain of the Serine/Threonine Kinase, Pre-mRNA-Processing factor 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PRP4 phosphorylates a number of factors involved in the formation of active spliceosomes, which catalyze pre-mRNA splicing. It phosphorylates PRP6 and PRP31, components of the U4/U6-U5 tri-small nuclear ribonucleoprotein (snRNP), during spliceosomal complex formation. In fission yeast, PRP4 phosphorylates the splicing factor PRP1 (U5-102 kD in mammals). Thus, PRP4 plays a key role in regulating spliceosome assembly and pre-mRNA splicing. It also plays an important role in mitosis by acting as a spindle assembly checkpoint kinase that is required for chromosome alignment and the recruitment of the checkpoint proteins MPS1, MAD1, and MAD2 at kinetochores. The PRP4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271037 [Multi-domain]  Cd Length: 318  Bit Score: 40.28  E-value: 3.83e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 772 KNC--IHRDVAARNVLLTNGH-VAKIGDFGLARDIM-ND-SNYIVKGNARlpvkwmAPESIFDCVYTVQSDVWSYGILLW 846
Cdd:cd14135  122 KKCniLHADIKPDNILVNEKKnTLKLCDFGSASDIGeNEiTPYLVSRFYR------APEIILGLPYDYPIDMWSVGCTLY 195

                 ....
gi 569026720 847 EIFS 850
Cdd:cd14135  196 ELYT 199
STKc_ROCK1 cd05622
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
758-856 3.98e-03

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: 40.76  E-value: 3.98e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 758 FSSQVAQGMAFLASKNCIHRDVAARNVLL-TNGHVaKIGDFGLARDiMNDSNYIVKGNARLPVKWMAPESIF----DCVY 832
Cdd:cd05622  177 YTAEVVLALDAIHSMGFIHRDVKPDNMLLdKSGHL-KLADFGTCMK-MNKEGMVRCDTAVGTPDYISPEVLKsqggDGYY 254
                         90       100
                 ....*....|....*....|....
gi 569026720 833 TVQSDVWSYGILLWEIFsLGLNPY 856
Cdd:cd05622  255 GRECDWWSVGVFLYEML-VGDTPF 277
IgC2_D1_D2_LILR_KIR_like cd16843
Immunoglobulin (Ig)-like domain found in Leukocyte Ig-like receptors, Natural killer ...
28-91 5.06e-03

Immunoglobulin (Ig)-like domain found in Leukocyte Ig-like receptors, Natural killer inhibitory receptors (KIRs) and similar domains; member of Immunoglobulin Constant-2 set of IgSF domains; The members here are composed of the first and second immunoglobulin (Ig)-like domains found in Leukocyte Ig-like receptors (LILRs), Natural killer inhibitory receptors (KIRs, also known as also known as cluster of differentiation (CD) 158), and similar proteins. This group includes LILRB1 (also known as LIR-1), LILRA5 (also known as LIR9), an activating natural cytotoxicity receptor NKp46, the immune-type receptor glycoprotein VI (GPVI), and the IgA-specific receptor Fc-alphaRI (also known as cluster of differentiation (CD) 89). LILRs are a family of immunoreceptors expressed on expressed on T and B cells, on monocytes, dendritic cells, and subgroups of natural killer (NK) cells. The human LILR family contains nine proteins (LILRA1-3, and 5, and LILRB1-5). From functional assays, and as the cytoplasmic domains of various LILRs, for example LILRB1, LILRB2 (also known as LIR-2), and LILRB3 (also known as LIR-3) contain immunoreceptor tyrosine-based inhibitory motifs (ITIMs), it is thought that LIR proteins are inhibitory receptors. Of the eight LIR family proteins, only LILRB1, and LILRB2, show detectable binding to class I MHC molecules; ligands for the other members have yet to be determined. The extracellular portions of the different LIR proteins contain different numbers of Ig-like domains for example, four in the case of LILRB1, and LILRB2, and two in the case of LILRB4 (also known as LIR-5). The activating natural cytotoxicity receptor NKp46 is expressed in natural killer cells, and is organized as an extracellular portion having two Ig-like extracellular domains, a transmembrane domain, and a small cytoplasmic portion. GPVI, which also contains two Ig-like domains, participates in the processes of collagen-mediated platelet activation and arterial thrombus formation. Fc-alphaRI is expressed on monocytes, eosinophils, neutrophils, and macrophages; it mediates IgA-induced immune effector responses such as phagocytosis, antibody-dependent cell-mediated cytotoxicity and respiratory burst. Killer cell immunoglobulin-like receptors (KIRs; also known as CD158 for human KIR) are transmembrane glycoproteins expressed by natural killer cells and subsets of T cells. KIRs are a family of highly polymorphic activating and inhibitory receptors that serve as key regulators of human NK cell function. The KIR proteins are classified by the number of extracellular immunoglobulin domains (2D or 3D) and by whether they have a long (L) or short (S) cytoplasmic domain. KIR proteins with the long cytoplasmic domain transduce inhibitory signals upon ligand binding via an immune tyrosine-based inhibitory motif (ITIM), while KIR proteins with the short cytoplasmic domain lack the ITIM motif and instead associate with the TYRO protein tyrosine kinase binding protein to transduce activating signals. The major ligands for KIR are MHC class I (HLA-A, -B or -C) molecules.


Pssm-ID: 409518 [Multi-domain]  Cd Length: 90  Bit Score: 36.97  E-value: 5.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720  28 PELVVKPGATVTLRCVGNgsvewdgPPSPHWTLYSDGSSSILST--------------NNATFQNTGTYRC--------T 85
Cdd:cd16843    8 PSSVVPLGENVTIRCQGP-------PEAVLFQLYKEGNSLSQGTvrekepqnkaefyiPHMDRNHAGRYRCryrsgtlwS 80

                 ....*.
gi 569026720  86 EPGDPL 91
Cdd:cd16843   81 EPSDPL 86
STKc_PKD cd14082
Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer ...
739-846 5.31e-03

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


Pssm-ID: 270984 [Multi-domain]  Cd Length: 260  Bit Score: 39.70  E-value: 5.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 739 EQDLDKEDGRpLELRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLL---TNGHVAKIGDFGLARDIMNDS--NYIVKG 813
Cdd:cd14082   90 EMILSSEKGR-LPERITKFLVTQILVALRYLHSKNIVHCDLKPENVLLasaEPFPQVKLCDFGFARIIGEKSfrRSVVGT 168
                         90       100       110
                 ....*....|....*....|....*....|...
gi 569026720 814 NArlpvkWMAPESIFDCVYTVQSDVWSYGILLW 846
Cdd:cd14082  169 PA-----YLAPEVLRNKGYNRSLDMWSVGVIIY 196
STKc_NDR_like cd05599
Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs ...
775-847 5.75e-03

Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NDR kinases regulate mitosis, cell growth, embryonic development, and neurological processes. They are also required for proper centrosome duplication. Higher eukaryotes contain two NDR isoforms, NDR1 and NDR2. This subfamily also contains fungal NDR-like kinases. NDR kinase contains an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Like many other AGC kinases, NDR kinase requires phosphorylation at two sites, the activation loop (A-loop) and the hydrophobic motif (HM), for activity. The NDR kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270750 [Multi-domain]  Cd Length: 324  Bit Score: 39.91  E-value: 5.75e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 775 IHRDVAARNVLLT-NGHVaKIGDFGLA----RDIMNDSN-----YIvkgnarlpvkwmAPESIFDCVYTVQSDVWSYGIL 844
Cdd:cd05599  123 IHRDIKPDNLLLDaRGHI-KLSDFGLCtglkKSHLAYSTvgtpdYI------------APEVFLQKGYGKECDWWSLGVI 189

                 ...
gi 569026720 845 LWE 847
Cdd:cd05599  190 MYE 192
STKc_aPKC cd05588
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the ...
758-856 5.79e-03

Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. aPKCs only require phosphatidylserine (PS) for activation. They contain a C2-like region, instead of a calcium-binding (C2) region found in classical PKCs, in their regulatory domain. There are two aPKC isoforms, zeta and iota. aPKCs are involved in many cellular functions including proliferation, migration, apoptosis, polarity maintenance and cytoskeletal regulation. They also play a critical role in the regulation of glucose metabolism and in the pathogenesis of type 2 diabetes. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. The aPKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270740 [Multi-domain]  Cd Length: 328  Bit Score: 40.10  E-value: 5.79e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 758 FSSQVAQGMAFLASKNCIHRDVAARNVLL-TNGHVaKIGDFGLARDIMNDS----------NYIvkgnarlpvkwmAPES 826
Cdd:cd05588  101 YSAEISLALNFLHEKGIIYRDLKLDNVLLdSEGHI-KLTDYGMCKEGLRPGdttstfcgtpNYI------------APEI 167
                         90       100       110
                 ....*....|....*....|....*....|
gi 569026720 827 IFDCVYTVQSDVWSYGILLWEIFSlGLNPY 856
Cdd:cd05588  168 LRGEDYGFSVDWWALGVLMFEMLA-GRSPF 196
STKc_aPKC_iota cd05618
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze ...
758-856 6.93e-03

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: 39.63  E-value: 6.93e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 758 FSSQVAQGMAFLASKNCIHRDVAARNVLL-TNGHVaKIGDFGLARDIM--NDSNYIVKGNArlpvKWMAPESIFDCVYTV 834
Cdd:cd05618  126 YSAEISLALNYLHERGIIYRDLKLDNVLLdSEGHI-KLTDYGMCKEGLrpGDTTSTFCGTP----NYIAPEILRGEDYGF 200
                         90       100
                 ....*....|....*....|..
gi 569026720 835 QSDVWSYGILLWEIFSlGLNPY 856
Cdd:cd05618  201 SVDWWALGVLMFEMMA-GRSPF 221
Ig_2 pfam13895
Immunoglobulin domain; This domain contains immunoglobulin-like domains.
203-292 7.39e-03

Immunoglobulin domain; This domain contains immunoglobulin-like domains.


Pssm-ID: 433563 [Multi-domain]  Cd Length: 76  Bit Score: 36.22  E-value: 7.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720  203 PALTLVPAELVRirGEAAQIVCSASSvDVNFDVFLQHNNTklAIPQQSDFHnnryqkVLTLNLDqvdfqHAGNYSCVASN 282
Cdd:pfam13895   2 PVLTPSPTVVTE--GEPVTLTCSAPG-NPPASYTWYKGGE--ALNSSPNFF------ILAVSAE-----DSGTYTCVARN 65
                          90
                  ....*....|
gi 569026720  283 VQGKHSTSMF 292
Cdd:pfam13895  66 GRGGKVSNPV 75
STKc_GRK2 cd14223
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs ...
754-856 8.63e-03

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: 39.26  E-value: 8.63e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569026720 754 DLLHFSSQVAQGMAFLASKNCIHRDVAARNVLL-TNGHVaKIGDFGLARDIMNDSNYIVKGNArlpvKWMAPESIFDCV- 831
Cdd:cd14223  104 EMRFYAAEIILGLEHMHSRFVVYRDLKPANILLdEFGHV-RISDLGLACDFSKKKPHASVGTH----GYMAPEVLQKGVa 178
                         90       100
                 ....*....|....*....|....*
gi 569026720 832 YTVQSDVWSYGILLWEIFSlGLNPY 856
Cdd:cd14223  179 YDSSADWFSLGCMLFKLLR-GHSPF 202
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
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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