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Conserved domains on  [gi|1034633499|ref|XP_016861960|]
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myosin light chain kinase, smooth muscle isoform X9 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PKc_like super family cl21453
Protein Kinases, catalytic domain; The protein kinase superfamily is mainly composed of the ...
261-519 0e+00

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


The actual alignment was detected with superfamily member cd14191:

Pssm-ID: 473864 [Multi-domain]  Cd Length: 259  Bit Score: 544.21  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 261 SDFYDIEERLGSGKFGQVFRLVEKKTRKVWAGKFFKAYSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEI 340
Cdd:cd14191     1 SDFYDIEERLGSGKFGQVFRLVEKKTKKVWAGKFFKAYSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 341 VSGGELFERIIDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKTGTRIKLIDFGLARRLENAGSLKV 420
Cdd:cd14191    81 VSGGELFERIIDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKTGTKIKLIDFGLARRLENAGSLKV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 421 LFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDFDDEAFDEISDDAKDFISNLL 500
Cdd:cd14191   161 LFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDFDDEAFDEISDDAKDFISNLL 240
                         250
                  ....*....|....*....
gi 1034633499 501 KKDMKNRLDCTQCLQHPWL 519
Cdd:cd14191   241 KKDMKARLTCTQCLQHPWL 259
IgI_8_hMLCK_like cd05762
Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar ...
37-135 2.28e-64

Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar protein; member of the I-set of IgSF domains; The members here are composed of the eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar proteins. Myosin light-chain kinase (MLCK) is a key regulator of different forms of cell motility involving actin and myosin II. Agonist stimulation of smooth muscle cells increases cytosolic Ca2+ which binds calmodulin. This Ca2+-calmodulin complex in turn binds to and activates MLCK. Activated MLCK leads to the phosphorylation of the 20 kDa myosin regulatory light chain (RLC) of myosin II and the stimulation of actin-activated myosin MgATPase activity. MLCK is widely present in vertebrate tissues; it phosphorylates the 20 kDa RLC of both smooth and nonmuscle myosin II. Phosphorylation leads to the activation of the myosin motor domain and altered structural properties of myosin II. In smooth muscle MLCK it is involved in initiating contraction. In nonmuscle cells, MLCK may participate in cell division and cell motility; it has been suggested MLCK plays a role in cardiomyocyte differentiation and contraction through regulation of nonmuscle myosin II.


:

Pssm-ID: 409419  Cd Length: 99  Bit Score: 208.27  E-value: 2.28e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499  37 PPQIIQFPEDQKVRAGESVELFGKVTGTQPITCTWMKFRKQIQESEHMKVENSENGSKLTILAARQEHCGCYTLLVENKL 116
Cdd:cd05762     1 PPQIIQFPEDMKVRAGESVELFCKVTGTQPITCTWMKFRKQIQEGEGIKIENTENSSKLTITEGQQEHCGCYTLEVENKL 80
                          90
                  ....*....|....*....
gi 1034633499 117 GSRQAQVNLTVVDKPDPPA 135
Cdd:cd05762    81 GSRQAQVNLTVVDKPDPPA 99
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
612-699 7.00e-50

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


:

Pssm-ID: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 168.91  E-value: 7.00e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 612 SKTIRDLEVVEGSAARFDCKIEGYPDPEVVWFKDDQSIRESRHFQIDYDEDGNCSLIISDVCGDDDAKYTCKAVNSLGEA 691
Cdd:cd20973     1 IQTLRDKEVVEGSAARFDCKVEGYPDPEVKWMKDDNPIVESRRFQIDQDEDGLCSLIISDVCGDDSGKYTCKAVNSLGEA 80

                  ....*...
gi 1034633499 692 TCTAELIV 699
Cdd:cd20973    81 TCSAELTV 88
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
131-223 9.32e-20

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


:

Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 84.47  E-value: 9.32e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 131 PDPPaGTPCASDIRSSSLTLSWyGSSYDGGSAVQSYSIEIWDSANKTWKELAT--CRSTSFNVQDLLPDHEYKFRVRAIN 208
Cdd:cd00063     1 PSPP-TNLRVTDVTSTSVTLSW-TPPEDDGGPITGYVVEYREKGSGDWKEVEVtpGSETSYTLTGLKPGTEYEFRVRAVN 78
                          90
                  ....*....|....*
gi 1034633499 209 VYGTSEPSQESELTT 223
Cdd:cd00063    79 GGGESPPSESVTVTT 93
 
Name Accession Description Interval E-value
STKc_MLCK1 cd14191
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze ...
261-519 0e+00

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: 544.21  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 261 SDFYDIEERLGSGKFGQVFRLVEKKTRKVWAGKFFKAYSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEI 340
Cdd:cd14191     1 SDFYDIEERLGSGKFGQVFRLVEKKTKKVWAGKFFKAYSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 341 VSGGELFERIIDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKTGTRIKLIDFGLARRLENAGSLKV 420
Cdd:cd14191    81 VSGGELFERIIDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKTGTKIKLIDFGLARRLENAGSLKV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 421 LFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDFDDEAFDEISDDAKDFISNLL 500
Cdd:cd14191   161 LFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDFDDEAFDEISDDAKDFISNLL 240
                         250
                  ....*....|....*....
gi 1034633499 501 KKDMKNRLDCTQCLQHPWL 519
Cdd:cd14191   241 KKDMKARLTCTQCLQHPWL 259
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
264-519 1.70e-95

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 295.98  E-value: 1.70e-95
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499  264 YDIEERLGSGKFGQVFRLVEKKTRKVWAGKFF-KAYSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEIVS 342
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIkKKKIKKDRERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVMEYCE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499  343 GGELFERIIDEDFeLTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKTgtRIKLIDFGLARRLENAGSLKVLF 422
Cdd:smart00220  81 GGDLFDLLKKRGR-LSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDG--HVKLADFGLARQLDPGEKLTTFV 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499  423 GTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLAN-VTSATWDFDDEaFDEISDDAKDFISNLLK 501
Cdd:smart00220 158 GTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDDQLLELFKkIGKPKPPFPPP-EWDISPEAKDLIRKLLV 236
                          250
                   ....*....|....*...
gi 1034633499  502 KDMKNRLDCTQCLQHPWL 519
Cdd:smart00220 237 KDPEKRLTAEEALQHPFF 254
Pkinase pfam00069
Protein kinase domain;
264-519 6.44e-73

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 235.60  E-value: 6.44e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 264 YDIEERLGSGKFGQVFRLVEKKTRKVWAGKFFKAYSAKEKE--NIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEIV 341
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKAKHRDTGKIVAIKKIKKEKIKKKKdkNILREIKILKKLNHPNIVRLYDAFEDKDNLYLVLEYV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 342 SGGELFERIIdEDFELTERECIKYMRQISEGveyihkqgivhldlkpenimcvnktgtriklidfglarrLENAGSLKVL 421
Cdd:pfam00069  81 EGGSLFDLLS-EKGAFSEREAKFIMKQILEG---------------------------------------LESGSSLTTF 120
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 422 FGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDFDDEaFDEISDDAKDFISNLLK 501
Cdd:pfam00069 121 VGTPWYMAPEVLGGNPYGPKVDVWSLGCILYELLTGKPPFPGINGNEIYELIIDQPYAFPEL-PSNLSEEAKDLLKKLLK 199
                         250
                  ....*....|....*...
gi 1034633499 502 KDMKNRLDCTQCLQHPWL 519
Cdd:pfam00069 200 KDPSKRLTATQALQHPWF 217
IgI_8_hMLCK_like cd05762
Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar ...
37-135 2.28e-64

Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar protein; member of the I-set of IgSF domains; The members here are composed of the eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar proteins. Myosin light-chain kinase (MLCK) is a key regulator of different forms of cell motility involving actin and myosin II. Agonist stimulation of smooth muscle cells increases cytosolic Ca2+ which binds calmodulin. This Ca2+-calmodulin complex in turn binds to and activates MLCK. Activated MLCK leads to the phosphorylation of the 20 kDa myosin regulatory light chain (RLC) of myosin II and the stimulation of actin-activated myosin MgATPase activity. MLCK is widely present in vertebrate tissues; it phosphorylates the 20 kDa RLC of both smooth and nonmuscle myosin II. Phosphorylation leads to the activation of the myosin motor domain and altered structural properties of myosin II. In smooth muscle MLCK it is involved in initiating contraction. In nonmuscle cells, MLCK may participate in cell division and cell motility; it has been suggested MLCK plays a role in cardiomyocyte differentiation and contraction through regulation of nonmuscle myosin II.


Pssm-ID: 409419  Cd Length: 99  Bit Score: 208.27  E-value: 2.28e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499  37 PPQIIQFPEDQKVRAGESVELFGKVTGTQPITCTWMKFRKQIQESEHMKVENSENGSKLTILAARQEHCGCYTLLVENKL 116
Cdd:cd05762     1 PPQIIQFPEDMKVRAGESVELFCKVTGTQPITCTWMKFRKQIQEGEGIKIENTENSSKLTITEGQQEHCGCYTLEVENKL 80
                          90
                  ....*....|....*....
gi 1034633499 117 GSRQAQVNLTVVDKPDPPA 135
Cdd:cd05762    81 GSRQAQVNLTVVDKPDPPA 99
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
264-507 1.16e-51

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 186.76  E-value: 1.16e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 264 YDIEERLGSGKFGQVFRLVEKKTRKVWAGKFFK---AYSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEI 340
Cdd:COG0515     9 YRILRLLGRGGMGVVYLARDLRLGRPVALKVLRpelAADPEARERFRREARALARLNHPNIVRVYDVGEEDGRPYLVMEY 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 341 VSGGELfERIIDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGtRIKLIDFGLARRLENAGSLK- 419
Cdd:COG0515    89 VEGESL-ADLLRRRGPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANIL-LTPDG-RVKLIDFGIARALGGATLTQt 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 420 -VLFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDFDDEAFDEISDDAKDFISN 498
Cdd:COG0515   166 gTVVGTPGYMAPEQARGEPVDPRSDVYSLGVTLYELLTGRPPFDGDSPAELLRAHLREPPPPPSELRPDLPPALDAIVLR 245

                  ....*....
gi 1034633499 499 LLKKDMKNR 507
Cdd:COG0515   246 ALAKDPEER 254
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
612-699 7.00e-50

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


Pssm-ID: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 168.91  E-value: 7.00e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 612 SKTIRDLEVVEGSAARFDCKIEGYPDPEVVWFKDDQSIRESRHFQIDYDEDGNCSLIISDVCGDDDAKYTCKAVNSLGEA 691
Cdd:cd20973     1 IQTLRDKEVVEGSAARFDCKVEGYPDPEVKWMKDDNPIVESRRFQIDQDEDGLCSLIISDVCGDDSGKYTCKAVNSLGEA 80

                  ....*...
gi 1034633499 692 TCTAELIV 699
Cdd:cd20973    81 TCSAELTV 88
I-set pfam07679
Immunoglobulin I-set domain;
609-699 3.35e-36

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 131.23  E-value: 3.35e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 609 PYFSKTIRDLEVVEGSAARFDCKIEGYPDPEVVWFKDDQSIRESRHFQIDYDeDGNCSLIISDVCGDDDAKYTCKAVNSL 688
Cdd:pfam07679   1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYE-GGTYTLTISNVQPDDSGKYTCVATNSA 79
                          90
                  ....*....|.
gi 1034633499 689 GEATCTAELIV 699
Cdd:pfam07679  80 GEAEASAELTV 90
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
259-508 6.41e-33

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 129.55  E-value: 6.41e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 259 KVSDFyDIEERLGSGKFGQVfRLVEKKTR-KVWAGKFFKAYS---AKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANI 334
Cdd:PTZ00263   16 KLSDF-EMGETLGTGSFGRV-RIAKHKGTgEYYAIKCLKKREilkMKQVQHVAQEKSILMELSHPFIVNMMCSFQDENRV 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 335 VMVLEIVSGGELFERIidedfelteRECIKYMRQISE--------GVEYIHKQGIVHLDLKPENIMCVNKTgtRIKLIDF 406
Cdd:PTZ00263   94 YFLLEFVVGGELFTHL---------RKAGRFPNDVAKfyhaelvlAFEYLHSKDIIYRDLKPENLLLDNKG--HVKVTDF 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 407 GLARRLENagSLKVLFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDFdDEAFD 486
Cdd:PTZ00263  163 GFAKKVPD--RTFTLCGTPEYLAPEVIQSKGHGKAVDWWTMGVLLYEFIAGYPPFFDDTPFRIYEKILAGRLKF-PNWFD 239
                         250       260
                  ....*....|....*....|..
gi 1034633499 487 EisdDAKDFISNLLKKDMKNRL 508
Cdd:PTZ00263  240 G---RARDLVKGLLQTDHTKRL 258
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
131-223 9.32e-20

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 84.47  E-value: 9.32e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 131 PDPPaGTPCASDIRSSSLTLSWyGSSYDGGSAVQSYSIEIWDSANKTWKELAT--CRSTSFNVQDLLPDHEYKFRVRAIN 208
Cdd:cd00063     1 PSPP-TNLRVTDVTSTSVTLSW-TPPEDDGGPITGYVVEYREKGSGDWKEVEVtpGSETSYTLTGLKPGTEYEFRVRAVN 78
                          90
                  ....*....|....*
gi 1034633499 209 VYGTSEPSQESELTT 223
Cdd:cd00063    79 GGGESPPSESVTVTT 93
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
316-465 1.33e-19

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 92.94  E-value: 1.33e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 316 LHHPKLVQCVDAFEEKAN--IVMvlEIVSGGELfERIIDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMc 393
Cdd:NF033483   64 LSHPNIVSVYDVGEDGGIpyIVM--EYVDGRTL-KDYIREHGPLSPEEAVEIMIQILSALEHAHRNGIVHRDIKPQNIL- 139
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034633499 394 VNKTGtRIKLIDFGLARRLENAgSL----KVLfGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDN 465
Cdd:NF033483  140 ITKDG-RVKVTDFGIARALSST-TMtqtnSVL-GTVHYLSPEQARGGTVDARSDIYSLGIVLYEMLTGRPPFDGDS 212
I-set pfam07679
Immunoglobulin I-set domain;
38-127 5.85e-18

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 79.22  E-value: 5.85e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499  38 PQIIQFPEDQKVRAGESVELFGKVTGTQPITCTWMKFRKQIQESEHMKVENSENGSKLTILAARQEHCGCYTLLVENKLG 117
Cdd:pfam07679   1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAG 80
                          90
                  ....*....|
gi 1034633499 118 SRQAQVNLTV 127
Cdd:pfam07679  81 EAEASAELTV 90
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
616-699 6.08e-18

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: 79.09  E-value: 6.08e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499  616 RDLEVVEGSAARFDCKIEGYPDPEVVWFKDDQS-IRESRHFQIDYDeDGNCSLIISDVCGDDDAKYTCKAVNSLGEATCT 694
Cdd:smart00410   2 PSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKlLAESGRFSVSRS-GSTSTLTISNVTPEDSGTYTCAATNSSGSASSG 80

                   ....*
gi 1034633499  695 AELIV 699
Cdd:smart00410  81 TTLTV 85
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
300-450 2.16e-17

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


Pssm-ID: 274846 [Multi-domain]  Cd Length: 1266  Bit Score: 86.82  E-value: 2.16e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499  300 AKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVM-VLEIVSGGELFERIIDEDfELTERECIKYMRQISEGVEYIHK 378
Cdd:TIGR03903   19 EHQRARFRRETALCARLYHPNIVALLDSGEAPPGLLFaVFEYVPGRTLREVLAADG-ALPAGETGRLMLQVLDALACAHN 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499  379 QGIVHLDLKPENIMCVNKTGTR-IKLIDFGLARRLENAGSLKVL--------FGTPEFVAPEVINYEPIGYATDMWSIGV 449
Cdd:TIGR03903   98 QGIVHRDLKPQNIMVSQTGVRPhAKVLDFGIGTLLPGVRDADVAtltrttevLGTPTYCAPEQLRGEPVTPNSDLYAWGL 177

                   .
gi 1034633499  450 I 450
Cdd:TIGR03903  178 I 178
fn3 pfam00041
Fibronectin type III domain;
133-216 1.60e-14

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 69.37  E-value: 1.60e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 133 PPAGTPCASDIRSSSLTLSWYGSSyDGGSAVQSYSIEIWD-SANKTWKELATCRST-SFNVQDLLPDHEYKFRVRAINVY 210
Cdd:pfam00041   1 SAPSNLTVTDVTSTSLTVSWTPPP-DGNGPITGYEVEYRPkNSGEPWNEITVPGTTtSVTLTGLKPGTEYEVRVQAVNGG 79

                  ....*.
gi 1034633499 211 GTSEPS 216
Cdd:pfam00041  80 GEGPPS 85
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
108-247 2.49e-14

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 76.58  E-value: 2.49e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 108 YTLLVENKLG----SRQAQVnLTVVDKPDPPAG-TpcASDIRSSSLTLSWYGSSydgGSAVQSYSIEIWDSANKTWKELA 182
Cdd:COG3401   207 YRVAATDTGGesapSNEVSV-TTPTTPPSAPTGlT--ATADTPGSVTLSWDPVT---ESDATGYRVYRSNSGDGPFTKVA 280
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034633499 183 TCRSTSFNVQDLLPDHEYKFRVRAINVYGT-SEPSQESELTTVGEKPEEPKDeVEVSDDDEKEPEV 247
Cdd:COG3401   281 TVTTTSYTDTGLTNGTTYYYRVTAVDAAGNeSAPSNVVSVTTDLTPPAAPSG-LTATAVGSSSITL 345
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
131-213 1.66e-13

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 66.48  E-value: 1.66e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499  131 PDPPaGTPCASDIRSSSLTLSWYGSSYDGG-SAVQSYSIEIWDSANKTWKELATCRSTSFNVQDLLPDHEYKFRVRAINV 209
Cdd:smart00060   1 PSPP-SNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNG 79

                   ....
gi 1034633499  210 YGTS 213
Cdd:smart00060  80 AGEG 83
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
44-127 2.99e-12

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: 62.91  E-value: 2.99e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499   44 PEDQKVRAGESVELFGKVTGTQPITCTWMKFRKQ-IQESEHMKVENSENGSKLTILAARQEHCGCYTLLVENKLGSRQAQ 122
Cdd:smart00410   1 PPSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKlLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSG 80

                   ....*
gi 1034633499  123 VNLTV 127
Cdd:smart00410  81 TTLTV 85
 
Name Accession Description Interval E-value
STKc_MLCK1 cd14191
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze ...
261-519 0e+00

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: 544.21  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 261 SDFYDIEERLGSGKFGQVFRLVEKKTRKVWAGKFFKAYSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEI 340
Cdd:cd14191     1 SDFYDIEERLGSGKFGQVFRLVEKKTKKVWAGKFFKAYSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 341 VSGGELFERIIDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKTGTRIKLIDFGLARRLENAGSLKV 420
Cdd:cd14191    81 VSGGELFERIIDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKTGTKIKLIDFGLARRLENAGSLKV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 421 LFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDFDDEAFDEISDDAKDFISNLL 500
Cdd:cd14191   161 LFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDFDDEAFDEISDDAKDFISNLL 240
                         250
                  ....*....|....*....
gi 1034633499 501 KKDMKNRLDCTQCLQHPWL 519
Cdd:cd14191   241 KKDMKARLTCTQCLQHPWL 259
STKc_MLCK cd14103
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the ...
270-519 0e+00

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: 515.24  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 270 LGSGKFGQVFRLVEKKTRKVWAGKFFKAYSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEIVSGGELFER 349
Cdd:cd14103     1 LGRGKFGTVYRCVEKATGKELAAKFIKCRKAKDREDVRNEIEIMNQLRHPRLLQLYDAFETPREMVLVMEYVAGGELFER 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 350 IIDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKTGTRIKLIDFGLARRLENAGSLKVLFGTPEFVA 429
Cdd:cd14103    81 VVDDDFELTERDCILFMRQICEGVQYMHKQGILHLDLKPENILCVSRTGNQIKIIDFGLARKYDPDKKLKVLFGTPEFVA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 430 PEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDFDDEAFDEISDDAKDFISNLLKKDMKNRLD 509
Cdd:cd14103   161 PEVVNYEPISYATDMWSVGVICYVLLSGLSPFMGDNDAETLANVTRAKWDFDDEAFDDISDEAKDFISKLLVKDPRKRMS 240
                         250
                  ....*....|
gi 1034633499 510 CTQCLQHPWL 519
Cdd:cd14103   241 AAQCLQHPWL 250
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
270-518 7.76e-120

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: 358.50  E-value: 7.76e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 270 LGSGKFGQVFRLVEKKTRKVWAGKFFKaYSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEIVSGGELFER 349
Cdd:cd14006     1 LGRGRFGVVKRCIEKATGREFAAKFIP-KRDKKKEAVLREISILNQLQHPRIIQLHEAYESPTELVLILELCSGGELLDR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 350 IIDEdFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKTGTRIKLIDFGLARRLENAGSLKVLFGTPEFVA 429
Cdd:cd14006    80 LAER-GSLSEEEVRTYMRQLLEGLQYLHNHHILHLDLKPENILLADRPSPQIKIIDFGLARKLNPGEELKEIFGTPEFVA 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 430 PEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDFDDEAFDEISDDAKDFISNLLKKDMKNRLD 509
Cdd:cd14006   159 PEIVNGEPVSLATDMWSIGVLTYVLLSGLSPFLGEDDQETLANISACRVDFSEEYFSSVSQEAKDFIRKLLVKEPRKRPT 238

                  ....*....
gi 1034633499 510 CTQCLQHPW 518
Cdd:cd14006   239 AQEALQHPW 247
STKc_Twitchin_like cd14114
The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs ...
262-519 1.07e-113

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


Pssm-ID: 271016 [Multi-domain]  Cd Length: 259  Bit Score: 343.41  E-value: 1.07e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 262 DFYDIEERLGSGKFGQVFRLVEKKTRKVWAGKFFKAYSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEIV 341
Cdd:cd14114     2 DHYDILEELGTGAFGVVHRCTERATGNNFAAKFIMTPHESDKETVRKEIQIMNQLHHPKLINLHDAFEDDNEMVLILEFL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 342 SGGELFERIIDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKTGTRIKLIDFGLARRLENAGSLKVL 421
Cdd:cd14114    82 SGGELFERIAAEHYKMSEAEVINYMRQVCEGLCHMHENNIVHLDIKPENIMCTTKRSNEVKLIDFGLATHLDPKESVKVT 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 422 FGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDFDDEAFDEISDDAKDFISNLLK 501
Cdd:cd14114   162 TGTAEFAAPEIVEREPVGFYTDMWAVGVLSYVLLSGLSPFAGENDDETLRNVKSCDWNFDDSAFSGISEEAKDFIRKLLL 241
                         250
                  ....*....|....*...
gi 1034633499 502 KDMKNRLDCTQCLQHPWL 519
Cdd:cd14114   242 ADPNKRMTIHQALEHPWL 259
STKc_MLCK3 cd14192
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze ...
268-519 7.97e-113

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: 341.17  E-value: 7.97e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 268 ERLGSGKFGQVFRLVEKKTRKVWAGKFFKAYSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEIVSGGELF 347
Cdd:cd14192    10 EVLGGGRFGQVHKCTELSTGLTLAAKIIKVKGAKEREEVKNEINIMNQLNHVNLIQLYDAFESKTNLTLIMEYVDGGELF 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 348 ERIIDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKTGTRIKLIDFGLARRLENAGSLKVLFGTPEF 427
Cdd:cd14192    90 DRITDESYQLTELDAILFTRQICEGVHYLHQHYILHLDLKPENILCVNSTGNQIKIIDFGLARRYKPREKLKVNFGTPEF 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 428 VAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDFDDEAFDEISDDAKDFISNLLKKDMKNR 507
Cdd:cd14192   170 LAPEVVNYDFVSFPTDMWSVGVITYMLLSGLSPFLGETDAETMNNIVNCKWDFDAEAFENLSEEAKDFISRLLVKEKSCR 249
                         250
                  ....*....|..
gi 1034633499 508 LDCTQCLQHPWL 519
Cdd:cd14192   250 MSATQCLKHEWL 261
STKc_MLCK2 cd14190
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze ...
261-519 2.27e-111

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: 337.28  E-value: 2.27e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 261 SDFYDI--EERLGSGKFGQVFRLVEKKTRKVWAGKFFKAYSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVL 338
Cdd:cd14190     1 SSTFSIhsKEVLGGGKFGKVHTCTEKRTGLKLAAKVINKQNSKDKEMVLLEIQVMNQLNHRNLIQLYEAIETPNEIVLFM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 339 EIVSGGELFERIIDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKTGTRIKLIDFGLARRLENAGSL 418
Cdd:cd14190    81 EYVEGGELFERIVDEDYHLTEVDAMVFVRQICEGIQFMHQMRVLHLDLKPENILCVNRTGHQVKIIDFGLARRYNPREKL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 419 KVLFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDFDDEAFDEISDDAKDFISN 498
Cdd:cd14190   161 KVNFGTPEFLSPEVVNYDQVSFPTDMWSMGVITYMLLSGLSPFLGDDDTETLNNVLMGNWYFDEETFEHVSDEAKDFVSN 240
                         250       260
                  ....*....|....*....|.
gi 1034633499 499 LLKKDMKNRLDCTQCLQHPWL 519
Cdd:cd14190   241 LIIKERSARMSATQCLKHPWL 261
STKc_MLCK4 cd14193
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze ...
261-519 3.00e-110

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: 334.57  E-value: 3.00e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 261 SDFYDI--EERLGSGKFGQVFRLVEKKTRKVWAGKFFKAYSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVL 338
Cdd:cd14193     1 NSYYNVnkEEILGGGRFGQVHKCEEKSSGLKLAAKIIKARSQKEKEEVKNEIEVMNQLNHANLIQLYDAFESRNDIVLVM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 339 EIVSGGELFERIIDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKTGTRIKLIDFGLARRLENAGSL 418
Cdd:cd14193    81 EYVDGGELFDRIIDENYNLTELDTILFIKQICEGIQYMHQMYILHLDLKPENILCVSREANQVKIIDFGLARRYKPREKL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 419 KVLFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDFDDEAFDEISDDAKDFISN 498
Cdd:cd14193   161 RVNFGTPEFLAPEVVNYEFVSFPTDMWSLGVIAYMLLSGLSPFLGEDDNETLNNILACQWDFEDEEFADISEEAKDFISK 240
                         250       260
                  ....*....|....*....|.
gi 1034633499 499 LLKKDMKNRLDCTQCLQHPWL 519
Cdd:cd14193   241 LLIKEKSWRMSASEALKHPWL 261
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
263-518 7.99e-104

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: 317.50  E-value: 7.99e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 263 FYDIEERLGSGKFGQVFRLVEKKTRKVWAGKFF--KAYSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEI 340
Cdd:cd05117     1 KYELGKVLGRGSFGVVRLAVHKKTGEEYAVKIIdkKKLKSEDEEMLRREIEILKRLDHPNIVKLYEVFEDDKNLYLVMEL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 341 VSGGELFERIIDEDFeLTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNK-TGTRIKLIDFGLARRLENAGSLK 419
Cdd:cd05117    81 CTGGELFDRIVKKGS-FSEREAAKIMKQILSAVAYLHSQGIVHRDLKPENILLASKdPDSPIKIIDFGLAKIFEEGEKLK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 420 VLFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDFDDEAFDEISDDAKDFISNL 499
Cdd:cd05117   160 TVCGTPYYVAPEVLKGKGYGKKCDIWSLGVILYILLCGYPPFYGETEQELFEKILKGKYSFDSPEWKNVSEEAKDLIKRL 239
                         250
                  ....*....|....*....
gi 1034633499 500 LKKDMKNRLDCTQCLQHPW 518
Cdd:cd05117   240 LVVDPKKRLTAAEALNHPW 258
STKc_DAPK cd14105
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs ...
258-519 3.78e-101

Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DAPKs mediate cell death and act as tumor suppressors. They are necessary to induce cell death and their overexpression leads to death-associated changes including membrane blebbing, cell rounding, and formation of autophagic vesicles. Vertebrates contain three subfamily members with different domain architecture, localization, and function. DAPK1 is the prototypical member of the subfamily and is also simply referred to as DAPK. DAPK2 is also called DAPK-related protein 1 (DRP-1), while DAPK3 has also been named DAP-like kinase (DLK) and zipper-interacting protein kinase (ZIPk). These proteins are ubiquitously expressed in adult tissues, are capable of cross talk with each other, and may act synergistically in regulating cell death. The DAPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271007 [Multi-domain]  Cd Length: 269  Bit Score: 311.34  E-value: 3.78e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 258 QKVSDFYDIEERLGSGKFGQVFRLVEKKTRKVWAGKFFKAYSAK------EKENIRQEISIMNCLHHPKLVQCVDAFEEK 331
Cdd:cd14105     1 ENVEDFYDIGEELGSGQFAVVKKCREKSTGLEYAAKFIKKRRSKasrrgvSREDIEREVSILRQVLHPNIITLHDVFENK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 332 ANIVMVLEIVSGGELFErIIDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKT--GTRIKLIDFGLA 409
Cdd:cd14105    81 TDVVLILELVAGGELFD-FLAEKESLSEEEATEFLKQILDGVNYLHTKNIAHFDLKPENIMLLDKNvpIPRIKLIDFGLA 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 410 RRLENAGSLKVLFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDFDDEAFDEIS 489
Cdd:cd14105   160 HKIEDGNEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVNYDFDDEYFSNTS 239
                         250       260       270
                  ....*....|....*....|....*....|
gi 1034633499 490 DDAKDFISNLLKKDMKNRLDCTQCLQHPWL 519
Cdd:cd14105   240 ELAKDFIRQLLVKDPRKRMTIQESLRHPWI 269
STKc_DAPK2 cd14196
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs ...
258-519 3.56e-97

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


Pssm-ID: 271098 [Multi-domain]  Cd Length: 269  Bit Score: 301.11  E-value: 3.56e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 258 QKVSDFYDIEERLGSGKFGQVFRLVEKKTRKVWAGKFFKAYSAKE------KENIRQEISIMNCLHHPKLVQCVDAFEEK 331
Cdd:cd14196     1 QKVEDFYDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRAsrrgvsREEIEREVSILRQVLHPNIITLHDVYENR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 332 ANIVMVLEIVSGGELFERIIDEDfELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKTGT--RIKLIDFGLA 409
Cdd:cd14196    81 TDVVLILELVSGGELFDFLAQKE-SLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIPipHIKLIDFGLA 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 410 RRLENAGSLKVLFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDFDDEAFDEIS 489
Cdd:cd14196   160 HEIEDGVEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYDFDEEFFSHTS 239
                         250       260       270
                  ....*....|....*....|....*....|
gi 1034633499 490 DDAKDFISNLLKKDMKNRLDCTQCLQHPWL 519
Cdd:cd14196   240 ELAKDFIRKLLVKETRKRLTIQEALRHPWI 269
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
264-519 1.70e-95

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 295.98  E-value: 1.70e-95
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499  264 YDIEERLGSGKFGQVFRLVEKKTRKVWAGKFF-KAYSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEIVS 342
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIkKKKIKKDRERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVMEYCE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499  343 GGELFERIIDEDFeLTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKTgtRIKLIDFGLARRLENAGSLKVLF 422
Cdd:smart00220  81 GGDLFDLLKKRGR-LSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDG--HVKLADFGLARQLDPGEKLTTFV 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499  423 GTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLAN-VTSATWDFDDEaFDEISDDAKDFISNLLK 501
Cdd:smart00220 158 GTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDDQLLELFKkIGKPKPPFPPP-EWDISPEAKDLIRKLLV 236
                          250
                   ....*....|....*...
gi 1034633499  502 KDMKNRLDCTQCLQHPWL 519
Cdd:smart00220 237 KDPEKRLTAEEALQHPFF 254
STKc_DAPK1 cd14194
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs ...
258-519 1.65e-92

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


Pssm-ID: 271096 [Multi-domain]  Cd Length: 269  Bit Score: 288.84  E-value: 1.65e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 258 QKVSDFYDIEERLGSGKFGQVFRLVEKKTRKVWAGKFFKAYSAKE------KENIRQEISIMNCLHHPKLVQCVDAFEEK 331
Cdd:cd14194     1 ENVDDYYDTGEELGSGQFAVVKKCREKSTGLQYAAKFIKKRRTKSsrrgvsREDIEREVSILKEIQHPNVITLHEVYENK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 332 ANIVMVLEIVSGGELFERIIDEDfELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKTGT--RIKLIDFGLA 409
Cdd:cd14194    81 TDVILILELVAGGELFDFLAEKE-SLTEEEATEFLKQILNGVYYLHSLQIAHFDLKPENIMLLDRNVPkpRIKIIDFGLA 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 410 RRLENAGSLKVLFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDFDDEAFDEIS 489
Cdd:cd14194   160 HKIDFGNEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANVSAVNYEFEDEYFSNTS 239
                         250       260       270
                  ....*....|....*....|....*....|
gi 1034633499 490 DDAKDFISNLLKKDMKNRLDCTQCLQHPWL 519
Cdd:cd14194   240 ALAKDFIRRLLVKDPKKRMTIQDSLQHPWI 269
STKc_Titin cd14104
Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the ...
264-539 2.64e-91

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: 285.99  E-value: 2.64e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 264 YDIEERLGSGKFGQVFRLVEKKTRKVWAGKFFKAYSAkEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEIVSG 343
Cdd:cd14104     2 YMIAEELGRGQFGIVHRCVETSSKKTYMAKFVKVKGA-DQVLVKKEISILNIARHRNILRLHESFESHEELVMIFEFISG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 344 GELFERIIDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKTGTRIKLIDFGLARRLENAGSLKVLFG 423
Cdd:cd14104    81 VDIFERITTARFELNEREIVSYVRQVCEALEFLHSKNIGHFDIRPENIIYCTRRGSYIKIIEFGQSRQLKPGDKFRLQYT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 424 TPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDFDDEAFDEISDDAKDFISNLLKKD 503
Cdd:cd14104   161 SAEFYAPEVHQHESVSTATDMWSLGCLVYVLLSGINPFEAETNQQTIENIRNAEYAFDDEAFKNISIEALDFVDRLLVKE 240
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1034633499 504 MKNRLDCTQCLQHPWLMKDTKNMEAKKLSKDRMKKY 539
Cdd:cd14104   241 RKSRMTAQEALNHPWLKQGMETVSSKDIKTTRHRRY 276
STKc_DAPK3 cd14195
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs ...
258-519 3.15e-85

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: 269.95  E-value: 3.15e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 258 QKVSDFYDIEERLGSGKFGQVFRLVEKKTRKVWAGKFFK------AYSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEK 331
Cdd:cd14195     1 SMVEDHYEMGEELGSGQFAIVRKCREKGTGKEYAAKFIKkrrlssSRRGVSREEIEREVNILREIQHPNIITLHDIFENK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 332 ANIVMVLEIVSGGELFERIIDEDfELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKT--GTRIKLIDFGLA 409
Cdd:cd14195    81 TDVVLILELVSGGELFDFLAEKE-SLTEEEATQFLKQILDGVHYLHSKRIAHFDLKPENIMLLDKNvpNPRIKLIDFGIA 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 410 RRLENAGSLKVLFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDFDDEAFDEIS 489
Cdd:cd14195   160 HKIEAGNEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGETKQETLTNISAVNYDFDEEYFSNTS 239
                         250       260       270
                  ....*....|....*....|....*....|
gi 1034633499 490 DDAKDFISNLLKKDMKNRLDCTQCLQHPWL 519
Cdd:cd14195   240 ELAKDFIRRLLVKDPKKRMTIAQSLEHSWI 269
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
260-519 9.02e-83

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: 263.44  E-value: 9.02e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 260 VSDFYDIEER-LGSGKFGQVFRLVEKKTRKVWAGKFFKAY--SAKEKENIRQEISI-MNCLHHPKLVQCVDAFEEKANIV 335
Cdd:cd14106     5 INEVYTVESTpLGRGKFAVVRKCIHKETGKEYAAKFLRKRrrGQDCRNEILHEIAVlELCKDCPRVVNLHEVYETRSELI 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 336 MVLEIVSGGELFeRIIDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKT-GTRIKLIDFGLARRLEN 414
Cdd:cd14106    85 LILELAAGGELQ-TLLDEEECLTEADVRRLMRQILEGVQYLHERNIVHLDLKPQNILLTSEFpLGDIKLCDFGISRVIGE 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 415 AGSLKVLFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDFDDEAFDEISDDAKD 494
Cdd:cd14106   164 GEEIREILGTPDYVAPEILSYEPISLATDMWSIGVLTYVLLTGHSPFGGDDKQETFLNISQCNLDFPEELFKDVSPLAID 243
                         250       260
                  ....*....|....*....|....*
gi 1034633499 495 FISNLLKKDMKNRLDCTQCLQHPWL 519
Cdd:cd14106   244 FIKRLLVKDPEKRLTAKECLEHPWL 268
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
260-518 1.43e-78

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: 251.91  E-value: 1.43e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 260 VSDFYDIEERLGSGKFGQVFRLVEKKTRKVWAGKFFKAYSAKEKEN-IRQEISIMNCLHHPKLVQCVDAFEEKANIVMVL 338
Cdd:cd14083     1 IRDKYEFKEVLGTGAFSEVVLAEDKATGKLVAIKCIDKKALKGKEDsLENEIAVLRKIKHPNIVQLLDIYESKSHLYLVM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 339 EIVSGGELFERIIDEDFeLTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIM-CVNKTGTRIKLIDFGLARrLENAGS 417
Cdd:cd14083    81 ELVTGGELFDRIVEKGS-YTEKDASHLIRQVLEAVDYLHSLGIVHRDLKPENLLyYSPDEDSKIMISDFGLSK-MEDSGV 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 418 LKVLFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDFDDEAFDEISDDAKDFIS 497
Cdd:cd14083   159 MSTACGTPGYVAPEVLAQKPYGKAVDCWSIGVISYILLCGYPPFYDENDSKLFAQILKAEYEFDSPYWDDISDSAKDFIR 238
                         250       260
                  ....*....|....*....|.
gi 1034633499 498 NLLKKDMKNRLDCTQCLQHPW 518
Cdd:cd14083   239 HLMEKDPNKRYTCEQALEHPW 259
STKc_DRAK2 cd14198
The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
262-519 7.21e-76

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: 245.22  E-value: 7.21e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 262 DFYDIEER-LGSGKFGQVFRLVEKKTRKVWAGKFFKAYSAKE--KENIRQEISIMNCL-HHPKLVQCVDAFEEKANIVMV 337
Cdd:cd14198     7 NFYILTSKeLGRGKFAVVRQCISKSTGQEYAAKFLKKRRRGQdcRAEILHEIAVLELAkSNPRVVNLHEVYETTSEIILI 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 338 LEIVSGGELFERII-DEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIM--CVNKTGTrIKLIDFGLARRLEN 414
Cdd:cd14198    87 LEYAAGGEIFNLCVpDLAEMVSENDIIRLIRQILEGVYYLHQNNIVHLDLKPQNILlsSIYPLGD-IKIVDFGMSRKIGH 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 415 AGSLKVLFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDFDDEAFDEISDDAKD 494
Cdd:cd14198   166 ACELREIMGTPEYLAPEILNYDPITTATDMWNIGVIAYMLLTHESPFVGEDNQETFLNISQVNVDYSEETFSSVSQLATD 245
                         250       260
                  ....*....|....*....|....*
gi 1034633499 495 FISNLLKKDMKNRLDCTQCLQHPWL 519
Cdd:cd14198   246 FIQKLLVKNPEKRPTAEICLSHSWL 270
Pkinase pfam00069
Protein kinase domain;
264-519 6.44e-73

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 235.60  E-value: 6.44e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 264 YDIEERLGSGKFGQVFRLVEKKTRKVWAGKFFKAYSAKEKE--NIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEIV 341
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKAKHRDTGKIVAIKKIKKEKIKKKKdkNILREIKILKKLNHPNIVRLYDAFEDKDNLYLVLEYV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 342 SGGELFERIIdEDFELTERECIKYMRQISEGveyihkqgivhldlkpenimcvnktgtriklidfglarrLENAGSLKVL 421
Cdd:pfam00069  81 EGGSLFDLLS-EKGAFSEREAKFIMKQILEG---------------------------------------LESGSSLTTF 120
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 422 FGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDFDDEaFDEISDDAKDFISNLLK 501
Cdd:pfam00069 121 VGTPWYMAPEVLGGNPYGPKVDVWSLGCILYELLTGKPPFPGINGNEIYELIIDQPYAFPEL-PSNLSEEAKDLLKKLLK 199
                         250
                  ....*....|....*...
gi 1034633499 502 KDMKNRLDCTQCLQHPWL 519
Cdd:pfam00069 200 KDPSKRLTATQALQHPWF 217
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
260-519 1.63e-72

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: 236.08  E-value: 1.63e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 260 VSDFYDIEERLGSGKFGQVFRLVEKKTRKVWAGKFFKAYSAKEKEN-IRQEISIMNCLHHPKLVQCVDAFEEKANIVMVL 338
Cdd:cd14167     1 IRDIYDFREVLGTGAFSEVVLAEEKRTQKLVAIKCIAKKALEGKETsIENEIAVLHKIKHPNIVALDDIYESGGHLYLIM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 339 EIVSGGELFERIIDEDFeLTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVN-KTGTRIKLIDFGLARrLENAGS 417
Cdd:cd14167    81 QLVSGGELFDRIVEKGF-YTERDASKLIFQILDAVKYLHDMGIVHRDLKPENLLYYSlDEDSKIMISDFGLSK-IEGSGS 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 418 -LKVLFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDFDDEAFDEISDDAKDFI 496
Cdd:cd14167   159 vMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDAKLFEQILKAEYEFDSPYWDDISDSAKDFI 238
                         250       260
                  ....*....|....*....|...
gi 1034633499 497 SNLLKKDMKNRLDCTQCLQHPWL 519
Cdd:cd14167   239 QHLMEKDPEKRFTCEQALQHPWI 261
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
264-518 3.13e-72

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: 235.10  E-value: 3.13e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 264 YDIEERLGSGKFGQVFRLVEKKTRKVWAGKFFKAYSAKEK--ENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEIV 341
Cdd:cd14003     2 YELGKTLGEGSFGKVKLARHKLTGEKVAIKIIDKSKLKEEieEKIKREIEIMKLLNHPNIIKLYEVIETENKIYLVMEYA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 342 SGGELFERIIDEDfELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGtRIKLIDFGLARRLENAGSLKVL 421
Cdd:cd14003    82 SGGELFDYIVNNG-RLSEDEARRFFQQLISAVDYCHSNGIVHRDLKLENIL-LDKNG-NLKIIDFGLSNEFRGGSLLKTF 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 422 FGTPEFVAPEVINYEP-IGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATwdFDDEAFdeISDDAKDFISNLL 500
Cdd:cd14003   159 CGTPAYAAPEVLLGRKyDGPKADVWSLGVILYAMLTGYLPFDDDNDSKLFRKILKGK--YPIPSH--LSPDARDLIRRML 234
                         250
                  ....*....|....*...
gi 1034633499 501 KKDMKNRLDCTQCLQHPW 518
Cdd:cd14003   235 VVDPSKRITIEEILNHPW 252
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
262-519 1.22e-70

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: 230.82  E-value: 1.22e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 262 DFyDIEERLGSGKFGQVFRLVEKKTRKVWAGK-FFKA--YSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVL 338
Cdd:cd14007     1 DF-EIGKPLGKGKFGNVYLAREKKSGFIVALKvISKSqlQKSGLEHQLRREIEIQSHLRHPNILRLYGYFEDKKRIYLIL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 339 EIVSGGELFeRIIDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGtRIKLIDFGLARRLENAGsL 418
Cdd:cd14007    80 EYAPNGELY-KELKKQKRFDEKEAAKYIYQLALALDYLHSKNIIHRDIKPENIL-LGSNG-ELKLADFGWSVHAPSNR-R 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 419 KVLFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDFDdeafDEISDDAKDFISN 498
Cdd:cd14007   156 KTFCGTLDYLPPEMVEGKEYDYKVDIWSLGVLCYELLVGKPPFESKSHQETYKRIQNVDIKFP----SSVSPEAKDLISK 231
                         250       260
                  ....*....|....*....|.
gi 1034633499 499 LLKKDMKNRLDCTQCLQHPWL 519
Cdd:cd14007   232 LLQKDPSKRLSLEQVLNHPWI 252
PK_Unc-89_rpt1 cd14109
Pseudokinase domain, first repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein ...
260-519 2.88e-69

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: 227.39  E-value: 2.88e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 260 VSDFYDI-EERLGSGKFGQVFRLVEKKTrkvwaGKFFKAYSAKEKENIRQEISIMNCLHHPKLVQCVDAFE-EKANIVMV 337
Cdd:cd14109     1 VRELYEIgEEDEKRAAQGAPFHVTERST-----GRNFLAQLRYGDPFLMREVDIHNSLDHPNIVQMHDAYDdEKLAVTVI 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 338 LEIVSGGELFERIIDEDFEL-TERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKtgtRIKLIDFGLARRLENAG 416
Cdd:cd14109    76 DNLASTIELVRDNLLPGKDYyTERQVAVFVRQLLLALKHMHDLGIAHLDLRPEDILLQDD---KLKLADFGQSRRLLRGK 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 417 SLKVLFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDFDDEAFDEISDDAKDFI 496
Cdd:cd14109   153 LTTLIYGSPEFVSPEIVNSYPVTLATDMWSVGVLTYVLLGGISPFLGDNDRETLTNVRSGKWSFDSSPLGNISDDARDFI 232
                         250       260
                  ....*....|....*....|...
gi 1034633499 497 SNLLKKDMKNRLDCTQCLQHPWL 519
Cdd:cd14109   233 KKLLVYIPESRLTVDEALNHPWF 255
STKc_DRAK1 cd14197
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
258-519 4.89e-69

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: 227.13  E-value: 4.89e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 258 QKVSDFYDIE--ERLGSGKFGQVFRLVEKKTRKVWAGKFFKAYSAKE--KENIRQEISIMNCLH-HPKLVQCVDAFEEKA 332
Cdd:cd14197     3 EPFQERYSLSpgRELGRGKFAVVRKCVEKDSGKEFAAKFMRKRRKGQdcRMEIIHEIAVLELAQaNPWVINLHEVYETAS 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 333 NIVMVLEIVSGGELFERII-DEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKTGT-RIKLIDFGLAR 410
Cdd:cd14197    83 EMILVLEYAAGGEIFNQCVaDREEAFKEKDVKRLMKQILEGVSFLHNNNVVHLDLKPQNILLTSESPLgDIKIVDFGLSR 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 411 RLENAGSLKVLFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDFDDEAFDEISD 490
Cdd:cd14197   163 ILKNSEELREIMGTPEYVAPEILSYEPISTATDMWSIGVLAYVMLTGISPFLGDDKQETFLNISQMNVSYSEEEFEHLSE 242
                         250       260
                  ....*....|....*....|....*....
gi 1034633499 491 DAKDFISNLLKKDMKNRLDCTQCLQHPWL 519
Cdd:cd14197   243 SAIDFIKTLLIKKPENRATAEDCLKHPWL 271
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
260-523 5.37e-67

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: 222.18  E-value: 5.37e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 260 VSDFYDIEERLGSGKFGQVFRLVEKKTRKVWAGKFFKAYSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLE 339
Cdd:cd14166     1 IRETFIFMEVLGSGAFSEVYLVKQRSTGKLYALKCIKKSPLSRDSSLENEIAVLKRIKHENIVTLEDIYESTTHYYLVMQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 340 IVSGGELFERIIDEDFeLTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVN-KTGTRIKLIDFGLARrLENAGSL 418
Cdd:cd14166    81 LVSGGELFDRILERGV-YTEKDASRVINQVLSAVKYLHENGIVHRDLKPENLLYLTpDENSKIMITDFGLSK-MEQNGIM 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 419 KVLFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDFDDEAFDEISDDAKDFISN 498
Cdd:cd14166   159 STACGTPGYVAPEVLAQKPYSKAVDCWSIGVITYILLCGYPPFYEETESRLFEKIKEGYYEFESPFWDDISESAKDFIRH 238
                         250       260
                  ....*....|....*....|....*
gi 1034633499 499 LLKKDMKNRLDCTQCLQHPWLMKDT 523
Cdd:cd14166   239 LLEKNPSKRYTCEKALSHPWIIGNT 263
STKc_CaMKIV cd14085
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
260-554 6.69e-66

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: 219.70  E-value: 6.69e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 260 VSDFYDIEERLGSGKFGQVFRLVEKKTRKVWAGKFFKaySAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLE 339
Cdd:cd14085     1 LEDFFEIESELGRGATSVVYRCRQKGTQKPYAVKKLK--KTVDKKIVRTEIGVLLRLSHPNIIKLKEIFETPTEISLVLE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 340 IVSGGELFERIIDEDFeLTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVN-KTGTRIKLIDFGLARRLENAGSL 418
Cdd:cd14085    79 LVTGGELFDRIVEKGY-YSERDAADAVKQILEAVAYLHENGIVHRDLKPENLLYATpAPDAPLKIADFGLSKIVDQQVTM 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 419 KVLFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDN-DNETLANVTSATWDFDDEAFDEISDDAKDFIS 497
Cdd:cd14085   158 KTVCGTPGYCAPEILRGCAYGPEVDMWSVGVITYILLCGFEPFYDERgDQYMFKRILNCDYDFVSPWWDDVSLNAKDLVK 237
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1034633499 498 NLLKKDMKNRLDCTQCLQHPWLMKDTKNMEAKKLSKDRMKKYMARRKWQKTGNAVRA 554
Cdd:cd14085   238 KLIVLDPKKRLTTQQALQHPWVTGKAANFAHMDTAQKKLQEFNARRKLKAAVKAVVA 294
IgI_8_hMLCK_like cd05762
Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar ...
37-135 2.28e-64

Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar protein; member of the I-set of IgSF domains; The members here are composed of the eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar proteins. Myosin light-chain kinase (MLCK) is a key regulator of different forms of cell motility involving actin and myosin II. Agonist stimulation of smooth muscle cells increases cytosolic Ca2+ which binds calmodulin. This Ca2+-calmodulin complex in turn binds to and activates MLCK. Activated MLCK leads to the phosphorylation of the 20 kDa myosin regulatory light chain (RLC) of myosin II and the stimulation of actin-activated myosin MgATPase activity. MLCK is widely present in vertebrate tissues; it phosphorylates the 20 kDa RLC of both smooth and nonmuscle myosin II. Phosphorylation leads to the activation of the myosin motor domain and altered structural properties of myosin II. In smooth muscle MLCK it is involved in initiating contraction. In nonmuscle cells, MLCK may participate in cell division and cell motility; it has been suggested MLCK plays a role in cardiomyocyte differentiation and contraction through regulation of nonmuscle myosin II.


Pssm-ID: 409419  Cd Length: 99  Bit Score: 208.27  E-value: 2.28e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499  37 PPQIIQFPEDQKVRAGESVELFGKVTGTQPITCTWMKFRKQIQESEHMKVENSENGSKLTILAARQEHCGCYTLLVENKL 116
Cdd:cd05762     1 PPQIIQFPEDMKVRAGESVELFCKVTGTQPITCTWMKFRKQIQEGEGIKIENTENSSKLTITEGQQEHCGCYTLEVENKL 80
                          90
                  ....*....|....*....
gi 1034633499 117 GSRQAQVNLTVVDKPDPPA 135
Cdd:cd05762    81 GSRQAQVNLTVVDKPDPPA 99
STKc_CaMKI_beta cd14169
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
260-523 3.21e-64

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


Pssm-ID: 271071 [Multi-domain]  Cd Length: 277  Bit Score: 214.75  E-value: 3.21e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 260 VSDFYDIEERLGSGKFGQVFRLVEKKTRKVWAGKFFKAYSAKEKEN-IRQEISIMNCLHHPKLVQCVDAFEEKANIVMVL 338
Cdd:cd14169     1 INSVYELKEKLGEGAFSEVVLAQERGSQRLVALKCIPKKALRGKEAmVENEIAVLRRINHENIVSLEDIYESPTHLYLAM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 339 EIVSGGELFERIIDEDFeLTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNK-TGTRIKLIDFGLARrLENAGS 417
Cdd:cd14169    81 ELVTGGELFDRIIERGS-YTEKDASQLIGQVLQAVKYLHQLGIVHRDLKPENLLYATPfEDSKIMISDFGLSK-IEAQGM 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 418 LKVLFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDFDDEAFDEISDDAKDFIS 497
Cdd:cd14169   159 LSTACGTPGYVAPELLEQKPYGKAVDVWAIGVISYILLCGYPPFYDENDSELFNQILKAEYEFDSPYWDDISESAKDFIR 238
                         250       260
                  ....*....|....*....|....*.
gi 1034633499 498 NLLKKDMKNRLDCTQCLQHPWLMKDT 523
Cdd:cd14169   239 HLLERDPEKRFTCEQALQHPWISGDT 264
STKc_SPEG_rpt1 cd14108
Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle ...
261-519 3.51e-64

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


Pssm-ID: 271010 [Multi-domain]  Cd Length: 255  Bit Score: 213.61  E-value: 3.51e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 261 SDFYDIEERLGSGKFGQVFRLVEKKTRKVWAGKFFKAySAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEI 340
Cdd:cd14108     1 TDYYDIHKEIGRGAFSYLRRVKEKSSDLSFAAKFIPV-RAKKKTSARRELALLAELDHKSIVRFHDAFEKRRVVIIVTEL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 341 VSGgELFERIIDEDfELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKTGTRIKLIDFGLARRLENAGSLKV 420
Cdd:cd14108    80 CHE-ELLERITKRP-TVCESEVRSYMRQLLEGIEYLHQNDVLHLDLKPENLLMADQKTDQVRICDFGNAQELTPNEPQYC 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 421 LFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDFDDEAFDEISDDAKDFISNLL 500
Cdd:cd14108   158 KYGTPEFVAPEIVNQSPVSKVTDIWPVGVIAYLCLTGISPFVGENDRTTLMNIRNYNVAFEESMFKDLCREAKGFIIKVL 237
                         250
                  ....*....|....*....
gi 1034633499 501 KKDmKNRLDCTQCLQHPWL 519
Cdd:cd14108   238 VSD-RLRPDAEETLEHPWF 255
STKc_obscurin_rpt1 cd14107
Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
263-519 1.66e-63

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


Pssm-ID: 271009 [Multi-domain]  Cd Length: 257  Bit Score: 212.06  E-value: 1.66e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 263 FYDIEERLGSGKFGQVFRLVEKKTRKVWAGKFFKAYSaKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEIVS 342
Cdd:cd14107     3 VYEVKEEIGRGTFGFVKRVTHKGNGECCAAKFIPLRS-STRARAFQERDILARLSHRRLTCLLDQFETRKTLILILELCS 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 343 GGELFERIIDEDFeLTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKTGTRIKLIDFGLARRLENAGSLKVLF 422
Cdd:cd14107    82 SEELLDRLFLKGV-VTEAEVKLYIQQVLEGIGYLHGMNILHLDIKPDNILMVSPTREDIKICDFGFAQEITPSEHQFSKY 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 423 GTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDFDDEAFDEISDDAKDFISNLLKK 502
Cdd:cd14107   161 GSPEFVAPEIVHQEPVSAATDIWALGVIAYLSLTCHSPFAGENDRATLLNVAEGVVSWDTPEITHLSEDAKDFIKRVLQP 240
                         250
                  ....*....|....*..
gi 1034633499 503 DMKNRLDCTQCLQHPWL 519
Cdd:cd14107   241 DPEKRPSASECLSHEWF 257
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
262-544 3.25e-63

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: 212.28  E-value: 3.25e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 262 DFYDIEERLGSGKFGQVFRLVEKKTRKVWAGKFF--KAYSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLE 339
Cdd:cd14086     1 DEYDLKEELGKGAFSVVRRCVQKSTGQEFAAKIIntKKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGFHYLVFD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 340 IVSGGELFERIIDEDFeLTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKT-GTRIKLIDFGLArrLENAGSL 418
Cdd:cd14086    81 LVTGGELFEDIVAREF-YSEADASHCIQQILESVNHCHQNGIVHRDLKPENLLLASKSkGAAVKLADFGLA--IEVQGDQ 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 419 KVLFG---TPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDFDDEAFDEISDDAKDF 495
Cdd:cd14086   158 QAWFGfagTPGYLSPEVLRKDPYGKPVDIWACGVILYILLVGYPPFWDEDQHRLYAQIKAGAYDYPSPEWDTVTPEAKDL 237
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1034633499 496 ISNLLKKDMKNRLDCTQCLQHPWLMKDTK--NMEAKKLSKDRMKKYMARRK 544
Cdd:cd14086   238 INQMLTVNPAKRITAAEALKHPWICQRDRvaSMVHRQETVDCLKKFNARRK 288
STKc_CaMKI_delta cd14168
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
258-551 4.47e-63

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


Pssm-ID: 271070 [Multi-domain]  Cd Length: 301  Bit Score: 212.60  E-value: 4.47e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 258 QKVSDFYDIEERLGSGKFGQVFRLVEKKTRKVWAGKFFKAYSAKEKEN-IRQEISIMNCLHHPKLVQCVDAFEEKANIVM 336
Cdd:cd14168     6 EDIKKIFEFKEVLGTGAFSEVVLAEERATGKLFAVKCIPKKALKGKESsIENEIAVLRKIKHENIVALEDIYESPNHLYL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 337 VLEIVSGGELFERIIDEDFeLTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVN-KTGTRIKLIDFGLARRLENA 415
Cdd:cd14168    86 VMQLVSGGELFDRIVEKGF-YTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYFSqDEESKIMISDFGLSKMEGKG 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 416 GSLKVLFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDFDDEAFDEISDDAKDF 495
Cdd:cd14168   165 DVMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKADYEFDSPYWDDISDSAKDF 244
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1034633499 496 ISNLLKKDMKNRLDCTQCLQHPWLMKDTK-NMEAKKLSKDRMKKYMARRKWQKTGNA 551
Cdd:cd14168   245 IRNLMEKDPNKRYTCEQALRHPWIAGDTAlCKNIHESVSAQIRKNFAKSKWRQAFNA 301
STKc_Kalirin_C cd14115
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
270-518 2.89e-61

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


Pssm-ID: 271017 [Multi-domain]  Cd Length: 248  Bit Score: 205.58  E-value: 2.89e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 270 LGSGKFGQVFRLVEKKTRKVWAGKFFkAYSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEIVSGGELFER 349
Cdd:cd14115     1 IGRGRFSIVKKCLHKATRKDVAVKFV-SKKMKKKEQAAHEAALLQHLQHPQYITLHDTYESPTSYILVLELMDDGRLLDY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 350 IIDEDfELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMC-VNKTGTRIKLIDFGLARRLENAGSLKVLFGTPEFV 428
Cdd:cd14115    80 LMNHD-ELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIdLRIPVPRVKLIDLEDAVQISGHRHVHHLLGNPEFA 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 429 APEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDFDDEAFDEISDDAKDFISNLLKKDMKNRL 508
Cdd:cd14115   159 APEVIQGTPVSLATDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSFPDEYFGDVSQAARDFINVILQEDPRRRP 238
                         250
                  ....*....|
gi 1034633499 509 DCTQCLQHPW 518
Cdd:cd14115   239 TAATCLQHPW 248
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
258-519 5.02e-61

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: 206.09  E-value: 5.02e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 258 QKVSDFYDIEERLGSGKFGQVFRLVEKKTRKVWAGK-----FFKAYSAKEKE---NIRQEISIMNCLHHPKLVQCVDAFE 329
Cdd:cd14084     2 KELRKKYIMSRTLGSGACGEVKLAYDKSTCKKVAIKiinkrKFTIGSRREINkprNIETEIEILKKLSHPCIIKIEDFFD 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 330 EKANIVMVLEIVSGGELFERIIDeDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKTG-TRIKLIDFGL 408
Cdd:cd14084    82 AEDDYYIVLELMEGGELFDRVVS-NKRLKEAICKLYFYQMLLAVKYLHSNGIIHRDLKPENVLLSSQEEeCLIKITDFGL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 409 ARRLENAGSLKVLFGTPEFVAPEVINY---EPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLAN-VTSATWDFDDEA 484
Cdd:cd14084   161 SKILGETSLMKTLCGTPTYLAPEVLRSfgtEGYTRAVDCWSLGVILFICLSGYPPFSEEYTQMSLKEqILSGKYTFIPKA 240
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1034633499 485 FDEISDDAKDFISNLLKKDMKNRLDCTQCLQHPWL 519
Cdd:cd14084   241 WKNVSEEAKDLVKKMLVVDPSRRPSIEEALEHPWL 275
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
264-518 9.09e-61

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: 204.48  E-value: 9.09e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 264 YDIEERLGSGKFGQVFRLVEKKTRKVWAGKFFKAYSAKEKEN-IRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEIVS 342
Cdd:cd14095     2 YDIGRVIGDGNFAVVKECRDKATDKEYALKIIDKAKCKGKEHmIENEVAILRRVKHPNIVQLIEEYDTDTELYLVMELVK 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 343 GGELFERIIdEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIM-CVNKTGTR-IKLIDFGLARRLEnagslKV 420
Cdd:cd14095    82 GGDLFDAIT-SSTKFTERDASRMVTDLAQALKYLHSLSIVHRDIKPENLLvVEHEDGSKsLKLADFGLATEVK-----EP 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 421 LF---GTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMG-DNDNETLAN-VTSATWDFDDEAFDEISDDAKDF 495
Cdd:cd14095   156 LFtvcGTPTYVAPEILAETGYGLKVDIWAAGVITYILLCGFPPFRSpDRDQEELFDlILAGEFEFLSPYWDNISDSAKDL 235
                         250       260
                  ....*....|....*....|...
gi 1034633499 496 ISNLLKKDMKNRLDCTQCLQHPW 518
Cdd:cd14095   236 ISRMLVVDPEKRYSAGQVLDHPW 258
STKc_Trio_C cd14113
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
263-519 2.60e-60

C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide Exchange Factor, Triple functional domain protein; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Triple functional domain protein (Trio), also called PTPRF-interacting protein, is a large multidomain protein containing a series of spectrin-like repeats, two each of RhoGEF and SH3 domains, an immunoglobulin-like (Ig) domain and a C-terminal kinase. Trio plays important roles in neuronal cell migration and axon guidance. It was originally identified as an interacting partner of the of the receptor-like tyrosine phosphatase (RPTP) LAR (leukocyte-antigen-related protein), a family of receptors that function in the signaling to the actin cytoskeleton during development. Trio functions as a GEF for Rac1, RhoG, and RhoA, and is involved in the regulation of lamellipodia formation, mediating Rac1-dependent cell spreading and migration. The Trio subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271015 [Multi-domain]  Cd Length: 263  Bit Score: 203.67  E-value: 2.60e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 263 FYDIEERLGSGKFGQVFRLVEKKTRKVWAGKFFKAYSAKeKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEIVS 342
Cdd:cd14113     8 FYSEVAELGRGRFSVVKKCDQRGTKRAVATKFVNKKLMK-RDQVTHELGVLQSLQHPQLVGLLDTFETPTSYILVLEMAD 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 343 GGELFERIIDEDfELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGTR--IKLIDFGLARRLENAGSLKV 420
Cdd:cd14113    87 QGRLLDYVVRWG-NLTEEKIRFYLREILEALQYLHNCRIAHLDLKPENIL-VDQSLSKptIKLADFGDAVQLNTTYYIHQ 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 421 LFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDFDDEAFDEISDDAKDFISNLL 500
Cdd:cd14113   165 LLGSPEFAAPEIILGNPVSLTSDLWSIGVLTYVLLSGVSPFLDESVEETCLNICRLDFSFPDDYFKGVSQKAKDFVCFLL 244
                         250
                  ....*....|....*....
gi 1034633499 501 KKDMKNRLDCTQCLQHPWL 519
Cdd:cd14113   245 QMDPAKRPSAALCLQEQWL 263
STKc_RSK_C cd14091
C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs ...
264-520 3.30e-58

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: 199.01  E-value: 3.30e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 264 YDIEERLGSGKFGQVFRLVEKKTRKVWAGKFFKaysaKEKENIRQEISIMncL---HHPKLVQCVDAFEEKANIVMVLEI 340
Cdd:cd14091     2 YEIKEEIGKGSYSVCKRCIHKATGKEYAVKIID----KSKRDPSEEIEIL--LrygQHPNIITLRDVYDDGNSVYLVTEL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 341 VSGGELFERIIDEDFeLTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKTGT--RIKLIDFGLARRL--ENAg 416
Cdd:cd14091    76 LRGGELLDRILRQKF-FSEREASAVMKTLTKTVEYLHSQGVVHRDLKPSNILYADESGDpeSLRICDFGFAKQLraENG- 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 417 slkvLFGTP----EFVAPEVINYEpiGY--ATDMWSIGVICYILVSGLSPF-MGDND--NETLANVTSATWDFDDEAFDE 487
Cdd:cd14091   154 ----LLMTPcytaNFVAPEVLKKQ--GYdaACDIWSLGVLLYTMLAGYTPFaSGPNDtpEVILARIGSGKIDLSGGNWDH 227
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1034633499 488 ISDDAKDFISNLLKKDMKNRLDCTQCLQHPWLM 520
Cdd:cd14091   228 VSDSAKDLVRKMLHVDPSQRPTAAQVLQHPWIR 260
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
264-519 3.82e-58

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: 197.96  E-value: 3.82e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 264 YDIEERLGSGKFGQVFRLVEKKTRKVWAGKF-------FKAYSAKE-KENIRQEISIMN-CLHHPKLVQCVDAFEEKANI 334
Cdd:cd14093     5 YEPKEILGRGVSSTVRRCIEKETGQEFAVKIiditgekSSENEAEElREATRREIEILRqVSGHPNIIELHDVFESPTFI 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 335 VMVLEIVSGGELFErIIDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKtgTRIKLIDFGLARRLEN 414
Cdd:cd14093    85 FLVFELCRKGELFD-YLTEVVTLSEKKTRRIMRQLFEAVEFLHSLNIVHRDLKPENILLDDN--LNVKISDFGFATRLDE 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 415 AGSLKVLFGTPEFVAPEVI------NYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDFDDEAFDEI 488
Cdd:cd14093   162 GEKLRELCGTPGYLAPEVLkcsmydNAPGYGKEVDMWACGVIMYTLLAGCPPFWHRKQMVMLRNIMEGKYEFGSPEWDDI 241
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1034633499 489 SDDAKDFISNLLKKDMKNRLDCTQCLQHPWL 519
Cdd:cd14093   242 SDTAKDLISKLLVVDPKKRLTAEEALEHPFF 272
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
270-518 3.95e-57

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: 194.66  E-value: 3.95e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 270 LGSGKFGQVFRLVEKKTRKVWAGK---FFKAYSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEIVSGGEL 346
Cdd:cd05123     1 LGKGSFGKVLLVRKKDTGKLYAMKvlrKKEIIKRKEVEHTLNERNILERVNHPFIVKLHYAFQTEEKLYLVLDYVPGGEL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 347 F-----ERIIDEdfelterECIK-YMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGtRIKLIDFGLARRLENAGSLKV 420
Cdd:cd05123    81 FshlskEGRFPE-------ERARfYAAEIVLALEYLHSLGIIYRDLKPENIL-LDSDG-HIKLTDFGLAKELSSDGDRTY 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 421 LF-GTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDFDdeafDEISDDAKDFISNL 499
Cdd:cd05123   152 TFcGTPEYLAPEVLLGKGYGKAVDWWSLGVLLYEMLTGKPPFYAENRKEIYEKILKSPLKFP----EYVSPEAKSLISGL 227
                         250       260
                  ....*....|....*....|..
gi 1034633499 500 LKKDMKNRLDCT---QCLQHPW 518
Cdd:cd05123   228 LQKDPTKRLGSGgaeEIKAHPF 249
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
264-518 1.69e-56

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: 193.46  E-value: 1.69e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 264 YDIEERLGSGKFGQVFRLVEKKTRKVWAGKFFK----AYSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLE 339
Cdd:cd14098     2 YQIIDRLGSGTFAEVKKAVEVETGKMRAIKQIVkrkvAGNDKNLQLFQREINILKSLEHPGIVRLIDWYEDDQHIYLVME 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 340 IVSGGELFERIIDEDfELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKTGTRIKLIDFGLARRLENAGSLK 419
Cdd:cd14098    82 YVEGGDLMDFIMAWG-AIPEQHARELTKQILEAMAYTHSMGITHRDLKPENILITQDDPVIVKISDFGLAKVIHTGTFLV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 420 VLFGTPEFVAPEVI----NYEPIGYAT--DMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDFDDEAFDEISDDAK 493
Cdd:cd14098   161 TFCGTMAYLAPEILmskeQNLQGGYSNlvDMWSVGCLVYVMLTGALPFDGSSQLPVEKRIRKGRYTQPPLVDFNISEEAI 240
                         250       260
                  ....*....|....*....|....*
gi 1034633499 494 DFISNLLKKDMKNRLDCTQCLQHPW 518
Cdd:cd14098   241 DFILRLLDVDPEKRMTAAQALDHPW 265
STKc_PSKH1 cd14087
Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the ...
264-519 2.07e-56

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: 193.13  E-value: 2.07e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 264 YDIEERLGSGKFGQVFRLVEKKTRKVWAGKFFKAySAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEIVSG 343
Cdd:cd14087     3 YDIKALIGRGSFSRVVRVEHRVTRQPYAIKMIET-KCRGREVCESELNVLRRVRHTNIIQLIEVFETKERVYMVMELATG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 344 GELFERIIDEDfELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVN-KTGTRIKLIDFGLA--RRLENAGSLKV 420
Cdd:cd14087    82 GELFDRIIAKG-SFTERDATRVLQMVLDGVKYLHGLGITHRDLKPENLLYYHpGPDSKIMITDFGLAstRKKGPNCLMKT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 421 LFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDFDDEAFDEISDDAKDFISNLL 500
Cdd:cd14087   161 TCGTPEYIAPEILLRKPYTQSVDMWAVGVIAYILLSGTMPFDDDNRTRLYRQILRAKYSYSGEPWPSVSNLAKDFIDRLL 240
                         250
                  ....*....|....*....
gi 1034633499 501 KKDMKNRLDCTQCLQHPWL 519
Cdd:cd14087   241 TVNPGERLSATQALKHPWI 259
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
270-517 3.00e-56

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: 190.94  E-value: 3.00e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 270 LGSGKFGQVFRLVEKKTRKVWAGKFF-KAYSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEIVSGGELFE 348
Cdd:cd00180     1 LGKGSFGKVYKARDKETGKKVAVKVIpKEKLKKLLEELLREIEILKKLNHPNIVKLYDVFETENFLYLVMEYCEGGSLKD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 349 RIIDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGTrIKLIDFGLARRLENAGSLKVLFGTPEFV 428
Cdd:cd00180    81 LLKENKGPLSEEEALSILRQLLSALEYLHSNGIIHRDLKPENIL-LDSDGT-VKLADFGLAKDLDSDDSLLKTTGGTTPP 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 429 ---APEVINYEPIGYATDMWSIGVICYILvsglspfmgdndnetlanvtsatwdfddeafdeisDDAKDFISNLLKKDMK 505
Cdd:cd00180   159 yyaPPELLGGRYYGPKVDIWSLGVILYEL-----------------------------------EELKDLIRRMLQYDPK 203
                         250
                  ....*....|..
gi 1034633499 506 NRLDCTQCLQHP 517
Cdd:cd00180   204 KRPSAKELLEHL 215
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
264-519 7.27e-56

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: 191.23  E-value: 7.27e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 264 YDIEERLGSGKFGQVFRLVEKKTRKVWAGKFFK---AYSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEI 340
Cdd:cd14099     3 YRRGKFLGKGGFAKCYEVTDMSTGKVYAGKVVPkssLTKPKQREKLKSEIKIHRSLKHPNIVKFHDCFEDEENVYILLEL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 341 VSGGELFErIIDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGtRIKLIDFGLARRLENAGSLKV 420
Cdd:cd14099    83 CSNGSLME-LLKRRKALTEPEVRYFMRQILSGVKYLHSNRIIHRDLKLGNLF-LDENM-NVKIGDFGLAARLEYDGERKK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 421 -LFGTPEFVAPEVIN-YEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDFDDEafDEISDDAKDFISN 498
Cdd:cd14099   160 tLCGTPNYIAPEVLEkKKGHSFEVDIWSLGVILYTLLVGKPPFETSDVKETYKRIKKNEYSFPSH--LSISDEAKDLIRS 237
                         250       260
                  ....*....|....*....|.
gi 1034633499 499 LLKKDMKNRLDCTQCLQHPWL 519
Cdd:cd14099   238 MLQPDPTKRPSLDEILSHPFF 258
STKc_MSK_C cd14092
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
264-524 9.00e-56

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


Pssm-ID: 270994 [Multi-domain]  Cd Length: 311  Bit Score: 192.90  E-value: 9.00e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 264 YDI---EERLGSGKFGQVFRLVEKKTRKVWAGKFfkaysAKEKENIRQEISIMN-CLHHPKLVQCVDAFEEKANIVMVLE 339
Cdd:cd14092     5 YELdlrEEALGDGSFSVCRKCVHKKTGQEFAVKI-----VSRRLDTSREVQLLRlCQGHPNIVKLHEVFQDELHTYLVME 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 340 IVSGGELFERIIDEDfELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKT-GTRIKLIDFGLARRLENAGSL 418
Cdd:cd14092    80 LLRGGELLERIRKKK-RFTESEASRIMRQLVSAVSFMHSKGVVHRDLKPENLLFTDEDdDAEIKIVDFGFARLKPENQPL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 419 KvlfgTPEFV----APEVIN--YEPIGY--ATDMWSIGVICYILVSGLSPFMGDNDNETLANV----TSATWDFDDEAFD 486
Cdd:cd14092   159 K----TPCFTlpyaAPEVLKqaLSTQGYdeSCDLWSLGVILYTMLSGQVPFQSPSRNESAAEImkriKSGDFSFDGEEWK 234
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1034633499 487 EISDDAKDFISNLLKKDMKNRLDCTQCLQHPWLMKDTK 524
Cdd:cd14092   235 NVSSEAKSLIQGLLTVDPSKRLTMSELRNHPWLQGSSS 272
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
270-519 1.38e-55

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: 190.84  E-value: 1.38e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 270 LGSGKFGQVFRLVEKKTRKVWAGKFFK----------AYSAKEKEN----IRQEISIMNCLHHPKLVQCV----DAFEEK 331
Cdd:cd14008     1 LGRGSFGKVKLALDTETGQLYAIKIFNksrlrkrregKNDRGKIKNalddVRREIAIMKKLDHPNIVRLYevidDPESDK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 332 anIVMVLEIVSGGELFERIIDEDFE-LTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGTrIKLIDFGLAR 410
Cdd:cd14008    81 --LYLVLEYCEGGPVMELDSGDRVPpLPEETARKYFRDLVLGLEYLHENGIVHRDIKPENLL-LTADGT-VKISDFGVSE 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 411 RLEN-AGSLKVLFGTPEFVAPEVINYEP---IGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDFDDEafD 486
Cdd:cd14008   157 MFEDgNDTLQKTAGTPAFLAPELCDGDSktySGKAADIWALGVTLYCLVFGRLPFNGDNILELYEAIQNQNDEFPIP--P 234
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1034633499 487 EISDDAKDFISNLLKKDMKNRLDCTQCLQHPWL 519
Cdd:cd14008   235 ELSPELKDLLRRMLEKDPEKRITLKEIKEHPWV 267
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
264-519 3.74e-55

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: 189.34  E-value: 3.74e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 264 YDIEERLGSGKFGQVFRLVEKKTRKVWAGKFFKAYSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEIVSG 343
Cdd:cd05122     2 FEILEKIGKGGFGVVYKARHKKTGQIVAIKKINLESKEKKESILNEIAILKKCKHPNIVKYYGSYLKKDELWIVMEFCSG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 344 GELFERIIDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGtRIKLIDFGLARRLENAGSLKVLFG 423
Cdd:cd05122    82 GSLKDLLKNTNKTLTEQQIAYVCKEVLKGLEYLHSHGIIHRDIKAANIL-LTSDG-EVKLIDFGLSAQLSDGKTRNTFVG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 424 TPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMgdNDNETLANVTSATWDFddEAFDEI---SDDAKDFISNLL 500
Cdd:cd05122   160 TPYWMAPEVIQGKPYGFKADIWSLGITAIEMAEGKPPYS--ELPPMKALFLIATNGP--PGLRNPkkwSKEFKDFLKKCL 235
                         250
                  ....*....|....*....
gi 1034633499 501 KKDMKNRLDCTQCLQHPWL 519
Cdd:cd05122   236 QKDPEKRPTAEQLLKHPFI 254
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
264-507 4.57e-55

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: 189.33  E-value: 4.57e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 264 YDIEERLGSGKFGQVFRLVEKKTRKVWAGKFFK---AYSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEI 340
Cdd:cd14014     2 YRLVRLLGRGGMGEVYRARDTLLGRPVAIKVLRpelAEDEEFRERFLREARALARLSHPNIVRVYDVGEDDGRPYIVMEY 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 341 VSGGELFERIiDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGtRIKLIDFGLARRLENAGSL-- 418
Cdd:cd14014    82 VEGGSLADLL-RERGPLPPREALRILAQIADALAAAHRAGIVHRDIKPANIL-LTEDG-RVKLTDFGIARALGDSGLTqt 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 419 KVLFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDFDDEAFDEISDDAKDFISN 498
Cdd:cd14014   159 GSVLGTPAYMAPEQARGGPVDPRSDIYSLGVVLYELLTGRPPFDGDSPAAVLAKHLQEAPPPPSPLNPDVPPALDAIILR 238

                  ....*....
gi 1034633499 499 LLKKDMKNR 507
Cdd:cd14014   239 ALAKDPEER 247
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
264-518 1.53e-54

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: 188.58  E-value: 1.53e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 264 YDIEERLGSGKFGQVFRLVEKKTRKVWAGKFF-KAYSAKEK--ENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEI 340
Cdd:cd05581     3 FKFGKPLGEGSYSTVVLAKEKETGKEYAIKVLdKRHIIKEKkvKYVTIEKEVLSRLAHPGIVKLYYTFQDESKLYFVLEY 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 341 VSGGELFERI-----IDEDfeltereCIK-YMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGtRIKLIDFGLA----R 410
Cdd:cd05581    83 APNGDLLEYIrkygsLDEK-------CTRfYTAEIVLALEYLHSKGIIHRDLKPENIL-LDEDM-HIKITDFGTAkvlgP 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 411 RLENAGSLKVLF--------------GTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSA 476
Cdd:cd05581   154 DSSPESTKGDADsqiaynqaraasfvGTAEYVSPELLNEKPAGKSSDLWALGCIIYQMLTGKPPFRGSNEYLTFQKIVKL 233
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1034633499 477 TWDFDdeafDEISDDAKDFISNLLKKDMKNRL------DCTQCLQHPW 518
Cdd:cd05581   234 EYEFP----ENFPPDAKDLIQKLLVLDPSKRLgvnengGYDELKAHPF 277
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
268-519 4.18e-54

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: 186.57  E-value: 4.18e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 268 ERLGSGKFGQVFRLVEKKTRKVWAGK--FFKAYSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEIVSGGE 345
Cdd:cd06606     6 ELLGKGSFGSVYLALNLDTGELMAVKevELSGDSEEELEALEREIRILSSLKHPNIVRYLGTERTENTLNIFLEYVPGGS 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 346 LFERIidEDFE-LTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGtRIKLIDFGLARRLE---NAGSLKVL 421
Cdd:cd06606    86 LASLL--KKFGkLPEPVVRKYTRQILEGLEYLHSNGIVHRDIKGANIL-VDSDG-VVKLADFGCAKRLAeiaTGEGTKSL 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 422 FGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFmgdndnETLANVTSATW--DFDDEAfDEI----SDDAKDF 495
Cdd:cd06606   162 RGTPYWMAPEVIRGEGYGRAADIWSLGCTVIEMATGKPPW------SELGNPVAALFkiGSSGEP-PPIpehlSEEAKDF 234
                         250       260
                  ....*....|....*....|....
gi 1034633499 496 ISNLLKKDMKNRLDCTQCLQHPWL 519
Cdd:cd06606   235 LRKCLQRDPKKRPTADELLQHPFL 258
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
264-507 1.16e-51

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 186.76  E-value: 1.16e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 264 YDIEERLGSGKFGQVFRLVEKKTRKVWAGKFFK---AYSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEI 340
Cdd:COG0515     9 YRILRLLGRGGMGVVYLARDLRLGRPVALKVLRpelAADPEARERFRREARALARLNHPNIVRVYDVGEEDGRPYLVMEY 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 341 VSGGELfERIIDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGtRIKLIDFGLARRLENAGSLK- 419
Cdd:COG0515    89 VEGESL-ADLLRRRGPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANIL-LTPDG-RVKLIDFGIARALGGATLTQt 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 420 -VLFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDFDDEAFDEISDDAKDFISN 498
Cdd:COG0515   166 gTVVGTPGYMAPEQARGEPVDPRSDVYSLGVTLYELLTGRPPFDGDSPAELLRAHLREPPPPPSELRPDLPPALDAIVLR 245

                  ....*....
gi 1034633499 499 LLKKDMKNR 507
Cdd:COG0515   246 ALAKDPEER 254
STKc_CaMK_like cd14088
Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to ...
262-519 3.07e-51

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


Pssm-ID: 270990 [Multi-domain]  Cd Length: 265  Bit Score: 179.07  E-value: 3.07e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 262 DFYDIEERLGSGKFGQVFRLVEKKTRKVWA-GKFFKAYSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEI 340
Cdd:cd14088     1 DRYDLGQVIKTEEFCEIFRAKDKTTGKLYTcKKFLKRDGRKVRKAAKNEINILKMVKHPNILQLVDVFETRKEYFIFLEL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 341 VSGGELFERIIDEDFeLTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNK-TGTRIKLIDFGLARrLENaGSLK 419
Cdd:cd14088    81 ATGREVFDWILDQGY-YSERDTSNVIRQVLEAVAYLHSLKIVHRNLKLENLVYYNRlKNSKIVISDFHLAK-LEN-GLIK 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 420 VLFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLAN--------VTSATWDFDDEAFDEISDD 491
Cdd:cd14088   158 EPCGTPEYLAPEVVGRQRYGRPVDCWAIGVIMYILLSGNPPFYDEAEEDDYENhdknlfrkILAGDYEFDSPYWDDISQA 237
                         250       260
                  ....*....|....*....|....*...
gi 1034633499 492 AKDFISNLLKKDMKNRLDCTQCLQHPWL 519
Cdd:cd14088   238 AKDLVTRLMEVEQDQRITAEEAISHEWI 265
STKc_MAPKAPK cd14089
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated ...
268-518 9.72e-51

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


Pssm-ID: 270991 [Multi-domain]  Cd Length: 263  Bit Score: 177.48  E-value: 9.72e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 268 ERLGSGKFGQVFRLVEKKTRKVWAGKFFKaysakEKENIRQEISI-MNCLHHPKLVQCVDAFE----EKANIVMVLEIVS 342
Cdd:cd14089     7 QVLGLGINGKVLECFHKKTGEKFALKVLR-----DNPKARREVELhWRASGCPHIVRIIDVYEntyqGRKCLLVVMECME 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 343 GGELFERIIDE-DFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKTGTRI-KLIDFGLARRLENAGSLKV 420
Cdd:cd14089    82 GGELFSRIQERaDSAFTEREAAEIMRQIGSAVAHLHSMNIAHRDLKPENLLYSSKGPNAIlKLTDFGFAKETTTKKSLQT 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 421 LFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDnetLA-------NVTSATWDFDDEAFDEISDDAK 493
Cdd:cd14089   162 PCYTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGYPPFYSNHG---LAispgmkkRIRNGQYEFPNPEWSNVSEEAK 238
                         250       260
                  ....*....|....*....|....*
gi 1034633499 494 DFISNLLKKDMKNRLDCTQCLQHPW 518
Cdd:cd14089   239 DLIRGLLKTDPSERLTIEEVMNHPW 263
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
264-519 2.54e-50

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: 176.29  E-value: 2.54e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 264 YDIEERLGSGKFGQVFRLVEKKTRKVWAGKFF--KAYSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEIV 341
Cdd:cd14002     3 YHVLELIGEGSFGKVYKGRRKYTGQVVALKFIpkRGKSEKELRNLRQEIEILRKLNHPNIIEMLDSFETKKEFVVVTEYA 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 342 SgGELFErIIDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGtRIKLIDFGLARRL-ENAGSLKV 420
Cdd:cd14002    83 Q-GELFQ-ILEDDGTLPEEEVRSIAKQLVSALHYLHSNRIIHRDMKPQNIL-IGKGG-VVKLCDFGFARAMsCNTLVLTS 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 421 LFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSatwdfDDEAF-DEISDDAKDFISNL 499
Cdd:cd14002   159 IKGTPLYMAPELVQEQPYDHTADLWSLGCILYELFVGQPPFYTNSIYQLVQMIVK-----DPVKWpSNMSPEFKSFLQGL 233
                         250       260
                  ....*....|....*....|
gi 1034633499 500 LKKDMKNRLDCTQCLQHPWL 519
Cdd:cd14002   234 LNKDPSKRLSWPDLLEHPFV 253
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
612-699 7.00e-50

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


Pssm-ID: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 168.91  E-value: 7.00e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 612 SKTIRDLEVVEGSAARFDCKIEGYPDPEVVWFKDDQSIRESRHFQIDYDEDGNCSLIISDVCGDDDAKYTCKAVNSLGEA 691
Cdd:cd20973     1 IQTLRDKEVVEGSAARFDCKVEGYPDPEVKWMKDDNPIVESRRFQIDQDEDGLCSLIISDVCGDDSGKYTCKAVNSLGEA 80

                  ....*...
gi 1034633499 692 TCTAELIV 699
Cdd:cd20973    81 TCSAELTV 88
STKc_DCKL3 cd14185
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called ...
263-518 7.04e-50

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: 175.14  E-value: 7.04e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 263 FYDIEERLGSGKFGQVFRLVEKKTRKVWAGKFFKAYSAKEKEN-IRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEIV 341
Cdd:cd14185     1 HYEIGRTIGDGNFAVVKECRHWNENQEYAMKIIDKSKLKGKEDmIESEILIIKSLSHPNIVKLFEVYETEKEIYLILEYV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 342 SGGELFERIIdEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKT--GTRIKLIDFGLARRLenAGSLK 419
Cdd:cd14185    81 RGGDLFDAII-ESVKFTEHDAALMIIDLCEALVYIHSKHIVHRDLKPENLLVQHNPdkSTTLKLADFGLAKYV--TGPIF 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 420 VLFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMG-DNDNETLAN-VTSATWDFDDEAFDEISDDAKDFIS 497
Cdd:cd14185   158 TVCGTPTYVAPEILSEKGYGLEVDMWAAGVILYILLCGFPPFRSpERDQEELFQiIQLGHYEFLPPYWDNISEAAKDLIS 237
                         250       260
                  ....*....|....*....|.
gi 1034633499 498 NLLKKDMKNRLDCTQCLQHPW 518
Cdd:cd14185   238 RLLVVDPEKRYTAKQVLQHPW 258
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
264-517 1.13e-49

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: 174.57  E-value: 1.13e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 264 YDIEERLGSGKFGQVFRLVEKKTRKVWAGK--FFKAYSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEIV 341
Cdd:cd08215     2 YEKIRVIGKGSFGSAYLVRRKSDGKLYVLKeiDLSNMSEKEREEALNEVKLLSKLKHPNIVKYYESFEENGKLCIVMEYA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 342 SGGELFERIIDEDFE---LTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGtRIKLIDFGLARRLENAGSL 418
Cdd:cd08215    82 DGGDLAQKIKKQKKKgqpFPEEQILDWFVQICLALKYLHSRKILHRDLKTQNIF-LTKDG-VVKLGDFGISKVLESTTDL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 419 -KVLFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDFDDEAFdeiSDDAKDFIS 497
Cdd:cd08215   160 aKTVVGTPYYLSPELCENKPYNYKSDIWALGCVLYELCTLKHPFEANNLPALVYKIVKGQYPPIPSQY---SSELRDLVN 236
                         250       260
                  ....*....|....*....|
gi 1034633499 498 NLLKKDMKNRLDCTQCLQHP 517
Cdd:cd08215   237 SMLQKDPEKRPSANEILSSP 256
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
264-519 1.55e-49

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: 173.98  E-value: 1.55e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 264 YDIEERLGSGKFGQVFRLVEKKTRKVWAGKFF---KAYSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEI 340
Cdd:cd14081     3 YRLGKTLGKGQTGLVKLAKHCVTGQKVAIKIVnkeKLSKESVLMKVEREIAIMKLIEHPNVLKLYDVYENKKYLYLVLEY 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 341 VSGGELFERIIdEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCvnKTGTRIKLIDFGLArRLENAGS-LK 419
Cdd:cd14081    83 VSGGELFDYLV-KKGRLTEKEARKFFRQIISALDYCHSHSICHRDLKPENLLL--DEKNNIKIADFGMA-SLQPEGSlLE 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 420 VLFGTPEFVAPEVINYEPI-GYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDFDdeafDEISDDAKDFISN 498
Cdd:cd14081   159 TSCGSPHYACPEVIKGEKYdGRKADIWSCGVILYALLVGALPFDDDNLRQLLEKVKRGVFHIP----HFISPDAQDLLRR 234
                         250       260
                  ....*....|....*....|.
gi 1034633499 499 LLKKDMKNRLDCTQCLQHPWL 519
Cdd:cd14081   235 MLEVNPEKRITIEEIKKHPWF 255
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
270-518 1.56e-49

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: 173.95  E-value: 1.56e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 270 LGSGKFGQVFRLVEKKTRKVWAGKFF--KAYSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEIVSGGELf 347
Cdd:cd14009     1 IGRGSFATVWKGRHKQTGEVVAIKEIsrKKLNKKLQENLESEIAILKSIKHPNIVRLYDVQKTEDFIYLVLEYCAGGDL- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 348 ERIIDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCV-NKTGTRIKLIDFGLARRLENAGSLKVLFGTPE 426
Cdd:cd14009    80 SQYIRKRGRLPEAVARHFMQQLASGLKFLRSKNIIHRDLKPQNLLLStSGDDPVLKIADFGFARSLQPASMAETLCGSPL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 427 FVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDFDDEAFDEISDDAKDFISNLLKKDMKN 506
Cdd:cd14009   160 YMAPEILQFQKYDAKADLWSVGAILFEMLVGKPPFRGSNHVQLLRNIERSDAVIPFPIAAQLSPDCKDLLRRLLRRDPAE 239
                         250
                  ....*....|..
gi 1034633499 507 RLDCTQCLQHPW 518
Cdd:cd14009   240 RISFEEFFAHPF 251
STKc_RSK1_C cd14175
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called ...
262-524 1.92e-49

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: 175.22  E-value: 1.92e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 262 DFYDIEERLGSGKFGQVFRLVEKKTRKVWAGKFFKaysaKEKENIRQEISIM-NCLHHPKLVQCVDAFEEKANIVMVLEI 340
Cdd:cd14175     1 DGYVVKETIGVGSYSVCKRCVHKATNMEYAVKVID----KSKRDPSEEIEILlRYGQHPNIITLKDVYDDGKHVYLVTEL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 341 VSGGELFERIIDEDFeLTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKTGT--RIKLIDFGLARRLE-NAGS 417
Cdd:cd14175    77 MRGGELLDKILRQKF-FSEREASSVLHTICKTVEYLHSQGVVHRDLKPSNILYVDESGNpeSLRICDFGFAKQLRaENGL 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 418 LKVLFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPF---MGDNDNETLANVTSATWDFDDEAFDEISDDAKD 494
Cdd:cd14175   156 LMTPCYTANFVAPEVLKRQGYDEGCDIWSLGILLYTMLAGYTPFangPSDTPEEILTRIGSGKFTLSGGNWNTVSDAAKD 235
                         250       260       270
                  ....*....|....*....|....*....|
gi 1034633499 495 FISNLLKKDMKNRLDCTQCLQHPWLMKDTK 524
Cdd:cd14175   236 LVSKMLHVDPHQRLTAKQVLQHPWITQKDK 265
STKc_Mnk cd14090
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase ...
262-518 5.44e-49

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: 173.75  E-value: 5.44e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 262 DFYDI-EERLGSGKFGQVFRLVEKKTRKVWAGKFFKAYSAKEKENIRQEISIM-NCLHHPKLVQCVDAFEEKANIVMVLE 339
Cdd:cd14090     1 DLYKLtGELLGEGAYASVQTCINLYTGKEYAVKIIEKHPGHSRSRVFREVETLhQCQGHPNILQLIEYFEDDERFYLVFE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 340 IVSGGELFERIiDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMC--VNKTgTRIKLIDFGLARRLENAGS 417
Cdd:cd14090    81 KMRGGPLLSHI-EKRVHFTEQEASLVVRDIASALDFLHDKGIAHRDLKPENILCesMDKV-SPVKICDFDLGSGIKLSST 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 418 ---------LKVLFGTPEFVAPEVIN---YEPIGY--ATDMWSIGVICYILVSGLSPFMG---------------DNDNE 468
Cdd:cd14090   159 smtpvttpeLLTPVGSAEYMAPEVVDafvGEALSYdkRCDLWSLGVILYIMLCGYPPFYGrcgedcgwdrgeacqDCQEL 238
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1034633499 469 TLANVTSATWDFDDEAFDEISDDAKDFISNLLKKDMKNRLDCTQCLQHPW 518
Cdd:cd14090   239 LFHSIQEGEYEFPEKEWSHISAEAKDLISHLLVRDASQRYTAEQVLQHPW 288
STKc_RSK2_C cd14176
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called ...
259-544 5.77e-49

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: 175.21  E-value: 5.77e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 259 KVSDFYDIEERLGSGKFGQVFRLVEKKTRKVWAGKFFKaysaKEKENIRQEISIM-NCLHHPKLVQCVDAFEEKANIVMV 337
Cdd:cd14176    16 QFTDGYEVKEDIGVGSYSVCKRCIHKATNMEFAVKIID----KSKRDPTEEIEILlRYGQHPNIITLKDVYDDGKYVYVV 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 338 LEIVSGGELFERIIDEDFeLTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKTGT--RIKLIDFGLARRL--E 413
Cdd:cd14176    92 TELMKGGELLDKILRQKF-FSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDESGNpeSIRICDFGFAKQLraE 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 414 NaGSLKVLFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMG---DNDNETLANVTSATWDFDDEAFDEISD 490
Cdd:cd14176   171 N-GLLMTPCYTANFVAPEVLERQGYDAACDIWSLGVLLYTMLTGYTPFANgpdDTPEEILARIGSGKFSLSGGYWNSVSD 249
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1034633499 491 DAKDFISNLLKKDMKNRLDCTQCLQHPWLmkdtknmeakkLSKDRMKKYMARRK 544
Cdd:cd14176   250 TAKDLVSKMLHVDPHQRLTAALVLRHPWI-----------VHWDQLPQYQLNRQ 292
STKc_RSK3_C cd14178
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called ...
261-520 8.71e-49

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: 173.28  E-value: 8.71e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 261 SDFYDIEERLGSGKFGQVFRLVEKKTRKVWAGKFFKaysaKEKENIRQEISIM-NCLHHPKLVQCVDAFEEKANIVMVLE 339
Cdd:cd14178     2 TDGYEIKEDIGIGSYSVCKRCVHKATSTEYAVKIID----KSKRDPSEEIEILlRYGQHPNIITLKDVYDDGKFVYLVME 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 340 IVSGGELFERIIDEDFeLTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKTGT--RIKLIDFGLARRL--ENa 415
Cdd:cd14178    78 LMRGGELLDRILRQKC-FSEREASAVLCTITKTVEYLHSQGVVHRDLKPSNILYMDESGNpeSIRICDFGFAKQLraEN- 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 416 GSLKVLFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMG---DNDNETLANVTSATWDFDDEAFDEISDDA 492
Cdd:cd14178   156 GLLMTPCYTANFVAPEVLKRQGYDAACDIWSLGILLYTMLAGFTPFANgpdDTPEEILARIGSGKYALSGGNWDSISDAA 235
                         250       260
                  ....*....|....*....|....*...
gi 1034633499 493 KDFISNLLKKDMKNRLDCTQCLQHPWLM 520
Cdd:cd14178   236 KDIVSKMLHVDPHQRLTAPQVLRHPWIV 263
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
264-519 9.34e-49

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: 171.80  E-value: 9.34e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 264 YDIEERLGSGKFGQVFRLVEKKTRKVWAGKFFKAYSAKEKEN---IRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEI 340
Cdd:cd14073     3 YELLETLGKGTYGKVKLAIERATGREVAIKSIKKDKIEDEQDmvrIRREIEIMSSLNHPHIIRIYEVFENKDKIVIVMEY 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 341 VSGGELFErIIDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGTrIKLIDFGLARRLENAGSLKV 420
Cdd:cd14073    83 ASGGELYD-YISERRRLPEREARRIFRQIVSAVHYCHKNGVVHRDLKLENIL-LDQNGN-AKIADFGLSNLYSKDKLLQT 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 421 LFGTPEFVAPEVINYEP-IGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWdFDDEAfdeiSDDAKDFISNL 499
Cdd:cd14073   160 FCGSPLYASPEIVNGTPyQGPEVDCWSLGVLLYTLVYGTMPFDGSDFKRLVKQISSGDY-REPTQ----PSDASGLIRWM 234
                         250       260
                  ....*....|....*....|
gi 1034633499 500 LKKDMKNRLDCTQCLQHPWL 519
Cdd:cd14073   235 LTVNPKRRATIEDIANHWWV 254
STKc_PKD cd14082
Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer ...
267-518 1.18e-47

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: 169.13  E-value: 1.18e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 267 EERLGSGKFGQVFRLVEKKTRKVWAGKFFKA--YSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEIVSGg 344
Cdd:cd14082     8 DEVLGSGQFGIVYGGKHRKTGRDVAIKVIDKlrFPTKQESQLRNEVAILQQLSHPGVVNLECMFETPERVFVVMEKLHG- 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 345 ELFERIID-EDFELTEReCIKYM-RQISEGVEYIHKQGIVHLDLKPENIMCVNKTG-TRIKLIDFGLARRLENAGSLKVL 421
Cdd:cd14082    87 DMLEMILSsEKGRLPER-ITKFLvTQILVALRYLHSKNIVHCDLKPENVLLASAEPfPQVKLCDFGFARIIGEKSFRRSV 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 422 FGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDND-NETLANvtsATWDFDDEAFDEISDDAKDFISNLL 500
Cdd:cd14082   166 VGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFNEDEDiNDQIQN---AAFMYPPNPWKEISPDAIDLINNLL 242
                         250
                  ....*....|....*...
gi 1034633499 501 KKDMKNRLDCTQCLQHPW 518
Cdd:cd14082   243 QVKMRKRYSVDKSLSHPW 260
STKc_RCK1-like cd14096
Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
264-519 5.26e-47

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


Pssm-ID: 270998 [Multi-domain]  Cd Length: 295  Bit Score: 168.38  E-value: 5.26e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 264 YDIEERLGSGKFGQVFRLV-EKKTRKVWAGKFFKAY-------SAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIV 335
Cdd:cd14096     3 YRLINKIGEGAFSNVYKAVpLRNTGKPVAIKVVRKAdlssdnlKGSSRANILKEVQIMKRLSHPNIVKLLDFQESDEYYY 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 336 MVLEIVSGGELFERII-----DEDFeltERECIkymRQISEGVEYIHKQGIVHLDLKPENIM--CVNKTGTR-------- 400
Cdd:cd14096    83 IVLELADGGEIFHQIVrltyfSEDL---SRHVI---TQVASAVKYLHEIGVVHRDIKPENLLfePIPFIPSIvklrkadd 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 401 ---------------------IKLIDFGLARRLENAgSLKVLFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLS 459
Cdd:cd14096   157 detkvdegefipgvggggigiVKLADFGLSKQVWDS-NTKTPCGTVGYTAPEVVKDERYSKKVDMWALGCVLYTLLCGFP 235
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 460 PFMGDNDNETLANVTSATWDFDDEAFDEISDDAKDFISNLLKKDMKNRLDCTQCLQHPWL 519
Cdd:cd14096   236 PFYDESIETLTEKISRGDYTFLSPWWDEISKSAKDLISHLLTVDPAKRYDIDEFLAHPWI 295
STKc_DCKL2 cd14184
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called ...
262-518 6.41e-47

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: 167.13  E-value: 6.41e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 262 DFYDIEERLGSGKFGQVFRLVEKKTRKVWAGKFFKAYSAKEKEN-IRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEI 340
Cdd:cd14184     1 EKYKIGKVIGDGNFAVVKECVERSTGKEFALKIIDKAKCCGKEHlIENEVSILRRVKHPNIIMLIEEMDTPAELYLVMEL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 341 VSGGELFERIIDEDfELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIM-CVNKTGTR-IKLIDFGLARRLEnaGSL 418
Cdd:cd14184    81 VKGGDLFDAITSST-KYTERDASAMVYNLASALKYLHGLCIVHRDIKPENLLvCEYPDGTKsLKLGDFGLATVVE--GPL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 419 KVLFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDND--NETLANVTSATWDFDDEAFDEISDDAKDFI 496
Cdd:cd14184   158 YTVCGTPTYVAPEIIAETGYGLKVDIWAAGVITYILLCGFPPFRSENNlqEDLFDQILLGKLEFPSPYWDNITDSAKELI 237
                         250       260
                  ....*....|....*....|..
gi 1034633499 497 SNLLKKDMKNRLDCTQCLQHPW 518
Cdd:cd14184   238 SHMLQVNVEARYTAEQILSHPW 259
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
264-518 6.85e-47

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: 166.81  E-value: 6.85e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 264 YDIEERLGSGKFGQVFRLVEKKTRKVWAGKFF-KAYSAKEK--ENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEI 340
Cdd:cd14663     2 YELGRTLGEGTFAKVKFARNTKTGESVAIKIIdKEQVAREGmvEQIKREIAIMKLLRHPNIVELHEVMATKTKIFFVMEL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 341 VSGGELFERIIDeDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGTrIKLIDFGL---ARRLENAGS 417
Cdd:cd14663    82 VTGGELFSKIAK-NGRLKEDKARKYFQQLIDAVDYCHSRGVFHRDLKPENLL-LDEDGN-LKISDFGLsalSEQFRQDGL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 418 LKVLFGTPEFVAPEVI---NYEpiGYATDMWSIGVICYILVSGLSPFmgdnDNETLANVTSATWDFDDEAFDEISDDAKD 494
Cdd:cd14663   159 LHTTCGTPNYVAPEVLarrGYD--GAKADIWSCGVILFVLLAGYLPF----DDENLMALYRKIMKGEFEYPRWFSPGAKS 232
                         250       260
                  ....*....|....*....|....
gi 1034633499 495 FISNLLKKDMKNRLDCTQCLQHPW 518
Cdd:cd14663   233 LIKRILDPNPSTRITVEQIMASPW 256
STKc_SPEG_rpt2 cd14111
Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle ...
264-519 7.44e-47

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: 166.92  E-value: 7.44e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 264 YDIEERLGSGKFGQVFRLVEKKTRKVWAGKFfKAYSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEIVSG 343
Cdd:cd14111     5 YTFLDEKARGRFGVIRRCRENATGKNFPAKI-VPYQAEEKQGVLQEYEILKSLHHERIMALHEAYITPRYLVLIAEFCSG 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 344 GELFERIIDEdFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKTGtrIKLIDFGLARRLeNAGSLKVL-- 421
Cdd:cd14111    84 KELLHSLIDR-FRYSEDDVVGYLVQILQGLEYLHGRRVLHLDIKPDNIMVTNLNA--IKIVDFGSAQSF-NPLSLRQLgr 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 422 -FGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDfDDEAFDEISDDAKDFISNLL 500
Cdd:cd14111   160 rTGTLEYMAPEMVKGEPVGPPADIWSIGVLTYIMLSGRSPFEDQDPQETEAKILVAKFD-AFKLYPNVSQSASLFLKKVL 238
                         250
                  ....*....|....*....
gi 1034633499 501 KKDMKNRLDCTQCLQHPWL 519
Cdd:cd14111   239 SSYPWSRPTTKDCFAHAWL 257
STKc_CASK cd14094
Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein ...
262-544 1.13e-46

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: 167.72  E-value: 1.13e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 262 DFYDIEERLGSGKFGQVFRLVEKKTRKVWAGKF-----FKAYSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVM 336
Cdd:cd14094     3 DVYELCEVIGKGPFSVVRRCIHRETGQQFAVKIvdvakFTSSPGLSTEDLKREASICHMLKHPHIVELLETYSSDGMLYM 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 337 VLEIVSGGEL-FE--RIIDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNK-TGTRIKLIDFGLARRL 412
Cdd:cd14094    83 VFEFMDGADLcFEivKRADAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKeNSAPVKLGGFGVAIQL 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 413 ENAGSL---KVlfGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDnETLANVTSATWDFDDEAFDEIS 489
Cdd:cd14094   163 GESGLVaggRV--GTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKE-RLFEGIIKGKYKMNPRQWSHIS 239
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1034633499 490 DDAKDFISNLLKKDMKNRLDCTQCLQHPWLmKDTKNMEAKKL---SKDRMKKYMARRK 544
Cdd:cd14094   240 ESAKDLVRRMLMLDPAERITVYEALNHPWI-KERDRYAYRIHlpeTVEQLRKFNARRK 296
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
272-519 2.19e-46

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: 165.85  E-value: 2.19e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 272 SGKFGQVFrLVEKK-TRKVWAGKFFKAYSAKEK---ENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEIVSGGELF 347
Cdd:cd05579     3 RGAYGRVY-LAKKKsTGDLYAIKVIKKRDMIRKnqvDSVLAERNILSQAQNPFVVKLYYSFQGKKNLYLVMEYLPGGDLY 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 348 eRIIDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGtRIKLIDFGLAR-----RLENAGSLKV-- 420
Cdd:cd05579    82 -SLLENVGALDEDVARIYIAEIVLALEYLHSHGIIHRDLKPDNIL-IDANG-HLKLTDFGLSKvglvrRQIKLSIQKKsn 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 421 ---------LFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDFDDEafDEISDD 491
Cdd:cd05579   159 gapekedrrIVGTPDYLAPEILLGQGHGKTVDWWSLGVILYEFLVGIPPFHAETPEEIFQNILNGKIEWPED--PEVSDE 236
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1034633499 492 AKDFISNLLKKDMKNRLDC---TQCLQHPWL 519
Cdd:cd05579   237 AKDLISKLLTPDPEKRLGAkgiEEIKNHPFF 267
STKc_DCKL1 cd14183
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called ...
260-522 3.85e-46

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: 165.17  E-value: 3.85e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 260 VSDFYDIEERLGSGKFGQVFRLVEKKTRKVWAGKFFKAYSAKEKEN-IRQEISIMNCLHHPKLVQCVDAFEEKANIVMVL 338
Cdd:cd14183     4 ISERYKVGRTIGDGNFAVVKECVERSTGREYALKIINKSKCRGKEHmIQNEVSILRRVKHPNIVLLIEEMDMPTELYLVM 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 339 EIVSGGELFERIIDEDfELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCV-NKTGTR-IKLIDFGLARRLEnaG 416
Cdd:cd14183    84 ELVKGGDLFDAITSTN-KYTERDASGMLYNLASAIKYLHSLNIVHRDIKPENLLVYeHQDGSKsLKLGDFGLATVVD--G 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 417 SLKVLFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNET--LANVTSATWDFDDEAFDEISDDAKD 494
Cdd:cd14183   161 PLYTVCGTPTYVAPEIIAETGYGLKVDIWAAGVITYILLCGFPPFRGSGDDQEvlFDQILMGQVDFPSPYWDNVSDSAKE 240
                         250       260
                  ....*....|....*....|....*...
gi 1034633499 495 FISNLLKKDMKNRLDCTQCLQHPWLMKD 522
Cdd:cd14183   241 LITMMLQVDVDQRYSALQVLEHPWVNDD 268
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
264-519 5.19e-45

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: 161.62  E-value: 5.19e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 264 YDIEERLGSGKFGQVFRLVEKKTRKVWAGKFFKAYSAKEKE--NIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEIV 341
Cdd:cd06627     2 YQLGDLIGRGAFGSVYKGLNLNTGEFVAIKQISLEKIPKSDlkSVMGEIDLLKKLNHPNIVKYIGSVKTKDSLYIILEYV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 342 SGGELFERIidEDFE-LTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCvNKTGTrIKLIDFGLARRL-ENAGSLK 419
Cdd:cd06627    82 ENGSLASII--KKFGkFPESLVAVYIYQVLEGLAYLHEQGVIHRDIKGANILT-TKDGL-VKLADFGVATKLnEVEKDEN 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 420 VLFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSatwdfDDEAF--DEISDDAKDFIS 497
Cdd:cd06627   158 SVVGTPYWMAPEVIEMSGVTTASDIWSVGCTVIELLTGNPPYYDLQPMAALFRIVQ-----DDHPPlpENISPELRDFLL 232
                         250       260
                  ....*....|....*....|..
gi 1034633499 498 NLLKKDMKNRLDCTQCLQHPWL 519
Cdd:cd06627   233 QCFQKDPTLRPSAKELLKHPWL 254
STKc_MELK cd14078
Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; ...
260-519 1.43e-44

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: 160.63  E-value: 1.43e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 260 VSDFYDIEERLGSGKFGQVFRLVEKKTRKVWAGKFF-KAYSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVL 338
Cdd:cd14078     1 LLKYYELHETIGSGGFAKVKLATHILTGEKVAIKIMdKKALGDDLPRVKTEIEALKNLSHQHICRLYHVIETDNKIFMVL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 339 EIVSGGELFERIIDEDfELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTgTRIKLIDFGLARRLENAGS- 417
Cdd:cd14078    81 EYCPGGELFDYIVAKD-RLSEDEARVFFRQIVSAVAYVHSQGYAHRDLKPENLL-LDED-QNLKLIDFGLCAKPKGGMDh 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 418 -LKVLFGTPEFVAPEVINYEP-IGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDFDdeafDEISDDAKDF 495
Cdd:cd14078   158 hLETCCGSPAYAAPELIQGKPyIGSEADVWSMGVLLYALLCGFLPFDDDNVMALYRKIQSGKYEEP----EWLSPSSKLL 233
                         250       260
                  ....*....|....*....|....
gi 1034633499 496 ISNLLKKDMKNRLDCTQCLQHPWL 519
Cdd:cd14078   234 LDQMLQVDPKKRITVKELLNHPWV 257
STKc_RSK4_C cd14177
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called ...
259-519 2.55e-44

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: 160.95  E-value: 2.55e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 259 KVSDFYDIEERLGSGKFGQVFRLVEKKTRKVWAGKFFKaysaKEKENIRQEISI-MNCLHHPKLVQCVDAFEEKANIVMV 337
Cdd:cd14177     1 QFTDVYELKEDIGVGSYSVCKRCIHRATNMEFAVKIID----KSKRDPSEEIEIlMRYGQHPNIITLKDVYDDGRYVYLV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 338 LEIVSGGELFERIIDEDFeLTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKTGT--RIKLIDFGLARRLE-N 414
Cdd:cd14177    77 TELMKGGELLDRILRQKF-FSEREASAVLYTITKTVDYLHCQGVVHRDLKPSNILYMDDSANadSIRICDFGFAKQLRgE 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 415 AGSLKVLFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFM-GDNDN--ETLANVTSATWDFDDEAFDEISDD 491
Cdd:cd14177   156 NGLLLTPCYTANFVAPEVLMRQGYDAACDIWSLGVLLYTMLAGYTPFAnGPNDTpeEILLRIGSGKFSLSGGNWDTVSDA 235
                         250       260
                  ....*....|....*....|....*...
gi 1034633499 492 AKDFISNLLKKDMKNRLDCTQCLQHPWL 519
Cdd:cd14177   236 AKDLLSHMLHVDPHQRYTAEQVLKHSWI 263
STKc_AMPK_alpha cd14079
Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein ...
264-519 3.38e-44

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: 159.36  E-value: 3.38e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 264 YDIEERLGSGKFGQVFRLVEKKTRKVWAGKFF---KAYSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEI 340
Cdd:cd14079     4 YILGKTLGVGSFGKVKLAEHELTGHKVAVKILnrqKIKSLDMEEKIRREIQILKLFRHPHIIRLYEVIETPTDIFMVMEY 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 341 VSGGELFERIIDEDfELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIM---CVNktgtrIKLIDFGLARRLENAGS 417
Cdd:cd14079    84 VSGGELFDYIVQKG-RLSEDEARRFFQQIISGVEYCHRHMVVHRDLKPENLLldsNMN-----VKIADFGLSNIMRDGEF 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 418 LKVLFGTPEFVAPEVIN---YepIGYATDMWSIGVICYILVSGLSPFmgdnDNETLANVtsatwdfddeaFDEI------ 488
Cdd:cd14079   158 LKTSCGSPNYAAPEVISgklY--AGPEVDVWSCGVILYALLCGSLPF----DDEHIPNL-----------FKKIksgiyt 220
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1034633499 489 -----SDDAKDFISNLLKKDMKNRLDCTQCLQHPWL 519
Cdd:cd14079   221 ipshlSPGARDLIKRMLVVDPLKRITIPEIRQHPWF 256
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
264-519 6.84e-44

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: 158.65  E-value: 6.84e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 264 YDIEERLGSGKFGQVFRLVEKKTRKVWAGKFFKAYSAKE--KENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEIV 341
Cdd:cd14069     3 WDLVQTLGEGAFGEVFLAVNRNTEEAVAVKFVDMKRAPGdcPENIKKEVCIQKMLSHKNVVRFYGHRREGEFQYLFLEYA 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 342 SGGELFERIiDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGTrIKLIDFGLARRLENAGSLKVL 421
Cdd:cd14069    83 SGGELFDKI-EPDVGMPEDVAQFYFQQLMAGLKYLHSCGITHRDIKPENLL-LDENDN-LKISDFGLATVFRYKGKERLL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 422 ---FGTPEFVAPEVINYEPI-GYATDMWSIGVICYILVSGLSPF--MGDNDNETLANVTSATWDFDdeAFDEISDDAKDF 495
Cdd:cd14069   160 nkmCGTLPYVAPELLAKKKYrAEPVDVWSCGIVLFAMLAGELPWdqPSDSCQEYSDWKENKKTYLT--PWKKIDTAALSL 237
                         250       260
                  ....*....|....*....|....
gi 1034633499 496 ISNLLKKDMKNRLDCTQCLQHPWL 519
Cdd:cd14069   238 LRKILTENPNKRITIEDIKKHPWY 261
STKc_PhKG1 cd14182
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs ...
264-521 8.01e-44

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: 158.92  E-value: 8.01e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 264 YDIEERLGSGKFGQVFRLVEKKTRKVWAGKFFK-----AYSAKEKENIRQ----EISIMNCLH-HPKLVQCVDAFEEKAN 333
Cdd:cd14182     5 YEPKEILGRGVSSVVRRCIHKPTRQEYAVKIIDitgggSFSPEEVQELREatlkEIDILRKVSgHPNIIQLKDTYETNTF 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 334 IVMVLEIVSGGELFErIIDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKTGtrIKLIDFGLARRLE 413
Cdd:cd14182    85 FFLVFDLMKKGELFD-YLTEKVTLSEKETRKIMRALLEVICALHKLNIVHRDLKPENILLDDDMN--IKLTDFGFSCQLD 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 414 NAGSLKVLFGTPEFVAPEVI------NYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDFDDEAFDE 487
Cdd:cd14182   162 PGEKLREVCGTPGYLAPEIIecsmddNHPGYGKEVDMWSTGVIMYTLLAGSPPFWHRKQMLMLRMIMSGNYQFGSPEWDD 241
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1034633499 488 ISDDAKDFISNLLKKDMKNRLDCTQCLQHPWLMK 521
Cdd:cd14182   242 RSDTVKDLISRFLVVQPQKRYTAEEALAHPFFQQ 275
STKc_SNRK cd14074
Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the ...
264-519 8.51e-44

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


Pssm-ID: 270976 [Multi-domain]  Cd Length: 258  Bit Score: 158.35  E-value: 8.51e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 264 YDIEERLGSGKFGQVfrlveKKTRKVWAG-----KFFKAYSAKE--KENIRQEISIMNCLHHPKLVQCVDAFEEKANIVM 336
Cdd:cd14074     5 YDLEETLGRGHFAVV-----KLARHVFTGekvavKVIDKTKLDDvsKAHLFQEVRCMKLVQHPNVVRLYEVIDTQTKLYL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 337 VLEIVSGGELFERIIDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKTGTrIKLIDFGLARRLENAG 416
Cdd:cd14074    80 ILELGDGGDMYDYIMKHENGLNEDLARKYFRQIVSAISYCHKLHVVHRDLKPENVVFFEKQGL-VKLTDFGFSNKFQPGE 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 417 SLKVLFGTPEFVAPEVI---NYEPIgyATDMWSIGVICYILVSGLSPFMGDNDNETLANVTsatwDFDDEAFDEISDDAK 493
Cdd:cd14074   159 KLETSCGSLAYSAPEILlgdEYDAP--AVDIWSLGVILYMLVCGQPPFQEANDSETLTMIM----DCKYTVPAHVSPECK 232
                         250       260
                  ....*....|....*....|....*.
gi 1034633499 494 DFISNLLKKDMKNRLDCTQCLQHPWL 519
Cdd:cd14074   233 DLIRRMLIRDPKKRASLEEIENHPWL 258
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
263-519 1.17e-43

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: 157.76  E-value: 1.17e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 263 FYDIEERLGSGKFGQVFRLVEKKTRKVWAGKFFKaYSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEIVS 342
Cdd:cd06614     1 LYKNLEKIGEGASGEVYKATDRATGKEVAIKKMR-LRKQNKELIINEILIMKECKHPNIVDYYDSYLVGDELWVVMEYMD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 343 GGELFERIIDEDFELTEREcIKY-MRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGtRIKLIDFGLARRLENAGSLKV- 420
Cdd:cd06614    80 GGSLTDIITQNPVRMNESQ-IAYvCREVLQGLEYLHSQNVIHRDIKSDNIL-LSKDG-SVKLADFGFAAQLTKEKSKRNs 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 421 LFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANV-TSATWDFDDEafDEISDDAKDFISNL 499
Cdd:cd06614   157 VVGTPYWMAPEVIKRKDYGPKVDIWSLGIMCIEMAEGEPPYLEEPPLRALFLItTKGIPPLKNP--EKWSPEFKDFLNKC 234
                         250       260
                  ....*....|....*....|
gi 1034633499 500 LKKDMKNRLDCTQCLQHPWL 519
Cdd:cd06614   235 LVKDPEKRPSAEELLQHPFL 254
STKc_MAPKAPK5 cd14171
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
260-519 4.52e-43

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated protein kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK-activated protein kinase 5 (MAPKAP5 or MK5) is also called PRAK (p38-regulated/activated protein kinase). It contains 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. MK5 is a ubiquitous protein that is implicated in neuronal morphogenesis, cell migration, and tumor angiogenesis. It interacts with PKA, which induces cytoplasmic translocation of MK5. Its substrates includes p53, ERK3/4, Hsp27, and cytosolic phospholipase A2 (cPLA2). The MAPKAPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271073 [Multi-domain]  Cd Length: 289  Bit Score: 157.24  E-value: 4.52e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 260 VSDFYDI--EERLGSGKFGQVFRLVEKKTRKVWAGKFFKaysakEKENIRQEISI-MNCLHHPKLVQCVDAF-------- 328
Cdd:cd14171     2 ILEEYEVnwTQKLGTGISGPVRVCVKKSTGERFALKILL-----DRPKARTEVRLhMMCSGHPNIVQIYDVYansvqfpg 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 329 --EEKANIVMVLEIVSGGELFERIIDEDfELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKT-GTRIKLID 405
Cdd:cd14171    77 esSPRARLLIVMELMEGGELFDRISQHR-HFTEKQAAQYTKQIALAVQHCHSLNIAHRDLKPENLLLKDNSeDAPIKLCD 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 406 FGLARrlENAGSLKVLFGTPEFVAPEVINYE---------------PIGY--ATDMWSIGVICYILVSGLSPFMGDNDNE 468
Cdd:cd14171   156 FGFAK--VDQGDLMTPQFTPYYVAPQVLEAQrrhrkersgiptsptPYTYdkSCDMWSLGVIIYIMLCGYPPFYSEHPSR 233
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1034633499 469 TLAN-----VTSATWDFDDEAFDEISDDAKDFISNLLKKDMKNRLDCTQCLQHPWL 519
Cdd:cd14171   234 TITKdmkrkIMTGSYEFPEEEWSQISEMAKDIVRKLLCVDPEERMTIEEVLHHPWL 289
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
264-519 2.39e-42

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: 153.93  E-value: 2.39e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 264 YDIEERLGSGKFGQVFRLVEKKTRKVWAGKFFKAYSAKEKENIRqEISIMNCL----HHPKLVQCVDAFEEKA--NIVMV 337
Cdd:cd05118     1 YEVLRKIGEGAFGTVWLARDKVTGEKVAIKKIKNDFRHPKAALR-EIKLLKHLndveGHPNIVKLLDVFEHRGgnHLCLV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 338 LEIVsGGELFERIIDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKTGTrIKLIDFGLARRL-ENAG 416
Cdd:cd05118    80 FELM-GMNLYELIKDYPRGLPLDLIKSYLYQLLQALDFLHSNGIIHRDLKPENILINLELGQ-LKLADFGLARSFtSPPY 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 417 SLKVlfGTPEFVAPEVI-NYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLAnvtsatwdfddEAFDEI-SDDAKD 494
Cdd:cd05118   158 TPYV--ATRWYRAPEVLlGAKPYGSSIDIWSLGCILAELLTGRPLFPGDSEVDQLA-----------KIVRLLgTPEALD 224
                         250       260
                  ....*....|....*....|....*
gi 1034633499 495 FISNLLKKDMKNRLDCTQCLQHPWL 519
Cdd:cd05118   225 LLSKMLKYDPAKRITASQALAHPYF 249
STKc_MSK1_C cd14179
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
265-524 3.60e-42

C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSK1 plays a role in the regulation of translational control and transcriptional activation. It phosphorylates the transcription factors, CREB and NFkB. It also phosphorylates the nucleosomal proteins H3 and HMG-14. Increased phosphorylation of MSK1 is associated with the development of cerebral ischemic/hypoxic preconditioning. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, which trigger phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. The MSK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271081 [Multi-domain]  Cd Length: 310  Bit Score: 155.58  E-value: 3.60e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 265 DIEER-LGSGKFGQVFRLVEKKTRKVWAgkfFKAYSAKEKENIRQEISIMN-CLHHPKLVQCVDAFEEKANIVMVLEIVS 342
Cdd:cd14179     9 DLKDKpLGEGSFSICRKCLHKKTNQEYA---VKIVSKRMEANTQREIAALKlCEGHPNIVKLHEVYHDQLHTFLVMELLK 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 343 GGELFERIIDEDfELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKT-GTRIKLIDFGLAR-RLENAGSLKV 420
Cdd:cd14179    86 GGELLERIKKKQ-HFSETEASHIMRKLVSAVSHMHDVGVVHRDLKPENLLFTDESdNSEIKIIDFGFARlKPPDNQPLKT 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 421 LFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDN-------ETLANVTSATWDFDDEAFDEISDDAK 493
Cdd:cd14179   165 PCFTLHYAAPELLNYNGYDESCDLWSLGVILYTMLSGQVPFQCHDKSltctsaeEIMKKIKQGDFSFEGEAWKNVSQEAK 244
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1034633499 494 DFISNLLKKDMKNRLDCTQCLQHPWLMKDTK 524
Cdd:cd14179   245 DLIQGLLTVDPNKRIKMSGLRYNEWLQDGSQ 275
STKc_MAPKAPK3 cd14172
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
260-519 5.47e-42

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: 153.61  E-value: 5.47e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 260 VSDFYDIEER-LGSGKFGQVFRLVEKKTRKVWAGKFFKAySAKEKENIRQEISIMNClhhPKLVQCVDAFEE----KANI 334
Cdd:cd14172     1 VTDDYKLSKQvLGLGVNGKVLECFHRRTGQKCALKLLYD-SPKARREVEHHWRASGG---PHIVHILDVYENmhhgKRCL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 335 VMVLEIVSGGELFERIIDE-DFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNK-TGTRIKLIDFGLARRL 412
Cdd:cd14172    77 LIIMECMEGGELFSRIQERgDQAFTEREASEIMRDIGTAIQYLHSMNIAHRDVKPENLLYTSKeKDAVLKLTDFGFAKET 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 413 ENAGSLKVLFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMgDNDNETLA-----NVTSATWDFDDEAFDE 487
Cdd:cd14172   157 TVQNALQTPCYTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGFPPFY-SNTGQAISpgmkrRIRMGQYGFPNPEWAE 235
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1034633499 488 ISDDAKDFISNLLKKDMKNRLDCTQCLQHPWL 519
Cdd:cd14172   236 VSEEAKQLIRHLLKTDPTERMTITQFMNHPWI 267
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
270-519 5.91e-42

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: 153.18  E-value: 5.91e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 270 LGSGKFGQVFRLVEKKTRKVWAGKFFKaysaKEK--------ENIRQEISIMNCLHHPKLVQCVDAF--EEKANIVMVLE 339
Cdd:cd14119     1 LGEGSYGKVKEVLDTETLCRRAVKILK----KRKlrripngeANVKREIQILRRLNHRNVIKLVDVLynEEKQKLYMVME 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 340 IVSGG--ELFERIIDEDFELTERECikYMRQISEGVEYIHKQGIVHLDLKPENIMCvnKTGTRIKLIDFGLARRLE---N 414
Cdd:cd14119    77 YCVGGlqEMLDSAPDKRLPIWQAHG--YFVQLIDGLEYLHSQGIIHKDIKPGNLLL--TTDGTLKISDFGVAEALDlfaE 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 415 AGSLKVLFGTPEFVAPEVINYEPI--GYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDFDdeafDEISDDA 492
Cdd:cd14119   153 DDTCTTSQGSPAFQPPEIANGQDSfsGFKVDIWSAGVTLYNMTTGKYPFEGDNIYKLFENIGKGEYTIP----DDVDPDL 228
                         250       260
                  ....*....|....*....|....*..
gi 1034633499 493 KDFISNLLKKDMKNRLDCTQCLQHPWL 519
Cdd:cd14119   229 QDLLRGMLEKDPEKRFTIEQIRQHPWF 255
STKc_STK33 cd14097
Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the ...
264-519 9.88e-42

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: 153.09  E-value: 9.88e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 264 YDIEERLGSGKFGQVFRLVEKKTRKVWAGKFF---KAYSAKEKEnIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEI 340
Cdd:cd14097     3 YTFGRKLGQGSFGVVIEATHKETQTKWAIKKInreKAGSSAVKL-LEREVDILKHVNHAHIIHLEEVFETPKRMYLVMEL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 341 VSGGELfERIIDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCV-----NKTGTRIKLIDFGLARRLENA 415
Cdd:cd14097    82 CEDGEL-KELLLRKGFFSENETRHIIQSLASAVAYLHKNDIVHRDLKLENILVKssiidNNDKLNIKVTDFGLSVQKYGL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 416 GS--LKVLFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDFDDEAFDEISDDAK 493
Cdd:cd14097   161 GEdmLQETCGTPIYMAPEVISAHGYSQQCDIWSIGVIMYMLLCGEPPFVAKSEEKLFEEIRKGDLTFTQSVWQSVSDAAK 240
                         250       260
                  ....*....|....*....|....*.
gi 1034633499 494 DFISNLLKKDMKNRLDCTQCLQHPWL 519
Cdd:cd14097   241 NVLQQLLKVDPAHRMTASELLDNPWI 266
STKc_p70S6K cd05584
Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs ...
270-518 1.23e-41

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: 154.48  E-value: 1.23e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 270 LGSGKFGQVFrLVEKKTR----KVWAGKFFK----AYSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEIV 341
Cdd:cd05584     4 LGKGGYGKVF-QVRKTTGsdkgKIFAMKVLKkasiVRNQKDTAHTKAERNILEAVKHPFIVDLHYAFQTGGKLYLILEYL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 342 SGGELFERIIDEDFELTERECIkYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGtRIKLIDFGLAR-RLENAGSLKV 420
Cdd:cd05584    83 SGGELFMHLEREGIFMEDTACF-YLAEITLALGHLHSLGIIYRDLKPENIL-LDAQG-HVKLTDFGLCKeSIHDGTVTHT 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 421 LFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSAtwDFDDEAFdeISDDAKDFISNLL 500
Cdd:cd05584   160 FCGTIEYMAPEILTRSGHGKAVDWWSLGALMYDMLTGAPPFTAENRKKTIDKILKG--KLNLPPY--LTNEARDLLKKLL 235
                         250       260
                  ....*....|....*....|...
gi 1034633499 501 KKDMKNRL-----DCTQCLQHPW 518
Cdd:cd05584   236 KRNVSSRLgsgpgDAEEIKAHPF 258
STKc_PhKG2 cd14181
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs ...
264-519 1.33e-41

Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Phosphorylase kinase (PhK) catalyzes the phosphorylation of inactive phosphorylase b to form the active phosphorylase a. It coordinates hormonal, metabolic, and neuronal signals to initiate the breakdown of glycogen stores, which enables the maintenance of blood-glucose homeostasis during fasting, and is also used as a source of energy for muscle contraction. PhK is one of the largest and most complex protein kinases, composed of a heterotetramer containing four molecules each of four subunit types: one catalytic (gamma) and three regulatory (alpha, beta, and delta). The gamma 2 subunit (PhKG2) is also referred to as the testis/liver gamma isoform. Mutations in its gene cause autosomal-recessive glycogenosis of the liver. The gamma subunit, when isolated, is constitutively active and does not require phosphorylation of the A-loop for activity. The regulatory subunits restrain this kinase activity until signals are received to relieve this inhibition. For example, the kinase is activated in response to hormonal stimulation, after autophosphorylation or phosphorylation by cAMP-dependent kinase of the alpha and beta subunits. The high-affinity binding of ADP to the beta subunit also stimulates kinase activity, whereas calcium relieves inhibition by binding to the delta (calmodulin) subunit. The PhKG2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271083 [Multi-domain]  Cd Length: 279  Bit Score: 152.82  E-value: 1.33e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 264 YDIEERLGSGKFGQVFRLVEKKTRKVWAGKFFKAYSAKE--------KENIRQEISIMNCLH-HPKLVQCVDAFEEKANI 334
Cdd:cd14181    12 YDPKEVIGRGVSSVVRRCVHRHTGQEFAVKIIEVTAERLspeqleevRSSTLKEIHILRQVSgHPSIITLIDSYESSTFI 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 335 VMVLEIVSGGELFErIIDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKTgtRIKLIDFGLARRLEN 414
Cdd:cd14181    92 FLVFDLMRRGELFD-YLTEKVTLSEKETRSIMRSLLEAVSYLHANNIVHRDLKPENILLDDQL--HIKLSDFGFSCHLEP 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 415 AGSLKVLFGTPEFVAPEVI------NYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDFDDEAFDEI 488
Cdd:cd14181   169 GEKLRELCGTPGYLAPEILkcsmdeTHPGYGKEVDLWACGVILFTLLAGSPPFWHRRQMLMLRMIMEGRYQFSSPEWDDR 248
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1034633499 489 SDDAKDFISNLLKKDMKNRLDCTQCLQHPWL 519
Cdd:cd14181   249 SSTVKDLISRLLVVDPEIRLTAEQALQHPFF 279
STKc_MAPKAPK2 cd14170
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
262-521 2.03e-41

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: 153.27  E-value: 2.03e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 262 DFYDIEERLGSGKFGQVFRLVEKKTRKVWAGKFFKAySAKEKENIRQEISIMNCLHhpkLVQCVDAFEE----KANIVMV 337
Cdd:cd14170     2 DYKVTSQVLGLGINGKVLQIFNKRTQEKFALKMLQD-CPKARREVELHWRASQCPH---IVRIVDVYENlyagRKCLLIV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 338 LEIVSGGELFERIIDE-DFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKTGTRI-KLIDFGLARRLENA 415
Cdd:cd14170    78 MECLDGGELFSRIQDRgDQAFTEREASEIMKSIGEAIQYLHSINIAHRDVKPENLLYTSKRPNAIlKLTDFGFAKETTSH 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 416 GSLKVLFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMgdnDNETLA-------NVTSATWDFDDEAFDEI 488
Cdd:cd14170   158 NSLTTPCYTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGYPPFY---SNHGLAispgmktRIRMGQYEFPNPEWSEV 234
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1034633499 489 SDDAKDFISNLLKKDMKNRLDCTQCLQHPWLMK 521
Cdd:cd14170   235 SEEVKMLIRNLLKTEPTQRMTITEFMNHPWIMQ 267
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
270-518 3.30e-41

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: 151.22  E-value: 3.30e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 270 LGSGKFGQVFRLVEKKTRKVWAGKFFKA---YSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEIVSGGEL 346
Cdd:cd05572     1 LGVGGFGRVELVQLKSKGRTFALKCVKKrhiVQTRQQEHIFSEKEILEECNSPFIVKLYRTFKDKKYLYMLMEYCLGGEL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 347 FERIIDEDfELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGtRIKLIDFGLARRLENAGSLKVLFGTPE 426
Cdd:cd05572    81 WTILRDRG-LFDEYTARFYTACVVLAFEYLHSRGIIYRDLKPENLL-LDSNG-YVKLVDFGFAKKLGSGRKTWTFCGTPE 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 427 FVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDN--ETLANVTSATWDFDDEAFdeISDDAKDFISNLLKKDM 504
Cdd:cd05572   158 YVAPEIILNKGYDFSVDYWSLGILLYELLTGRPPFGGDDEDpmKIYNIILKGIDKIEFPKY--IDKNAKNLIKQLLRRNP 235
                         250
                  ....*....|....*....
gi 1034633499 505 KNRLDCTQ-----CLQHPW 518
Cdd:cd05572   236 EERLGYLKggirdIKKHKW 254
STKc_PKA cd14209
Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze ...
262-523 3.30e-41

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: 152.17  E-value: 3.30e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 262 DFYDIEERLGSGKFGQVFRLVEKKTRKVWAGKFF---KAYSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVL 338
Cdd:cd14209     1 DDFDRIKTLGTGSFGRVMLVRHKETGNYYAMKILdkqKVVKLKQVEHTLNEKRILQAINFPFLVKLEYSFKDNSNLYMVM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 339 EIVSGGELFERIiDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGTrIKLIDFGLARRLEnaGSL 418
Cdd:cd14209    81 EYVPGGEMFSHL-RRIGRFSEPHARFYAAQIVLAFEYLHSLDLIYRDLKPENLL-IDQQGY-IKVTDFGFAKRVK--GRT 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 419 KVLFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDFDdeafDEISDDAKDFISN 498
Cdd:cd14209   156 WTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFP----SHFSSDLKDLLRN 231
                         250       260       270
                  ....*....|....*....|....*....|
gi 1034633499 499 LLKKDMKNRL-----DCTQCLQHPWLmKDT 523
Cdd:cd14209   232 LLQVDLTKRFgnlknGVNDIKNHKWF-ATT 260
STKc_Mnk1 cd14174
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
262-519 9.31e-41

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


Pssm-ID: 271076 [Multi-domain]  Cd Length: 289  Bit Score: 150.95  E-value: 9.31e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 262 DFYDI-EERLGSGKFGQVFRLVEKKTRKVWAGKFFKAYSAKEKENIRQEI-SIMNCLHHPKLVQCVDAFEEKANIVMVLE 339
Cdd:cd14174     1 DLYRLtDELLGEGAYAKVQGCVSLQNGKEYAVKIIEKNAGHSRSRVFREVeTLYQCQGNKNILELIEFFEDDTRFYLVFE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 340 IVSGGELFERIIDEDFeLTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKTG-TRIKLIDFGLAR--RLENAG 416
Cdd:cd14174    81 KLRGGSILAHIQKRKH-FNEREASRVVRDIASALDFLHTKGIAHRDLKPENILCESPDKvSPVKICDFDLGSgvKLNSAC 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 417 S------LKVLFGTPEFVAPEVINY---EPIGY--ATDMWSIGVICYILVSGLSPFMGDN---------------DNETL 470
Cdd:cd14174   160 TpittpeLTTPCGSAEYMAPEVVEVftdEATFYdkRCDLWSLGVILYIMLSGYPPFVGHCgtdcgwdrgevcrvcQNKLF 239
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1034633499 471 ANVTSATWDFDDEAFDEISDDAKDFISNLLKKDMKNRLDCTQCLQHPWL 519
Cdd:cd14174   240 ESIQEGKYEFPDKDWSHISSEAKDLISKLLVRDAKERLSAAQVLQHPWV 288
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
264-478 1.12e-40

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: 149.72  E-value: 1.12e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 264 YDIEERLGSGKFGQVFRLVEKKTRKVWAGKFFKAYSAKEKE--NIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEIV 341
Cdd:cd14161     5 YEFLETLGKGTYGRVKKARDSSGRLVAIKSIRKDRIKDEQDllHIRREIEIMSSLNHPHIISVYEVFENSSKIVIVMEYA 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 342 SGGELFERIIDEDfELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGTrIKLIDFGLARRLENAGSLKVL 421
Cdd:cd14161    85 SRGDLYDYISERQ-RLSELEARHFFRQIVSAVHYCHANGIVHRDLKLENIL-LDANGN-IKIADFGLSNLYNQDKFLQTY 161
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1034633499 422 FGTPEFVAPEVINYEP-IGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATW 478
Cdd:cd14161   162 CGSPLYASPEIVNGRPyIGPEVDSWSLGVLLYILVHGTMPFDGHDYKILVKQISSGAY 219
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
261-508 1.32e-40

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: 150.42  E-value: 1.32e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 261 SDFyDIEERLGSGKFGQVFRLVEKKTRKVWAGKFFKAYSA---KEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMV 337
Cdd:cd05580     1 DDF-EFLKTLGTGSFGRVRLVKHKDSGKYYALKILKKAKIiklKQVEHVLNEKRILSEVRHPFIVNLLGSFQDDRNLYMV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 338 LEIVSGGELFERIIDED-FELTErecIK-YMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGtRIKLIDFGLARRLENa 415
Cdd:cd05580    80 MEYVPGGELFSLLRRSGrFPNDV---AKfYAAEVVLALEYLHSLDIVYRDLKPENLL-LDSDG-HIKITDFGFAKRVKD- 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 416 gSLKVLFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDFDdeafDEISDDAKDF 495
Cdd:cd05580   154 -RTYTLCGTPEYLAPEIILSKGHGKAVDWWALGILIYEMLAGYPPFFDENPMKIYEKILEGKIRFP----SFFDPDAKDL 228
                         250
                  ....*....|...
gi 1034633499 496 ISNLLKKDMKNRL 508
Cdd:cd05580   229 IKRLLVVDLTKRL 241
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
261-521 2.44e-40

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: 148.89  E-value: 2.44e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 261 SDFyDIEERLGSGKFGQVFRLVEKKTRKVWAGKFFKAYSAKEKEN-IRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLE 339
Cdd:cd06623     1 SDL-ERVKVLGQGSSGVVYKVRHKPTGKIYALKKIHVDGDEEFRKqLLRELKTLRSCESPYVVKCYGAFYKEGEISIVLE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 340 IVSGGELfERIIDEDFELTERECIKYMRQISEGVEYIHKQ-GIVHLDLKPENIMcVNKTGtRIKLIDFGLARRLENAGSL 418
Cdd:cd06623    80 YMDGGSL-ADLLKKVGKIPEPVLAYIARQILKGLDYLHTKrHIIHRDIKPSNLL-INSKG-EVKIADFGISKVLENTLDQ 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 419 KVLF-GTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMgDNDNETLANVTSATWDFDDEAFDE--ISDDAKDF 495
Cdd:cd06623   157 CNTFvGTVTYMSPERIQGESYSYAADIWSLGLTLLECALGKFPFL-PPGQPSFFELMQAICDGPPPSLPAeeFSPEFRDF 235
                         250       260
                  ....*....|....*....|....*.
gi 1034633499 496 ISNLLKKDMKNRLDCTQCLQHPWLMK 521
Cdd:cd06623   236 ISACLQKDPKKRPSAAELLQHPFIKK 261
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
264-519 2.70e-40

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: 148.87  E-value: 2.70e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 264 YDIEERLGSGKFGQVFRLVEKK-------------TRKvwAGKFFKaysakEKENIRqEISIMNCLHHPKLVQCVDAFEE 330
Cdd:cd14080     2 YRLGKTIGEGSYSKVKLAEYTKsglkekvackiidKKK--APKDFL-----EKFLPR-ELEILRKLRHPNIIQVYSIFER 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 331 KANIVMVLEIVSGGELFERIIDEDFeLTERECIKYMRQISEGVEYIHKQGIVHLDLKPENI-MCVNKTgtrIKLIDFGLA 409
Cdd:cd14080    74 GSKVFIFMEYAEHGDLLEYIQKRGA-LSESQARIWFRQLALAVQYLHSLDIAHRDLKCENIlLDSNNN---VKLSDFGFA 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 410 RRLENAGSL---KVLFGTPEFVAPEV---INYEPIGYatDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDFdDE 483
Cdd:cd14080   150 RLCPDDDGDvlsKTFCGSAAYAAPEIlqgIPYDPKKY--DIWSLGVILYIMLCGSMPFDDSNIKKMLKDQQNRKVRF-PS 226
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1034633499 484 AFDEISDDAKDFISNLLKKDMKNRLDCTQCLQHPWL 519
Cdd:cd14080   227 SVKKLSPECKDLIDQLLEPDPTKRATIEEILNHPWL 262
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
270-463 1.37e-39

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: 146.14  E-value: 1.37e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 270 LGSGKFGQVFRlvekktrKVWAG-----KFFKA--YSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEIVS 342
Cdd:cd13999     1 IGSGSFGEVYK-------GKWRGtdvaiKKLKVedDNDELLKEFRREVSILSKLRHPNIVQFIGACLSPPPLCIVTEYMP 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 343 GGELFERIIDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGTrIKLIDFGLARRL-ENAGSLKVL 421
Cdd:cd13999    74 GGSLYDLLHKKKIPLSWSLRLKIALDIARGMNYLHSPPIIHRDLKSLNIL-LDENFT-VKIADFGLSRIKnSTTEKMTGV 151
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1034633499 422 FGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMG 463
Cdd:cd13999   152 VGTPRWMAPEVLRGEPYTEKADVYSFGIVLWELLTGEVPFKE 193
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
261-518 2.86e-39

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: 148.59  E-value: 2.86e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 261 SDFyDIEERLGSGKFGQVFRLVEKKTRKVWAGKFFKAYSAKEKE---NIRQEISIMNCLHHPKLVQCVDAFEEKANIVMV 337
Cdd:cd05573     1 DDF-EVIKVIGRGAFGEVWLVRDKDTGQVYAMKILRKSDMLKREqiaHVRAERDILADADSPWIVRLHYAFQDEDHLYLV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 338 LEIVSGGELFERIIDEDfELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGtRIKLIDFGLARRLENAGS 417
Cdd:cd05573    80 MEYMPGGDLMNLLIKYD-VFPEETARFYIAELVLALDSLHKLGFIHRDIKPDNIL-LDADG-HIKLADFGLCTKMNKSGD 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 418 --------------------------LKVLF----GTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDN 467
Cdd:cd05573   157 resylndsvntlfqdnvlarrrphkqRRVRAysavGTPDYIAPEVLRGTGYGPECDWWSLGVILYEMLYGFPPFYSDSLV 236
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1034633499 468 ETLANVTSatWD----FDDEafDEISDDAKDFISNLLkKDMKNRLDCT-QCLQHPW 518
Cdd:cd05573   237 ETYSKIMN--WKeslvFPDD--PDVSPEAIDLIRRLL-CDPEDRLGSAeEIKAHPF 287
STKc_PKC cd05570
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer ...
270-537 1.14e-38

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: 145.82  E-value: 1.14e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 270 LGSGKFGQVFrLVE-KKTRKVWAGKFFKaysakeKENIRQE---ISIMN-------CLHHPKLVQCVDAFEEKANIVMVL 338
Cdd:cd05570     3 LGKGSFGKVM-LAErKKTDELYAIKVLK------KEVIIEDddvECTMTekrvlalANRHPFLTGLHACFQTEDRLYFVM 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 339 EIVSGGEL-FEriIDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGtRIKLIDFGLARR-LENAG 416
Cdd:cd05570    76 EYVNGGDLmFH--IQRARRFTEERARFYAAEICLALQFLHERGIIYRDLKLDNVL-LDAEG-HIKIADFGMCKEgIWGGN 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 417 SLKVLFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETlanvtsatwdFDDEAFDEI------SD 490
Cdd:cd05570   152 TTSTFCGTPDYIAPEILREQDYGFSVDWWALGVLLYEMLAGQSPFEGDDEDEL----------FEAILNDEVlyprwlSR 221
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1034633499 491 DAKDFISNLLKKDMKNRLDCT-----QCLQHPWLmkdtKNMEAKKLSKDRMK 537
Cdd:cd05570   222 EAVSILKGLLTKDPARRLGCGpkgeaDIKAHPFF----RNIDWDKLEKKEVE 269
STKc_NIM1 cd14075
Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the ...
263-519 1.50e-38

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: 143.63  E-value: 1.50e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 263 FYDIEERLGSGKFGQVFRLVEKKTRKVWAGKFF-KA-YSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEI 340
Cdd:cd14075     3 FYRIRGELGSGNFSQVKLGIHQLTKEKVAIKILdKTkLDQKTQRLLSREISSMEKLHHPNIIRLYEVVETLSKLHLVMEY 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 341 VSGGELFERIIDEDfELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKtgTRIKLIDFGLARRLENAGSLKV 420
Cdd:cd14075    83 ASGGELYTKISTEG-KLSESEAKPLFAQIVSAVKHMHENNIIHRDLKAENVFYASN--NCVKVGDFGFSTHAKRGETLNT 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 421 LFGTPEFVAPEVI---NYepIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDFDdeafDEISDDAKDFIS 497
Cdd:cd14075   160 FCGSPPYAAPELFkdeHY--IGIYVDIWALGVLLYFMVTGVMPFRAETVAKLKKCILEGTYTIP----SYVSEPCQELIR 233
                         250       260
                  ....*....|....*....|..
gi 1034633499 498 NLLKKDMKNRLDCTQCLQHPWL 519
Cdd:cd14075   234 GILQPVPSDRYSIDEIKNSEWL 255
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
264-519 1.97e-38

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: 143.74  E-value: 1.97e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 264 YDIEERLGSGKFGQVFRLVEKKTRKVWAGKFFKAYS----------------AKEKENIRqEISIMNCLHHPKLVQCVDA 327
Cdd:cd14077     3 WEFVKTIGAGSMGKVKLAKHIRTGEKCAIKIIPRASnaglkkerekrlekeiSRDIRTIR-EAALSSLLNHPHICRLRDF 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 328 FEEKANIVMVLEIVSGGELFERIIDEDfELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGtRIKLIDFG 407
Cdd:cd14077    82 LRTPNHYYMLFEYVDGGQLLDYIISHG-KLKEKQARKFARQIASALDYLHRNSIVHRDLKIENIL-ISKSG-NIKIIDFG 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 408 LARRLENAGSLKVLFGTPEFVAPEVINYEP-IGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDFDdeafD 486
Cdd:cd14077   159 LSNLYDPRRLLRTFCGSLYFAAPELLQAQPyTGPEVDVWSFGVVLYVLVCGKVPFDDENMPALHAKIKKGKVEYP----S 234
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1034633499 487 EISDDAKDFISNLLKKDMKNRLDCTQCLQHPWL 519
Cdd:cd14077   235 YLSSECKSLISRMLVVDPKKRATLEQVLNHPWM 267
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
269-519 2.30e-38

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: 143.21  E-value: 2.30e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 269 RLGSGKFGQVFRLVEKKTRKVWAGKFFKAYSAKEK--ENIRQEISIMNCLHHPKLVQC--VDAFEEKANIVMvlEIVSGG 344
Cdd:cd06626     7 KIGEGTFGKVYTAVNLDTGELMAMKEIRFQDNDPKtiKEIADEMKVLEGLDHPNLVRYygVEVHREEVYIFM--EYCQEG 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 345 ELFE-----RIIDEdfelterECIK-YMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGTrIKLIDFGLARRLENA--- 415
Cdd:cd06626    85 TLEEllrhgRILDE-------AVIRvYTLQLLEGLAYLHENGIVHRDIKPANIF-LDSNGL-IKLGDFGSAVKLKNNttt 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 416 ---GSLKVLFGTPEFVAPEVINYEP---IGYATDMWSIGviCYIL--VSGLSPfmgdndnetlanvtsatWDFDDEAF-- 485
Cdd:cd06626   156 mapGEVNSLVGTPAYMAPEVITGNKgegHGRAADIWSLG--CVVLemATGKRP-----------------WSELDNEWai 216
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1034633499 486 ---------------DEISDDAKDFISNLLKKDMKNRLDCTQCLQHPWL 519
Cdd:cd06626   217 myhvgmghkppipdsLQLSPEGKDFLSRCLESDPKKRPTASELLDHPFI 265
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
262-540 3.21e-38

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: 143.15  E-value: 3.21e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 262 DFYDIEERLGSGKFGQVFRLVEKKTRKVWAGKFFKAYSAKEK-ENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEI 340
Cdd:cd06609     1 ELFTLLERIGKGSFGEVYKGIDKRTNQVVAIKVIDLEEAEDEiEDIQQEIQFLSQCDSPYITKYYGSFLKGSKLWIIMEY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 341 VSGGELFE----RIIDEDFelterecIKY-MRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGTrIKLIDFGLARRLENA 415
Cdd:cd06609    81 CGGGSVLDllkpGPLDETY-------IAFiLREVLLGLEYLHSEGKIHRDIKAANIL-LSEEGD-VKLADFGVSGQLTST 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 416 GSLKVLF-GTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMG-----------DNDNETLANvtsatwdfdde 483
Cdd:cd06609   152 MSKRNTFvGTPFWMAPEVIKQSGYDEKADIWSLGITAIELAKGEPPLSDlhpmrvlflipKNNPPSLEG----------- 220
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1034633499 484 afDEISDDAKDFISNLLKKDMKNRLDCTQCLQHPWLMKDTKNMEAKKLsKDRMKKYM 540
Cdd:cd06609   221 --NKFSKPFKDFVELCLNKDPKERPSAKELLKHKFIKKAKKTSYLTLL-IERIKKWK 274
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
268-518 4.28e-38

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: 142.04  E-value: 4.28e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 268 ERLGSGKFGQVFRLVEKK-TRKVWAGKFF--KAYSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEIVSGG 344
Cdd:cd14121     1 EKLGSGTYATVYKAYRKSgAREVVAVKCVskSSLNKASTENLLTEIELLKKLKHPHIVELKDFQWDEEHIYLIMEYCSGG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 345 ELfERIIDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKTGTRIKLIDFGLARRLENAGSLKVLFGT 424
Cdd:cd14121    81 DL-SRFIRSRRTLPESTVRRFLQQLASALQFLREHNISHMDLKPQNLLLSSRYNPVLKLADFGFAQHLKPNDEAHSLRGS 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 425 PEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATwDFDDEAFDEISDDAKDFISNLLKKDM 504
Cdd:cd14121   160 PLYMAPEMILKKKYDARVDLWSVGVILYECLFGRAPFASRSFEELEEKIRSSK-PIEIPTRPELSADCRDLLLRLLQRDP 238
                         250
                  ....*....|....
gi 1034633499 505 KNRLDCTQCLQHPW 518
Cdd:cd14121   239 DRRISFEEFFAHPF 252
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
270-519 6.44e-38

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: 141.77  E-value: 6.44e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 270 LGSGKFGQVFRLVEKKTRKVWAGKFFKAYSA--KEKENIRQ---EISIMNCLHHPKLVQCVDAFEEKANIVMVLEIVSGG 344
Cdd:cd06632     8 LGSGSFGSVYEGFNGDTGDFFAVKEVSLVDDdkKSRESVKQleqEIALLSKLRHPNIVQYYGTEREEDNLYIFLEYVPGG 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 345 ELFEriIDEDFELTERECIK-YMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGtRIKLIDFGLARRLENAGSLKVLFG 423
Cdd:cd06632    88 SIHK--LLQRYGAFEEPVIRlYTRQILSGLAYLHSRNTVHRDIKGANIL-VDTNG-VVKLADFGMAKHVEAFSFAKSFKG 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 424 TPEFVAPEVIN--YEPIGYATDMWSIGVICYILVSGLSPFmgdNDNETLANVTSATWDFDDEAF-DEISDDAKDFISNLL 500
Cdd:cd06632   164 SPYWMAPEVIMqkNSGYGLAVDIWSLGCTVLEMATGKPPW---SQYEGVAAIFKIGNSGELPPIpDHLSPDAKDFIRLCL 240
                         250
                  ....*....|....*....
gi 1034633499 501 KKDMKNRLDCTQCLQHPWL 519
Cdd:cd06632   241 QRDPEDRPTASQLLEHPFV 259
STKc_Mnk2 cd14173
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
262-519 2.30e-37

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: 141.32  E-value: 2.30e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 262 DFYDI-EERLGSGKFGQVFRLVEKKTRKVWAGKFFKAYSAKEKENIRQEISIM-NCLHHPKLVQCVDAFEEKANIVMVLE 339
Cdd:cd14173     1 DVYQLqEEVLGEGAYARVQTCINLITNKEYAVKIIEKRPGHSRSRVFREVEMLyQCQGHRNVLELIEFFEEEDKFYLVFE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 340 IVSGGELFERIiDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKTG-TRIKLIDFGLARRLE----- 413
Cdd:cd14173    81 KMRGGSILSHI-HRRRHFNELEASVVVQDIASALDFLHNKGIAHRDLKPENILCEHPNQvSPVKICDFDLGSGIKlnsdc 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 414 ---NAGSLKVLFGTPEFVAPEVI---NYEPIGY--ATDMWSIGVICYILVSGLSPFMGDN---------------DNETL 470
Cdd:cd14173   160 spiSTPELLTPCGSAEYMAPEVVeafNEEASIYdkRCDLWSLGVILYIMLSGYPPFVGRCgsdcgwdrgeacpacQNMLF 239
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1034633499 471 ANVTSATWDFDDEAFDEISDDAKDFISNLLKKDMKNRLDCTQCLQHPWL 519
Cdd:cd14173   240 ESIQEGKYEFPEKDWAHISCAAKDLISKLLVRDAKQRLSAAQVLQHPWV 288
STKc_Yank1 cd05578
Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the ...
271-519 3.24e-37

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: 139.70  E-value: 3.24e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 271 GSGKFGQVFRLVEKKTRKVWAGKffkaYSAKEK-------ENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEIVSG 343
Cdd:cd05578     9 GKGSFGKVCIVQKKDTKKMFAMK----YMNKQKciekdsvRNVLNELEILQELEHPFLVNLWYSFQDEEDMYMVVDLLLG 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 344 GELfeRI-IDEDFELTErECIK-YMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGtRIKLIDFGLARRLENAGSLKVL 421
Cdd:cd05578    85 GDL--RYhLQQKVKFSE-ETVKfYICEIVLALDYLHSKNIIHRDIKPDNIL-LDEQG-HVHITDFNIATKLTDGTLATST 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 422 FGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGdNDNETLANVT----------SATWdfddeafdeiSDD 491
Cdd:cd05578   160 SGTKPYMAPEVFMRAGYSFAVDWWSLGVTAYEMLRGKRPYEI-HSRTSIEEIRakfetasvlyPAGW----------SEE 228
                         250       260
                  ....*....|....*....|....*....
gi 1034633499 492 AKDFISNLLKKDMKNRLDCTQCLQ-HPWL 519
Cdd:cd05578   229 AIDLINKLLERDPQKRLGDLSDLKnHPYF 257
STKc_PLK2 cd14188
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the ...
270-516 5.55e-37

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: 139.38  E-value: 5.55e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 270 LGSGKFGQVFRLVEKKTRKVWAGKFF---KAYSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEIVSGGEL 346
Cdd:cd14188     9 LGKGGFAKCYEMTDLTTNKVYAAKIIphsRVSKPHQREKIDKEIELHRILHHKHVVQFYHYFEDKENIYILLEYCSRRSM 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 347 fERIIDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTgTRIKLIDFGLARRLENAGSL-KVLFGTP 425
Cdd:cd14188    89 -AHILKARKVLTEPEVRYYLRQIVSGLKYLHEQEILHRDLKLGNFF-INEN-MELKVGDFGLAARLEPLEHRrRTICGTP 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 426 EFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDFDdeafDEISDDAKDFISNLLKKDMK 505
Cdd:cd14188   166 NYLSPEVLNKQGHGCESDIWALGCVMYTMLLGRPPFETTNLKETYRCIREARYSLP----SSLLAPAKHLIASMLSKNPE 241
                         250
                  ....*....|.
gi 1034633499 506 NRLDCTQCLQH 516
Cdd:cd14188   242 DRPSLDEIIRH 252
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
264-519 9.06e-37

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: 139.37  E-value: 9.06e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 264 YDIEERLGSGKFGQVFRLVEKKTRKVWAGKFFK-AYSAKE-KENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEIV 341
Cdd:cd07833     3 YEVLGVVGEGAYGVVLKCRNKATGEIVAIKKFKeSEDDEDvKKTALREVKVLRQLRHENIVNLKEAFRRKGRLYLVFEYV 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 342 sggelfERIIDEDFELT----ERECIK-YMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGTrIKLIDFGLARRLE--N 414
Cdd:cd07833    83 ------ERTLLELLEASpgglPPDAVRsYIWQLLQAIAYCHSHNIIHRDIKPENIL-VSESGV-LKLCDFGFARALTarP 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 415 AGSLKVLFGTPEFVAPEV-INYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNE-------TLANVTSA-TWDFDD--- 482
Cdd:cd07833   155 ASPLTDYVATRWYRAPELlVGDTNYGKPVDVWAIGCIMAELLDGEPLFPGDSDIDqlyliqkCLGPLPPShQELFSSnpr 234
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1034633499 483 ---EAFDEI--------------SDDAKDFISNLLKKDMKNRLDCTQCLQHPWL 519
Cdd:cd07833   235 fagVAFPEPsqpeslerrypgkvSSPALDFLKACLRMDPKERLTCDELLQHPYF 288
STKc_PASK cd14004
Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs ...
264-519 1.08e-36

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: 138.29  E-value: 1.08e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 264 YDIEERLGSGKFGQVFRLVEKKTRKVWAGKFFKaysaKEK------------ENIRQEISIMNCLH---HPKLVQCVDAF 328
Cdd:cd14004     2 YTILKEMGEGAYGQVNLAIYKSKGKEVVIKFIF----KERilvdtwvrdrklGTVPLEIHILDTLNkrsHPNIVKLLDFF 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 329 EEKANIVMVLEIV-SGGELFERIiDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGTrIKLIDFG 407
Cdd:cd14004    78 EDDEFYYLVMEKHgSGMDLFDFI-ERKPNMDEKEAKYIFRQVADAVKHLHDQGIVHRDIKDENVI-LDGNGT-IKLIDFG 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 408 LARRLENaGSLKVLFGTPEFVAPEVINYEP-IGYATDMWSIGVICYILVSGLSPFMgdNDNETLanvtsatwDFDDEAFD 486
Cdd:cd14004   155 SAAYIKS-GPFDTFVGTIDYAAPEVLRGNPyGGKEQDIWALGVLLYTLVFKENPFY--NIEEIL--------EADLRIPY 223
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1034633499 487 EISDDAKDFISNLLKKDMKNRLDCTQCLQHPWL 519
Cdd:cd14004   224 AVSEDLIDLISRMLNRDVGDRPTIEELLTDPWL 256
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
264-518 1.15e-36

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: 139.63  E-value: 1.15e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 264 YDIEERLGSGKFGQVFRLVEKKTRKVWAGKFFKA---YSAKEKEN---IRqEISIMNCLHHPKLVQCVDAFEEKANIVMV 337
Cdd:cd07841     2 YEKGKKLGEGTYAVVYKARDKETGRIVAIKKIKLgerKEAKDGINftaLR-EIKLLQELKHPNIIGLLDVFGHKSNINLV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 338 LEIVSGgELfERII-DEDFELTEREcIK-YMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGTrIKLIDFGLARRlena 415
Cdd:cd07841    81 FEFMET-DL-EKVIkDKSIVLTPAD-IKsYMLMTLRGLEYLHSNWILHRDLKPNNLL-IASDGV-LKLADFGLARS---- 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 416 gslkvlFGTP-EFVAPEVIN--YEP---------IGYATDMWSIGVICYILVSGLSPFMGDNDNETLANV-------TSA 476
Cdd:cd07841   152 ------FGSPnRKMTHQVVTrwYRApellfgarhYGVGVDMWSVGCIFAELLLRVPFLPGDSDIDQLGKIfealgtpTEE 225
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 477 TW------------------DFDDEaFDEISDDAKDFISNLLKKDMKNRLDCTQCLQHPW 518
Cdd:cd07841   226 NWpgvtslpdyvefkpfpptPLKQI-FPAASDDALDLLQRLLTLNPNKRITARQALEHPY 284
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
270-519 2.97e-36

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: 137.44  E-value: 2.97e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 270 LGSGKFGQVfRLVEKK---TRKVWAGKFFKAYSAKEKEN-----IRQEISIMNCLHHPKLVQCVDAF-EEKANIVMVLEI 340
Cdd:cd13994     1 IGKGATSVV-RIVTKKnprSGVLYAVKEYRRRDDESKRKdyvkrLTSEYIISSKLHHPNIVKVLDLCqDLHGKWCLVMEY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 341 VSGGELFERIIDED-FELTERECikYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGTrIKLIDFGLARRLENAGSLK 419
Cdd:cd13994    80 CPGGDLFTLIEKADsLSLEEKDC--FFKQILRGVAYLHSHGIAHRDLKPENIL-LDEDGV-LKLTDFGTAEVFGMPAEKE 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 420 V-----LFGTPEFVAPEVinYEPIGY---ATDMWSIGVICYILVSGLSPF-MGDNDNETLANVTSA---TWDFDDEAFDE 487
Cdd:cd13994   156 SpmsagLCGSEPYMAPEV--FTSGSYdgrAVDVWSCGIVLFALFTGRFPWrSAKKSDSAYKAYEKSgdfTNGPYEPIENL 233
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1034633499 488 ISDDAKDFISNLLKKDMKNRLDCTQCLQHPWL 519
Cdd:cd13994   234 LPSECRRLIYRMLHPDPEKRITIDEALNDPWV 265
I-set pfam07679
Immunoglobulin I-set domain;
609-699 3.35e-36

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 131.23  E-value: 3.35e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 609 PYFSKTIRDLEVVEGSAARFDCKIEGYPDPEVVWFKDDQSIRESRHFQIDYDeDGNCSLIISDVCGDDDAKYTCKAVNSL 688
Cdd:pfam07679   1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYE-GGTYTLTISNVQPDDSGKYTCVATNSA 79
                          90
                  ....*....|.
gi 1034633499 689 GEATCTAELIV 699
Cdd:pfam07679  80 GEAEASAELTV 90
STKc_Aurora-B_like cd14117
Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs ...
262-524 3.69e-36

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: 137.30  E-value: 3.69e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 262 DFYDIEERLGSGKFGQVFRLVEKKTRKVWAGK-FFKAYSAKE--KENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVL 338
Cdd:cd14117     6 DDFDIGRPLGKGKFGNVYLAREKQSKFIVALKvLFKSQIEKEgvEHQLRREIEIQSHLRHPNILRLYNYFHDRKRIYLIL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 339 EIVSGGELFERIiDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKTgtRIKLIDFGLArrlENAGSL 418
Cdd:cd14117    86 EYAPRGELYKEL-QKHGRFDEQRTATFMEELADALHYCHEKKVIHRDIKPENLLMGYKG--ELKIADFGWS---VHAPSL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 419 --KVLFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDFDdeafDEISDDAKDFI 496
Cdd:cd14117   160 rrRTMCGTLDYLPPEMIEGRTHDEKVDLWCIGVLCYELLVGMPPFESASHTETYRRIVKVDLKFP----PFLSDGSRDLI 235
                         250       260
                  ....*....|....*....|....*...
gi 1034633499 497 SNLLKKDMKNRLDCTQCLQHPWLMKDTK 524
Cdd:cd14117   236 SKLLRYHPSERLPLKGVMEHPWVKANSR 263
STKc_Unc-89_rpt2 cd14112
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Uncoordinated ...
260-519 3.83e-36

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: 136.89  E-value: 3.83e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 260 VSDFYDIEERLGSGKFGQVFRLVEKKTR--KVWAGKFFKAYSakEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMV 337
Cdd:cd14112     1 PTGRFSFGSEIFRGRFSVIVKAVDSTTEtdAHCAVKIFEVSD--EASEAVREFESLRTLQHENVQRLIAAFKPSNFAYLV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 338 LEIVSGgELFERIIDEDfELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKTGTRIKLIDFGLARRLENAGS 417
Cdd:cd14112    79 MEKLQE-DVFTRFSSND-YYSEEQVATTVRQILDALHYLHFKGIAHLDVQPDNIMFQSVRSWQVKLVDFGRAQKVSKLGK 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 418 LKVLFGTpEFVAPEVINYE-PIGYATDMWSIGVICYILVSGLSPFMG--DNDNETLANVTSATWDFDDeAFDEISDDAKD 494
Cdd:cd14112   157 VPVDGDT-DWASPEFHNPEtPITVQSDIWGLGVLTFCLLSGFHPFTSeyDDEEETKENVIFVKCRPNL-IFVEATQEALR 234
                         250       260
                  ....*....|....*....|....*
gi 1034633499 495 FISNLLKKDMKNRLDCTQCLQHPWL 519
Cdd:cd14112   235 FATWALKKSPTRRMRTDEALEHRWL 259
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
270-518 4.19e-36

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: 136.72  E-value: 4.19e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 270 LGSGKFGQVFRLVEKKTRKVWAGKFFK-----AYSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEIVSGG 344
Cdd:cd06625     8 LGQGAFGQVYLCYDADTGRELAVKQVEidpinTEASKEVKALECEIQLLKNLQHERIVQYYGCLQDEKSLSIFMEYMPGG 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 345 ELFERIIDEDfELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGTrIKLIDFGLARRLE---NAGSLKVL 421
Cdd:cd06625    88 SVKDEIKAYG-ALTENVTRKYTRQILEGLAYLHSNMIVHRDIKGANIL-RDSNGN-VKLGDFGASKRLQticSSTGMKSV 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 422 FGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFmgdNDNETLANVTS-ATWDFDDEAFDEISDDAKDFISNLL 500
Cdd:cd06625   165 TGTPYWMSPEVINGEGYGRKADIWSVGCTVVEMLTTKPPW---AEFEPMAAIFKiATQPTNPQLPPHVSEDARDFLSLIF 241
                         250
                  ....*....|....*...
gi 1034633499 501 KKDMKNRLDCTQCLQHPW 518
Cdd:cd06625   242 VRNKKQRPSAEELLSHSF 259
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
264-519 4.31e-36

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: 136.63  E-value: 4.31e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 264 YDIEERLGSGKFGQVFRLVEKKTRKVWAGK-FFKAYSAKE--KENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEI 340
Cdd:cd14116     7 FEIGRPLGKGKFGNVYLAREKQSKFILALKvLFKAQLEKAgvEHQLRREVEIQSHLRHPNILRLYGYFHDATRVYLILEY 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 341 VSGGELFeRIIDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCvnKTGTRIKLIDFGLARRLENAgSLKV 420
Cdd:cd14116    87 APLGTVY-RELQKLSKFDEQRTATYITELANALSYCHSKRVIHRDIKPENLLL--GSAGELKIADFGWSVHAPSS-RRTT 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 421 LFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDFDdeafDEISDDAKDFISNLL 500
Cdd:cd14116   163 LCGTLDYLPPEMIEGRMHDEKVDLWSLGVLCYEFLVGKPPFEANTYQETYKRISRVEFTFP----DFVTEGARDLISRLL 238
                         250
                  ....*....|....*....
gi 1034633499 501 KKDMKNRLDCTQCLQHPWL 519
Cdd:cd14116   239 KHNPSQRPMLREVLEHPWI 257
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
264-519 2.80e-35

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: 134.92  E-value: 2.80e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 264 YDIEERLGSGKFGQVFRLVEKKTRKVWAGKFFKaySAKEKENI-----RqEISIMNCLHHPKLVQCVDAFEEKANIVMVL 338
Cdd:cd07829     1 YEKLEKLGEGTYGVVYKAKDKKTGEIVALKKIR--LDNEEEGIpstalR-EISLLKELKHPNIVKLLDVIHTENKLYLVF 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 339 EIVSggELFERIIDE-DFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGTrIKLIDFGLARrlenags 417
Cdd:cd07829    78 EYCD--QDLKKYLDKrPGPLPPNLIKSIMYQLLRGLAYCHSHRILHRDLKPQNLL-INRDGV-LKLADFGLAR------- 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 418 lkvLFG------TPEFV-----APEVI----NYepiGYATDMWSIGVICYILVSGLSPFMGDNDNETLANV-------TS 475
Cdd:cd07829   147 ---AFGiplrtyTHEVVtlwyrAPEILlgskHY---STAVDIWSVGCIFAELITGKPLFPGDSEIDQLFKIfqilgtpTE 220
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034633499 476 ATW-DFDD-----------------EAFDEISDDAKDFISNLLKKDMKNRLDCTQCLQHPWL 519
Cdd:cd07829   221 ESWpGVTKlpdykptfpkwpkndleKVLPRLDPEGIDLLSKMLQYNPAKRISAKEALKHPYF 282
STKc_SIK cd14071
Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the ...
263-519 4.10e-35

Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SIKs are part of a complex network that regulates Na,K-ATPase to maintain sodium homeostasis and blood pressure. Vertebrates contain three forms of SIKs (SIK1-3) from three distinct genes, which display tissue-specific effects. SIK1, also called SNF1LK, controls steroidogenic enzyme production in adrenocortical cells. In the brain, both SIK1 and SIK2 regulate energy metabolism. SIK2, also called QIK or SNF1LK2, is involved in the regulation of gluconeogenesis in the liver and lipogenesis in adipose tissues, where it phosphorylates the insulin receptor substrate-1. In the liver, SIK3 (also called QSK) regulates cholesterol and bile acid metabolism. In addition, SIK2 plays an important role in the initiation of mitosis and regulates the localization of C-Nap1, a centrosome linker protein. The SIK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270973 [Multi-domain]  Cd Length: 253  Bit Score: 133.67  E-value: 4.10e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 263 FYDIEERLGSGKFGQVFRLVEKKTRKVWAGKFFKAySAKEKEN---IRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLE 339
Cdd:cd14071     1 FYDIERTIGKGNFAVVKLARHRITKTEVAIKIIDK-SQLDEENlkkIYREVQIMKMLNHPHIIKLYQVMETKDMLYLVTE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 340 IVSGGELFERIIDEDfELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKTGtrIKLIDFGLARRLENAGSLK 419
Cdd:cd14071    80 YASNGEIFDYLAQHG-RMSEKEARKKFWQILSAVEYCHKRHIVHRDLKAENLLLDANMN--IKIADFGFSNFFKPGELLK 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 420 VLFGTPEFVAPEVIN---YEpiGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATwdFDDEAFdeISDDAKDFI 496
Cdd:cd14071   157 TWCGSPPYAAPEVFEgkeYE--GPQLDIWSLGVVLYVLVCGALPFDGSTLQTLRDRVLSGR--FRIPFF--MSTDCEHLI 230
                         250       260
                  ....*....|....*....|...
gi 1034633499 497 SNLLKKDMKNRLDCTQCLQHPWL 519
Cdd:cd14071   231 RRMLVLDPSKRLTIEQIKKHKWM 253
STKc_MSK1_N cd05613
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
264-531 6.65e-35

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: 134.36  E-value: 6.65e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 264 YDIEERLGSGKFGQVFrLVEK----KTRKVWAGKFFKAYS----AKEKENIRQEISIMNCLHH-PKLVQCVDAFEEKANI 334
Cdd:cd05613     2 FELLKVLGTGAYGKVF-LVRKvsghDAGKLYAMKVLKKATivqkAKTAEHTRTERQVLEHIRQsPFLVTLHYAFQTDTKL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 335 VMVLEIVSGGELFERIIDEDfELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGtRIKLIDFGLARRL-- 412
Cdd:cd05613    81 HLILDYINGGELFTHLSQRE-RFTENEVQIYIGEIVLALEHLHKLGIIYRDIKLENIL-LDSSG-HVVLTDFGLSKEFll 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 413 -ENAGSLKVLfGTPEFVAPEVINYEPIGY--ATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDFDDEAFDEIS 489
Cdd:cd05613   158 dENERAYSFC-GTIEYMAPEIVRGGDSGHdkAVDWWSLGVLMYELLTGASPFTVDGEKNSQAEISRRILKSEPPYPQEMS 236
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1034633499 490 DDAKDFISNLLKKDMKNRL-----DCTQCLQHPWLMK-DTKNMEAKKL 531
Cdd:cd05613   237 ALAKDIIQRLLMKDPKKRLgcgpnGADEIKKHPFFQKiNWDDLAAKKV 284
STKc_MSK2_C cd14180
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
267-519 9.80e-35

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: 134.23  E-value: 9.80e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 267 EERLGSGKFGQVFRLVEKKTRKVWAgkfFKAYSAKEKENIRQEISIMN-CLHHPKLVQCVDAFEEKANIVMVLEIVSGGE 345
Cdd:cd14180    11 EPALGEGSFSVCRKCRHRQSGQEYA---VKIISRRMEANTQREVAALRlCQSHPNIVALHEVLHDQYHTYLVMELLRGGE 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 346 LFERIIDEDFeLTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKT-GTRIKLIDFGLAR-RLENAGSLKVLFG 423
Cdd:cd14180    88 LLDRIKKKAR-FSESEASQLMRSLVSAVSFMHEAGVVHRDLKPENILYADESdGAVLKVIDFGFARlRPQGSRPLQTPCF 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 424 TPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDN-------ETLANVTSATWDFDDEAFDEISDDAKDFI 496
Cdd:cd14180   167 TLQYAAPELFSNQGYDESCDLWSLGVILYTMLSGQVPFQSKRGKmfhnhaaDIMHKIKEGDFSLEGEAWKGVSEEAKDLV 246
                         250       260
                  ....*....|....*....|...
gi 1034633499 497 SNLLKKDMKNRLDCTQCLQHPWL 519
Cdd:cd14180   247 RGLLTVDPAKRLKLSELRESDWL 269
STKc_PKB cd05571
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer ...
270-518 1.25e-34

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: 134.41  E-value: 1.25e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 270 LGSGKFGQVFRLVEKKTRKVWAGKFFKAYSAKEKENIRQ---EISIMNCLHHPKLVQCVDAFEEKANIVMVLEIVSGGEL 346
Cdd:cd05571     3 LGKGTFGKVILCREKATGELYAIKILKKEVIIAKDEVAHtltENRVLQNTRHPFLTSLKYSFQTNDRLCFVMEYVNGGEL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 347 F-----ERIIDED---FelterecikYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGtRIKLIDFGLARRLENAGSL 418
Cdd:cd05571    83 FfhlsrERVFSEDrtrF---------YGAEIVLALGYLHSQGIVYRDLKLENLL-LDKDG-HIKITDFGLCKEEISYGAT 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 419 KVLF-GTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMgDNDNETLANVTSAtwdfDDEAF-DEISDDAKDFI 496
Cdd:cd05571   152 TKTFcGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFY-NRDHEVLFELILM----EEVRFpSTLSPEAKSLL 226
                         250       260
                  ....*....|....*....|....*..
gi 1034633499 497 SNLLKKDMKNRL-----DCTQCLQHPW 518
Cdd:cd05571   227 AGLLKKDPKKRLgggprDAKEIMEHPF 253
STKc_MSK_N cd05583
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
270-518 1.60e-34

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


Pssm-ID: 270735 [Multi-domain]  Cd Length: 268  Bit Score: 132.52  E-value: 1.60e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 270 LGSGKFGQVFrLVEKKTR----KVWAGKFFKAYS----AKEKENIRQEISIMNCLHH-PKLVQCVDAFEEKANIVMVLEI 340
Cdd:cd05583     2 LGTGAYGKVF-LVRKVGGhdagKLYAMKVLKKATivqkAKTAEHTMTERQVLEAVRQsPFLVTLHYAFQTDAKLHLILDY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 341 VSGGELFERIID-EDFelTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGtRIKLIDFGLARRLENaGSLK 419
Cdd:cd05583    81 VNGGELFTHLYQrEHF--TESEVRIYIGEIVLALEHLHKLGIIYRDIKLENIL-LDSEG-HVVLTDFGLSKEFLP-GEND 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 420 VLF---GTPEFVAPEVINYEPIGY--ATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDFDDEAFDEISDDAKD 494
Cdd:cd05583   156 RAYsfcGTIEYMAPEVVRGGSDGHdkAVDWWSLGVLTYELLTGASPFTVDGERNSQSEISKRILKSHPPIPKTFSAEAKD 235
                         250       260
                  ....*....|....*....|....*....
gi 1034633499 495 FISNLLKKDMKNRLDC-----TQCLQHPW 518
Cdd:cd05583   236 FILKLLEKDPKKRLGAgprgaHEIKEHPF 264
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
264-515 1.68e-34

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: 132.39  E-value: 1.68e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 264 YDIEERLGSGKFGQVFRLVEKKTRKVWAGK---FFKAYSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEI 340
Cdd:cd08224     2 YEIEKKIGKGQFSVVYRARCLLDGRLVALKkvqIFEMMDAKARQDCLKEIDLLQQLNHPNIIKYLASFIENNELNIVLEL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 341 VSGGELfERII----DEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGTrIKLIDFGLARRLEN-- 414
Cdd:cd08224    82 ADAGDL-SRLIkhfkKQKRLIPERTIWKYFVQLCSALEHMHSKRIMHRDIKPANVF-ITANGV-VKLGDLGLGRFFSSkt 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 415 --AGSLkvlFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDN--ETLANVTSAtwDFDDEAFDEISD 490
Cdd:cd08224   159 taAHSL---VGTPYYMSPERIREQGYDFKSDIWSLGCLLYEMAALQSPFYGEKMNlySLCKKIEKC--EYPPLPADLYSQ 233
                         250       260
                  ....*....|....*....|....*
gi 1034633499 491 DAKDFISNLLKKDMKNRLDCTQCLQ 515
Cdd:cd08224   234 ELRDLVAACIQPDPEKRPDISYVLD 258
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
264-519 3.09e-34

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: 132.45  E-value: 3.09e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 264 YDIEERLGSGKFGQVFRLVEKKTRKVWAGKffKAYSAKEKENI-----RQEISIMNCLHHPKLVQCVDAFEEKANIVMVL 338
Cdd:cd07832     2 YKILGRIGEGAHGIVFKAKDRETGETVALK--KVALRKLEGGIpnqalREIKALQACQGHPYVVKLRDVFPHGTGFVLVF 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 339 EIVsGGELFERIIDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGTrIKLIDFGLARRLENAG-- 416
Cdd:cd07832    80 EYM-LSSLSEVLRDEERPLTEAQVKRYMRMLLKGVAYMHANRIMHRDLKPANLL-ISSTGV-LKIADFGLARLFSEEDpr 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 417 --SLKVlfGTPEFVAPEVI----NYEPigyATDMWSIGVICYILVSGLSPFMGDNDNETLANV-------TSATW----- 478
Cdd:cd07832   157 lySHQV--ATRWYRAPELLygsrKYDE---GVDLWAVGCIFAELLNGSPLFPGENDIEQLAIVlrtlgtpNEKTWpelts 231
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1034633499 479 --DFD------------DEAFDEISDDAKDFISNLLKKDMKNRLDCTQCLQHPWL 519
Cdd:cd07832   232 lpDYNkitfpeskgirlEEIFPDCSPEAIDLLKGLLVYNPKKRLSAEEALRHPYF 286
STKc_SnRK2-3 cd14665
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
264-518 3.35e-34

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


Pssm-ID: 271135 [Multi-domain]  Cd Length: 257  Bit Score: 131.26  E-value: 3.35e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 264 YDIEERLGSGKFGQVFRLVEKKTRKVWAGKFFKAySAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEIVSG 343
Cdd:cd14665     2 YELVKDIGSGNFGVARLMRDKQTKELVAVKYIER-GEKIDENVQREIINHRSLRHPNIVRFKEVILTPTHLAIVMEYAAG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 344 GELFERIIDEDfELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKTGTRIKLIDFGLARRLENAGSLKVLFG 423
Cdd:cd14665    81 GELFERICNAG-RFSEDEARFFFQQLISGVSYCHSMQICHRDLKLENTLLDGSPAPRLKICDFGYSKSSVLHSQPKSTVG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 424 TPEFVAPEVI-NYEPIGYATDMWSIGVICYILVSGLSPFMGDND----NETLANVTSATWDFDDEAfdEISDDAKDFISN 498
Cdd:cd14665   160 TPAYIAPEVLlKKEYDGKIADVWSCGVTLYVMLVGAYPFEDPEEprnfRKTIQRILSVQYSIPDYV--HISPECRHLISR 237
                         250       260
                  ....*....|....*....|
gi 1034633499 499 LLKKDMKNRLDCTQCLQHPW 518
Cdd:cd14665   238 IFVADPATRITIPEIRNHEW 257
STKc_CRIK cd05601
Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze ...
261-517 3.67e-34

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: 133.20  E-value: 3.67e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 261 SDFyDIEERLGSGKFGQVFRLVEKKTRKVWAGKFFKAYSAKEKENI---RQEISIMNCLHHPKLVQCVDAFEEKANIVMV 337
Cdd:cd05601     1 KDF-EVKNVIGRGHFGEVQVVKEKATGDIYAMKVLKKSETLAQEEVsffEEERDIMAKANSPWITKLQYAFQDSENLYLV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 338 LEIVSGGELFERIIDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGtRIKLIDFGLARRLENAGS 417
Cdd:cd05601    80 MEYHPGGDLLSLLSRYDDIFEESMARFYLAELVLAIHSLHSMGYVHRDIKPENIL-IDRTG-HIKLADFGSAAKLSSDKT 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 418 L--KVLFGTPEFVAPEV---INYEPIGY---ATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDFDDEAFDEIS 489
Cdd:cd05601   158 VtsKMPVGTPDYIAPEVltsMNGGSKGTygvECDWWSLGIVAYEMLYGKTPFTEDTVIKTYSNIMNFKKFLKFPEDPKVS 237
                         250       260
                  ....*....|....*....|....*...
gi 1034633499 490 DDAKDFISNLLkKDMKNRLDCTQCLQHP 517
Cdd:cd05601   238 ESAVDLIKGLL-TDAKERLGYEGLCCHP 264
STKc_PLK4 cd14186
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the ...
264-519 4.71e-34

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: 130.75  E-value: 4.71e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 264 YDIEERLGSGKFGQVFRLVEKKTRKVWAGKFF--KA-YSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEI 340
Cdd:cd14186     3 FKVLNLLGKGSFACVYRARSLHTGLEVAIKMIdkKAmQKAGMVQRVRNEVEIHCQLKHPSILELYNYFEDSNYVYLVLEM 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 341 VSGGELFERIIDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCvnKTGTRIKLIDFGLARRLENAGSLK- 419
Cdd:cd14186    83 CHNGEMSRYLKNRKKPFTEDEARHFMHQIVTGMLYLHSHGILHRDLTLSNLLL--TRNMNIKIADFGLATQLKMPHEKHf 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 420 VLFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSAtwdfDDEAFDEISDDAKDFISNL 499
Cdd:cd14186   161 TMCGTPNYISPEIATRSAHGLESDVWSLGCMFYTLLVGRPPFDTDTVKNTLNKVVLA----DYEMPAFLSREAQDLIHQL 236
                         250       260
                  ....*....|....*....|
gi 1034633499 500 LKKDMKNRLDCTQCLQHPWL 519
Cdd:cd14186   237 LRKNPADRLSLSSVLDHPFM 256
STKc_RSK_N cd05582
N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; ...
270-508 5.07e-34

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: 132.52  E-value: 5.07e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 270 LGSGKFGQVFrLVEKKTRK----VWAGKFFKAYSAKEKENIRQ--EISIMNCLHHPKLVQCVDAFEEKANIVMVLEIVSG 343
Cdd:cd05582     3 LGQGSFGKVF-LVRKITGPdagtLYAMKVLKKATLKVRDRVRTkmERDILADVNHPFIVKLHYAFQTEGKLYLILDFLRG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 344 GELFERIIDEdFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGtRIKLIDFGLARR-LENAGSLKVLF 422
Cdd:cd05582    82 GDLFTRLSKE-VMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENIL-LDEDG-HIKLTDFGLSKEsIDHEKKAYSFC 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 423 GTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDFDdeafDEISDDAKDFISNLLKK 502
Cdd:cd05582   159 GTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGSLPFQGKDRKETMTMILKAKLGMP----QFLSPEAQSLLRALFKR 234

                  ....*.
gi 1034633499 503 DMKNRL 508
Cdd:cd05582   235 NPANRL 240
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
273-518 6.90e-34

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: 130.68  E-value: 6.90e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 273 GKFGQVFRLVEKKTRKVWAGKFFKAYS--AKEK-ENIRQEISI-MNCLHHPKLVQCVDAFEEKANIVMVLEIVSGGELfE 348
Cdd:cd05611     7 GAFGSVYLAKKRSTGDYFAIKVLKKSDmiAKNQvTNVKAERAImMIQGESPYVAKLYYSFQSKDYLYLVMEYLNGGDC-A 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 349 RIIDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENiMCVNKTGtRIKLIDFGLARRLENAGSLKVLFGTPEFV 428
Cdd:cd05611    86 SLIKTLGGLPEDWAKQYIAEVVLGVEDLHQRGIIHRDIKPEN-LLIDQTG-HLKLTDFGLSRNGLEKRHNKKFVGTPDYL 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 429 APEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDFDDEAFDEISDDAKDFISNLLKKDMKNRL 508
Cdd:cd05611   164 APETILGVGDDKMSDWWSLGCVIFEFLFGYPPFHAETPDAVFDNILSRRINWPEEVKEFCSPEAVDLINRLLCMDPAKRL 243
                         250
                  ....*....|...
gi 1034633499 509 DCT---QCLQHPW 518
Cdd:cd05611   244 GANgyqEIKSHPF 256
STKc_MAST cd05609
Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine ...
273-520 9.71e-34

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: 130.60  E-value: 9.71e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 273 GKFGQVFRLVEKKTRKVWAGKFFKAYSAKEKENIRQ---EISIMNCLHHPKLVQCVDAFEEKANIVMVLEIVSGGE---L 346
Cdd:cd05609    11 GAYGAVYLVRHRETRQRFAMKKINKQNLILRNQIQQvfvERDILTFAENPFVVSMYCSFETKRHLCMVMEYVEGGDcatL 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 347 FERIIDEDFELTERecikYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGtRIKLIDFGLAR-----RLENA--GSL- 418
Cdd:cd05609    91 LKNIGPLPVDMARM----YFAETVLALEYLHSYGIVHRDLKPDNLL-ITSMG-HIKLTDFGLSKiglmsLTTNLyeGHIe 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 419 --------KVLFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDFDDEAfDEISD 490
Cdd:cd05609   165 kdtrefldKQVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVISDEIEWPEGD-DALPD 243
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1034633499 491 DAKDFISNLLKKDMKNRL---DCTQCLQHPWLM 520
Cdd:cd05609   244 DAQDLITRLLQQNPLERLgtgGAEEVKQHPFFQ 276
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
264-510 1.07e-33

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: 131.02  E-value: 1.07e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 264 YDIEERLGSGKFGQVFRLVEKKTRKVWAGKFFK---AYSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEI 340
Cdd:cd05612     3 FERIKTIGTGTFGRVHLVRDRISEHYYALKVMAipeVIRLKQEQHVHNEKRVLKEVSHPFIIRLFWTEHDQRFLYMLMEY 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 341 VSGGELFERIIDEDfELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGtRIKLIDFGLARRLENagSLKV 420
Cdd:cd05612    83 VPGGELFSYLRNSG-RFSNSTGLFYASEIVCALEYLHSKEIVYRDLKPENIL-LDKEG-HIKLTDFGFAKKLRD--RTWT 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 421 LFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDFdDEAFDEIsddAKDFISNLL 500
Cdd:cd05612   158 LCGTPEYLAPEVIQSKGHNKAVDWWALGILIYEMLVGYPPFFDDNPFGIYEKILAGKLEF-PRHLDLY---AKDLIKKLL 233
                         250
                  ....*....|
gi 1034633499 501 KKDMKNRLDC 510
Cdd:cd05612   234 VVDRTRRLGN 243
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
264-517 1.17e-33

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: 129.82  E-value: 1.17e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 264 YDIEERLGSGKFGQVFRLVEKKTRKVWAGKFFK--AYSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEIV 341
Cdd:cd08530     2 FKVLKKLGKGSYGSVYKVKRLSDNQVYALKEVNlgSLSQKEREDSVNEIRLLASVNHPNIIRYKEAFLDGNRLCIVMEYA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 342 SGGELFERIIDEDFE---LTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNktGTRIKLIDFGLARRLENaGSL 418
Cdd:cd08530    82 PFGDLSKLISKRKKKrrlFPEDDIWRIFIQMLRGLKALHDQKILHRDLKSANILLSA--GDLVKIGDLGISKVLKK-NLA 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 419 KVLFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDFDDEAFdeiSDDAKDFISN 498
Cdd:cd08530   159 KTQIGTPLYAAPEVWKGRPYDYKSDIWSLGCLLYEMATFRPPFEARTMQELRYKVCRGKFPPIPPVY---SQDLQQIIRS 235
                         250
                  ....*....|....*....
gi 1034633499 499 LLKKDMKNRLDCTQCLQHP 517
Cdd:cd08530   236 LLQVNPKKRPSCDKLLQSP 254
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
309-519 1.92e-33

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: 129.34  E-value: 1.92e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 309 EISIMNCLHHPKLVQCVDAFEEKANIVMVLEIVSGGELFERIIDEDFeLTERECIKYMRQISEGVEYIHKQGIVHLDLKP 388
Cdd:cd14162    50 EIEVIKGLKHPNLICFYEAIETTSRVYIIMELAENGDLLDYIRKNGA-LPEPQARRWFRQLVAGVEYCHSKGVVHRDLKC 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 389 ENIMcVNKTGtRIKLIDFGLARR-LENAGSLKVLF----GTPEFVAPEV---INYEPigYATDMWSIGVICYILVSGLSP 460
Cdd:cd14162   129 ENLL-LDKNN-NLKITDFGFARGvMKTKDGKPKLSetycGSYAYASPEIlrgIPYDP--FLSDIWSMGVVLYTMVYGRLP 204
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 461 FmgDNDN-ETLANVTSATWDFddEAFDEISDDAKDFISNLLKKdMKNRLDCTQCLQHPWL 519
Cdd:cd14162   205 F--DDSNlKVLLKQVQRRVVF--PKNPTVSEECKDLILRMLSP-VKKRITIEEIKRDPWF 259
STKc_Sid2p_like cd05600
Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the ...
256-519 2.03e-33

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


Pssm-ID: 270751 [Multi-domain]  Cd Length: 386  Bit Score: 132.46  E-value: 2.03e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 256 TEQKVSDFyDIEERLGSGKFGQVFrLVEKK-TRKVWAGKFFKA---YSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEK 331
Cdd:cd05600     6 TRLKLSDF-QILTQVGQGGYGSVF-LARKKdTGEICALKIMKKkvlFKLNEVNHVLTERDILTTTNSPWLVKLLYAFQDP 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 332 ANIVMVLEIVSGGElFERIIDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGtRIKLIDFGLAR- 410
Cdd:cd05600    84 ENVYLAMEYVPGGD-FRTLLNNSGILSEEHARFYIAEMFAAISSLHQLGYIHRDLKPENFL-IDSSG-HIKLTDFGLASg 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 411 ------------RLENAGSLKVLF-------------------------GTPEFVAPEVINYEPIGYATDMWSIGVICYI 453
Cdd:cd05600   161 tlspkkiesmkiRLEEVKNTAFLEltakerrniyramrkedqnyansvvGSPDYMAPEVLRGEGYDLTVDYWSLGCILFE 240
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034633499 454 LVSGLSPFMGDNDNETLANVTS-------ATWDFDDEAFdEISDDAKDFISNLLkKDMKNRLDCTQCLQ-HPWL 519
Cdd:cd05600   241 CLVGFPPFSGSTPNETWANLYHwkktlqrPVYTDPDLEF-NLSDEAWDLITKLI-TDPQDRLQSPEQIKnHPFF 312
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
266-473 2.77e-33

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


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 128.80  E-value: 2.77e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499  266 IEERLGSGKFGQVFR-----LVEKKTRKVwAGKFFKA-YSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLE 339
Cdd:smart00219   3 LGKKLGEGAFGEVYKgklkgKGGKKKVEV-AVKTLKEdASEQQIEEFLREARIMRKLDHPNVVKLLGVCTEEEPLYIVME 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499  340 IVSGGELFERIIDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGTrIKLIDFGLARRLENaGSLK 419
Cdd:smart00219  82 YMEGGDLLSYLRKNRPKLSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCL-VGENLV-VKISDFGLSRDLYD-DDYY 158
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1034633499  420 VLFGTPEFV---APEVINYEPIGYATDMWSIGVICY-ILVSGLSPFMGDNDNETLANV 473
Cdd:smart00219 159 RKRGGKLPIrwmAPESLKEGKFTSKSDVWSFGVLLWeIFTLGEQPYPGMSNEEVLEYL 216
STKc_PKB_beta cd05595
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); ...
270-516 2.78e-33

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: 130.51  E-value: 2.78e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 270 LGSGKFGQVFRLVEKKTRKVWAGKFFKAYSAKEKENIRQEIS---IMNCLHHPKLVQCVDAFEEKANIVMVLEIVSGGEL 346
Cdd:cd05595     3 LGKGTFGKVILVREKATGRYYAMKILRKEVIIAKDEVAHTVTesrVLQNTRHPFLTALKYAFQTHDRLCFVMEYANGGEL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 347 F-----ERIIDEDfelterECIKYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGtRIKLIDFGLARR-LENAGSLKV 420
Cdd:cd05595    83 FfhlsrERVFTED------RARFYGAEIVSALEYLHSRDVVYRDIKLENLM-LDKDG-HIKITDFGLCKEgITDGATMKT 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 421 LFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMgDNDNETLanvtsatwdFDDEAFDEI------SDDAKD 494
Cdd:cd05595   155 FCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFY-NQDHERL---------FELILMEEIrfprtlSPEAKS 224
                         250       260
                  ....*....|....*....|....*..
gi 1034633499 495 FISNLLKKDMKNRL-----DCTQCLQH 516
Cdd:cd05595   225 LLAGLLKKDPKQRLgggpsDAKEVMEH 251
STKc_SLK cd06643
Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer ...
262-531 2.97e-33

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: 129.38  E-value: 2.97e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 262 DFYDIEERLGSGKFGQVFRLVEKKTRKVWAGKFFKAYSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEIV 341
Cdd:cd06643     5 DFWEIVGELGDGAFGKVYKAQNKETGILAAAKVIDTKSEEELEDYMVEIDILASCDHPNIVKLLDAFYYENNLWILIEFC 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 342 SGGELFERIIDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVnkTGTRIKLIDFGLARRleNAGSLK-- 419
Cdd:cd06643    85 AGGAVDAVMLELERPLTEPQIRVVCKQTLEALVYLHENKIIHRDLKAGNILFT--LDGDIKLADFGVSAK--NTRTLQrr 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 420 -VLFGTPEFVAPEVINYE-----PIGYATDMWSIGVICYILVS------GLSPF-----MGDNDNETLANvtSATWdfdd 482
Cdd:cd06643   161 dSFIGTPYWMAPEVVMCEtskdrPYDYKADVWSLGVTLIEMAQiepphhELNPMrvllkIAKSEPPTLAQ--PSRW---- 234
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1034633499 483 eafdeiSDDAKDFISNLLKKDMKNRLDCTQCLQHPWLMKDTKNMEAKKL 531
Cdd:cd06643   235 ------SPEFKDFLRKCLEKNVDARWTTSQLLQHPFVSVLVSNKPLREL 277
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
264-519 4.20e-33

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: 128.15  E-value: 4.20e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 264 YDIEERLGSGKFGQVFRLVEKKTRK--VWAGKFFKAYSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEIV 341
Cdd:cd08225     2 YEIIKKIGEGSFGKIYLAKAKSDSEhcVIKEIDLTKMPVKEKEASKKEVILLAKMKHPNIVTFFASFQENGRLFIVMEYC 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 342 SGGELFERI-IDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGTRIKLIDFGLARRLENAGSL-K 419
Cdd:cd08225    82 DGGDLMKRInRQRGVLFSEDQILSWFVQISLGLKHIHDRKILHRDIKSQNIF-LSKNGMVAKLGDFGIARQLNDSMELaY 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 420 VLFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDFDDEAFdeiSDDAKDFISNL 499
Cdd:cd08225   161 TCVGTPYYLSPEICQNRPYNNKTDIWSLGCVLYELCTLKHPFEGNNLHQLVLKICQGYFAPISPNF---SRDLRSLISQL 237
                         250       260
                  ....*....|....*....|
gi 1034633499 500 LKKDMKNRLDCTQCLQHPWL 519
Cdd:cd08225   238 FKVSPRDRPSITSILKRPFL 257
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
259-508 6.41e-33

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 129.55  E-value: 6.41e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 259 KVSDFyDIEERLGSGKFGQVfRLVEKKTR-KVWAGKFFKAYS---AKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANI 334
Cdd:PTZ00263   16 KLSDF-EMGETLGTGSFGRV-RIAKHKGTgEYYAIKCLKKREilkMKQVQHVAQEKSILMELSHPFIVNMMCSFQDENRV 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 335 VMVLEIVSGGELFERIidedfelteRECIKYMRQISE--------GVEYIHKQGIVHLDLKPENIMCVNKTgtRIKLIDF 406
Cdd:PTZ00263   94 YFLLEFVVGGELFTHL---------RKAGRFPNDVAKfyhaelvlAFEYLHSKDIIYRDLKPENLLLDNKG--HVKVTDF 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 407 GLARRLENagSLKVLFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDFdDEAFD 486
Cdd:PTZ00263  163 GFAKKVPD--RTFTLCGTPEYLAPEVIQSKGHGKAVDWWTMGVLLYEFIAGYPPFFDDTPFRIYEKILAGRLKF-PNWFD 239
                         250       260
                  ....*....|....*....|..
gi 1034633499 487 EisdDAKDFISNLLKKDMKNRL 508
Cdd:PTZ00263  240 G---RARDLVKGLLQTDHTKRL 258
STKc_CaMKK2 cd14199
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; ...
304-519 6.73e-33

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: 128.54  E-value: 6.73e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 304 ENIRQEISIMNCLHHPKLVQCVDAFEEKA--NIVMVLEIVSGGELFEriIDEDFELTERECIKYMRQISEGVEYIHKQGI 381
Cdd:cd14199    70 ERVYQEIAILKKLDHPNVVKLVEVLDDPSedHLYMVFELVKQGPVME--VPTLKPLSEDQARFYFQDLIKGIEYLHYQKI 147
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 382 VHLDLKPENIMcVNKTGtRIKLIDFGLARRLENAGS-LKVLFGTPEFVAPEVINYEP---IGYATDMWSIGVICYILVSG 457
Cdd:cd14199   148 IHRDVKPSNLL-VGEDG-HIKIADFGVSNEFEGSDAlLTNTVGTPAFMAPETLSETRkifSGKALDVWAMGVTLYCFVFG 225
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034633499 458 LSPFMGDNDNETLANVTSATWDFDDEAfdEISDDAKDFISNLLKKDMKNRLDCTQCLQHPWL 519
Cdd:cd14199   226 QCPFMDERILSLHSKIKTQPLEFPDQP--DISDDLKDLLFRMLDKNPESRISVPEIKLHPWV 285
STKc_phototropin_like cd05574
Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
261-518 7.60e-33

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


Pssm-ID: 270726 [Multi-domain]  Cd Length: 316  Bit Score: 129.28  E-value: 7.60e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 261 SDFYDIEeRLGSGKFGQVFrLVE-KKTRKVWAgkfFKAYSAKE--KEN----IRQEISIMNCLHHPKLVQCVDAFEEKAN 333
Cdd:cd05574     1 DHFKKIK-LLGKGDVGRVY-LVRlKGTGKLFA---MKVLDKEEmiKRNkvkrVLTEREILATLDHPFLPTLYASFQTSTH 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 334 IVMVLEIVSGGELF-------ERIIDED---FelterecikYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGtRIKL 403
Cdd:cd05574    76 LCFVMDYCPGGELFrllqkqpGKRLPEEvarF---------YAAEVLLALEYLHLLGFVYRDLKPENIL-LHESG-HIML 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 404 IDFGL------------------ARRLENAGSLKVLF------------GTPEFVAPEVINYEPIGYATDMWSIGVICYI 453
Cdd:cd05574   145 TDFDLskqssvtpppvrkslrkgSRRSSVKSIEKETFvaepsarsnsfvGTEEYIAPEVIKGDGHGSAVDWWTLGILLYE 224
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034633499 454 LVSGLSPFMGDNDNETLANVTSATWDFDDEafDEISDDAKDFISNLLKKDMKNRLDC----TQCLQHPW 518
Cdd:cd05574   225 MLYGTTPFKGSNRDETFSNILKKELTFPES--PPVSSEAKDLIRKLLVKDPSKRLGSkrgaSEIKRHPF 291
STKc_SnRK2 cd14662
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
264-518 8.89e-33

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


Pssm-ID: 271132 [Multi-domain]  Cd Length: 257  Bit Score: 127.19  E-value: 8.89e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 264 YDIEERLGSGKFGqVFRLV-EKKTRKVWAGKFFKAySAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEIVS 342
Cdd:cd14662     2 YELVKDIGSGNFG-VARLMrNKETKELVAVKYIER-GLKIDENVQREIINHRSLRHPNIIRFKEVVLTPTHLAIVMEYAA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 343 GGELFERIIDEDfELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKTGTRIKLIDFGLARRLENAGSLKVLF 422
Cdd:cd14662    80 GGELFERICNAG-RFSEDEARYFFQQLISGVSYCHSMQICHRDLKLENTLLDGSPAPRLKICDFGYSKSSVLHSQPKSTV 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 423 GTPEFVAPEVINY-EPIGYATDMWSIGVICYILVSGLSPFMGDND----NETLANVTSATWDFDDeaFDEISDDAKDFIS 497
Cdd:cd14662   159 GTPAYIAPEVLSRkEYDGKVADVWSCGVTLYVMLVGAYPFEDPDDpknfRKTIQRIMSVQYKIPD--YVRVSQDCRHLLS 236
                         250       260
                  ....*....|....*....|.
gi 1034633499 498 NLLKKDMKNRLDCTQCLQHPW 518
Cdd:cd14662   237 RIFVANPAKRITIPEIKNHPW 257
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
264-507 9.92e-33

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: 127.47  E-value: 9.92e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 264 YDIEERLGSGKFGQVFRLVEKKTRKVWAGKFF-------KAYSAKEKENIRQEISIMNCLH-HPKLVQCVDAFEEKANIV 335
Cdd:cd13993     2 YQLISPIGEGAYGVVYLAVDLRTGRKYAIKCLyksgpnsKDGNDFQKLPQLREIDLHRRVSrHPNIITLHDVFETEVAIY 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 336 MVLEIVSGGELFERIIDEDFELTERECIK-YMRQISEGVEYIHKQGIVHLDLKPENIMCvNKTGTRIKLIDFGLARRleN 414
Cdd:cd13993    82 IVLEYCPNGDLFEAITENRIYVGKTELIKnVFLQLIDAVKHCHSLGIYHRDIKPENILL-SQDEGTVKLCDFGLATT--E 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 415 AGSLKVLFGTPEFVAPEVI-NYEPI--GYAT---DMWSIGVICYILVSGLSPFM--GDNDNETLANVTSATWDFDdeAFD 486
Cdd:cd13993   159 KISMDFGVGSEFYMAPECFdEVGRSlkGYPCaagDIWSLGIILLNLTFGRNPWKiaSESDPIFYDYYLNSPNLFD--VIL 236
                         250       260
                  ....*....|....*....|.
gi 1034633499 487 EISDDAKDFISNLLKKDMKNR 507
Cdd:cd13993   237 PMSDDFYNLLRQIFTVNPNNR 257
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
264-518 1.15e-32

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: 127.41  E-value: 1.15e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 264 YDIEERLGSGKFGQVFrlvekKTRKVWAGKFFKAYSA--KEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEIV 341
Cdd:cd14010     2 YVLYDEIGRGKHSVVY-----KGRRKGTIEFVAIKCVdkSKRPEVLNEVRLTHELKHPNVLKFYEWYETSNHLWLVVEYC 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 342 SGGELfERIIDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGTrIKLIDFGLARRL-ENAGSLKV 420
Cdd:cd14010    77 TGGDL-ETLLRQDGNLPESSVRKFGRDLVRGLHYIHSKGIIYCDLKPSNIL-LDGNGT-LKLSDFGLARREgEILKELFG 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 421 LF----------------GTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSAtwDFD--- 481
Cdd:cd14010   154 QFsdegnvnkvskkqakrGTPYYMAPELFQGGVHSFASDLWALGCVLYEMFTGKPPFVAESFTELVEKILNE--DPPppp 231
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1034633499 482 DEAFDEISDDAKDFISNLLKKDMKNRLDCTQCLQHP-W 518
Cdd:cd14010   232 PKVSSKPSPDFKSLLKGLLEKDPAKRLSWDELVKHPfW 269
STKc_PLK3 cd14189
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the ...
270-516 1.30e-32

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: 126.58  E-value: 1.30e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 270 LGSGKFGQVFRLVEKKTRKVWAGKFF---KAYSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEIVSGGEL 346
Cdd:cd14189     9 LGKGGFARCYEMTDLATNKTYAVKVIphsRVAKPHQREKIVNEIELHRDLHHKHVVKFSHHFEDAENIYIFLELCSRKSL 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 347 fERIIDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTgTRIKLIDFGLARRLENAGSLK-VLFGTP 425
Cdd:cd14189    89 -AHIWKARHTLLEPEVRYYLKQIISGLKYLHLKGILHRDLKLGNFF-INEN-MELKVGDFGLAARLEPPEQRKkTICGTP 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 426 EFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSAtwDFDDEAFdeISDDAKDFISNLLKKDMK 505
Cdd:cd14189   166 NYLAPEVLLRQGHGPESDVWSLGCVMYTLLCGNPPFETLDLKETYRCIKQV--KYTLPAS--LSLPARHLLAGILKRNPG 241
                         250
                  ....*....|.
gi 1034633499 506 NRLDCTQCLQH 516
Cdd:cd14189   242 DRLTLDQILEH 252
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
264-519 1.47e-32

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: 127.26  E-value: 1.47e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 264 YDIEERLGSGKFGQVFRLVEKKTRKVWAGKFFKA--YSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEIV 341
Cdd:cd07830     1 YKVIKQLGDGTFGSVYLARNKETGELVAIKKMKKkfYSWEECMNLREVKSLRKLNEHPNIVKLKEVFRENDELYFVFEYM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 342 SGgELFERIIDEDFELTERECIK-YMRQISEGVEYIHKQGIVHLDLKPENIMCVNKtgTRIKLIDFGLARRLENAGSLKV 420
Cdd:cd07830    81 EG-NLYQLMKDRKGKPFSESVIRsIIYQILQGLAHIHKHGFFHRDLKPENLLVSGP--EVVKIADFGLAREIRSRPPYTD 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 421 LFGTPEFVAPEVI----NYE-PIgyatDMWSIGVICYILVSgLSP-FMGDNDN-------ETLANVTSATWdfdDEAFD- 486
Cdd:cd07830   158 YVSTRWYRAPEILlrstSYSsPV----DIWALGCIMAELYT-LRPlFPGSSEIdqlykicSVLGTPTKQDW---PEGYKl 229
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1034633499 487 ---------------------EISDDAKDFISNLLKKDMKNRLDCTQCLQHPWL 519
Cdd:cd07830   230 asklgfrfpqfaptslhqlipNASPEAIDLIKDMLRWDPKKRPTASQALQHPYF 283
STKc_FA2-like cd08529
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar ...
264-519 1.50e-32

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: 126.37  E-value: 1.50e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 264 YDIEERLGSGKFGQVFRLVEKKTRKVWAGKF--FKAYSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEIV 341
Cdd:cd08529     2 FEILNKLGKGSFGVVYKVVRKVDGRVYALKQidISRMSRKMREEAIDEARVLSKLNSPYVIKYYDSFVDKGKLNIVMEYA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 342 SGGELFERIIDEDFE-LTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGtRIKLIDFGLARRLENAGSL-K 419
Cdd:cd08529    82 ENGDLHSLIKSQRGRpLPEDQIWKFFIQTLLGLSHLHSKKILHRDIKSMNIF-LDKGD-NVKIGDLGVAKILSDTTNFaQ 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 420 VLFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDFDDEAFdeiSDDAKDFISNL 499
Cdd:cd08529   160 TIVGTPYYLSPELCEDKPYNEKSDVWALGCVLYELCTGKHPFEAQNQGALILKIVRGKYPPISASY---SQDLSQLIDSC 236
                         250       260
                  ....*....|....*....|
gi 1034633499 500 LKKDMKNRLDCTQCLQHPWL 519
Cdd:cd08529   237 LTKDYRQRPDTTELLRNPSL 256
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
266-473 1.75e-32

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: 126.51  E-value: 1.75e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499  266 IEERLGSGKFGQVFR-----LVEKKTRKVwAGKFFKAY-SAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLE 339
Cdd:smart00221   3 LGKKLGEGAFGEVYKgtlkgKGDGKEVEV-AVKTLKEDaSEQQIEEFLREARIMRKLDHPNIVKLLGVCTEEEPLMIVME 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499  340 IVSGGELFERIID-EDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGTrIKLIDFGLARRLENaGSL 418
Cdd:smart00221  82 YMPGGDLLDYLRKnRPKELSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCL-VGENLV-VKISDFGLSRDLYD-DDY 158
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1034633499  419 KVLFGTPEFV---APEVINYEPIGYATDMWSIGVICYILVS-GLSPFMGDNDNETLANV 473
Cdd:smart00221 159 YKVKGGKLPIrwmAPESLKEGKFTSKSDVWSFGVLLWEIFTlGEEPYPGMSNAEVLEYL 217
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
261-515 2.51e-32

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: 126.25  E-value: 2.51e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 261 SDFYDIEeRLGSGKFGQVFRLVEKKTRKVWAGKFFKAYSAKEK-ENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLE 339
Cdd:cd13996     6 NDFEEIE-LLGSGGFGSVYKVRNKVDGVTYAIKKIRLTEKSSAsEKVLREVKALAKLNHPNIVRYYTAWVEEPPLYIQME 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 340 IVSGGELFERIIDEDFE--LTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKTGTrIKLIDFGLARRLENA-- 415
Cdd:cd13996    85 LCEGGTLRDWIDRRNSSskNDRKLALELFKQILKGVSYIHSKGIVHRDLKPSNIFLDNDDLQ-VKIGDFGLATSIGNQkr 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 416 -------------GSLKVLFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMgdndnE---TLANVTSATWd 479
Cdd:cd13996   164 elnnlnnnnngntSNNSVGIGTPLYASPEQLDGENYNEKADIYSLGIILFEMLHPFKTAM-----ErstILTDLRNGIL- 237
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1034633499 480 fdDEAFDEISDDAKDFISNLLKKDMKNRLDCTQCLQ 515
Cdd:cd13996   238 --PESFKAKHPKEADLIQSLLSKNPEERPSAEQLLR 271
STKc_CAMKK cd14118
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; ...
304-518 4.15e-32

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: 125.93  E-value: 4.15e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 304 ENIRQEISIMNCLHHPKLVQCVDAFEEKA--NIVMVLEIVSGGELFERIIDEDFEltERECIKYMRQISEGVEYIHKQGI 381
Cdd:cd14118    59 DRVYREIAILKKLDHPNVVKLVEVLDDPNedNLYMVFELVDKGAVMEVPTDNPLS--EETARSYFRDIVLGIEYLHYQKI 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 382 VHLDLKPENIMcVNKTGtRIKLIDFGLARRLENA-GSLKVLFGTPEFVAPEVINYEPI---GYATDMWSIGVICYILVSG 457
Cdd:cd14118   137 IHRDIKPSNLL-LGDDG-HVKIADFGVSNEFEGDdALLSSTAGTPAFMAPEALSESRKkfsGKALDIWAMGVTLYCFVFG 214
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034633499 458 LSPFMGDNDNETLANVTSATWDFDDEAfdEISDDAKDFISNLLKKDMKNRLDCTQCLQHPW 518
Cdd:cd14118   215 RCPFEDDHILGLHEKIKTDPVVFPDDP--VVSEQLKDLILRMLDKNPSERITLPEIKEHPW 273
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
270-519 5.20e-32

Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. ULK1 is required for efficient amino acid starvation-induced autophagy and mitochondrial clearance. It associates with three autophagy-related proteins (Atg13, FIP200 amd Atg101) to form the ULK1 complex. All fours proteins are essential for autophagosome formation. ULK1 is regulated by both mammalian target-of rapamycin complex 1 (mTORC1) and AMP-activated protein kinase (AMPK). mTORC1 negatively regulates the ULK1 complex in a nutrient-dependent manner while AMPK stimulates autophagy by inhibiting mTORC1. ULK1 also plays neuron-specific roles and is involved in non-clathrin-coated endocytosis in growth cones, filopodia extension, neurite extension, and axon branching. The ULK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271104 [Multi-domain]  Cd Length: 267  Bit Score: 125.51  E-value: 5.20e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 270 LGSGKFGQVF--RLVEKKTRKVWAGKFFKAYSAKEKENIRQEISIMNCLHHPKLVQCVDaFEEKANIV-MVLEIVSGGEL 346
Cdd:cd14202    10 IGHGAFAVVFkgRHKEKHDLEVAVKCINKKNLAKSQTLLGKEIKILKELKHENIVALYD-FQEIANSVyLVMEYCNGGDL 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 347 FE-----RIIDEDfelTEReciKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKTG-------TRIKLIDFGLARRLEN 414
Cdd:cd14202    89 ADylhtmRTLSED---TIR---LFLQQIAGAMKMLHSKGIIHRDLKPQNILLSYSGGrksnpnnIRIKIADFGFARYLQN 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 415 AGSLKVLFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNEtLANVTSATWDFDDEAFDEISDDAKD 494
Cdd:cd14202   163 NMMAATLCGSPMYMAPEVIMSQHYDAKADLWSIGTIIYQCLTGKAPFQASSPQD-LRLFYEKNKSLSPNIPRETSSHLRQ 241
                         250       260
                  ....*....|....*....|....*
gi 1034633499 495 FISNLLKKDMKNRLDCTQCLQHPWL 519
Cdd:cd14202   242 LLLGLLQRNQKDRMDFDEFFHHPFL 266
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
264-518 5.68e-32

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: 125.75  E-value: 5.68e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 264 YDIEERLGSGKFGQVFRLVEKKTRKVWAGKFFKAYSakEKEN-----IRqEISIMNCLHHPKLVQ----CVD--AFEEKA 332
Cdd:cd07840     1 YEKIAQIGEGTYGQVYKARNKKTGELVALKKIRMEN--EKEGfpitaIR-EIKLLQKLDHPNVVRlkeiVTSkgSAKYKG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 333 NIVMVLEIVSGGelFERIIDE-DFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGtRIKLIDFGLARR 411
Cdd:cd07840    78 SIYMVFEYMDHD--LTGLLDNpEVKFTESQIKCYMKQLLEGLQYLHSNGILHRDIKGSNIL-INNDG-VLKLADFGLARP 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 412 LENAGSL----KVLfgTPEFVAPEVI----NYepiGYATDMWSIGVICYILVSGLSPFMGDNDNETLANV-------TSA 476
Cdd:cd07840   154 YTKENNAdytnRVI--TLWYRPPELLlgatRY---GPEVDMWSVGCILAELFTGKPIFQGKTELEQLEKIfelcgspTEE 228
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034633499 477 TW-DFDD------------------EAFDE-ISDDAKDFISNLLKKDMKNRLDCTQCLQHPW 518
Cdd:cd07840   229 NWpGVSDlpwfenlkpkkpykrrlrEVFKNvIDPSALDLLDKLLTLDPKKRISADQALQHEY 290
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
264-517 6.58e-32

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: 124.96  E-value: 6.58e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 264 YDIEERLGSGKFGQVFRLVEKKTRKVWAGK--FFKAYSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKAN----IVMv 337
Cdd:cd08217     2 YEVLETIGKGSFGTVRKVRRKSDGKILVWKeiDYGKMSEKEKQQLVSEVNILRELKHPNIVRYYDRIVDRANttlyIVM- 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 338 lEIVSGGELFERI---------IDEDFeltereCIKYMRQISEGVEYIH-----KQGIVHLDLKPENI-MCVNKTgtrIK 402
Cdd:cd08217    81 -EYCEGGDLAQLIkkckkenqyIPEEF------IWKIFTQLLLALYECHnrsvgGGKILHRDLKPANIfLDSDNN---VK 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 403 LIDFGLARRLENAGSL-KVLFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATwdfd 481
Cdd:cd08217   151 LGDFGLARVLSHDSSFaKTYVGTPYYMSPELLNEQSYDEKSDIWSLGCLIYELCALHPPFQAANQLELAKKIKEGK---- 226
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1034633499 482 deaFDEI----SDDAKDFISNLLKKDMKNRLDCTQCLQHP 517
Cdd:cd08217   227 ---FPRIpsrySSELNEVIKSMLNVDPDKRPSVEELLQLP 263
STKc_HUNK cd14070
Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase ...
264-461 8.79e-32

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: 124.54  E-value: 8.79e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 264 YDIEERLGSGKFGQVFRLVEKKTRKVWAGKFFKAYSAKEK----ENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLE 339
Cdd:cd14070     4 YLIGRKLGEGSFAKVREGLHAVTGEKVAIKVIDKKKAKKDsyvtKNLRREGRIQQMIRHPNITQLLDILETENSYYLVME 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 340 IVSGGELFERIIDEDfELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCvnKTGTRIKLIDFGL---ARRLENAG 416
Cdd:cd14070    84 LCPGGNLMHRIYDKK-RLEEREARRYIRQLVSAVEHLHRAGVVHRDLKIENLLL--DENDNIKLIDFGLsncAGILGYSD 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1034633499 417 SLKVLFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPF 461
Cdd:cd14070   161 PFSTQCGSPAYAAPELLARKKYGPKVDVWSIGVNMYAMLTGTLPF 205
STKc_ULK1_2-like cd14120
Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar ...
270-517 1.47e-31

Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. ULK1 is required for efficient amino acid starvation-induced autophagy and mitochondrial clearance. ULK2 is ubiquitously expressed and is essential in autophagy induction. ULK1 and ULK2 have unique and cell-type specific roles, but also display partially redundant roles in starvation-induced autophagy. They both display neuron-specific functions: ULK1 is involved in non-clathrin-coated endocytosis in growth cones, filopodia extension, and axon branching; ULK2 plays a role in axon development. The ULK1/2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271022 [Multi-domain]  Cd Length: 256  Bit Score: 123.63  E-value: 1.47e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 270 LGSGKFGQVFR-LVEKKTRKVWAGKFF-KAYSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEIVSGGELF 347
Cdd:cd14120     1 IGHGAFAVVFKgRHRKKPDLPVAIKCItKKNLSKSQNLLGKEIKILKELSHENVVALLDCQETSSSVYLVMEYCNGGDLA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 348 ERIiDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNK-------TGTRIKLIDFGLARRLENAGSLKV 420
Cdd:cd14120    81 DYL-QAKGTLSEDTIRVFLQQIAAAMKALHSKGIVHRDLKPQNILLSHNsgrkpspNDIRLKIADFGFARFLQDGMMAAT 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 421 LFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNEtLANVTSATWDFDDEAFDEISDDAKDFISNLL 500
Cdd:cd14120   160 LCGSPMYMAPEVIMSLQYDAKADLWSIGTIVYQCLTGKAPFQAQTPQE-LKAFYEKNANLRPNIPSGTSPALKDLLLGLL 238
                         250
                  ....*....|....*..
gi 1034633499 501 KKDMKNRLDCTQCLQHP 517
Cdd:cd14120   239 KRNPKDRIDFEDFFSHP 255
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
264-517 1.49e-31

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: 123.65  E-value: 1.49e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 264 YDIEERLGSGKFGQVFRLVEKKTRKVWAGKFFKA--YSAKEKENIRQEISIMNCL-HHPKLVQCVDAFEEKANIVMVLEI 340
Cdd:cd13997     2 FHELEQIGSGSFSEVFKVRSKVDGCLYAVKKSKKpfRGPKERARALREVEAHAALgQHPNIVRYYSSWEEGGHLYIQMEL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 341 VSGGELfERIIDE---DFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKtgTRIKLIDFGLARRLENAGs 417
Cdd:cd13997    82 CENGSL-QDALEElspISKLSEAEVWDLLLQVALGLAFIHSKGIVHLDIKPDNIFISNK--GTCKIGDFGLATRLETSG- 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 418 lKVLFGTPEFVAPEVINYEP-IGYATDMWSIGVICYILVSGLSpfMGDNDNETLaNVTSAtwDFDDEAFDEISDDAKDFI 496
Cdd:cd13997   158 -DVEEGDSRYLAPELLNENYtHLPKADIFSLGVTVYEAATGEP--LPRNGQQWQ-QLRQG--KLPLPPGLVLSQELTRLL 231
                         250       260
                  ....*....|....*....|.
gi 1034633499 497 SNLLKKDMKNRLDCTQCLQHP 517
Cdd:cd13997   232 KVMLDPDPTRRPTADQLLAHD 252
STKc_CaMKK1 cd14200
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; ...
304-519 1.87e-31

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: 124.29  E-value: 1.87e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 304 ENIRQEISIMNCLHHPKLVQCVDAFEEKA--NIVMVLEIVSGGELFERIIDEDFelTERECIKYMRQISEGVEYIHKQGI 381
Cdd:cd14200    68 ERVYQEIAILKKLDHVNIVKLIEVLDDPAedNLYMVFDLLRKGPVMEVPSDKPF--SEDQARLYFRDIVLGIEYLHYQKI 145
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 382 VHLDLKPENIMcVNKTGtRIKLIDFGLARRLE-NAGSLKVLFGTPEFVAPEVINYEPIGY---ATDMWSIGVICYILVSG 457
Cdd:cd14200   146 VHRDIKPSNLL-LGDDG-HVKIADFGVSNQFEgNDALLSSTAGTPAFMAPETLSDSGQSFsgkALDVWAMGVTLYCFVYG 223
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034633499 458 LSPFMgDNDNETLAN-VTSATWDFDDEAfdEISDDAKDFISNLLKKDMKNRLDCTQCLQHPWL 519
Cdd:cd14200   224 KCPFI-DEFILALHNkIKNKPVEFPEEP--EISEELKDLILKMLDKNPETRITVPEIKVHPWV 283
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
261-519 2.16e-31

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: 123.14  E-value: 2.16e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 261 SDFYDIEERLGSGKFGQVFRLVEKKTRKVWAGKFFKAYSakEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEI 340
Cdd:cd06612     2 EEVFDILEKLGEGSYGSVYKAIHKETGQVVAIKVVPVEE--DLQEIIKEISILKQCDSPYIVKYYGSYFKNTDLWIVMEY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 341 VSGGELFERIIDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGTrIKLIDFGLARRLENA-GSLK 419
Cdd:cd06612    80 CGAGSVSDIMKITNKTLTEEEIAAILYQTLKGLEYLHSNKKIHRDIKAGNIL-LNEEGQ-AKLADFGVSGQLTDTmAKRN 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 420 VLFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSP----------FM-GDNDNETLANVTSatWdfddeafdei 488
Cdd:cd06612   158 TVIGTPFWMAPEVIQEIGYNNKADIWSLGITAIEMAEGKPPysdihpmraiFMiPNKPPPTLSDPEK--W---------- 225
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1034633499 489 SDDAKDFISNLLKKDMKNRLDCTQCLQHPWL 519
Cdd:cd06612   226 SPEFNDFVKKCLVKDPEERPSAIQLLQHPFI 256
STKc_NDR_like cd05599
Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs ...
271-519 2.20e-31

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: 125.03  E-value: 2.20e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 271 GSGKFGQVfRLVEKK-TRKVWAGKFFKAYSAKEKE---NIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEIVSGGEL 346
Cdd:cd05599    10 GRGAFGEV-RLVRKKdTGHVYAMKKLRKSEMLEKEqvaHVRAERDILAEADNPWVVKLYYSFQDEENLYLIMEFLPGGDM 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 347 FERIIDEDFeLTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGtRIKLIDFGLARRLENAGSLKVLFGTPE 426
Cdd:cd05599    89 MTLLMKKDT-LTEEETRFYIAETVLAIESIHKLGYIHRDIKPDNLL-LDARG-HIKLSDFGLCTGLKKSHLAYSTVGTPD 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 427 FVAPEVinYEPIGY--ATDMWSIGVICYILVSGLSPFMGDNDNETLANVTS--ATWDFDDEAfdEISDDAKDFISNLLkK 502
Cdd:cd05599   166 YIAPEV--FLQKGYgkECDWWSLGVIMYEMLIGYPPFCSDDPQETCRKIMNwrETLVFPPEV--PISPEAKDLIERLL-C 240
                         250       260
                  ....*....|....*....|
gi 1034633499 503 DMKNRL---DCTQCLQHPWL 519
Cdd:cd05599   241 DAEHRLganGVEEIKSHPFF 260
STKc_PKB_gamma cd05593
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); ...
253-519 3.27e-31

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: 125.19  E-value: 3.27e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 253 TINTEQKVSDFYDIEERLGSGKFGQVFRLVEKKTRKVWAGKFFKAYSAKEKENIRQEIS---IMNCLHHPKLVQCVDAFE 329
Cdd:cd05593     6 TTHHKRKTMNDFDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVAHTLTesrVLKNTRHPFLTSLKYSFQ 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 330 EKANIVMVLEIVSGGELF-----ERIIDEDfelterECIKYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGtRIKLI 404
Cdd:cd05593    86 TKDRLCFVMEYVNGGELFfhlsrERVFSED------RTRFYGAEIVSALDYLHSGKIVYRDLKLENLM-LDKDG-HIKIT 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 405 DFGLARR-LENAGSLKVLFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMgDNDNETLANVTSatwdFDDE 483
Cdd:cd05593   158 DFGLCKEgITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFY-NQDHEKLFELIL----MEDI 232
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1034633499 484 AFDE-ISDDAKDFISNLLKKDMKNRL-----DCTQCLQHPWL 519
Cdd:cd05593   233 KFPRtLSADAKSLLSGLLIKDPNKRLgggpdDAKEIMRHSFF 274
STKc_SGK cd05575
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; ...
270-532 8.17e-31

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: 123.58  E-value: 8.17e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 270 LGSGKFGQVFRLVEKKTRKVWAGKFF-KAYSAKEKE--NIRQEISI-MNCLHHPKLVQCVDAFEEKANIVMVLEIVSGGE 345
Cdd:cd05575     3 IGKGSFGKVLLARHKAEGKLYAVKVLqKKAILKRNEvkHIMAERNVlLKNVKHPFLVGLHYSFQTKDKLYFVLDYVNGGE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 346 LFeriidedFELTERECIK------YMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGtRIKLIDFGLARRLENAGSLK 419
Cdd:cd05575    83 LF-------FHLQRERHFPeprarfYAAEIASALGYLHSLNIIYRDLKPENIL-LDSQG-HVVLTDFGLCKEGIEPSDTT 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 420 VLF-GTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDFDdeafDEISDDAKDFISN 498
Cdd:cd05575   154 STFcGTPEYLAPEVLRKQPYDRTVDWWCLGAVLYEMLYGLPPFYSRDTAEMYDNILHKPLRLR----TNVSPSARDLLEG 229
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1034633499 499 LLKKDMKNRL----DCTQCLQHPWLMK-DTKNMEAKKLS 532
Cdd:cd05575   230 LLQKDRTKRLgsgnDFLEIKNHSFFRPiNWDDLEAKKIP 268
STKc_SGK1 cd05602
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
255-508 8.74e-31

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: 123.97  E-value: 8.74e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 255 NTEQKVSDFyDIEERLGSGKFGQVFRLVEKKTRKVWAGKFFKAYS---AKEKENIRQEISIM-NCLHHPKLVQCVDAFEE 330
Cdd:cd05602     1 NPHAKPSDF-HFLKVIGKGSFGKVLLARHKSDEKFYAVKVLQKKAilkKKEEKHIMSERNVLlKNVKHPFLVGLHFSFQT 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 331 KANIVMVLEIVSGGELFERIIDEDFELTERECIkYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGtRIKLIDFGLAR 410
Cdd:cd05602    80 TDKLYFVLDYINGGELFYHLQRERCFLEPRARF-YAAEIASALGYLHSLNIVYRDLKPENIL-LDSQG-HIVLTDFGLCK 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 411 R-LENAGSLKVLFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDFDdeafDEIS 489
Cdd:cd05602   157 EnIEPNGTTSTFCGTPEYLAPEVLHKQPYDRTVDWWCLGAVLYEMLYGLPPFYSRNTAEMYDNILNKPLQLK----PNIT 232
                         250
                  ....*....|....*....
gi 1034633499 490 DDAKDFISNLLKKDMKNRL 508
Cdd:cd05602   233 NSARHLLEGLLQKDRTKRL 251
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
262-531 9.51e-31

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: 122.16  E-value: 9.51e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 262 DFYDIEERLGSGKFGQVFRLVEKKTRKVWAGKFFKAYSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEIV 341
Cdd:cd06611     5 DIWEIIGELGDGAFGKVYKAQHKETGLFAAAKIIQIESEEELEDFMVEIDILSECKHPNIVGLYEAYFYENKLWILIEFC 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 342 SGGELfERIIDE-DFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGTrIKLIDFGLARRLENAGSLKV 420
Cdd:cd06611    85 DGGAL-DSIMLElERGLTEPQIRYVCRQMLEALNFLHSHKVIHRDLKAGNIL-LTLDGD-VKLADFGVSAKNKSTLQKRD 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 421 LF-GTPEFVAPEVINYE-----PIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSAtwdfDDEAFDE---ISDD 491
Cdd:cd06611   162 TFiGTPYWMAPEVVACEtfkdnPYDYKADIWSLGITLIELAQMEPPHHELNPMRVLLKILKS----EPPTLDQpskWSSS 237
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1034633499 492 AKDFISNLLKKDMKNRLDCTQCLQHPWLMKDTKNMEAKKL 531
Cdd:cd06611   238 FNDFLKSCLVKDPDDRPTAAELLKHPFVSDQSDNKAIKDL 277
STKc_obscurin_rpt2 cd14110
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
264-519 1.92e-30

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: 120.41  E-value: 1.92e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 264 YDIEERLGSGKFGQVFRLVEKKTRKVWAGKFFkAYSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEIVSG 343
Cdd:cd14110     5 YAFQTEINRGRFSVVRQCEEKRSGQMLAAKII-PYKPEDKQLVLREYQVLRRLSHPRIAQLHSAYLSPRHLVLIEELCSG 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 344 GELFERIIdEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKtgTRIKLIDFGLARRLENAgslKVLFG 423
Cdd:cd14110    84 PELLYNLA-ERNSYSEAEVTDYLWQILSAVDYLHSRRILHLDLRSENMIITEK--NLLKIVDLGNAQPFNQG---KVLMT 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 424 TP-----EFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDFdDEAFDEISDDAKDFISN 498
Cdd:cd14110   158 DKkgdyvETMAPELLEGQGAGPQTDIWAIGVTAFIMLSADYPVSSDLNWERDRNIRKGKVQL-SRCYAGLSGGAVNFLKS 236
                         250       260
                  ....*....|....*....|.
gi 1034633499 499 LLKKDMKNRLDCTQCLQHPWL 519
Cdd:cd14110   237 TLCAKPWGRPTASECLQNPWL 257
STKc_Kin4 cd14076
Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the ...
264-519 2.29e-30

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: 120.67  E-value: 2.29e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 264 YDIEERLGSGKFGQVFRLVEKKTRKVWAG-----KFFKAYSAKEKEN---IRQEISIMNCLHHPKLVQCVDAFEEKANIV 335
Cdd:cd14076     3 YILGRTLGEGEFGKVKLGWPLPKANHRSGvqvaiKLIRRDTQQENCQtskIMREINILKGLTHPNIVRLLDVLKTKKYIG 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 336 MVLEIVSGGELFERIIDEDFeLTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCvnKTGTRIKLIDFGLARRL-EN 414
Cdd:cd14076    83 IVLEFVSGGELFDYILARRR-LKDSVACRLFAQLISGVAYLHKKGVVHRDLKLENLLL--DKNRNLVITDFGFANTFdHF 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 415 AGSL-KVLFGTPEFVAPEVINYEPI--GYATDMWSIGVICYILVSGLSPFMGDNDNETLANV-------TSATWDFDdea 484
Cdd:cd14076   160 NGDLmSTSCGSPCYAAPELVVSDSMyaGRKADIWSCGVILYAMLAGYLPFDDDPHNPNGDNVprlyryiCNTPLIFP--- 236
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1034633499 485 fDEISDDAKDFISNLLKKDMKNRLDCTQCLQHPWL 519
Cdd:cd14076   237 -EYVTPKARDLLRRILVPNPRKRIRLSAIMRHAWL 270
STKc_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
270-461 2.61e-30

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: 120.42  E-value: 2.61e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 270 LGSGKFGQVFRLVEKKTRKVWAGKFF-KAYSAK--EKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEIVSGGEL 346
Cdd:cd14187    15 LGKGGFAKCYEITDADTKEVFAGKIVpKSLLLKphQKEKMSMEIAIHRSLAHQHVVGFHGFFEDNDFVYVVLELCRRRSL 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 347 FErIIDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKTgtRIKLIDFGLARRLENAGSLK-VLFGTP 425
Cdd:cd14187    95 LE-LHKRRKALTEPEARYYLRQIILGCQYLHRNRVIHRDLKLGNLFLNDDM--EVKIGDFGLATKVEYDGERKkTLCGTP 171
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1034633499 426 EFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPF 461
Cdd:cd14187   172 NYIAPEVLSKKGHSFEVDIWSIGCIMYTLLVGKPPF 207
PKc_DYRK_like cd14133
Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like ...
264-519 2.69e-30

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: 120.07  E-value: 2.69e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 264 YDIEERLGSGKFGQVFRLVEKKTRKVWAGKFFKaysaKEKENIRQ---EISIMNCL--HHPK----LVQCVDAFEEKANI 334
Cdd:cd14133     1 YEVLEVLGKGTFGQVVKCYDLLTGEEVALKIIK----NNKDYLDQsldEIRLLELLnkKDKAdkyhIVRLKDVFYFKNHL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 335 VMVLEIVsGGELFERIIDEDFE-LTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKTGTRIKLIDFGLARRLE 413
Cdd:cd14133    77 CIVFELL-SQNLYEFLKQNKFQyLSLPRIRKIAQQILEALVFLHSLGLIHCDLKPENILLASYSRCQIKIIDFGSSCFLT 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 414 NAGS--LKVLFgtpeFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDFDDEAFDE-ISD 490
Cdd:cd14133   156 QRLYsyIQSRY----YRAPEVILGLPYDEKIDMWSLGCILAELYTGEPLFPGASEVDQLARIIGTIGIPPAHMLDQgKAD 231
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1034633499 491 DAK--DFISNLLKKDMKNRLDCTQCLQHPWL 519
Cdd:cd14133   232 DELfvDFLKKLLEIDPKERPTASQALSHPWL 262
STKc_nPKC_theta_like cd05592
Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and ...
270-517 4.66e-30

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: 121.34  E-value: 4.66e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 270 LGSGKFGQVFrLVE-KKTRKVWAGKFFKAYSAKEKEN-----IRQEISIMNClHHPKLVQCVDAFEEKANIVMVLEIVSG 343
Cdd:cd05592     3 LGKGSFGKVM-LAElKGTNQYFAIKALKKDVVLEDDDvectmIERRVLALAS-QHPFLTHLFCTFQTESHLFFVMEYLNG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 344 GELFERIIDEDfELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGtRIKLIDFGLARRLENAGSLKVLF- 422
Cdd:cd05592    81 GDLMFHIQQSG-RFDEDRARFYGAEIICGLQFLHSRGIIYRDLKLDNVL-LDREG-HIKIADFGMCKENIYGENKASTFc 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 423 GTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSAT-----WdfddeafdeISDDAKDFIS 497
Cdd:cd05592   158 GTPDYIAPEILKGQKYNQSVDWWSFGVLLYEMLIGQSPFHGEDEDELFWSICNDTphyprW---------LTKEAASCLS 228
                         250       260
                  ....*....|....*....|
gi 1034633499 498 NLLKKDMKNRLDCTQCLQHP 517
Cdd:cd05592   229 LLLERNPEKRLGVPECPAGD 248
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
268-519 5.21e-30

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: 119.46  E-value: 5.21e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 268 ERLGSGKFGQVF------------RLVEKKTRKVWAGKffkaysaKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIV 335
Cdd:cd06631     7 NVLGKGAYGTVYcgltstgqliavKQVELDTSDKEKAE-------KEYEKLQEEVDLLKTLKHVNIVGYLGTCLEDNVVS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 336 MVLEIVSGGELfERIIDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVnKTGTrIKLIDFGLARRLENA 415
Cdd:cd06631    80 IFMEFVPGGSI-ASILARFGALEEPVFCRYTKQILEGVAYLHNNNVIHRDIKGNNIMLM-PNGV-IKLIDFGCAKRLCIN 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 416 GS-------LKVLFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATwDFDDEAFDEI 488
Cdd:cd06631   157 LSsgsqsqlLKSMRGTPYWMAPEVINETGHGRKSDIWSIGCTVFEMATGKPPWADMNPMAAIFAIGSGR-KPVPRLPDKF 235
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1034633499 489 SDDAKDFISNLLKKDMKNRLDCTQCLQHPWL 519
Cdd:cd06631   236 SPEARDFVHACLTRDQDERPSAEQLLKHPFI 266
STKc_GRK4_like cd05605
Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs ...
270-531 6.26e-30

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: 119.77  E-value: 6.26e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 270 LGSGKFGQVFRLVEKKTRKVWAGKFFkaysakEKENIRQ---------EISIMNCLHHPKLVQCVDAFEEKANIVMVLEI 340
Cdd:cd05605     8 LGKGGFGEVCACQVRATGKMYACKKL------EKKRIKKrkgeamalnEKQILEKVNSRFVVSLAYAYETKDALCLVLTI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 341 VSGGELFERIID-EDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKTGTRIKliDFGLARRLENAGSLK 419
Cdd:cd05605    82 MNGGDLKFHIYNmGNPGFEEERAVFYAAEITCGLEHLHSERIVYRDLKPENILLDDHGHVRIS--DLGLAVEIPEGETIR 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 420 VLFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDFDDEAFDEISDDAKDFISNL 499
Cdd:cd05605   160 GRVGTVGYMAPEVVKNERYTFSPDWWGLGCLIYEMIEGQAPFRARKEKVKREEVDRRVKEDQEEYSEKFSEEAKSICSQL 239
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1034633499 500 LKKDMKNRLDC-----TQCLQHPWLMK-DTKNMEAKKL 531
Cdd:cd05605   240 LQKDPKTRLGCrgegaEDVKSHPFFKSiNFKRLEAGLL 277
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
264-467 6.46e-30

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: 119.36  E-value: 6.46e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 264 YDIEERLGSGKFGQVFR---LVEKKTRKVWAGKFFKAYSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEI 340
Cdd:cd08228     4 FQIEKKIGRGQFSEVYRatcLLDRKPVALKKVQIFEMMDAKARQDCVKEIDLLKQLNHPNVIKYLDSFIEDNELNIVLEL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 341 VSGGELFERII---DEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGTrIKLIDFGLARRLEN-AG 416
Cdd:cd08228    84 ADAGDLSQMIKyfkKQKRLIPERTVWKYFVQLCSAVEHMHSRRVMHRDIKPANVF-ITATGV-VKLGDLGLGRFFSSkTT 161
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1034633499 417 SLKVLFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDN 467
Cdd:cd08228   162 AAHSLVGTPYYMSPERIHENGYNFKSDIWSLGCLLYEMAALQSPFYGDKMN 212
STKc_MARK cd14072
Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; ...
264-468 7.01e-30

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: 118.78  E-value: 7.01e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 264 YDIEERLGSGKFGQVFRLVEKKTRKVWAGKFF--KAYSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEIV 341
Cdd:cd14072     2 YRLLKTIGKGNFAKVKLARHVLTGREVAIKIIdkTQLNPSSLQKLFREVRIMKILNHPNIVKLFEVIETEKTLYLVMEYA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 342 SGGELFERIIDEDfELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCvnKTGTRIKLIDFGLARRLENAGSLKVL 421
Cdd:cd14072    82 SGGEVFDYLVAHG-RMKEKEARAKFRQIVSAVQYCHQKRIVHRDLKAENLLL--DADMNIKIADFGFSNEFTPGNKLDTF 158
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1034633499 422 FGTPEFVAPEVIN---YEpiGYATDMWSIGVICYILVSGLSPFMGDNDNE 468
Cdd:cd14072   159 CGSPPYAAPELFQgkkYD--GPEVDVWSLGVILYTLVSGSLPFDGQNLKE 206
STKc_ULK2 cd14201
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the ...
258-519 8.74e-30

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: 118.96  E-value: 8.74e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 258 QKVSDF-YDIEERLGSGKFGQVF--RLVEKKTRKVWAGKFFKAYSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANI 334
Cdd:cd14201     1 EVVGDFeYSRKDLVGHGAFAVVFkgRHRKKTDWEVAIKSINKKNLSKSQILLGKEIKILKELQHENIVALYDVQEMPNSV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 335 VMVLEIVSGGELFErIIDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMC-------VNKTGTRIKLIDFG 407
Cdd:cd14201    81 FLVMEYCNGGDLAD-YLQAKGTLSEDTIRVFLQQIAAAMRILHSKGIIHRDLKPQNILLsyasrkkSSVSGIRIKIADFG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 408 LARRLENAGSLKVLFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGdNDNETLANVTSATWDFDDEAFDE 487
Cdd:cd14201   160 FARYLQSNMMAATLCGSPMYMAPEVIMSQHYDAKADLWSIGTVIYQCLVGKPPFQA-NSPQDLRMFYEKNKNLQPSIPRE 238
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1034633499 488 ISDDAKDFISNLLKKDMKNRLDCTQCLQHPWL 519
Cdd:cd14201   239 TSPYLADLLLGLLQRNQKDRMDFEAFFSHPFL 270
PKc_Mps1 cd14131
Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle ...
263-519 1.12e-29

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: 118.86  E-value: 1.12e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 263 FYDIEERLGSGKFGQVFRLVEKKtRKVWAGKF--FKAYSAKEKENIRQEISIMNCL-HHPKLVQCVDA--FEEKANIVMV 337
Cdd:cd14131     2 PYEILKQLGKGGSSKVYKVLNPK-KKIYALKRvdLEGADEQTLQSYKNEIELLKKLkGSDRIIQLYDYevTDEDDYLYMV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 338 LEIvsgGEL-FERIIDEDFE--LTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKtgtRIKLIDFGLARRLEN 414
Cdd:cd14131    81 MEC---GEIdLATILKKKRPkpIDPNFIRYYWKQMLEAVHTIHEEGIVHSDLKPANFLLVKG---RLKLIDFGIAKAIQN 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 415 aGSLKVL----FGTPEFVAPEVI-------NYEP---IGYATDMWSIGVICYILVSGLSPF-MGDNDNETLANVTSATWD 479
Cdd:cd14131   155 -DTTSIVrdsqVGTLNYMSPEAIkdtsasgEGKPkskIGRPSDVWSLGCILYQMVYGKTPFqHITNPIAKLQAIIDPNHE 233
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1034633499 480 FDDEAFDEisDDAKDFISNLLKKDMKNRLDCTQCLQHPWL 519
Cdd:cd14131   234 IEFPDIPN--PDLIDVMKRCLQRDPKKRPSIPELLNHPFL 271
STKc_WNK cd13983
Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze ...
267-519 1.61e-29

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: 117.71  E-value: 1.61e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 267 EERLGSGKFGQVFR-LVEKKTRKV-WAGKFFKAYSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKA--NIVMVLEIVS 342
Cdd:cd13983     6 NEVLGRGSFKTVYRaFDTEEGIEVaWNEIKLRKLPKAERQRFKQEIEILKSLKHPNIIKFYDSWESKSkkEVIFITELMT 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 343 GGELFERIidEDFELTERECIK-YMRQISEGVEYIHKQG--IVHLDLKPENIMcVNKTGTRIKLIDFGLARRLeNAGSLK 419
Cdd:cd13983    86 SGTLKQYL--KRFKRLKLKVIKsWCRQILEGLNYLHTRDppIIHRDLKCDNIF-INGNTGEVKIGDLGLATLL-RQSFAK 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 420 VLFGTPEFVAPEVinYEPiGY--ATDMWSIGVICYILVSGLSPFMG-DNDNETLANVTSAtwdFDDEAFDEISD-DAKDF 495
Cdd:cd13983   162 SVIGTPEFMAPEM--YEE-HYdeKVDIYAFGMCLLEMATGEYPYSEcTNAAQIYKKVTSG---IKPESLSKVKDpELKDF 235
                         250       260
                  ....*....|....*....|....
gi 1034633499 496 ISNLLKKDmKNRLDCTQCLQHPWL 519
Cdd:cd13983   236 IEKCLKPP-DERPSARELLEHPFF 258
pk1 PHA03390
serine/threonine-protein kinase 1; Provisional
258-519 1.82e-29

serine/threonine-protein kinase 1; Provisional


Pssm-ID: 223069 [Multi-domain]  Cd Length: 267  Bit Score: 118.03  E-value: 1.82e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 258 QKVSDFYD---IEERLGS--GKFGQVFRLVEKKTRKVWAGKFFKA--YSAKE-------KENiRQEISIMNCLHHPKlvq 323
Cdd:PHA03390    7 SELVQFLKnceIVKKLKLidGKFGKVSVLKHKPTQKLFVQKIIKAknFNAIEpmvhqlmKDN-PNFIKLYYSVTTLK--- 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 324 cvdafeekaNIVMVLEIVSGGELFERIIDEDFeLTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCvNKTGTRIKL 403
Cdd:PHA03390   83 ---------GHVLIMDYIKDGDLFDLLKKEGK-LSEAEVKKIIRQLVEALNDLHKHNIIHNDIKLENVLY-DRAKDRIYL 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 404 IDFGLARRlenAGSLKVLFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDN----ETLANVTSatWD 479
Cdd:PHA03390  152 CDYGLCKI---IGTPSCYDGTLDYFSPEKIKGHNYDVSFDWWAVGVLTYELLTGKHPFKEDEDEeldlESLLKRQQ--KK 226
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1034633499 480 FddEAFDEISDDAKDFISNLLKKDMKNRLdCT--QCLQHPWL 519
Cdd:PHA03390  227 L--PFIKNVSKNANDFVQSMLKYNINYRL-TNynEIIKHPFL 265
PTKc_Wee1_fungi cd14052
Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the ...
264-450 1.99e-29

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: 118.29  E-value: 1.99e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 264 YDIEERLGSGKFGQVFRLVEKK-TRKVWAGKFFKAY--SAKEKENIRQEISIMNCLH---HPKLVQCVDAFEEKANIVMV 337
Cdd:cd14052     2 FANVELIGSGEFSQVYKVSERVpTGKVYAVKKLKPNyaGAKDRLRRLEEVSILRELTldgHDNIVQLIDSWEYHGHLYIQ 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 338 LEIVSGGELferiideDFELTERECIKYMR---------QISEGVEYIHKQGIVHLDLKPENIMcVNKTGTrIKLIDFGL 408
Cdd:cd14052    82 TELCENGSL-------DVFLSELGLLGRLDefrvwkilvELSLGLRFIHDHHFVHLDLKPANVL-ITFEGT-LKIGDFGM 152
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1034633499 409 ARRLENAGSLKVLfGTPEFVAPEVINYEPIGYATDMWSIGVI 450
Cdd:cd14052   153 ATVWPLIRGIERE-GDREYIAPEILSEHMYDKPADIFSLGLI 193
STKc_GRK5 cd05632
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs ...
270-537 2.09e-29

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: 119.31  E-value: 2.09e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 270 LGSGKFGQVFRLVEKKTRKVWAGKFFKAYSAKEKEN---IRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEIVSGGEL 346
Cdd:cd05632    10 LGKGGFGEVCACQVRATGKMYACKRLEKKRIKKRKGesmALNEKQILEKVNSQFVVNLAYAYETKDALCLVLTIMNGGDL 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 347 FERIID---EDFEltERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKTGTRIKliDFGLARRLENAGSLKVLFG 423
Cdd:cd05632    90 KFHIYNmgnPGFE--EERALFYAAEILCGLEDLHRENTVYRDLKPENILLDDYGHIRIS--DLGLAVKIPEGESIRGRVG 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 424 TPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDFDDEAFDEISDDAKDFISNLLKKD 503
Cdd:cd05632   166 TVGYMAPEVLNNQRYTLSPDYWGLGCLIYEMIEGQSPFRGRKEKVKREEVDRRVLETEEVYSAKFSEEAKSICKMLLTKD 245
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1034633499 504 MKNRLDCT-----QCLQHPWLmkdtKNMEAKKLSKDRMK 537
Cdd:cd05632   246 PKQRLGCQeegagEVKRHPFF----RNMNFKRLEAGMLD 280
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
266-461 2.22e-29

Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role in most cellular activities, is a reversible process mediated by protein kinases and phosphoprotein phosphatases. Protein kinases catalyze the transfer of the gamma phosphate from nucleotide triphosphates (often ATP) to one or more amino acid residues in a protein substrate side chain, resulting in a conformational change affecting protein function. Phosphoprotein phosphatases catalyze the reverse process. Protein kinases fall into three broad classes, characterized with respect to substrate specificity; Serine/threonine-protein kinases, tyrosine-protein kinases, and dual specificity protein kinases (e.g. MEK - phosphorylates both Thr and Tyr on target proteins). This entry represents the catalytic domain found in a number of serine/threonine- and tyrosine-protein kinases. It does not include the catalytic domain of dual specificity kinases.


Pssm-ID: 462242 [Multi-domain]  Cd Length: 258  Bit Score: 117.60  E-value: 2.22e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 266 IEERLGSGKFGQVFR-----LVEKKTRKVwAGKFFKA-YSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLE 339
Cdd:pfam07714   3 LGEKLGEGAFGEVYKgtlkgEGENTKIKV-AVKTLKEgADEEEREDFLEEASIMKKLDHPNIVKLLGVCTQGEPLYIVTE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 340 IVSGGELFERIIDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGTrIKLIDFGLARRLENAGSLK 419
Cdd:pfam07714  82 YMPGGDLLDFLRKHKRKLTLKDLLSMALQIAKGMEYLESKNFVHRDLAARNCL-VSENLV-VKISDFGLSRDIYDDDYYR 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1034633499 420 VLFGTPEFV---APEVINYEPIGYATDMWSIGVICYILVS-GLSPF 461
Cdd:pfam07714 160 KRGGGKLPIkwmAPESLKDGKFTSKSDVWSFGVLLWEIFTlGEQPY 205
STKc_STK10 cd06644
Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase ...
261-531 2.26e-29

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: 118.60  E-value: 2.26e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 261 SDFYDIEERLGSGKFGQVFRLVEKKTRKVWAGKFFKAYSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEI 340
Cdd:cd06644    11 NEVWEIIGELGDGAFGKVYKAKNKETGALAAAKVIETKSEEELEDYMVEIEILATCNHPYIVKLLGAFYWDGKLWIMIEF 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 341 VSGGELFERIIDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGTrIKLIDFGL-ARRLENAGSLK 419
Cdd:cd06644    91 CPGGAVDAIMLELDRGLTEPQIQVICRQMLEALQYLHSMKIIHRDLKAGNVL-LTLDGD-IKLADFGVsAKNVKTLQRRD 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 420 VLFGTPEFVAPEVINYE-----PIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSAtwdfDDEAFDEISD---D 491
Cdd:cd06644   169 SFIGTPYWMAPEVVMCEtmkdtPYDYKADIWSLGITLIEMAQIEPPHHELNPMRVLLKIAKS----EPPTLSQPSKwsmE 244
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1034633499 492 AKDFISNLLKKDMKNRLDCTQCLQHPWLMKDTKNMEAKKL 531
Cdd:cd06644   245 FRDFLKTALDKHPETRPSAAQLLEHPFVSSVTSNRPLREL 284
STKc_MSK2_N cd05614
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
270-508 2.35e-29

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


Pssm-ID: 270765 [Multi-domain]  Cd Length: 332  Bit Score: 119.25  E-value: 2.35e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 270 LGSGKFGQVFrLVEK----KTRKVWAGKFFK--AYSAKEK--ENIRQEISIMNCLHH-PKLVQCVDAFEEKANIVMVLEI 340
Cdd:cd05614     8 LGTGAYGKVF-LVRKvsghDANKLYAMKVLRkaALVQKAKtvEHTRTERNVLEHVRQsPFLVTLHYAFQTDAKLHLILDY 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 341 VSGGELFERIIDEDFeLTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGtRIKLIDFGLARRL--ENAGSL 418
Cdd:cd05614    87 VSGGELFTHLYQRDH-FSEDEVRFYSGEIILALEHLHKLGIVYRDIKLENIL-LDSEG-HVVLTDFGLSKEFltEEKERT 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 419 KVLFGTPEFVAPEVINYEP-IGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDFDDEAFDEISDDAKDFIS 497
Cdd:cd05614   164 YSFCGTIEYMAPEIIRGKSgHGKAVDWWSLGILMFELLTGASPFTLEGEKNTQSEVSRRILKCDPPFPSFIGPVARDLLQ 243
                         250
                  ....*....|.
gi 1034633499 498 NLLKKDMKNRL 508
Cdd:cd05614   244 KLLCKDPKKRL 254
STKc_PIM cd14005
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
264-519 2.75e-29

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: 116.95  E-value: 2.75e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 264 YDIEERLGSGKFGQVFRLVEKKTRKVWAGKFFKAYSAKEKENIR------QEISIM---NCLHHPKLVQCVDAFEEKANI 334
Cdd:cd14005     2 YEVGDLLGKGGFGTVYSGVRIRDGLPVAVKFVPKSRVTEWAMINgpvpvpLEIALLlkaSKPGVPGVIRLLDWYERPDGF 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 335 VMVLEIVSGGE-LFERIIDEDfELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGTRIKLIDFGLARRLE 413
Cdd:cd14005    82 LLIMERPEPCQdLFDFITERG-ALSENLARIIFRQVVEAVRHCHQRGVLHRDIKDENLL-INLRTGEVKLIDFGCGALLK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 414 NagSLKVLF-GTPEFVAPEVINY-----EPigyATdMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWdfddeafde 487
Cdd:cd14005   160 D--SVYTDFdGTRVYSPPEWIRHgryhgRP---AT-VWSLGILLYDMLCGDIPFENDEQILRGNVLFRPRL--------- 224
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1034633499 488 iSDDAKDFISNLLKKDMKNRLDCTQCLQHPWL 519
Cdd:cd14005   225 -SKECCDLISRCLQFDPSKRPSLEQILSHPWF 255
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
269-521 3.45e-29

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 119.54  E-value: 3.45e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 269 RLGSGKFGQVFRLVEKKTRKVWAGKFFkaYSAKEKENIRQ---EISIMNCLHHPKLVQCVDAFEEKANIVMVLEIVSGGE 345
Cdd:PLN00034   81 RIGSGAGGTVYKVIHRPTGRLYALKVI--YGNHEDTVRRQicrEIEILRDVNHPNVVKCHDMFDHNGEIQVLLEFMDGGS 158
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 346 LFERIIDEDFELTErecikYMRQISEGVEYIHKQGIVHLDLKPENIMcVNkTGTRIKLIDFGLARRL-ENAGSLKVLFGT 424
Cdd:PLN00034  159 LEGTHIADEQFLAD-----VARQILSGIAYLHRRHIVHRDIKPSNLL-IN-SAKNVKIADFGVSRILaQTMDPCNSSVGT 231
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 425 PEFVAPEVIN-------YEpiGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDFDDEAFDEISDDAKDFIS 497
Cdd:PLN00034  232 IAYMSPERINtdlnhgaYD--GYAGDIWSLGVSILEFYLGRFPFGVGRQGDWASLMCAICMSQPPEAPATASREFRHFIS 309
                         250       260
                  ....*....|....*....|....
gi 1034633499 498 NLLKKDMKNRLDCTQCLQHPWLMK 521
Cdd:PLN00034  310 CCLQREPAKRWSAMQLLQHPFILR 333
STKc_GRK1 cd05608
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs ...
270-517 4.75e-29

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: 117.29  E-value: 4.75e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 270 LGSGKFGQVFRLVEKKTRKVWAGKFFKAYSAKEK---ENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEIVSGGEL 346
Cdd:cd05608     9 LGKGGFGEVSACQMRATGKLYACKKLNKKRLKKRkgyEGAMVEKRILAKVHSRFIVSLAYAFQTKTDLCLVMTIMNGGDL 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 347 FERIIDEDFE---LTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKTGTRIKliDFGLARRLENAGS-LKVLF 422
Cdd:cd05608    89 RYHIYNVDEEnpgFQEPRACFYTAQIISGLEHLHQRRIIYRDLKPENVLLDDDGNVRIS--DLGLAVELKDGQTkTKGYA 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 423 GTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDFDDEAFDEISDDAKDFISNLLKK 502
Cdd:cd05608   167 GTPGFMAPELLLGEEYDYSVDYFTLGVTLYEMIAARGPFRARGEKVENKELKQRILNDSVTYSEKFSPASKSICEALLAK 246
                         250       260
                  ....*....|....*....|
gi 1034633499 503 DMKNRL-----DCTQCLQHP 517
Cdd:cd05608   247 DPEKRLgfrdgNCDGLRTHP 266
STKc_MAP4K3_like cd06613
Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like ...
264-517 6.28e-29

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: 116.25  E-value: 6.28e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 264 YDIEERLGSGKFGQVFRLVEKKTRKVWAGKFFKAYSAKEKENIRQEISIMNCLHHPKLVQCVDAF--EEKANIVMvlEIV 341
Cdd:cd06613     2 YELIQRIGSGTYGDVYKARNIATGELAAVKVIKLEPGDDFEIIQQEISMLKECRHPNIVAYFGSYlrRDKLWIVM--EYC 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 342 SGGELFErIIDEDFELTEReCIKYM-RQISEGVEYIHKQGIVHLDLKPENIMcVNKTGtRIKLIDFGLARRLENAGSLKV 420
Cdd:cd06613    80 GGGSLQD-IYQVTGPLSEL-QIAYVcRETLKGLAYLHSTGKIHRDIKGANIL-LTEDG-DVKLADFGVSAQLTATIAKRK 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 421 LF-GTPEFVAPEVINYE-PIGYAT--DMWSIGVICYILVSGLSP----------FM---GDNDNETLANvtSATWdfdde 483
Cdd:cd06613   156 SFiGTPYWMAPEVAAVErKGGYDGkcDIWALGITAIELAELQPPmfdlhpmralFLipkSNFDPPKLKD--KEKW----- 228
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1034633499 484 afdeiSDDAKDFISNLLKKDMKNRLDCTQCLQHP 517
Cdd:cd06613   229 -----SPDFHDFIKKCLTKNPKKRPTATKLLQHP 257
STKc_GRK4 cd05631
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs ...
270-531 7.53e-29

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: 116.63  E-value: 7.53e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 270 LGSGKFGQVFRLVEKKTRKVWAGKFFKAYSAKEKEN---IRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEIVSGGEL 346
Cdd:cd05631     8 LGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKGeamALNEKRILEKVNSRFVVSLAYAYETKDALCLVLTIMNGGDL 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 347 FERIID-EDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKTGTRIKliDFGLARRLENAGSLKVLFGTP 425
Cdd:cd05631    88 KFHIYNmGNPGFDEQRAIFYAAELCCGLEDLQRERIVYRDLKPENILLDDRGHIRIS--DLGLAVQIPEGETVRGRVGTV 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 426 EFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDFDDEAFDEISDDAKDFISNLLKKDMK 505
Cdd:cd05631   166 GYMAPEVINNEKYTFSPDWWGLGCLIYEMIQGQSPFRKRKERVKREEVDRRVKEDQEEYSEKFSEDAKSICRMLLTKNPK 245
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1034633499 506 NRLDCT-----QCLQHPwLMKDT--KNMEAKKL 531
Cdd:cd05631   246 ERLGCRgngaaGVKQHP-IFKNInfKRLEANML 277
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
268-475 9.15e-29

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: 115.71  E-value: 9.15e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 268 ERLGSGKFGQVFR----LVEKKTRKVwAGKFFKAY-SAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEIVS 342
Cdd:cd00192     1 KKLGEGAFGEVYKgklkGGDGKTVDV-AVKTLKEDaSESERKDFLKEARVMKKLGHPNVVRLLGVCTEEEPLYLVMEYME 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 343 GGEL--------FERIIDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGTrIKLIDFGLARRLEN 414
Cdd:cd00192    80 GGDLldflrksrPVFPSPEPSTLSLKDLLSFAIQIAKGMEYLASKKFVHRDLAARNCL-VGEDLV-VKISDFGLSRDIYD 157
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034633499 415 AGSLKVLFGTPEFV---APEVINYEPIGYATDMWSIGVICYILVS-GLSPFMGDNDNETLANVTS 475
Cdd:cd00192   158 DDYYRKKTGGKLPIrwmAPESLKDGIFTSKSDVWSFGVLLWEIFTlGATPYPGLSNEEVLEYLRK 222
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
270-510 9.23e-29

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: 116.47  E-value: 9.23e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 270 LGSGKFGQVFRLVEKKTRKVWAGKFFKAYSAKEKENIR---QEISIMNCLHHPKLVQCVDAFEEKANIVMVLEIVSGGEL 346
Cdd:cd05577     1 LGRGGFGEVCACQVKATGKMYACKKLDKKRIKKKKGETmalNEKIILEKVSSPFIVSLAYAFETKDKLCLVLTLMNGGDL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 347 FERIIDEDFE-LTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKTGTRIKliDFGLARRLENAGSLKVLFGTP 425
Cdd:cd05577    81 KYHIYNVGTRgFSEARAIFYAAEIICGLEHLHNRFIVYRDLKPENILLDDHGHVRIS--DLGLAVEFKGGKKIKGRVGTH 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 426 EFVAPEVI-NYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDFDDEAFDEISDDAKDFISNLLKKDM 504
Cdd:cd05577   159 GYMAPEVLqKEVAYDFSVDWFALGCMLYEMIAGRSPFRQRKEKVDKEELKRRTLEMAVEYPDSFSPEARSLCEGLLQKDP 238

                  ....*.
gi 1034633499 505 KNRLDC 510
Cdd:cd05577   239 ERRLGC 244
STKc_TSSK1_2-like cd14165
Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; ...
308-519 1.66e-28

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: 115.26  E-value: 1.66e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 308 QEISIMNCLHHPKLVQCVDAFE-EKANIVMVLEIVSGGELFeRIIDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDL 386
Cdd:cd14165    50 RELEILARLNHKSIIKTYEIFEtSDGKVYIVMELGVQGDLL-EFIKLRGALPEDVARKMFHQLSSAIKYCHELDIVHRDL 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 387 KPENIMCVNKtgTRIKLIDFGLARRLENAGSLKVLF-----GTPEFVAPEVIN---YEPIGYatDMWSIGVICYILVSGL 458
Cdd:cd14165   129 KCENLLLDKD--FNIKLTDFGFSKRCLRDENGRIVLsktfcGSAAYAAPEVLQgipYDPRIY--DIWSLGVILYIMVCGS 204
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034633499 459 SPFMGDNDNETLANVTSATWDFDDEAFDeiSDDAKDFISNLLKKDMKNRLDCTQCLQHPWL 519
Cdd:cd14165   205 MPYDDSNVKKMLKIQKEHRVRFPRSKNL--TSECKDLIYRLLQPDVSQRLCIDEVLSHPWL 263
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
270-460 1.71e-28

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: 115.11  E-value: 1.71e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 270 LGSGKFGQVFRLVEKKTRKVWAGKFFKAYSAKEKENIRqEISIMNCL-HHPKLVQCVD-AFEEKANIVMVLEIVSGGELF 347
Cdd:cd13987     1 LGEGTYGKVLLAVHKGSGTKMALKFVPKPSTKLKDFLR-EYNISLELsVHPHIIKTYDvAFETEDYYVFAQEYAPYGDLF 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 348 ErIIDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKTGTRIKLIDFGLARRlenAGSL-KVLFGTPE 426
Cdd:cd13987    80 S-IIPPQVGLPEERVKRCAAQLASALDFMHSKNLVHRDIKPENVLLFDKDCRRVKLCDFGLTRR---VGSTvKRVSGTIP 155
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1034633499 427 FVAPEVINYEP-----IGYATDMWSIGVICYILVSGLSP 460
Cdd:cd13987   156 YTAPEVCEAKKnegfvVDPSIDVWAFGVLLFCCLTGNFP 194
STKc_SGK2 cd05603
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; ...
270-508 1.81e-28

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: 116.61  E-value: 1.81e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 270 LGSGKFGQVFRLVEKKTRKVWAGKFFKAYS---AKEKENIRQEISIM-NCLHHPKLVQCVDAFEEKANIVMVLEIVSGGE 345
Cdd:cd05603     3 IGKGSFGKVLLAKRKCDGKFYAVKVLQKKTilkKKEQNHIMAERNVLlKNLKHPFLVGLHYSFQTSEKLYFVLDYVNGGE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 346 LFeriidedFELTERECIK------YMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGtRIKLIDFGLARR-LENAGSL 418
Cdd:cd05603    83 LF-------FHLQRERCFLeprarfYAAEVASAIGYLHSLNIIYRDLKPENIL-LDCQG-HVVLTDFGLCKEgMEPEETT 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 419 KVLFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDFDDEAfdeiSDDAKDFISN 498
Cdd:cd05603   154 STFCGTPEYLAPEVLRKEPYDRTVDWWCLGAVLYEMLYGLPPFYSRDVSQMYDNILHKPLHLPGGK----TVAACDLLQG 229
                         250
                  ....*....|
gi 1034633499 499 LLKKDMKNRL 508
Cdd:cd05603   230 LLHKDQRRRL 239
STKc_Nek1 cd08218
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
264-519 2.05e-28

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: 114.52  E-value: 2.05e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 264 YDIEERLGSGKFGQVFRLVEKKTRKVWAGKFFK--AYSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEIV 341
Cdd:cd08218     2 YVRIKKIGEGSFGKALLVKSKEDGKQYVIKEINisKMSPKEREESRKEVAVLSKMKHPNIVQYQESFEENGNLYIVMDYC 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 342 SGGELFERI-IDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGTrIKLIDFGLARRLENAGSL-K 419
Cdd:cd08218    82 DGGDLYKRInAQRGVLFPEDQILDWFVQLCLALKHVHDRKILHRDIKSQNIF-LTKDGI-IKLGDFGIARVLNSTVELaR 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 420 VLFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDFDDEAFdeiSDDAKDFISNL 499
Cdd:cd08218   160 TCIGTPYYLSPEICENKPYNNKSDIWALGCVLYEMCTLKHAFEAGNMKNLVLKIIRGSYPPVPSRY---SYDLRSLVSQL 236
                         250       260
                  ....*....|....*....|
gi 1034633499 500 LKKDMKNRLDCTQCLQHPWL 519
Cdd:cd08218   237 FKRNPRDRPSINSILEKPFI 256
STKc_PAK_I cd06647
Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze ...
268-519 2.62e-28

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: 114.64  E-value: 2.62e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 268 ERLGSGKFGQVFRLVEKKTRKVWAGKFFKAYSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEIVSGGELF 347
Cdd:cd06647    13 EKIGQGASGTVYTAIDVATGQEVAIKQMNLQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSLT 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 348 ERIIDEDFEltERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGTrIKLIDFGLARRLENAGSLK-VLFGTPE 426
Cdd:cd06647    93 DVVTETCMD--EGQIAAVCRECLQALEFLHSNQVIHRDIKSDNIL-LGMDGS-VKLTDFGFCAQITPEQSKRsTMVGTPY 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 427 FVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANV-TSATWDFDDEafDEISDDAKDFISNLLKKDMK 505
Cdd:cd06647   169 WMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIaTNGTPELQNP--EKLSAIFRDFLNRCLEMDVE 246
                         250
                  ....*....|....
gi 1034633499 506 NRLDCTQCLQHPWL 519
Cdd:cd06647   247 KRGSAKELLQHPFL 260
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
270-519 3.05e-28

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: 114.06  E-value: 3.05e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 270 LGSGKFGQ--VFRLVEKKTRKVWAGKFFKAYSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEIVSGGELF 347
Cdd:cd08221     8 LGRGAFGEavLYRKTEDNSLVVWKEVNLSRLSEKERRDALNEIDILSLLNHDNIITYYNHFLDGESLFIEMEYCNGGNLH 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 348 ERIIDEDFELTERE-CIKYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGTrIKLIDFGLARRLENAGSL-KVLFGTP 425
Cdd:cd08221    88 DKIAQQKNQLFPEEvVLWYLYQIVSAVSHIHKAGILHRDIKTLNIF-LTKADL-VKLGDFGISKVLDSESSMaESIVGTP 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 426 EFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDFDDEAFdeiSDDAKDFISNLLKKDMK 505
Cdd:cd08221   166 YYMSPELVQGVKYNFKSDIWAVGCVLYELLTLKRTFDATNPLRLAVKIVQGEYEDIDEQY---SEEIIQLVHDCLHQDPE 242
                         250
                  ....*....|....
gi 1034633499 506 NRLDCTQCLQHPWL 519
Cdd:cd08221   243 DRPTAEELLERPLL 256
STKc_Cdc7 cd14019
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze ...
264-519 6.45e-28

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


Pssm-ID: 270921 [Multi-domain]  Cd Length: 252  Bit Score: 113.09  E-value: 6.45e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 264 YDIEERLGSGKFGQVFRLVEKKTRKVWA--GKFF---KAYSAKEKENIRQEISimnCLHHPKLVQCV----DAFEEKANI 334
Cdd:cd14019     3 YRIIEKIGEGTFSSVYKAEDKLHDLYDRnkGRLValkHIYPTSSPSRILNELE---CLERLGGSNNVsgliTAFRNEDQV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 335 VMVLEivsggeLFERIIDEDF--ELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKTGTRIkLIDFGLARRL 412
Cdd:cd14019    80 VAVLP------YIEHDDFRDFyrKMSLTDIRIYLRNLFKALKHVHSFGIIHRDVKPGNFLYNRETGKGV-LVDFGLAQRE 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 413 ENAGSLKV-LFGTPEFVAPEVI-NYEPIGYATDMWSIGVI-CYILVSGLSPFMGDNDNETLAnvtsatwdfddeafdEI- 488
Cdd:cd14019   153 EDRPEQRApRAGTRGFRAPEVLfKCPHQTTAIDIWSAGVIlLSILSGRFPFFFSSDDIDALA---------------EIa 217
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1034633499 489 ----SDDAKDFISNLLKKDMKNRLDCTQCLQHPWL 519
Cdd:cd14019   218 tifgSDEAYDLLDKLLELDPSKRITAEEALKHPFF 252
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
264-524 6.49e-28

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: 113.58  E-value: 6.49e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 264 YDIEERLGSGKFGQVFRLVEKKTRKVWAGKffKAYSAKEKEN--IRQEISIMNCL-HHPKLVQCVDA----FEEKANIVM 336
Cdd:cd13985     2 YQVTKQLGEGGFSYVYLAHDVNTGRRYALK--RMYFNDEEQLrvAIKEIEIMKRLcGHPNIVQYYDSailsSEGRKEVLL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 337 VLEIVsGGELFERI-IDEDFELTERECIKYMRQISEGVEYIHKQG--IVHLDLKPENIMCVNktGTRIKLIDFGLA---- 409
Cdd:cd13985    80 LMEYC-PGSLVDILeKSPPSPLSEEEVLRIFYQICQAVGHLHSQSppIIHRDIKIENILFSN--TGRFKLCDFGSAtteh 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 410 ---RRLENAGSLKVLFG---TPEFVAPEVIN---YEPIGYATDMWSIGVICYILVSGLSPFmgdNDNETLANVTSatwDF 480
Cdd:cd13985   157 yplERAEEVNIIEEEIQkntTPMYRAPEMIDlysKKPIGEKADIWALGCLLYKLCFFKLPF---DESSKLAIVAG---KY 230
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1034633499 481 DDEAFDEISDDAKDFISNLLKKDMKNRLDCTQCLQhpWLMKDTK 524
Cdd:cd13985   231 SIPEQPRYSPELHDLIRHMLTPDPAERPDIFQVIN--IITKDTK 272
STKc_Nek11 cd08222
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
264-519 7.43e-28

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: 113.29  E-value: 7.43e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 264 YDIEERLGSGKFGQVFRLVEKKTRKVWAGKFFKAYSA---KEKENIR--QEISIMNCLHHPKLVQCVDAFEEKANIVMVL 338
Cdd:cd08222     2 YRVVRKLGSGNFGTVYLVSDLKATADEELKVLKEISVgelQPDETVDanREAKLLSKLDHPAIVKFHDSFVEKESFCIVT 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 339 EIVSGGELFERI---IDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKTgtrIKLIDFGLARRLENA 415
Cdd:cd08222    82 EYCEGGDLDDKIseyKKSGTTIDENQILDWFIQLLLAVQYMHERRILHRDLKAKNIFLKNNV---IKVGDFGISRILMGT 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 416 GSLKVLF-GTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNdnetLANVTSATWDFDDEAFDEI-SDDAK 493
Cdd:cd08222   159 SDLATTFtGTPYYMSPEVLKHEGYNSKSDIWSLGCILYEMCCLKHAFDGQN----LLSVMYKIVEGETPSLPDKySKELN 234
                         250       260
                  ....*....|....*....|....*.
gi 1034633499 494 DFISNLLKKDMKNRLDCTQCLQHPWL 519
Cdd:cd08222   235 AIYSRMLNKDPALRPSAAEILKIPFI 260
STKc_myosinIII_N_like cd06608
N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze ...
261-519 7.65e-28

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: 113.55  E-value: 7.65e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 261 SDFYDIEERLGSGKFGQVFRLVEKKTRKVWAGKFFKaYSAKEKENIRQEISIMNCL-HHPKLVQCVDAFEEKANIVM--- 336
Cdd:cd06608     5 AGIFELVEVIGEGTYGKVYKARHKKTGQLAAIKIMD-IIEDEEEEIKLEINILRKFsNHPNIATFYGAFIKKDPPGGddq 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 337 ---VLEIVSGG---ELFERIIDEDFELTErECIKY-MRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGtRIKLIDFGLA 409
Cdd:cd06608    84 lwlVMEYCGGGsvtDLVKGLRKKGKRLKE-EWIAYiLRETLRGLAYLHENKVIHRDIKGQNIL-LTEEA-EVKLVDFGVS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 410 RRLENAGSLKVLF-GTPEFVAPEVI----NYEP-IGYATDMWSIGVICYILVSGLSPFmGD------------NDNETLA 471
Cdd:cd06608   161 AQLDSTLGRRNTFiGTPYWMAPEVIacdqQPDAsYDARCDVWSLGITAIELADGKPPL-CDmhpmralfkiprNPPPTLK 239
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1034633499 472 NVTSatWdfddeafdeiSDDAKDFISNLLKKDMKNRLDCTQCLQHPWL 519
Cdd:cd06608   240 SPEK--W----------SKEFNDFISECLIKNYEQRPFTEELLEHPFI 275
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
270-471 7.99e-28

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: 113.29  E-value: 7.99e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 270 LGSGKFGQVFRLVEKKTRKVWAGK--FFKAYSAKEK----ENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEIVSG 343
Cdd:cd06630     8 LGTGAFSSCYQARDVKTGTLMAVKqvSFCRNSSSEQeevvEAIREEIRMMARLNHPNIVRMLGATQHKSHFNIFVEWMAG 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 344 GELfERIIDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGTRIKLIDFGLARRLEN----AGSLK 419
Cdd:cd06630    88 GSV-ASLLSKYGAFSENVIINYTLQILRGLAYLHDNQIIHRDLKGANLL-VDSTGQRLRIADFGAAARLASkgtgAGEFQ 165
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1034633499 420 -VLFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLA 471
Cdd:cd06630   166 gQLLGTIAFMAPEVLRGEQYGRSCDVWSVGCVIIEMATAKPPWNAEKISNHLA 218
STKc_YPK1_like cd05585
Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the ...
270-531 8.32e-28

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: 114.59  E-value: 8.32e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 270 LGSGKFGQVFRLVEKKTRKVWAGKFF-KAY--SAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEIVSGGEL 346
Cdd:cd05585     2 IGKGSFGKVMQVRKKDTSRIYALKTIrKAHivSRSEVTHTLAERTVLAQVDCPFIVPLKFSFQSPEKLYLVLAFINGGEL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 347 FERIIDED-FELTERECikYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGtRIKLIDFGLAR-RLENAGSLKVLFGT 424
Cdd:cd05585    82 FHHLQREGrFDLSRARF--YTAELLCALECLHKFNVIYRDLKPENIL-LDYTG-HIALCDFGLCKlNMKDDDKTNTFCGT 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 425 PEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDFDdeafDEISDDAKDFISNLLKKDM 504
Cdd:cd05585   158 PEYLAPELLLGHGYTKAVDWWTLGVLLYEMLTGLPPFYDENTNEMYRKILQEPLRFP----DGFDRDAKDLLIGLLNRDP 233
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1034633499 505 KNRL---DCTQCLQHPWLMK-DTKNMEAKKL 531
Cdd:cd05585   234 TKRLgynGAQEIKNHPFFDQiDWKRLLMKKI 264
STKc_PKB_alpha cd05594
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); ...
270-532 8.48e-28

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: 115.51  E-value: 8.48e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 270 LGSGKFGQVFRLVEKKTRKVWAGKFFKAYSAKEKENIRQEIS---IMNCLHHPKLVQCVDAFEEKANIVMVLEIVSGGEL 346
Cdd:cd05594    33 LGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTenrVLQNSRHPFLTALKYSFQTHDRLCFVMEYANGGEL 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 347 FERIiDEDFELTERECIKYMRQISEGVEYIH-KQGIVHLDLKPENIMcVNKTGtRIKLIDFGLARR-LENAGSLKVLFGT 424
Cdd:cd05594   113 FFHL-SRERVFSEDRARFYGAEIVSALDYLHsEKNVVYRDLKLENLM-LDKDG-HIKITDFGLCKEgIKDGATMKTFCGT 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 425 PEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMgDNDNETLANVTSatwdFDDEAFDE-ISDDAKDFISNLLKKD 503
Cdd:cd05594   190 PEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFY-NQDHEKLFELIL----MEEIRFPRtLSPEAKSLLSGLLKKD 264
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1034633499 504 MKNRL-----DCTQCLQHPWLMK-DTKNMEAKKLS 532
Cdd:cd05594   265 PKQRLgggpdDAKEIMQHKFFAGiVWQDVYEKKLV 299
STKc_Sck1_like cd05586
Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine ...
270-536 9.64e-28

Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Schizosaccharomyces pombe Sck1 and similar fungal proteins. Sck1 plays a role in trehalase activation triggered by glucose and a nitrogen source. Trehalase catalyzes the cleavage of the disaccharide trehalose to glucose. Trehalose, as a carbohydrate reserve and stress metabolite, plays an important role in the response of yeast to environmental changes. The Sck1-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270738 [Multi-domain]  Cd Length: 330  Bit Score: 114.59  E-value: 9.64e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 270 LGSGKFGQVFRLVEKKTRKVWAGKFF-KAYSAKEKE--------NIRQEISIMNClhhPKLVQCVDAFEEKANIVMVLEI 340
Cdd:cd05586     1 IGKGTFGQVYQVRKKDTRRIYAMKVLsKKVIVAKKEvahtigerNILVRTALDES---PFIVGLKFSFQTPTDLYLVTDY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 341 VSGGELFERIiDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGtRIKLIDFGLAR-RLENAGSLK 419
Cdd:cd05586    78 MSGGELFWHL-QKEGRFSEDRAKFYIAELVLALEHLHKNDIVYRDLKPENIL-LDANG-HIALCDFGLSKaDLTDNKTTN 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 420 VLFGTPEFVAPEVInYEPIGYA--TDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDFDDeafDEISDDAKDFIS 497
Cdd:cd05586   155 TFCGTTEYLAPEVL-LDEKGYTkmVDFWSLGVLVFEMCCGWSPFYAEDTQQMYRNIAFGKVRFPK---DVLSDEGRSFVK 230
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1034633499 498 NLLKKDMKNRL----DCTQCLQHPWLmkdtKNMEAKKLSKDRM 536
Cdd:cd05586   231 GLLNRNPKHRLgahdDAVELKEHPFF----ADIDWDLLSKKKI 269
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
270-538 1.10e-27

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 114.47  E-value: 1.10e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 270 LGSGKFGQVFRLVEKKTRKVWAGKFFKAYS-AKEKENIRQ-------------EISIMNCLHHPKLVQCVDAFEEKANIV 335
Cdd:PTZ00024   17 LGEGTYGKVEKAYDTLTGKIVAIKKVKIIEiSNDVTKDRQlvgmcgihfttlrELKIMNEIKHENIMGLVDVYVEGDFIN 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 336 MVLEIVSGGelFERIIDEDFELTE--RECIkyMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGTrIKLIDFGLARRLE 413
Cdd:PTZ00024   97 LVMDIMASD--LKKVVDRKIRLTEsqVKCI--LLQILNGLNVLHKWYFMHRDLSPANIF-INSKGI-CKIADFGLARRYG 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 414 NAGSLKVLFG----------TPEFV-----APEVI-NYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANV---- 473
Cdd:PTZ00024  171 YPPYSDTLSKdetmqrreemTSKVVtlwyrAPELLmGAEKYHFAVDMWSVGCIFAELLTGKPLFPGENEIDQLGRIfell 250
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 474 ---TSATW------------------DFDDeAFDEISDDAKDFISNLLKKDMKNRLDCTQCLQHPWLMKDTKNMEAKKLS 532
Cdd:PTZ00024  251 gtpNEDNWpqakklplyteftprkpkDLKT-IFPNASDDAIDLLQSLLKLNPLERISAKEALKHEYFKSDPLPCDPSQLP 329

                  ....*.
gi 1034633499 533 KDRMKK 538
Cdd:PTZ00024  330 FNFLTK 335
STKc_TBK1 cd13988
Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the ...
270-461 1.29e-27

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


Pssm-ID: 270890 [Multi-domain]  Cd Length: 316  Bit Score: 114.13  E-value: 1.29e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 270 LGSGKFGQVFRLVEKKTRKVWAGKFFKAYSAKEKENIR-QEISIMNCLHHPKLVQCVdAFEEKANI---VMVLEIVSGGE 345
Cdd:cd13988     1 LGQGATANVFRGRHKKTGDLYAVKVFNNLSFMRPLDVQmREFEVLKKLNHKNIVKLF-AIEEELTTrhkVLVMELCPCGS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 346 LFErIIDE---DFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCV-NKTGTRI-KLIDFGLARRLENAGSLKV 420
Cdd:cd13988    80 LYT-VLEEpsnAYGLPESEFLIVLRDVVAGMNHLRENGIVHRDIKPGNIMRViGEDGQSVyKLTDFGAARELEDDEQFVS 158
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1034633499 421 LFGTPEFVAPEVinYE----------PIGYATDMWSIGVICYILVSGLSPF 461
Cdd:cd13988   159 LYGTEEYLHPDM--YEravlrkdhqkKYGATVDLWSIGVTFYHAATGSLPF 207
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
264-517 1.48e-27

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: 112.13  E-value: 1.48e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 264 YDIEERLGSGKFGQVF---RLVEKKTRKVWAGKFfKAYSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEI 340
Cdd:cd08220     2 YEKIRVVGRGAYGTVYlcrRKDDNKLVIIKQIPV-EQMTKEERQAALNEVKVLSMLHHPNIIEYYESFLEDKALMIVMEY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 341 VSGGELFERIIDE-DFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGTRIKLIDFGLARRLENAGSLK 419
Cdd:cd08220    81 APGGTLFEYIQQRkGSLLSEEEILHFFVQILLALHHVHSKQILHRDLKTQNIL-LNKKRTVVKIGDFGISKILSSKSKAY 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 420 VLFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATwdfddeaFDEISD----DAKDF 495
Cdd:cd08220   160 TVVGTPCYISPELCEGKPYNQKSDIWALGCVLYELASLKRAFEAANLPALVLKIMRGT-------FAPISDryseELRHL 232
                         250       260
                  ....*....|....*....|..
gi 1034633499 496 ISNLLKKDMKNRLDCTQCLQHP 517
Cdd:cd08220   233 ILSMLHLDPNKRPTLSEIMAQP 254
STKc_ASK cd06624
Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs ...
262-519 2.32e-27

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: 112.12  E-value: 2.32e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 262 DFYDIEER--LGSGKFGQVFRLVEKKTRKVWAGKFFKAYSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLE 339
Cdd:cd06624     6 EYDESGERvvLGKGTFGVVYAARDLSTQVRIAIKEIPERDSREVQPLHEEIALHSRLSHKNIVQYLGSVSEDGFFKIFME 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 340 IVSGGELFERIIDEDFELTERE--CIKYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGTRIKLIDFGLARRLE---- 413
Cdd:cd06624    86 QVPGGSLSALLRSKWGPLKDNEntIGYYTKQILEGLKYLHDNKIVHRDIKGDNVL-VNTYSGVVKISDFGTSKRLAginp 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 414 NAGSLKvlfGTPEFVAPEVINYEPIGY--ATDMWSIGVICYILVSGLSPFMGDNDNETlANVTSATWDFDDEAFDEISDD 491
Cdd:cd06624   165 CTETFT---GTLQYMAPEVIDKGQRGYgpPADIWSLGCTIIEMATGKPPFIELGEPQA-AMFKVGMFKIHPEIPESLSEE 240
                         250       260
                  ....*....|....*....|....*...
gi 1034633499 492 AKDFISNLLKKDMKNRLDCTQCLQHPWL 519
Cdd:cd06624   241 AKSFILRCFEPDPDKRATASDLLQDPFL 268
STKc_SGK3 cd05604
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
270-531 2.39e-27

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: 113.52  E-value: 2.39e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 270 LGSGKFGQVFRLVEKKTRKVWAGKFFKA---YSAKEKENIRQEISIM-NCLHHPKLVQCVDAFEEKANIVMVLEIVSGGE 345
Cdd:cd05604     4 IGKGSFGKVLLAKRKRDGKYYAVKVLQKkviLNRKEQKHIMAERNVLlKNVKHPFLVGLHYSFQTTDKLYFVLDFVNGGE 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 346 LFERIIDEDFeLTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGtRIKLIDFGLARR-LENAGSLKVLFGT 424
Cdd:cd05604    84 LFFHLQRERS-FPEPRARFYAAEIASALGYLHSINIVYRDLKPENIL-LDSQG-HIVLTDFGLCKEgISNSDTTTTFCGT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 425 PEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDFDdeafDEISDDAKDFISNLLKKDM 504
Cdd:cd05604   161 PEYLAPEVIRKQPYDNTVDWWCLGSVLYEMLYGLPPFYCRDTAEMYENILHKPLVLR----PGISLTAWSILEELLEKDR 236
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1034633499 505 KNRL----DCTQCLQHPWLMK-DTKNMEAKKL 531
Cdd:cd05604   237 QLRLgakeDFLEIKNHPFFESiNWTDLVQKKI 268
STKc_GRK6 cd05630
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs ...
270-531 2.42e-27

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: 112.42  E-value: 2.42e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 270 LGSGKFGQVFRLVEKKTRKVWAGKFFKAYSAKEKEN---IRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEIVSGGEL 346
Cdd:cd05630     8 LGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKGeamALNEKQILEKVNSRFVVSLAYAYETKDALCLVLTLMNGGDL 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 347 FERII---DEDFEltERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKTGTRIKliDFGLARRLENAGSLKVLFG 423
Cdd:cd05630    88 KFHIYhmgQAGFP--EARAVFYAAEICCGLEDLHRERIVYRDLKPENILLDDHGHIRIS--DLGLAVHVPEGQTIKGRVG 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 424 TPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDFDDEAFDEISDDAKDFISNLLKKD 503
Cdd:cd05630   164 TVGYMAPEVVKNERYTFSPDWWALGCLLYEMIAGQSPFQQRKKKIKREEVERLVKEVPEEYSEKFSPQARSLCSMLLCKD 243
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1034633499 504 MKNRLDC-----TQCLQHPWLMK-DTKNMEAKKL 531
Cdd:cd05630   244 PAERLGCrgggaREVKEHPLFKKlNFKRLGAGML 277
STKc_IKK cd13989
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
270-478 3.38e-27

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: 112.16  E-value: 3.38e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 270 LGSGKFGQVFRLVEKKTRKVWAGK---FFKAYSAKEKENIRQEISIMNCLHHPKLVQCVDAFE--EKANI----VMVLEI 340
Cdd:cd13989     1 LGSGGFGYVTLWKHQDTGEYVAIKkcrQELSPSDKNRERWCLEVQIMKKLNHPNVVSARDVPPelEKLSPndlpLLAMEY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 341 VSGGELfeRIIDEDFE----LTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKTGTRI-KLIDFGLARRLENA 415
Cdd:cd13989    81 CSGGDL--RKVLNQPEnccgLKESEVRTLLSDISSAISYLHENRIIHRDLKPENIVLQQGGGRVIyKLIDLGYAKELDQG 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034633499 416 GSLKVLFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFmgdndnetLANVTSATW 478
Cdd:cd13989   159 SLCTSFVGTLQYLAPELFESKKYTCTVDYWSFGTLAFECITGYRPF--------LPNWQPVQW 213
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
264-514 4.69e-27

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: 110.83  E-value: 4.69e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 264 YDIEERLGSGKFGQVFRLVEKKTRKVWAGKFFK-AYSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEIVS 342
Cdd:cd08219     2 YNVLRVVGEGSFGRALLVQHVNSDQKYAMKEIRlPKSSSAVEDSRKEAVLLAKMKHPNIVAFKESFEADGHLYIVMEYCD 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 343 GGELFERIIDEDFEL-TERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKtgTRIKLIDFGLARRLENAGSLKVL 421
Cdd:cd08219    82 GGDLMQKIKLQRGKLfPEDTILQWFVQMCLGVQHIHEKRVLHRDIKSKNIFLTQN--GKVKLGDFGSARLLTSPGAYACT 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 422 F-GTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDFDDEAFdeiSDDAKDFISNLL 500
Cdd:cd08219   160 YvGTPYYVPPEIWENMPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQGSYKPLPSHY---SYELRSLIKQMF 236
                         250
                  ....*....|....
gi 1034633499 501 KKDMKNRLDCTQCL 514
Cdd:cd08219   237 KRNPRSRPSATTIL 250
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
264-512 5.16e-27

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: 111.05  E-value: 5.16e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 264 YDIEERLGSGKFGQVFRlVEKKT--RKVWAGKFFKAYS------AKEKE----NIRQEISIM-NCLHHPKLVQCVDAFEE 330
Cdd:cd08528     2 YAVLELLGSGAFGCVYK-VRKKSngQTLLALKEINMTNpafgrtEQERDksvgDIISEVNIIkEQLRHPNIVRYYKTFLE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 331 KANIVMVLEIVSG---GELFERIIDEDFELTERECIKYMRQISEGVEYIHKQ-GIVHLDLKPENIMCvnKTGTRIKLIDF 406
Cdd:cd08528    81 NDRLYIVMELIEGaplGEHFSSLKEKNEHFTEDRIWNIFVQMVLALRYLHKEkQIVHRDLKPNNIML--GEDDKVTITDF 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 407 GLAR-RLENAGSLKVLFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNdNETLAN-VTSATWDFDDEa 484
Cdd:cd08528   159 GLAKqKGPESSKMTSVVGTILYSCPEIVQNEPYGEKADIWALGCILYQMCTLQPPFYSTN-MLTLATkIVEAEYEPLPE- 236
                         250       260
                  ....*....|....*....|....*...
gi 1034633499 485 fDEISDDAKDFISNLLKKDMKNRLDCTQ 512
Cdd:cd08528   237 -GMYSDDITFVIRSCLTPDPEARPDIVE 263
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
261-521 5.35e-27

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: 110.90  E-value: 5.35e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 261 SDFYDIEErLGSGKFGQVFRLVEKKTRKVWAGKFFKAYSAKEKEN-IRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLE 339
Cdd:cd06605     1 DDLEYLGE-LGEGNGGVVSKVRHRPSGQIMAVKVIRLEIDEALQKqILRELDVLHKCNSPYIVGFYGAFYSEGDISICME 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 340 IVSGGELfERIIDEDFELTERECIKYMRQISEGVEYIH-KQGIVHLDLKPENIMcVNKTGTrIKLIDFGLARRLENAGSl 418
Cdd:cd06605    80 YMDGGSL-DKILKEVGRIPERILGKIAVAVVKGLIYLHeKHKIIHRDVKPSNIL-VNSRGQ-VKLCDFGVSGQLVDSLA- 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 419 KVLFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFmgdndnetlANVTSATWDFDDEAFDEI---------- 488
Cdd:cd06605   156 KTFVGTRSYMAPERISGGKYTVKSDIWSLGLSLVELATGRFPY---------PPPNAKPSMMIFELLSYIvdepppllps 226
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1034633499 489 ---SDDAKDFISNLLKKDMKNRLDCTQCLQHPWLMK 521
Cdd:cd06605   227 gkfSPDFQDFVSQCLQKDPTERPSYKELMEHPFIKR 262
STKc_CK2_alpha cd14132
Catalytic subunit (alpha) of the Serine/Threonine Kinase, Casein Kinase 2; STKs catalyze the ...
248-517 6.56e-27

Catalytic subunit (alpha) of the Serine/Threonine Kinase, Casein Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CK2 is a tetrameric protein with two catalytic (alpha) and two regulatory (beta) subunits. It is constitutively active and ubiquitously expressed, and is found in the cytoplasm, nucleus, as well as in the plasma membrane. It phosphorylates a wide variety of substrates including gylcogen synthase, cell cycle proteins, nuclear proteins (e.g. DNA topoisomerase II), and ion channels (e.g. ENaC), among others. It may be considered a master kinase controlling the activity or lifespan of many other kinases and exerting its effect over cell fate, gene expression, protein synthesis and degradation, and viral infection. CK2 is implicated in every stage of the cell cycle and is required for cell cycle progression. It plays crucial roles in cell differentiation, proliferation, and survival, and is thus implicated in cancer. CK2 is not an oncogene by itself but elevated CK2 levels create an environment that enhances the survival of tumor cells. The CK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271034 [Multi-domain]  Cd Length: 306  Bit Score: 111.48  E-value: 6.56e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 248 DYRTVTINTEQkvSDFYDIEERLGSGKFGQVFRLVEKKTRKVWAGKFFKaySAKEKEnIRQEISIMNCLH-HPKLVQCVD 326
Cdd:cd14132     6 DYENLNVEWGS--QDDYEIIRKIGRGKYSEVFEGINIGNNEKVVIKVLK--PVKKKK-IKREIKILQNLRgGPNIVKLLD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 327 AF--EEKANIVMVLEIVSG---GELFERIIDEDfelterecIK-YMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGTR 400
Cdd:cd14132    81 VVkdPQSKTPSLIFEYVNNtdfKTLYPTLTDYD--------IRyYMYELLKALDYCHSKGIMHRDVKPHNIM-IDHEKRK 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 401 IKLIDFGLArrlE-----NAGSLKVlfGTPEFVAPEV-INYEPIGYATDMWSIGVICYILVSGLSPFM-GDNDNETL--- 470
Cdd:cd14132   152 LRLIDWGLA---EfyhpgQEYNVRV--ASRYYKGPELlVDYQYYDYSLDMWSLGCMLASMIFRKEPFFhGHDNYDQLvki 226
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034633499 471 ANV------------------------------TSATWDFDDEAFDEISDDAKDFISNLLKKDMKNRLDCTQCLQHP 517
Cdd:cd14132   227 AKVlgtddlyayldkygielpprlndilgrhskKPWERFVNSENQHLVTPEALDLLDKLLRYDHQERITAKEAMQHP 303
STKc_BUR1 cd07866
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), ...
259-518 1.70e-26

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: 110.48  E-value: 1.70e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 259 KVSDfYDIEERLGSGKFGQVFRLVEKKTRKVWAGKFFKAYSAKEKENIR--QEISIMNCLHHPKLVQCVDAFEEKAN--- 333
Cdd:cd07866     6 KLRD-YEILGKLGEGTFGEVYKARQIKTGRVVALKKILMHNEKDGFPITalREIKILKKLKHPNVVPLIDMAVERPDksk 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 334 -----IVMVLEI----VSGgeLFEriiDEDFELTEREcIK-YMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGTrIKL 403
Cdd:cd07866    85 rkrgsVYMVTPYmdhdLSG--LLE---NPSVKLTESQ-IKcYMLQLLEGINYLHENHILHRDIKAANIL-IDNQGI-LKI 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 404 IDFGLAR------------RLENAGSLKVLFGTPEFVAPEVI----NYEPigyATDMWSIGVICYILVSGLSPFMGDNDN 467
Cdd:cd07866   157 ADFGLARpydgpppnpkggGGGGTRKYTNLVVTRWYRPPELLlgerRYTT---AVDIWGIGCVFAEMFTRRPILQGKSDI 233
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034633499 468 ETLANV-------TSATW-------------DFDD------EAFDEISDDAKDFISNLLKKDMKNRLDCTQCLQHPW 518
Cdd:cd07866   234 DQLHLIfklcgtpTEETWpgwrslpgcegvhSFTNyprtleERFGKLGPEGLDLLSKLLSLDPYKRLTASDALEHPY 310
PKc_Myt1 cd14050
Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze ...
264-517 2.66e-26

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: 108.16  E-value: 2.66e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 264 YDIEERLGSGKFGQVFRLVEKKTRKVWAGKFFKAYSAKEKENIRQ--EI-SIMNCLHHPKLVQCVDAFEEKANIVMVLEI 340
Cdd:cd14050     3 FTILSKLGEGSFGEVFKVRSREDGKLYAVKRSRSRFRGEKDRKRKleEVeRHEKLGEHPNCVRFIKAWEEKGILYIQTEL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 341 VSGGelFERIIDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGtRIKLIDFGLARRLENAGSLKV 420
Cdd:cd14050    83 CDTS--LQQYCEETHSLPESEVWNILLDLLKGLKHLHDHGLIHLDIKPANIF-LSKDG-VCKLGDFGLVVELDKEDIHDA 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 421 LFGTPEFVAPEVINYEPiGYATDMWSIG-----VICYILVsglsPFMGDnDNETLANvtsatWDFDDEAFDEISDDAKDF 495
Cdd:cd14050   159 QEGDPRYMAPELLQGSF-TKAADIFSLGitileLACNLEL----PSGGD-GWHQLRQ-----GYLPEEFTAGLSPELRSI 227
                         250       260
                  ....*....|....*....|..
gi 1034633499 496 ISNLLKKDMKNRLDCTQCLQHP 517
Cdd:cd14050   228 IKLMMDPDPERRPTAEDLLALP 249
STKc_ROCK cd05596
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
255-508 2.69e-26

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


Pssm-ID: 270747 [Multi-domain]  Cd Length: 352  Bit Score: 110.93  E-value: 2.69e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 255 NTEQKVSDFyDIEERLGSGKFGQVFRLVEKKTRKVWAGKF---FKAYSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEK 331
Cdd:cd05596    20 KLRMNAEDF-DVIKVIGRGAFGEVQLVRHKSTKKVYAMKLlskFEMIKRSDSAFFWEERDIMAHANSEWIVQLHYAFQDD 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 332 ANIVMVLEIVSGGELFEriIDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENiMCVNKTGtRIKLIDFGLARR 411
Cdd:cd05596    99 KYLYMVMDYMPGGDLVN--LMSNYDVPEKWARFYTAEVVLALDAIHSMGFVHRDVKPDN-MLLDASG-HLKLADFGTCMK 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 412 LENAGSLK--VLFGTPEFVAPEVINYEP----IGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTS--ATWDFDDE 483
Cdd:cd05596   175 MDKDGLVRsdTAVGTPDYISPEVLKSQGgdgvYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYGKIMNhkNSLQFPDD 254
                         250       260
                  ....*....|....*....|....*
gi 1034633499 484 afDEISDDAKDFISNLLkKDMKNRL 508
Cdd:cd05596   255 --VEISKDAKSLICAFL-TDREVRL 276
STKc_cPKC cd05587
Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; ...
270-511 2.74e-26

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: 110.17  E-value: 2.74e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 270 LGSGKFGQVFrLVEKK-TRKVWAGKFFKaysakeKENIRQ---------EISIMNCLHHPK-LVQCVDAFEEKANIVMVL 338
Cdd:cd05587     4 LGKGSFGKVM-LAERKgTDELYAIKILK------KDVIIQdddvectmvEKRVLALSGKPPfLTQLHSCFQTMDRLYFVM 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 339 EIVSGGELFERIIDEDfELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGtRIKLIDFGLARRLENAGSL 418
Cdd:cd05587    77 EYVNGGDLMYHIQQVG-KFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVM-LDAEG-HIKIADFGMCKEGIFGGKT 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 419 KVLF-GTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDFDdeafDEISDDAKDFIS 497
Cdd:cd05587   154 TRTFcGTPDYIAPEIIAYQPYGKSVDWWAYGVLLYEMLAGQPPFDGEDEDELFQSIMEHNVSYP----KSLSKEAVSICK 229
                         250
                  ....*....|....
gi 1034633499 498 NLLKKDMKNRLDCT 511
Cdd:cd05587   230 GLLTKHPAKRLGCG 243
STKc_cPKC_beta cd05616
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs ...
270-510 3.40e-26

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: 110.09  E-value: 3.40e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 270 LGSGKFGQVFRLVEKKTRKVWAGKFFKAYSAKEKENIRQEISIMNCL----HHPKLVQCVDAFEEKANIVMVLEIVSGGE 345
Cdd:cd05616     8 LGKGSFGKVMLAERKGTDELYAVKILKKDVVIQDDDVECTMVEKRVLalsgKPPFLTQLHSCFQTMDRLYFVMEYVNGGD 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 346 LFERIiDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGtRIKLIDFGLARR-LENAGSLKVLFGT 424
Cdd:cd05616    88 LMYHI-QQVGRFKEPHAVFYAAEIAIGLFFLQSKGIIYRDLKLDNVM-LDSEG-HIKIADFGMCKEnIWDGVTTKTFCGT 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 425 PEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDFDdeafDEISDDAKDFISNLLKKDM 504
Cdd:cd05616   165 PDYIAPEIIAYQPYGKSVDWWAFGVLLYEMLAGQAPFEGEDEDELFQSIMEHNVAYP----KSMSKEAVAICKGLMTKHP 240

                  ....*.
gi 1034633499 505 KNRLDC 510
Cdd:cd05616   241 GKRLGC 246
STKc_ROCK2 cd05621
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
264-525 4.00e-26

Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ROCK2 was the first identified target of activated RhoA, and was found to play a role in stress fiber and focal adhesion formation. It is prominently expressed in the brain, heart, and skeletal muscles. It is implicated in vascular and neurological disorders, such as hypertension and vasospasm of the coronary and cerebral arteries. ROCK2 is also activated by caspase-2 cleavage, resulting in thrombin-induced microparticle generation in response to cell activation. Mice deficient in ROCK2 show intrauterine growth retardation and embryonic lethality because of placental dysfunction. ROCK contains an N-terminal extension, a catalytic kinase domain, and a C-terminal extension, which contains a coiled-coil region encompassing a Rho-binding domain (RBD) and a pleckstrin homology (PH) domain. ROCK is auto-inhibited by the RBD and PH domain interacting with the catalytic domain, and is activated via interaction with Rho GTPases. The ROCK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270771 [Multi-domain]  Cd Length: 379  Bit Score: 110.86  E-value: 4.00e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 264 YDIEERLGSGKFGQVFRLVEKKTRKVWAGKFFKAYSAKEKEN---IRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEI 340
Cdd:cd05621    54 YDVVKVIGRGAFGEVQLVRHKASQKVYAMKLLSKFEMIKRSDsafFWEERDIMAFANSPWVVQLFCAFQDDKYLYMVMEY 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 341 VSGGELFEriIDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENiMCVNKTGtRIKLIDFGLARRLENAGSLK- 419
Cdd:cd05621   134 MPGGDLVN--LMSNYDVPEKWAKFYTAEVVLALDAIHSMGLIHRDVKPDN-MLLDKYG-HLKLADFGTCMKMDETGMVHc 209
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 420 -VLFGTPEFVAPEVINYEP----IGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVT--SATWDFDDEAfdEISDDA 492
Cdd:cd05621   210 dTAVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLFEMLVGDTPFYADSLVGTYSKIMdhKNSLNFPDDV--EISKHA 287
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1034633499 493 KDFISNLLkKDMKNRL---DCTQCLQHPWLMKDTKN 525
Cdd:cd05621   288 KNLICAFL-TDREVRLgrnGVEEIKQHPFFRNDQWN 322
STKc_PKN cd05589
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer ...
270-508 4.50e-26

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: 109.70  E-value: 4.50e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 270 LGSGKFGQVFrLVEKKTRkvwaGKFFkAYSAKEKENI--RQEI-SIM---------NCLHHPKLVQCVDAFEEKANIVMV 337
Cdd:cd05589     7 LGRGHFGKVL-LAEYKPT----GELF-AIKALKKGDIiaRDEVeSLMcekrifetvNSARHPFLVNLFACFQTPEHVCFV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 338 LEIVSGGELFERIIDEDFelTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGTrIKLIDFGLARrlENAG- 416
Cdd:cd05589    81 MEYAAGGDLMMHIHEDVF--SEPRAVFYAACVVLGLQFLHEHKIVYRDLKLDNLL-LDTEGY-VKIADFGLCK--EGMGf 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 417 --SLKVLFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETlanvtsatwdFDDEAFDEI------ 488
Cdd:cd05589   155 gdRTSTFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLIYEMLVGESPFPGDDEEEV----------FDSIVNDEVryprfl 224
                         250       260
                  ....*....|....*....|
gi 1034633499 489 SDDAKDFISNLLKKDMKNRL 508
Cdd:cd05589   225 STEAISIMRRLLRKNPERRL 244
STKc_cPKC_alpha cd05615
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs ...
259-512 5.15e-26

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: 109.70  E-value: 5.15e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 259 KVSDFyDIEERLGSGKFGQVFRLVEKKTRKVWAGKFFKAYSAKEKENIR---QEISIMNCLHHPK-LVQCVDAFEEKANI 334
Cdd:cd05615     8 RLTDF-NFLMVLGKGSFGKVMLAERKGSDELYAIKILKKDVVIQDDDVEctmVEKRVLALQDKPPfLTQLHSCFQTVDRL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 335 VMVLEIVSGGELFERIiDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGtRIKLIDFGLARR-LE 413
Cdd:cd05615    87 YFVMEYVNGGDLMYHI-QQVGKFKEPQAVFYAAEISVGLFFLHKKGIIYRDLKLDNVM-LDSEG-HIKIADFGMCKEhMV 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 414 NAGSLKVLFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDFDdeafDEISDDAK 493
Cdd:cd05615   164 EGVTTRTFCGTPDYIAPEIIAYQPYGRSVDWWAYGVLLYEMLAGQPPFDGEDEDELFQSIMEHNVSYP----KSLSKEAV 239
                         250
                  ....*....|....*....
gi 1034633499 494 DFISNLLKKDMKNRLDCTQ 512
Cdd:cd05615   240 SICKGLMTKHPAKRLGCGP 258
STKc_GRK7 cd05607
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; ...
262-508 6.12e-26

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: 108.45  E-value: 6.12e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 262 DFYDIEER-LGSGKFGQVFRLVEKKTRKVWAGKFFKAYSAKEKENIRQ---EISIMNCLHHPKLVQCVDAFEEKANIVMV 337
Cdd:cd05607     1 DKYFYEFRvLGKGGFGEVCAVQVKNTGQMYACKKLDKKRLKKKSGEKMallEKEILEKVNSPFIVSLAYAFETKTHLCLV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 338 LEIVSGGELFERIidedFELTER-----ECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKTGTRikLIDFGLARRL 412
Cdd:cd05607    81 MSLMNGGDLKYHI----YNVGERgiemeRVIFYSAQITCGILHLHSLKIVYRDMKPENVLLDDNGNCR--LSDLGLAVEV 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 413 ENAGSLKVLFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWD----FDDEAFDEi 488
Cdd:cd05607   155 KEGKPITQRAGTNGYMAPEILKEESYSYPVDWFAMGCSIYEMVAGRTPFRDHKEKVSKEELKRRTLEdevkFEHQNFTE- 233
                         250       260
                  ....*....|....*....|
gi 1034633499 489 sdDAKDFISNLLKKDMKNRL 508
Cdd:cd05607   234 --EAKDICRLFLAKKPENRL 251
STKc_TLK cd13990
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the ...
270-518 9.22e-26

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: 107.40  E-value: 9.22e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 270 LGSGKFGQVFRLVEKKTRKVWAGKFF---KAYSAKEKENIRQ----EISIMNCLHHPKLVQCVDAFE-EKANIVMVLEIV 341
Cdd:cd13990     8 LGKGGFSEVYKAFDLVEQRYVACKIHqlnKDWSEEKKQNYIKhalrEYEIHKSLDHPRIVKLYDVFEiDTDSFCTVLEYC 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 342 SGGELfERIIDEDFELTERECIKYMRQISEGVEYI--HKQGIVHLDLKPENIMCVNKTGT-RIKLIDFGLARRLE--NAG 416
Cdd:cd13990    88 DGNDL-DFYLKQHKSIPEREARSIIMQVVSALKYLneIKPPIIHYDLKPGNILLHSGNVSgEIKITDFGLSKIMDdeSYN 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 417 SLKVLF-----GTPEFVAPE--VINYEP--IGYATDMWSIGVICYILVSGLSPFmGDNDNE-------TLANVTSATwdF 480
Cdd:cd13990   167 SDGMELtsqgaGTYWYLPPEcfVVGKTPpkISSKVDVWSVGVIFYQMLYGRKPF-GHNQSQeaileenTILKATEVE--F 243
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1034633499 481 DDEAfdEISDDAKDFISNLLKKDMKNRLDCTQCLQHPW 518
Cdd:cd13990   244 PSKP--VVSSEAKDFIRRCLTYRKEDRPDVLQLANDPY 279
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
270-519 1.25e-25

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: 106.85  E-value: 1.25e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 270 LGSGKFGQVFRLVEKKTRKVWAGK--FFKAYSAKEK-------ENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEI 340
Cdd:cd06628     8 IGSGSFGSVYLGMNASSGELMAVKqvELPSVSAENKdrkksmlDALQREIALLRELQHENIVQYLGSSSDANHLNIFLEY 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 341 VSGGELfERIIDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKTGtrIKLIDFGLARRLE------- 413
Cdd:cd06628    88 VPGGSV-ATLLNNYGAFEESLVRNFVRQILKGLNYLHNRGIIHRDIKGANILVDNKGG--IKISDFGISKKLEanslstk 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 414 NAGSLKVLFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANV-TSATWDFDdeafDEISDDA 492
Cdd:cd06628   165 NNGARPSLQGSVFWMAPEVVKQTSYTRKADIWSLGCLVVEMLTGTHPFPDCTQMQAIFKIgENASPTIP----SNISSEA 240
                         250       260
                  ....*....|....*....|....*..
gi 1034633499 493 KDFISNLLKKDMKNRLDCTQCLQHPWL 519
Cdd:cd06628   241 RDFLEKTFEIDHNKRPTADELLKHPFL 267
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
264-517 1.28e-25

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: 107.59  E-value: 1.28e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 264 YDIEERLGSGKFGQVFRLVEKKTR------KVWAGKFFKaysakekeniRQEISIMNCLHHPKLVQCVDAFEEKANivmv 337
Cdd:cd14137     6 YTIEKVIGSGSFGVVYQAKLLETGevvaikKVLQDKRYK----------NRELQIMRRLKHPNIVKLKYFFYSSGE---- 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 338 leivSGGELFERIIDEDFELTERECIK----------------YMRQISEGVEYIHKQGIVHLDLKPENIMCVNKTGTrI 401
Cdd:cd14137    72 ----KKDEVYLNLVMEYMPETLYRVIRhysknkqtipiiyvklYSYQLFRGLAYLHSLGICHRDIKPQNLLVDPETGV-L 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 402 KLIDFGLARRLeNAGSLKVlfgtPEFV-----APEVI----NYepiGYATDMWSIGviCYI--LVSGLSPFMGDNDNETL 470
Cdd:cd14137   147 KLCDFGSAKRL-VPGEPNV----SYICsryyrAPELIfgatDY---TTAIDIWSAG--CVLaeLLLGQPLFPGESSVDQL 216
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034633499 471 A-----------------NVTSATWDFD-------DEAFDEISD-DAKDFISNLLKKDMKNRLDCTQCLQHP 517
Cdd:cd14137   217 VeiikvlgtptreqikamNPNYTEFKFPqikphpwEKVFPKRTPpDAIDLLSKILVYNPSKRLTALEALAHP 288
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
268-465 2.26e-25

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


Pssm-ID: 270881 [Multi-domain]  Cd Length: 265  Bit Score: 105.93  E-value: 2.26e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 268 ERLGSGKFGQVFRlVEKKTRKVwAGKFFK--AYSAKEKENIRQEISIMNcLHHPKLVQCVDAF--EEKANIVMVL-EIVS 342
Cdd:cd13979     9 EPLGSGGFGSVYK-ATYKGETV-AVKIVRrrRKNRASRQSFWAELNAAR-LRHENIVRVLAAEtgTDFASLGLIImEYCG 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 343 GGELFERIIDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENI-MCVNKTgtrIKLIDFGLARRLEN----AGS 417
Cdd:cd13979    86 NGTLQQLIYEGSEPLPLAHRILISLDIARALRFCHSHGIVHLDVKPANIlISEQGV---CKLCDFGCSVKLGEgnevGTP 162
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1034633499 418 LKVLFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDN 465
Cdd:cd13979   163 RSHIGGTYTYRAPELLKGERVTPKADIYSFGITLWQMLTRELPYAGLR 210
STKc_nPKC_eta cd05590
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the ...
270-537 2.46e-25

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: 107.30  E-value: 2.46e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 270 LGSGKFGQVFRLVEKKTRKVWAGKFFKAYSAKEKENIR---QEISIMNCLH-HPKLVQCVDAFEEKANIVMVLEIVSGGE 345
Cdd:cd05590     3 LGKGSFGKVMLARLKESGRLYAVKVLKKDVILQDDDVEctmTEKRILSLARnHPFLTQLYCCFQTPDRLFFVMEFVNGGD 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 346 LF-----ERIIDEDfelteRECIkYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGtRIKLIDFGLARRLENAGSLKV 420
Cdd:cd05590    83 LMfhiqkSRRFDEA-----RARF-YAAEITSALMFLHDKGIIYRDLKLDNVL-LDHEG-HCKLADFGMCKEGIFNGKTTS 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 421 LF-GTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLA-----NVTSATWdfddeafdeISDDAKD 494
Cdd:cd05590   155 TFcGTPDYIAPEILQEMLYGPSVDWWAMGVLLYEMLCGHAPFEAENEDDLFEailndEVVYPTW---------LSQDAVD 225
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1034633499 495 FISNLLKKDMKNRLDCTQ------CLQHPWLmkdtKNMEAKKLSKDRMK 537
Cdd:cd05590   226 ILKAFMTKNPTMRLGSLTlggeeaILRHPFF----KELDWEKLNRRQIE 270
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
264-519 2.60e-25

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: 107.61  E-value: 2.60e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 264 YDIEERLGSGKFGQVFRLVEKKT-RKVWAGKFFKAYS----AKEkenIRQEISIMNCLHHPKLVQCVDAFEEKAN----- 333
Cdd:cd07834     2 YELLKPIGSGAYGVVCSAYDKRTgRKVAIKKISNVFDdlidAKR---ILREIKILRHLKHENIIGLLDILRPPSPeefnd 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 334 --IVMvleivsggELFE----RIIDEDFELTErECIKY-MRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGTrIKLIDF 406
Cdd:cd07834    79 vyIVT--------ELMEtdlhKVIKSPQPLTD-DHIQYfLYQILRGLKYLHSAGVIHRDLKPSNIL-VNSNCD-LKICDF 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 407 GLARRLENAGSLKVLfgTpEFV------APEVI----NYepiGYATDMWSIGVICYILVSG--LSP-------------F 461
Cdd:cd07834   148 GLARGVDPDEDKGFL--T-EYVvtrwyrAPELLlsskKY---TKAIDIWSVGCIFAELLTRkpLFPgrdyidqlnliveV 221
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034633499 462 MGDNDNETLANVTSAT---------------WdfdDEAFDEISDDAKDFISNLLKKDMKNRLDCTQCLQHPWL 519
Cdd:cd07834   222 LGTPSEEDLKFISSEKarnylkslpkkpkkpL---SEVFPGASPEAIDLLEKMLVFNPKKRITADEALAHPYL 291
STKc_PAK_II cd06648
Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze ...
269-519 2.77e-25

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: 105.60  E-value: 2.77e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 269 RLGSGKFGQVFRLVEKKTRKVWAGKFFKAYSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEIVSGGELFE 348
Cdd:cd06648    14 KIGEGSTGIVCIATDKSTGRQVAVKKMDLRKQQRRELLFNEVVIMRDYQHPNIVEMYSSYLVGDELWVVMEFLEGGALTD 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 349 riIDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGtRIKLIDFGLARRL-ENAGSLKVLFGTPEF 427
Cdd:cd06648    94 --IVTHTRMNEEQIATVCRAVLKALSFLHSQGVIHRDIKSDSIL-LTSDG-RVKLSDFGFCAQVsKEVPRRKSLVGTPYW 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 428 VAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDFDDEAFdEISDDAKDFISNLLKKDMKNR 507
Cdd:cd06648   170 MAPEVISRLPYGTEVDIWSLGIMVIEMVDGEPPYFNEPPLQAMKRIRDNEPPKLKNLH-KVSPRLRSFLDRMLVRDPAQR 248
                         250
                  ....*....|..
gi 1034633499 508 LDCTQCLQHPWL 519
Cdd:cd06648   249 ATAAELLNHPFL 260
STKc_IKK_alpha cd14039
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
270-478 3.00e-25

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: 106.54  E-value: 3.00e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 270 LGSGKFGQVFRLVEKKTRKVWAGKFFK-AYSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIV-----MVLEIVSG 343
Cdd:cd14039     1 LGTGGFGNVCLYQNQETGEKIAIKSCRlELSVKNKDRWCHEIQIMKKLNHPNVVKACDVPEEMNFLVndvplLAMEYCSG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 344 GELfERIIDEDFE---LTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKTGTRI-KLIDFGLARRLENaGSLK 419
Cdd:cd14039    81 GDL-RKLLNKPENccgLKESQVLSLLSDIGSGIQYLHENKIIHRDLKPENIVLQEINGKIVhKIIDLGYAKDLDQ-GSLC 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 420 VLF-GTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFmgdndnetLANVTSATW 478
Cdd:cd14039   159 TSFvGTLQYLAPELFENKSYTVTVDYWSFGTMVFECIAGFRPF--------LHNLQPFTW 210
STKc_PAK2 cd06655
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the ...
264-519 4.08e-25

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: 106.35  E-value: 4.08e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 264 YDIEERLGSGKFGQVFRLVEKKTRKVWAGKFFKAYSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEIVSG 343
Cdd:cd06655    21 YTRYEKIGQGASGTVFTAIDVATGQEVAIKQINLQKQPKKELIINEILVMKELKNPNIVNFLDSFLVGDELFVVMEYLAG 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 344 GELFERIIDEDFEltERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGTrIKLIDFGLARRLENAGSLK-VLF 422
Cdd:cd06655   101 GSLTDVVTETCMD--EAQIAAVCRECLQALEFLHANQVIHRDIKSDNVL-LGMDGS-VKLTDFGFCAQITPEQSKRsTMV 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 423 GTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANV-TSATWDFDDEafDEISDDAKDFISNLLK 501
Cdd:cd06655   177 GTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIaTNGTPELQNP--EKLSPIFRDFLNRCLE 254
                         250
                  ....*....|....*...
gi 1034633499 502 KDMKNRLDCTQCLQHPWL 519
Cdd:cd06655   255 MDVEKRGSAKELLQHPFL 272
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
268-541 5.69e-25

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: 105.58  E-value: 5.69e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 268 ERLGSGKFGQVFRLVEKKTRKVWAGKFFKAYSAKE-KENIRQEISIMNCLHHPKLVQCVDAF--EEKANIVMVLEIVSGG 344
Cdd:cd06621     7 SSLGEGAGGSVTKCRLRNTKTIFALKTITTDPNPDvQKQILRELEINKSCASPYIVKYYGAFldEQDSSIGIAMEYCEGG 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 345 ELfERIIDEDFELTERECIKYMRQISEGV----EYIHKQGIVHLDLKPENIMcVNKTGtRIKLIDFGLARRLENAGSlKV 420
Cdd:cd06621    87 SL-DSIYKKVKKKGGRIGEKVLGKIAESVlkglSYLHSRKIIHRDIKPSNIL-LTRKG-QVKLCDFGVSGELVNSLA-GT 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 421 LFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDN-----ETLAN-VTSATWDFDDEAFDEI--SDDA 492
Cdd:cd06621   163 FTGTSYYMAPERIQGGPYSITSDVWSLGLTLLEVAQNRFPFPPEGEPplgpiELLSYiVNMPNPELKDEPENGIkwSESF 242
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1034633499 493 KDFISNLLKKDMKNRLDCTQCLQHPWLmkdtKNMEAKKLSkdrMKKYMA 541
Cdd:cd06621   243 KDFIEKCLEKDGTRRPGPWQMLAHPWI----KAQEKKKVN---MAKFVK 284
STKc_CDK4_6_like cd07838
Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; ...
264-519 8.61e-25

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: 105.05  E-value: 8.61e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 264 YDIEERLGSGKFGQVFRLVEKKTRKVWAgkfFKAYSAKEKEN------IRqEISIM---NCLHHPKLVQCVDAF-----E 329
Cdd:cd07838     1 YEEVAEIGEGAYGTVYKARDLQDGRFVA---LKKVRVPLSEEgiplstIR-EIALLkqlESFEHPNVVRLLDVChgprtD 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 330 EKANIVMVLEIVsggelferiiDEDFELTEREC---------IKY-MRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGt 399
Cdd:cd07838    77 RELKLTLVFEHV----------DQDLATYLDKCpkpglppetIKDlMRQLLRGLDFLHSHRIVHRDLKPQNIL-VTSDG- 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 400 RIKLIDFGLARRLENAGSLkvlfgTPEFV-----APEVINYEPigYAT--DMWSIGVICYILVSgLSP-FMGDNDNETLA 471
Cdd:cd07838   145 QVKLADFGLARIYSFEMAL-----TSVVVtlwyrAPEVLLQSS--YATpvDMWSVGCIFAELFN-RRPlFRGSSEADQLG 216
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034633499 472 NV---------------TSATWD-FD-------DEAFDEISDDAKDFISNLLKKDMKNRLDCTQCLQHPWL 519
Cdd:cd07838   217 KIfdviglpseeewprnSALPRSsFPsytprpfKSFVPEIDEEGLDLLKKMLTFNPHKRISAFEALQHPYF 287
STKc_ROCK1 cd05622
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
261-500 1.06e-24

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: 107.01  E-value: 1.06e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 261 SDFYDIEERLGSGKFGQVFRLVEKKTRKVWAGKFFKAYSAKEKEN---IRQEISIMNCLHHPKLVQCVDAFEEKANIVMV 337
Cdd:cd05622    72 AEDYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDsafFWEERDIMAFANSPWVVQLFYAFQDDRYLYMV 151
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 338 LEIVSGGELFERIidEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENiMCVNKTGtRIKLIDFGLARRLENAGS 417
Cdd:cd05622   152 MEYMPGGDLVNLM--SNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDN-MLLDKSG-HLKLADFGTCMKMNKEGM 227
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 418 LK--VLFGTPEFVAPEVINYEP----IGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDFDDEAFDEISDD 491
Cdd:cd05622   228 VRcdTAVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMNHKNSLTFPDDNDISKE 307

                  ....*....
gi 1034633499 492 AKDFISNLL 500
Cdd:cd05622   308 AKNLICAFL 316
STKc_nPKC_theta cd05619
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze ...
259-519 2.13e-24

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: 105.01  E-value: 2.13e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 259 KVSDFYdIEERLGSGKFGQVFRLVEKKTRKVWAGKFFKAYSAKEKENI------RQEISImnCLHHPKLVQCVDAFEEKA 332
Cdd:cd05619     3 TIEDFV-LHKMLGKGSFGKVFLAELKGTNQFFAIKALKKDVVLMDDDVectmveKRVLSL--AWEHPFLTHLFCTFQTKE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 333 NIVMVLEIVSGGELFERIID-EDFELTEreCIKYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGtRIKLIDFGLARr 411
Cdd:cd05619    80 NLFFVMEYLNGGDLMFHIQScHKFDLPR--ATFYAAEIICGLQFLHSKGIVYRDLKLDNIL-LDKDG-HIKIADFGMCK- 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 412 lENA-GSLKV--LFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTsatwdFDDEAFDE- 487
Cdd:cd05619   155 -ENMlGDAKTstFCGTPDYIAPEILLGQKYNTSVDWWSFGVLLYEMLIGQSPFHGQDEEELFQSIR-----MDNPFYPRw 228
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1034633499 488 ISDDAKDFISNLLKKDMKNRLDCTQCL-QHPWL 519
Cdd:cd05619   229 LEKEAKDILVKLFVREPERRLGVRGDIrQHPFF 261
STKc_MST3 cd06641
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs ...
268-539 2.33e-24

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: 103.61  E-value: 2.33e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 268 ERLGSGKFGQVFRLVEKKTRKVWAGKFFKAYSAKEK-ENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEIVSGGEL 346
Cdd:cd06641    10 EKIGKGSFGEVFKGIDNRTQKVVAIKIIDLEEAEDEiEDIQQEITVLSQCDSPYVTKYYGSYLKDTKLWIIMEYLGGGSA 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 347 FERIidEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGtRIKLIDFGLARRLENAGSLKVLF-GTP 425
Cdd:cd06641    90 LDLL--EPGPLDETQIATILREILKGLDYLHSEKKIHRDIKAANVL-LSEHG-EVKLADFGVAGQLTDTQIKRN*FvGTP 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 426 EFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDFDDEAFdeiSDDAKDFISNLLKKDMK 505
Cdd:cd06641   166 FWMAPEVIKQSAYDSKADIWSLGITAIELARGEPPHSELHPMKVLFLIPKNNPPTLEGNY---SKPLKEFVEACLNKEPS 242
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1034633499 506 NRLDCTQCLQHPWLMKDTKNMEAKKLSKDRMKKY 539
Cdd:cd06641   243 FRPTAKELLKHKFILRNAKKTSYLTELIDRYKRW 276
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
270-521 2.51e-24

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: 103.67  E-value: 2.51e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 270 LGSGKFGQVFRLVEKKTRKVWAGK--FFKAYSAKEKENIRqEISIMNCLHHPKLVQCVDAF-EEKANIVMVLEIVSGGEL 346
Cdd:cd06620    13 LGAGNGGSVSKVLHIPTGTIMAKKviHIDAKSSVRKQILR-ELQILHECHSPYIVSFYGAFlNENNNIIICMEYMDCGSL 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 347 fERIIDEDFELTERECIKYMRQISEGVEYIHKQ-GIVHLDLKPENIMcVNKTGtRIKLIDFGLARRLENagSLKVLF-GT 424
Cdd:cd06620    92 -DKILKKKGPFPEEVLGKIAVAVLEGLTYLYNVhRIIHRDIKPSNIL-VNSKG-QIKLCDFGVSGELIN--SIADTFvGT 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 425 PEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDF-------------DDEAFDEisdD 491
Cdd:cd06620   167 STYMSPERIQGGKYSVKSDVWSLGLSIIELALGEFPFAGSNDDDDGYNGPMGILDLlqrivneppprlpKDRIFPK---D 243
                         250       260       270
                  ....*....|....*....|....*....|
gi 1034633499 492 AKDFISNLLKKDMKNRLDCTQCLQHPWLMK 521
Cdd:cd06620   244 LRDFVDRCLLKDPRERPSPQLLLDHDPFIQ 273
STKc_nPKC_delta cd05620
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze ...
270-519 2.82e-24

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: 104.26  E-value: 2.82e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 270 LGSGKFGQVFrLVEKKTRkvwaGKFFkAYSAKEKENIRQEISIMNCL----------HHPKLVQCVDAFEEKANIVMVLE 339
Cdd:cd05620     3 LGKGSFGKVL-LAELKGK----GEYF-AVKALKKDVVLIDDDVECTMvekrvlalawENPFLTHLYCTFQTKEHLFFVME 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 340 IVSGGELFERIIDED-FELTEreCIKYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGtRIKLIDFGLARRL---ENA 415
Cdd:cd05620    77 FLNGGDLMFHIQDKGrFDLYR--ATFYAAEIVCGLQFLHSKGIIYRDLKLDNVM-LDRDG-HIKIADFGMCKENvfgDNR 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 416 GSlkVLFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSAT-----WdfddeafdeISD 490
Cdd:cd05620   153 AS--TFCGTPDYIAPEILQGLKYTFSVDWWSFGVLLYEMLIGQSPFHGDDEDELFESIRVDTphyprW---------ITK 221
                         250       260       270
                  ....*....|....*....|....*....|
gi 1034633499 491 DAKDFISNLLKKDMKNRLDCTQCLQ-HPWL 519
Cdd:cd05620   222 ESKDILEKLFERDPTRRLGVVGNIRgHPFF 251
STKc_CDC2L1 cd07843
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze ...
262-518 3.93e-24

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: 103.07  E-value: 3.93e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 262 DFYDIEERLGSGKFGQVFRLVEKKTRKVWAGKFFKAYsaKEKE-----NIRqEISIMNCLHHPklvqcvdafeekaNIVM 336
Cdd:cd07843     5 DEYEKLNRIEEGTYGVVYRARDKKTGEIVALKKLKME--KEKEgfpitSLR-EINILLKLQHP-------------NIVT 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 337 VLEIVSGG---------ELFE-------RIIDEDFELTERECIkyMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGtR 400
Cdd:cd07843    69 VKEVVVGSnldkiymvmEYVEhdlkslmETMKQPFLQSEVKCL--MLQLLSGVAHLHDNWILHRDLKTSNLL-LNNRG-I 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 401 IKLIDFGLARRLEnaGSLKVLfgTPEFV-----APEVINYEPI-GYATDMWSIGVICYILVSGLSPFMGDNDNETLANV- 473
Cdd:cd07843   145 LKICDFGLAREYG--SPLKPY--TQLVVtlwyrAPELLLGAKEySTAIDMWSVGCIFAELLTKKPLFPGKSEIDQLNKIf 220
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034633499 474 ------TSATW------------DFDDEAFDEI---------SDDAKDFISNLLKKDMKNRLDCTQCLQHPW 518
Cdd:cd07843   221 kllgtpTEKIWpgfselpgakkkTFTKYPYNQLrkkfpalslSDNGFDLLNRLLTYDPAKRISAEDALKHPY 292
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
264-514 4.03e-24

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 108.67  E-value: 4.03e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499  264 YDIEERLGSGKFGQVFRLVEKKTRK--VWAGKFFKAYSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKAN--IVMVLE 339
Cdd:PTZ00266    15 YEVIKKIGNGRFGEVFLVKHKRTQEffCWKAISYRGLKEREKSQLVIEVNVMRELKHKNIVRYIDRFLNKANqkLYILME 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499  340 IVSGGELfERIIDEDFEL----TERECIKYMRQISEGVEYIH--KQG-----IVHLDLKPENIMCvnKTGTR-------- 400
Cdd:PTZ00266    95 FCDAGDL-SRNIQKCYKMfgkiEEHAIVDITRQLLHALAYCHnlKDGpngerVLHRDLKPQNIFL--STGIRhigkitaq 171
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499  401 ---------IKLIDFGLARRLENAGSLKVLFGTPEFVAPEVINYEPIGY--ATDMWSIGVICYILVSGLSPFMGDNDnet 469
Cdd:PTZ00266   172 annlngrpiAKIGDFGLSKNIGIESMAHSCVGTPYYWSPELLLHETKSYddKSDMWALGCIIYELCSGKTPFHKANN--- 248
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 1034633499  470 LANVTSATWDFDDEAFDEISDDAKDFISNLLKKDMKNRLDCTQCL 514
Cdd:PTZ00266   249 FSQLISELKRGPDLPIKGKSKELNILIKNLLNLSAKERPSALQCL 293
STKc_p38 cd07851
Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs ...
249-519 4.10e-24

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: 104.30  E-value: 4.10e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 249 YRTVTINTEQKVSDFYDIEERLGSGKFGQVFRLVEKKTRKVWAGK-----FFKAYSAKEkenIRQEISIMNCLHHPKLVQ 323
Cdd:cd07851     2 YRQELNKTVWEVPDRYQNLSPVGSGAYGQVCSAFDTKTGRKVAIKklsrpFQSAIHAKR---TYRELRLLKHMKHENVIG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 324 CVDAF------EEKANIVMVLEIVsGGELfERIIDEDfELTErECIKYM-RQISEGVEYIHKQGIVHLDLKPENImCVNK 396
Cdd:cd07851    79 LLDVFtpasslEDFQDVYLVTHLM-GADL-NNIVKCQ-KLSD-DHIQFLvYQILRGLKYIHSAGIIHRDLKPSNL-AVNE 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 397 TgTRIKLIDFGLARRLENAGSLKVlfGTPEFVAPEVI-NYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTS 475
Cdd:cd07851   154 D-CELKILDFGLARHTDDEMTGYV--ATRWYRAPEIMlNWMHYNQTVDIWSVGCIMAELLTGKTLFPGSDHIDQLKRIMN 230
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034633499 476 ATWDFDDEAFDEI-SDDAKDFIS----------------------NLLKK----DMKNRLDCTQCLQHPWL 519
Cdd:cd07851   231 LVGTPDEELLKKIsSESARNYIQslpqmpkkdfkevfsganplaiDLLEKmlvlDPDKRITAAEALAHPYL 301
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
264-517 4.85e-24

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: 102.05  E-value: 4.85e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 264 YDIEERLGSGKFGQVFR-LVEKKTRKVWAGKFFKAYSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEIVS 342
Cdd:cd06610     3 YELIEVIGSGATAVVYAaYCLPKKEKVAIKRIDLEKCQTSMDELRKEIQAMSQCNHPNVVSYYTSFVVGDELWLVMPLLS 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 343 GGELFERI--------IDEDFELTerecikYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGTrIKLIDFGLARRLEN 414
Cdd:cd06610    83 GGSLLDIMkssyprggLDEAIIAT------VLKEVLKGLEYLHSNGQIHRDVKAGNIL-LGEDGS-VKIADFGVSASLAT 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 415 AG-----SLKVLFGTPEFVAPEVINyEPIGY--ATDMWSIGVICYILVSGLSPFMGDNDNETLAN-VTSATWDFDDEA-F 485
Cdd:cd06610   155 GGdrtrkVRKTFVGTPCWMAPEVME-QVRGYdfKADIWSFGITAIELATGAAPYSKYPPMKVLMLtLQNDPPSLETGAdY 233
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1034633499 486 DEISDDAKDFISNLLKKDMKNRLDCTQCLQHP 517
Cdd:cd06610   234 KKYSKSFRKMISLCLQKDPSKRPTAEELLKHK 265
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
268-519 5.14e-24

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: 102.55  E-value: 5.14e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 268 ERLGSGKFGQVFRLVEKKTRKVWAGKFFKAYSAK-EKENIRQEISIMNCLHH---PKLVQCVDAFEEKANIVMVLEIVSG 343
Cdd:cd06917     7 ELVGRGSYGAVYRGYHVKTGRVVALKVLNLDTDDdDVSDIQKEVALLSQLKLgqpKNIIKYYGSYLKGPSLWIIMDYCEG 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 344 GELfeRIIDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGtRIKLIDFGLARRLeNAGSLK--VL 421
Cdd:cd06917    87 GSI--RTLMRAGPIAERYIAVIMREVLVALKFIHKDGIIHRDIKAANIL-VTNTG-NVKLCDFGVAASL-NQNSSKrsTF 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 422 FGTPEFVAPEVINyEPIGYAT--DMWSIGVICYILVSGLSPFmgdNDNETLANVT----SATWDFDDEAFdeiSDDAKDF 495
Cdd:cd06917   162 VGTPYWMAPEVIT-EGKYYDTkaDIWSLGITTYEMATGNPPY---SDVDALRAVMlipkSKPPRLEGNGY---SPLLKEF 234
                         250       260
                  ....*....|....*....|....
gi 1034633499 496 ISNLLKKDMKNRLDCTQCLQHPWL 519
Cdd:cd06917   235 VAACLDEEPKDRLSADELLKSKWI 258
STKc_CDK1_CdkB_like cd07835
Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of ...
268-519 5.87e-24

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: 102.37  E-value: 5.87e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 268 ERLGSGKFGQVFRLVEKKTRKVWAGKffKAYSAKEKEN-----IRqEISIMNCLHHPKLVQCVDAFEEKANIVMVLEIVS 342
Cdd:cd07835     5 EKIGEGTYGVVYKARDKLTGEIVALK--KIRLETEDEGvpstaIR-EISLLKELNHPNIVRLLDVVHSENKLYLVFEFLD 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 343 GGelFERIIDE--DFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGTrIKLIDFGLARrlenagslkv 420
Cdd:cd07835    82 LD--LKKYMDSspLTGLDPPLIKSYLYQLLQGIAFCHSHRVLHRDLKPQNLL-IDTEGA-LKLADFGLAR---------- 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 421 LFGTP------EFV-----APEVInyepIG---YAT--DMWSIGVICYILVSGLSPFMGDN---------------DNET 469
Cdd:cd07835   148 AFGVPvrtythEVVtlwyrAPEIL----LGskhYSTpvDIWSVGCIFAEMVTRRPLFPGDSeidqlfrifrtlgtpDEDV 223
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 470 LANVTSA--------TWDFDD--EAFDEISDDAKDFISNLLKKDMKNRLDCTQCLQHPWL 519
Cdd:cd07835   224 WPGVTSLpdykptfpKWARQDlsKVVPSLDEDGLDLLSQMLVYDPAKRISAKAALQHPYF 283
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
268-539 1.38e-23

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: 101.29  E-value: 1.38e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 268 ERLGSGKFGQVFRLVEKKTRKVWAGKFFKAYSAK-EKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEIVSGGEL 346
Cdd:cd06642    10 ERIGKGSFGEVYKGIDNRTKEVVAIKIIDLEEAEdEIEDIQQEITVLSQCDSPYITRYYGSYLKGTKLWIIMEYLGGGSA 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 347 FERIIDEDFELTERECIkyMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGTrIKLIDFGLARRLENAGSLKVLF-GTP 425
Cdd:cd06642    90 LDLLKPGPLEETYIATI--LREILKGLDYLHSERKIHRDIKAANVL-LSEQGD-VKLADFGVAGQLTDTQIKRNTFvGTP 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 426 EFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATwdfDDEAFDEISDDAKDFISNLLKKDMK 505
Cdd:cd06642   166 FWMAPEVIKQSAYDFKADIWSLGITAIELAKGEPPNSDLHPMRVLFLIPKNS---PPTLEGQHSKPFKEFVEACLNKDPR 242
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1034633499 506 NRLDCTQCLQHPWLMKDTKNMEAKKLSKDRMKKY 539
Cdd:cd06642   243 FRPTAKELLKHKFITRYTKKTSFLTELIDRYKRW 276
STKc_Nek7 cd08229
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
264-511 1.45e-23

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: 101.65  E-value: 1.45e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 264 YDIEERLGSGKFGQVFR---LVEKKTRKVWAGKFFKAYSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEI 340
Cdd:cd08229    26 FRIEKKIGRGQFSEVYRatcLLDGVPVALKKVQIFDLMDAKARADCIKEIDLLKQLNHPNVIKYYASFIEDNELNIVLEL 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 341 VSGGELFERIidEDFE-----LTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGTrIKLIDFGLARRLEN- 414
Cdd:cd08229   106 ADAGDLSRMI--KHFKkqkrlIPEKTVWKYFVQLCSALEHMHSRRVMHRDIKPANVF-ITATGV-VKLGDLGLGRFFSSk 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 415 AGSLKVLFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDFDDEAFDEISDDAKD 494
Cdd:cd08229   182 TTAAHSLVGTPYYMSPERIHENGYNFKSDIWSLGCLLYEMAALQSPFYGDKMNLYSLCKKIEQCDYPPLPSDHYSEELRQ 261
                         250
                  ....*....|....*..
gi 1034633499 495 FISNLLKKDMKNRLDCT 511
Cdd:cd08229   262 LVNMCINPDPEKRPDIT 278
PKc_CLK cd14134
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases; Dual-specificity ...
264-519 1.57e-23

Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. CLKs are involved in the phosphorylation and regulation of serine/arginine-rich (SR) proteins, which play a crucial role in pre-mRNA splicing by directing splice site selection. SR proteins are phosphorylated first by SR protein kinases (SRPKs) at the N-terminus, which leads to its assembly into nuclear speckles where splicing factors are stored. CLKs phosphorylate the C-terminal part of SR proteins, causing the nuclear speckles to dissolve and splicing factors to be recruited at sites of active transcription. Based on a conserved "EHLAMMERILG" signature motif which may be crucial for substrate specificity, CLKs are also referred to as LAMMER kinases. CLKs autophosphorylate at tyrosine residues and phosphorylate their substrates exclusively on S/T residues. In Drosophila, the CLK homolog DOA (Darkener of apricot) is essential for embryogenesis and its mutation leads to defects in sexual differentiation, eye formation, and neuronal development. In fission yeast, the CLK homolog Lkh1 is a negative regulator of filamentous growth and asexual flocculation, and is also involved in oxidative stress response. Vertebrates contain mutliple CLK proteins and mammals have four (CLK1-4). The CLK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271036 [Multi-domain]  Cd Length: 332  Bit Score: 102.26  E-value: 1.57e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 264 YDIEERLGSGKFGQVFRLVEKKTRKVWAGKFFKAYSaKEKENIRQEISIM--------NCLHHpkLVQCVDAFEEKANIV 335
Cdd:cd14134    14 YKILRLLGEGTFGKVLECWDRKRKRYVAVKIIRNVE-KYREAAKIEIDVLetlaekdpNGKSH--CVQLRDWFDYRGHMC 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 336 MVLEIVsGGELFERIIDEDFELTERECIK-YMRQISEGVEYIHKQGIVHLDLKPENIMCVNKT----------------- 397
Cdd:cd14134    91 IVFELL-GPSLYDFLKKNNYGPFPLEHVQhIAKQLLEAVAFLHDLKLTHTDLKPENILLVDSDyvkvynpkkkrqirvpk 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 398 GTRIKLIDFGLA---RrlENAGSLkvlFGTPEFVAPEVInyepIG----YATDMWSIGVICYILVSGLSPFMGDNDNETL 470
Cdd:cd14134   170 STDIKLIDFGSAtfdD--EYHSSI---VSTRHYRAPEVI----LGlgwsYPCDVWSIGCILVELYTGELLFQTHDNLEHL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 471 A-----------NVTSAT---------------WDFDDEAFDEISDDAK-----------------DFISNLLKKDMKNR 507
Cdd:cd14134   241 AmmerilgplpkRMIRRAkkgakyfyfyhgrldWPEGSSSGRSIKRVCKplkrlmllvdpehrllfDLIRKMLEYDPSKR 320
                         330
                  ....*....|..
gi 1034633499 508 LDCTQCLQHPWL 519
Cdd:cd14134   321 ITAKEALKHPFF 332
STKc_aPKC_iota cd05618
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze ...
264-510 2.14e-23

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: 102.42  E-value: 2.14e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 264 YDIEERLGSGKFGQVFRLVEKKTRKVWAGKFFKAYSAKEKENI---RQEISIM-NCLHHPKLVQCVDAFEEKANIVMVLE 339
Cdd:cd05618    22 FDLLRVIGRGSYAKVLLVRLKKTERIYAMKVVKKELVNDDEDIdwvQTEKHVFeQASNHPFLVGLHSCFQTESRLFFVIE 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 340 IVSGGELFERIiDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGtRIKLIDFGLARRLENAGSLK 419
Cdd:cd05618   102 YVNGGDLMFHM-QRQRKLPEEHARFYSAEISLALNYLHERGIIYRDLKLDNVL-LDSEG-HIKLTDYGMCKEGLRPGDTT 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 420 VLF-GTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPF--MGDNDNEtlanvTSATWDFDDEAFDE--------I 488
Cdd:cd05618   179 STFcGTPNYIAPEILRGEDYGFSVDWWALGVLMFEMMAGRSPFdiVGSSDNP-----DQNTEDYLFQVILEkqiriprsL 253
                         250       260
                  ....*....|....*....|..
gi 1034633499 489 SDDAKDFISNLLKKDMKNRLDC 510
Cdd:cd05618   254 SVKAASVLKSFLNKDPKERLGC 275
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
268-519 2.19e-23

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: 100.95  E-value: 2.19e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 268 ERLGSGKFGQVFRLVEKKTRKVWAGKFFKAYSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEIVSGGELF 347
Cdd:cd06656    25 EKIGQGASGTVYTAIDIATGQEVAIKQMNLQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSLT 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 348 ERIIDEDFEltERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGTrIKLIDFGLARRLENAGSLK-VLFGTPE 426
Cdd:cd06656   105 DVVTETCMD--EGQIAAVCRECLQALDFLHSNQVIHRDIKSDNIL-LGMDGS-VKLTDFGFCAQITPEQSKRsTMVGTPY 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 427 FVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANV-TSATWDFDDEafDEISDDAKDFISNLLKKDMK 505
Cdd:cd06656   181 WMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIaTNGTPELQNP--ERLSAVFRDFLNRCLEMDVD 258
                         250
                  ....*....|....
gi 1034633499 506 NRLDCTQCLQHPWL 519
Cdd:cd06656   259 RRGSAKELLQHPFL 272
STKc_IKK_beta cd14038
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
269-462 2.79e-23

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: 100.81  E-value: 2.79e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 269 RLGSGKFGQVFRLVEKKT-RKVWAGKFFKAYSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANI------VMVLEIV 341
Cdd:cd14038     1 RLGTGGFGNVLRWINQETgEQVAIKQCRQELSPKNRERWCLEIQIMKRLNHPNVVAARDVPEGLQKLapndlpLLAMEYC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 342 SGGELfeRIIDEDFE----LTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGTRI--KLIDFGLARRLENa 415
Cdd:cd14038    81 QGGDL--RKYLNQFEnccgLREGAILTLLSDISSALRYLHENRIIHRDLKPENIV-LQQGEQRLihKIIDLGYAKELDQ- 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1034633499 416 GSLKVLF-GTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFM 462
Cdd:cd14038   157 GSLCTSFvGTLQYLAPELLEQQKYTVTVDYWSFGTLAFECITGFRPFL 204
PKc_LIMK_like cd14065
Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of ...
270-454 2.85e-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: 99.49  E-value: 2.85e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 270 LGSGKFGQVFRLVEKKTRKVWAGKFFKAYSakEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEIVSGGELFER 349
Cdd:cd14065     1 LGKGFFGEVYKVTHRETGKVMVMKELKRFD--EQRSFLKEVKLMRRLSHPNILRFIGVCVKDNKLNFITEYVNGGTLEEL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 350 IIDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKTGTRIKLI-DFGLARRL----ENAGSLKV---L 421
Cdd:cd14065    79 LKSMDEQLPWSQRVSLAKDIASGMAYLHSKNIIHRDLNSKNCLVREANRGRNAVVaDFGLAREMpdekTKKPDRKKrltV 158
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1034633499 422 FGTPEFVAPEVINYEPIGYATDMWSIGVI-CYIL 454
Cdd:cd14065   159 VGSPYWMAPEMLRGESYDEKVDVFSFGIVlCEII 192
STKc_DMPK_like cd05597
Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; ...
261-518 3.07e-23

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


Pssm-ID: 270748 [Multi-domain]  Cd Length: 331  Bit Score: 101.27  E-value: 3.07e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 261 SDFyDIEERLGSGKFGQVFRLVEKKTRKVWAGKFFKAYSA---KEKENIRQEISIM--------NCLHHpklvqcvdAFE 329
Cdd:cd05597     1 DDF-EILKVIGRGAFGEVAVVKLKSTEKVYAMKILNKWEMlkrAETACFREERDVLvngdrrwiTKLHY--------AFQ 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 330 EKANIVMVLEIVSGGEL------FERIIDEDFELTerecikYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGtRIKL 403
Cdd:cd05597    72 DENYLYLVMDYYCGGDLltllskFEDRLPEEMARF------YLAEMVLAIDSIHQLGYVHRDIKPDNVL-LDRNG-HIRL 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 404 IDFGLARRLENAGSLK--VLFGTPEFVAPEVINYEPIG---YAT--DMWSIGVICYILVSGLSPFMGDNDNETLANVTSA 476
Cdd:cd05597   144 ADFGSCLKLREDGTVQssVAVGTPDYISPEILQAMEDGkgrYGPecDWWSLGVCMYEMLYGETPFYAESLVETYGKIMNH 223
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1034633499 477 TWDF---DDEafDEISDDAKDFISNLLkKDMKNRL---DCTQCLQHPW 518
Cdd:cd05597   224 KEHFsfpDDE--DDVSEEAKDLIRRLI-CSRERRLgqnGIDDFKKHPF 268
STKc_MEKK2 cd06652
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
270-516 3.15e-23

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: 99.73  E-value: 3.15e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 270 LGSGKFGQVFRLVEKKTRKVWAGKFFK-----AYSAKEKENIRQEISIMNCLHHPKLVQ---CV-DAFEEKANIVMvlEI 340
Cdd:cd06652    10 LGQGAFGRVYLCYDADTGRELAVKQVQfdpesPETSKEVNALECEIQLLKNLLHERIVQyygCLrDPQERTLSIFM--EY 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 341 VSGGELFERIIDEDfELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMcvNKTGTRIKLIDFGLARRLE----NAG 416
Cdd:cd06652    88 MPGGSIKDQLKSYG-ALTENVTRKYTRQILEGVHYLHSNMIVHRDIKGANIL--RDSVGNVKLGDFGASKRLQticlSGT 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 417 SLKVLFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMgdnDNETLANVTS-ATWDFDDEAFDEISDDAKDF 495
Cdd:cd06652   165 GMKSVTGTPYWMSPEVISGEGYGRKADIWSVGCTVVEMLTEKPPWA---EFEAMAAIFKiATQPTNPQLPAHVSDHCRDF 241
                         250       260
                  ....*....|....*....|.
gi 1034633499 496 ISNLLkKDMKNRLDCTQCLQH 516
Cdd:cd06652   242 LKRIF-VEAKLRPSADELLRH 261
STKc_MEKK3_like_u1 cd06653
Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP) ...
270-518 3.31e-23

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: 99.71  E-value: 3.31e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 270 LGSGKFGQVFRLVEKKTRKVWAGKFF-----KAYSAKEKENIRQEISIMNCLHHPKLVQ---CVDAFEEKaNIVMVLEIV 341
Cdd:cd06653    10 LGRGAFGEVYLCYDADTGRELAVKQVpfdpdSQETSKEVNALECEIQLLKNLRHDRIVQyygCLRDPEEK-KLSIFVEYM 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 342 SGGELFERIIDEDfELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMcvNKTGTRIKLIDFGLARRLE----NAGS 417
Cdd:cd06653    89 PGGSVKDQLKAYG-ALTENVTRRYTRQILQGVSYLHSNMIVHRDIKGANIL--RDSAGNVKLGDFGASKRIQticmSGTG 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 418 LKVLFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFmgdNDNETLANVTS-ATWDFDDEAFDEISDDAKDFI 496
Cdd:cd06653   166 IKSVTGTPYWMSPEVISGEGYGRKADVWSVACTVVEMLTEKPPW---AEYEAMAAIFKiATQPTKPQLPDGVSDACRDFL 242
                         250       260
                  ....*....|....*....|..
gi 1034633499 497 SNLLKKDmKNRLDCTQCLQHPW 518
Cdd:cd06653   243 RQIFVEE-KRRPTAEFLLRHPF 263
STKc_CDK1_euk cd07861
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher ...
262-519 3.96e-23

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: 100.19  E-value: 3.96e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 262 DFYDIEeRLGSGKFGQVFRLVEKKTRKVWAGKFFKAYSAKE---KENIRqEISIMNCLHHPKLVQCVDAFEEKANIVMVL 338
Cdd:cd07861     1 DYTKIE-KIGEGTYGVVYKGRNKKTGQIVAMKKIRLESEEEgvpSTAIR-EISLLKELQHPNIVCLEDVLMQENRLYLVF 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 339 EIVSGGelFERIIDE--DFELTERECIK-YMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGTrIKLIDFGLARrlenA 415
Cdd:cd07861    79 EFLSMD--LKKYLDSlpKGKYMDAELVKsYLYQILQGILFCHSRRVLHRDLKPQNLL-IDNKGV-IKLADFGLAR----A 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 416 GSLKVLFGTPEFV-----APEVINYEPIgYAT--DMWSIGVICYILVSGLSPFMGDN---------------DNETLANV 473
Cdd:cd07861   151 FGIPVRVYTHEVVtlwyrAPEVLLGSPR-YSTpvDIWSIGTIFAEMATKKPLFHGDSeidqlfrifrilgtpTEDIWPGV 229
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1034633499 474 TS--------ATW--DFDDEAFDEISDDAKDFISNLLKKDMKNRLDCTQCLQHPWL 519
Cdd:cd07861   230 TSlpdykntfPKWkkGSLRTAVKNLDEDGLDLLEKMLIYDPAKRISAKKALVHPYF 285
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
268-539 4.64e-23

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: 99.74  E-value: 4.64e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 268 ERLGSGKFGQVFRLVEKKTRKVWAGKFFKAYSAK-EKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEIVSGGEL 346
Cdd:cd06640    10 ERIGKGSFGEVFKGIDNRTQQVVAIKIIDLEEAEdEIEDIQQEITVLSQCDSPYVTKYYGSYLKGTKLWIIMEYLGGGSA 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 347 FERIIDEDFEltERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGtRIKLIDFGLARRLENAGSLKVLF-GTP 425
Cdd:cd06640    90 LDLLRAGPFD--EFQIATMLKEILKGLDYLHSEKKIHRDIKAANVL-LSEQG-DVKLADFGVAGQLTDTQIKRNTFvGTP 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 426 EFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPfmgDNDNETLANVTSATWDFDDEAFDEISDDAKDFISNLLKKDMK 505
Cdd:cd06640   166 FWMAPEVIQQSAYDSKADIWSLGITAIELAKGEPP---NSDMHPMRVLFLIPKNNPPTLVGDFSKPFKEFIDACLNKDPS 242
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1034633499 506 NRLDCTQCLQHPWLMKDTKNMEAKKLSKDRMKKY 539
Cdd:cd06640   243 FRPTAKELLKHKFIVKNAKKTSYLTELIDRFKRW 276
STKc_LATS cd05598
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the ...
262-518 5.58e-23

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: 100.85  E-value: 5.58e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 262 DFYDIEERLGSGKFGQVfRLVEKK-TRKVWAGKFFKAYSAKEKE---NIRQEISIMNCLHHPKLVQCVDAFEEKANIVMV 337
Cdd:cd05598     1 SMFEKIKTIGVGAFGEV-SLVRKKdTNALYAMKTLRKKDVLKRNqvaHVKAERDILAEADNEWVVKLYYSFQDKENLYFV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 338 LEIVSGGELFERIIDedFELTERECIK-YMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGtRIKLIDFGLA------- 409
Cdd:cd05598    80 MDYIPGGDLMSLLIK--KGIFEEDLARfYIAELVCAIESVHKMGFIHRDIKPDNIL-IDRDG-HIKLTDFGLCtgfrwth 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 410 -RRLENAGSLkvlFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDFDDEAFDEI 488
Cdd:cd05598   156 dSKYYLAHSL---VGTPNYIAPEVLLRTGYTQLCDWWSVGVILYEMLVGQPPFLAQTPAETQLKVINWRTTLKIPHEANL 232
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1034633499 489 SDDAKDFISNLLkKDMKNRLDC---TQCLQHPW 518
Cdd:cd05598   233 SPEAKDLILRLC-CDAEDRLGRngaDEIKAHPF 264
STKc_Nek4 cd08223
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
264-452 5.93e-23

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: 98.66  E-value: 5.93e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 264 YDIEERLGSGKFGQVFRLVEKKTRKVWAGKF--FKAYSAKEKENIRQEISIMNCLHHPKLVQCVDAFE-EKANIVMVLEI 340
Cdd:cd08223     2 YQFLRVIGKGSYGEVWLVRHKRDRKQYVIKKlnLKNASKRERKAAEQEAKLLSKLKHPNIVSYKESFEgEDGFLYIVMGF 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 341 VSGGELFERIIDEDFE-LTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGTrIKLIDFGLARRLENAGSL- 418
Cdd:cd08223    82 CEGGDLYTRLKEQKGVlLEERQVVEWFVQIAMALQYMHERNILHRDLKTQNIF-LTKSNI-IKVGDLGIARVLESSSDMa 159
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1034633499 419 KVLFGTPEFVAPEVINYEPIGYATDMWSIGVICY 452
Cdd:cd08223   160 TTLIGTPYYMSPELFSNKPYNHKSDVWALGCCVY 193
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
264-518 6.53e-23

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: 99.42  E-value: 6.53e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 264 YDIEERLGSGKFGQVFRLVEKKTRKVWAGKFFkaYSAKEKENIRQ----EISIMNCLHHPKLVQCVDAFEEKANIVMVLE 339
Cdd:cd07846     3 YENLGLVGEGSYGMVMKCRHKETGQIVAIKKF--LESEDDKMVKKiamrEIKMLKQLRHENLVNLIEVFRRKKRWYLVFE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 340 IVsggelfERIIDEDFE-----LTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGTrIKLIDFGLARRLEN 414
Cdd:cd07846    81 FV------DHTVLDDLEkypngLDESRVRKYLFQILRGIDFCHSHNIIHRDIKPENIL-VSQSGV-VKLCDFGFARTLAA 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 415 AGSLKVLF-GTPEFVAPEVINYEP-IGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWD--------FD--- 481
Cdd:cd07846   153 PGEVYTDYvATRWYRAPELLVGDTkYGKAVDVWAVGCLVTEMLTGEPLFPGDSDIDQLYHIIKCLGNliprhqelFQknp 232
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1034633499 482 ----------------DEAFDEISDDAKDFISNLLKKDMKNRLDCTQCLQHPW 518
Cdd:cd07846   233 lfagvrlpevkeveplERRYPKLSGVVIDLAKKCLHIDPDKRPSCSELLHHEF 285
STKc_PAK6 cd06659
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the ...
269-521 7.04e-23

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: 99.67  E-value: 7.04e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 269 RLGSGKFGQVFRLVEKKTRKVWAGKFFKAYSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEIVSGGELFE 348
Cdd:cd06659    28 KIGEGSTGVVCIAREKHSGRQVAVKMMDLRKQQRRELLFNEVVIMRDYQHPNVVEMYKSYLVGEELWVLMEYLQGGALTD 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 349 riIDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVnkTGTRIKLIDFGLARRL-ENAGSLKVLFGTPEF 427
Cdd:cd06659   108 --IVSQTRLNEEQIATVCEAVLQALAYLHSQGVIHRDIKSDSILLT--LDGRVKLSDFGFCAQIsKDVPKRKSLVGTPYW 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 428 VAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDnetlanvTSATWDFDDEA------FDEISDDAKDFISNLLK 501
Cdd:cd06659   184 MAPEVISRCPYGTEVDIWSLGIMVIEMVDGEPPYFSDSP-------VQAMKRLRDSPppklknSHKASPVLRDFLERMLV 256
                         250       260
                  ....*....|....*....|
gi 1034633499 502 KDMKNRLDCTQCLQHPWLMK 521
Cdd:cd06659   257 RDPQERATAQELLDHPFLLQ 276
STKc_TSSK3-like cd14163
Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs ...
264-519 7.04e-23

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


Pssm-ID: 271065 [Multi-domain]  Cd Length: 257  Bit Score: 98.52  E-value: 7.04e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 264 YDIEERLGSGKFGQVFRLVEKKTRKVWAGKFFKAYSAKE---KENIRQEISIMNCLHHPKLVQCVDAFEEK-ANIVMVLE 339
Cdd:cd14163     2 YQLGKTIGEGTYSKVKEAFSKKHQRKVAIKIIDKSGGPEefiQRFLPRELQIVERLDHKNIIHVYEMLESAdGKIYLVME 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 340 IVSGGELFERIIDEDfELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCvnkTGTRIKLIDFGLARRLENAG-SL 418
Cdd:cd14163    82 LAEDGDVFDCVLHGG-PLPEHRAKALFRQLVEAIRYCHGCGVAHRDLKCENALL---QGFTLKLTDFGFAKQLPKGGrEL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 419 KVLF-GTPEFVAPEVINYEP-IGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATwdfDDEAFDEISDDAKDFI 496
Cdd:cd14163   158 SQTFcGSTAYAAPEVLQGVPhDSRKGDIWSMGVVLYVMLCAQLPFDDTDIPKMLCQQQKGV---SLPGHLGVSRTCQDLL 234
                         250       260
                  ....*....|....*....|...
gi 1034633499 497 SNLLKKDMKNRLDCTQCLQHPWL 519
Cdd:cd14163   235 KRLLEPDMVLRPSIEEVSWHPWL 257
STKc_IRE1 cd13982
Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze ...
318-517 9.80e-23

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: 98.50  E-value: 9.80e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 318 HPKLVQCVDAFEEKANIVMVLEI--VSGGELFERiiDEDFELTER---ECIKYMRQISEGVEYIHKQGIVHLDLKPENIM 392
Cdd:cd13982    54 HPNVIRYFCTEKDRQFLYIALELcaASLQDLVES--PRESKLFLRpglEPVRLLRQIASGLAHLHSLNIVHRDLKPQNIL 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 393 CV--NKTGT-RIKLIDFGLARRLE-NAGSLKVLF---GTPEFVAPEVINYEPIG---YATDMWSIG-VICYILVSGLSPF 461
Cdd:cd13982   132 IStpNAHGNvRAMISDFGLCKKLDvGRSSFSRRSgvaGTSGWIAPEMLSGSTKRrqtRAVDIFSLGcVFYYVLSGGSHPF 211
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1034633499 462 mGDN---DNETLANVTSATWDFDDEAFDEisdDAKDFISNLLKKDMKNRLDCTQCLQHP 517
Cdd:cd13982   212 -GDKlerEANILKGKYSLDKLLSLGEHGP---EAQDLIERMIDFDPEKRPSAEEVLNHP 266
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
609-699 1.06e-22

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


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 92.94  E-value: 1.06e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 609 PYFSKTIRDLEVVEGSAARFDCKIEGYPDPEVVWFKDDQSIRESRHFQIDYDEDGNCSLIISDVCGDDDAKYTCKAVNSL 688
Cdd:cd05744     1 PHFLQAPGDLEVQEGRLCRFDCKVSGLPTPDLFWQLNGKPVRPDSAHKMLVRENGRHSLIIEPVTKRDAGIYTCIARNRA 80
                          90
                  ....*....|.
gi 1034633499 689 GEATCTAELIV 699
Cdd:cd05744    81 GENSFNAELVV 91
STKc_MLK1 cd14145
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the ...
262-463 1.13e-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: 98.19  E-value: 1.13e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 262 DFYD--IEERLGSGKFGQVFRlvekktrKVWAGKFFKAYSAKEK---------ENIRQEISIMNCLHHPKLVQCVDAFEE 330
Cdd:cd14145     4 DFSElvLEEIIGIGGFGKVYR-------AIWIGDEVAVKAARHDpdedisqtiENVRQEAKLFAMLKHPNIIALRGVCLK 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 331 KANIVMVLEIVSGGELfERIIDEDfELTERECIKYMRQISEGVEYIHKQGIV---HLDLKPENIMCVNK------TGTRI 401
Cdd:cd14145    77 EPNLCLVMEFARGGPL-NRVLSGK-RIPPDILVNWAVQIARGMNYLHCEAIVpviHRDLKSSNILILEKvengdlSNKIL 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034633499 402 KLIDFGLARRLENAGSLKVLfGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMG 463
Cdd:cd14145   155 KITDFGLAREWHRTTKMSAA-GTYAWMAPEVIRSSMFSKGSDVWSYGVLLWELLTGEVPFRG 215
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
264-516 1.22e-22

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: 98.33  E-value: 1.22e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 264 YDIEERLGSGKFGQVFRLVEKKTRKVWAGKFFKAYSakekENIRQEISIMNCLHHPKLVQ----------CVDAFEEKAN 333
Cdd:cd14047     8 FKEIELIGSGGFGQVFKAKHRIDGKTYAIKRVKLNN----EKAEREVKALAKLDHPNIVRyngcwdgfdyDPETSSSNSS 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 334 IVMV------LEIVSGGELFERIIDEDFELTER-ECIKYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGtRIKLIDF 406
Cdd:cd14047    84 RSKTkclfiqMEFCEKGTLESWIEKRNGEKLDKvLALEIFEQITKGVEYIHSKKLIHRDLKPSNIF-LVDTG-KVKIGDF 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 407 GLARRLENAGSLKVLFGTPEFVAPEVINYEPIGYATDMWSIGVI----CYILVSGL--SPFMGDNDNETLANVtsatwdf 480
Cdd:cd14047   162 GLVTSLKNDGKRTKSKGTLSYMSPEQISSQDYGKEVDIYALGLIlfelLHVCDSAFekSKFWTDLRNGILPDI------- 234
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1034633499 481 ddeaFDEISDDAKDFISNLLKKDMKNRLDCTQCLQH 516
Cdd:cd14047   235 ----FDKRYKIEKTIIKKMLSKKPEDRPNASEILRT 266
STKc_MAPK15-like cd07852
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and ...
257-519 1.55e-22

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: 99.55  E-value: 1.55e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 257 EQKVSDFYDIEERLGSGKFGQVFRLVEKKTRKVWAGKffKAYSAKEKENIRQ----EISIMNCL-HHPKLVQCVDAFEEK 331
Cdd:cd07852     2 DKHILRRYEILKKLGKGAYGIVWKAIDKKTGEVVALK--KIFDAFRNATDAQrtfrEIMFLQELnDHPNIIKLLNVIRAE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 332 AN--IVMVLEIvsggelferiIDEDF------ELTERECIKY-MRQISEGVEYIHKQGIVHLDLKPENIM----Cvnktg 398
Cdd:cd07852    80 NDkdIYLVFEY----------METDLhaviraNILEDIHKQYiMYQLLKALKYLHSGGVIHRDLKPSNILlnsdC----- 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 399 tRIKLIDFGLARRL---ENAGSLKVLfgTpEFVA------PEVI----NYEpigYATDMWSIGVICYILVSGLSPFMGDN 465
Cdd:cd07852   145 -RVKLADFGLARSLsqlEEDDENPVL--T-DYVAtrwyraPEILlgstRYT---KGVDMWSVGCILGEMLLGKPLFPGTS 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 466 DNETLANVTSATW---------------------------DFDDEAFDEISDDAKDFISNLLKKDMKNRLDCTQCLQHPW 518
Cdd:cd07852   218 TLNQLEKIIEVIGrpsaediesiqspfaatmleslppsrpKSLDELFPKASPDALDLLKKLLVFNPNKRLTAEEALRHPY 297

                  .
gi 1034633499 519 L 519
Cdd:cd07852   298 V 298
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
268-519 2.39e-22

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: 97.87  E-value: 2.39e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 268 ERLGSGKFGQVFRLVEKKTRKVWAGKFFKAYSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEIVSGGELF 347
Cdd:cd06654    26 EKIGQGASGTVYTAMDVATGQEVAIRQMNLQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSLT 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 348 ERIIDEDFEltERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGTrIKLIDFGLARRLENAGSLK-VLFGTPE 426
Cdd:cd06654   106 DVVTETCMD--EGQIAAVCRECLQALEFLHSNQVIHRDIKSDNIL-LGMDGS-VKLTDFGFCAQITPEQSKRsTMVGTPY 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 427 FVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANV-TSATWDFDDEafDEISDDAKDFISNLLKKDMK 505
Cdd:cd06654   182 WMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIaTNGTPELQNP--EKLSAIFRDFLNRCLEMDVE 259
                         250
                  ....*....|....
gi 1034633499 506 NRLDCTQCLQHPWL 519
Cdd:cd06654   260 KRGSAKELLQHQFL 273
PKc_DYRK cd14210
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
264-519 2.64e-22

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


Pssm-ID: 271112 [Multi-domain]  Cd Length: 311  Bit Score: 98.00  E-value: 2.64e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 264 YDIEERLGSGKFGQVFRLVEKKTRKVWAGKFFKaysakEKENIRQ----EISIMNCL--HHPK----LVQCVDAFEEKAN 333
Cdd:cd14210    15 YEVLSVLGKGSFGQVVKCLDHKTGQLVAIKIIR-----NKKRFHQqalvEVKILKHLndNDPDdkhnIVRYKDSFIFRGH 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 334 IVMVLEIVSGgELFERIIDEDFE-LTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKTGTRIKLIDFGLARrL 412
Cdd:cd14210    90 LCIVFELLSI-NLYELLKSNNFQgLSLSLIRKFAKQILQALQFLHKLNIIHCDLKPENILLKQPSKSSIKVIDFGSSC-F 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 413 ENagslKVLFgtpEFV------APEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNE---------------TLA 471
Cdd:cd14210   168 EG----EKVY---TYIqsrfyrAPEVILGLPYDTAIDMWSLGCILAELYTGYPLFPGENEEEqlacimevlgvppksLID 240
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034633499 472 NVTSATWDFD-----------------------DEAFDEISDDAKDFISNLLKKDMKNRLDCTQCLQHPWL 519
Cdd:cd14210   241 KASRRKKFFDsngkprpttnskgkkrrpgskslAQVLKCDDPSFLDFLKKCLRWDPSERMTPEEALQHPWI 311
PKc_LIMK_like_unk cd14156
Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs ...
270-454 3.64e-22

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: 96.43  E-value: 3.64e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 270 LGSGKFGQVFRLVEKKTRKVWAGKFFKaySAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEIVSGGELFER 349
Cdd:cd14156     1 IGSGFFSKVYKVTHGATGKVMVVKIYK--NDVDQHKIVREISLLQKLSHPNIVRYLGICVKDEKLHPILEYVSGGCLEEL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 350 IIDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMC-VNKTGTRIKLIDFGLARRL----ENAGSLKV-LFG 423
Cdd:cd14156    79 LAREELPLSWREKVELACDISRGMVYLHSKNIYHRDLNSKNCLIrVTPRGREAVVTDFGLAREVgempANDPERKLsLVG 158
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1034633499 424 TPEFVAPEVINYEPIGYATDMWSIG-VICYIL 454
Cdd:cd14156   159 SAFWMAPEMLRGEPYDRKVDVFSFGiVLCEIL 190
PTKc_Srm_Brk cd05148
Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal ...
264-475 5.32e-22

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: 95.96  E-value: 5.32e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 264 YDIEERLGSGKFGQVFRLVEKKTRKVwAGKFFKAYSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEIVSG 343
Cdd:cd05148     8 FTLERKLGSGYFGEVWEGLWKNRVRV-AIKILKSDDLLKQQDFQKEVQALKRLRHKHLISLFAVCSVGEPVYIITELMEK 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 344 GELFERIID-EDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCvnKTGTRIKLIDFGLARRLEN----AGSL 418
Cdd:cd05148    87 GSLLAFLRSpEGQVLPVASLIDMACQVAEGMAYLEEQNSIHRDLAARNILV--GEDLVCKVADFGLARLIKEdvylSSDK 164
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1034633499 419 KVLFgtpEFVAPEVINYEPIGYATDMWSIGVICYILVS-GLSPFMGDNDNETLANVTS 475
Cdd:cd05148   165 KIPY---KWTAPEAASHGTFSTKSDVWSFGILLYEMFTyGQVPYPGMNNHEVYDQITA 219
STKc_nPKC_epsilon cd05591
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze ...
270-545 5.97e-22

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


Pssm-ID: 270743 [Multi-domain]  Cd Length: 321  Bit Score: 97.56  E-value: 5.97e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 270 LGSGKFGQVFrLVEKK-TRKVWAGKFFKAYSAKEKENIRQEISIMNCL----HHPKLVQCVDAFEEKANIVMVLEIVSGG 344
Cdd:cd05591     3 LGKGSFGKVM-LAERKgTDEVYAIKVLKKDVILQDDDVDCTMTEKRILalaaKHPFLTALHSCFQTKDRLFFVMEYVNGG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 345 ELFERIiDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGtRIKLIDFGLARRLENAGSLKVLF-G 423
Cdd:cd05591    82 DLMFQI-QRARKFDEPRARFYAAEVTLALMFLHRHGVIYRDLKLDNIL-LDAEG-HCKLADFGMCKEGILNGKTTTTFcG 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 424 TPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSatwdfDDEAFDE-ISDDAKDFISNLLKK 502
Cdd:cd05591   159 TPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILH-----DDVLYPVwLSKEAVSILKAFMTK 233
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1034633499 503 DMKNRLDC--TQC-----LQHPWLMK-DTKNMEAKKLSKDRMKKYMARRKW 545
Cdd:cd05591   234 NPAKRLGCvaSQGgedaiRQHPFFREiDWEALEQRKVKPPFKPKIKTKRDA 284
PTKc_Src_like cd05034
Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
268-473 6.42e-22

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: 95.43  E-value: 6.42e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 268 ERLGSGKFGQVFRLVEKKTRKVwAGKFFKAySAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEIVSGGELF 347
Cdd:cd05034     1 KKLGAGQFGEVWMGVWNGTTKV-AVKTLKP-GTMSPEAFLQEAQIMKKLRHDKLVQLYAVCSDEEPIYIVTELMSKGSLL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 348 ERIIDEDFE-LTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNktGTRIKLIDFGLARRLEN------AGS--- 417
Cdd:cd05034    79 DYLRTGEGRaLRLPQLIDMAAQIASGMAYLESRNYIHRDLAARNILVGE--NNVCKVADFGLARLIEDdeytarEGAkfp 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1034633499 418 LKvlfgtpeFVAPEVINYEPIGYATDMWSIGVICYILVS-GLSPFMGDNDNETLANV 473
Cdd:cd05034   157 IK-------WTAPEAALYGRFTIKSDVWSFGILLYEIVTyGRVPYPGMTNREVLEQV 206
STKc_NDR_like_fungal cd05629
Catalytic domain of Fungal Nuclear Dbf2-Related kinase-like Serine/Threonine Kinases; STKs ...
248-508 6.93e-22

Catalytic domain of Fungal Nuclear Dbf2-Related kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This group is composed of fungal NDR-like proteins including Saccharomyces cerevisiae CBK1 (or CBK1p), Schizosaccharomyces pombe Orb6 (or Orb6p), Ustilago maydis Ukc1 (or Ukc1p), and Neurospora crassa Cot1. Like NDR kinase, group members contain an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. CBK1 is an essential component in the RAM (regulation of Ace2p activity and cellular morphogenesis) network. CBK1 and Orb6 play similar roles in coordinating cell morphology with cell cycle progression. Ukc1 is involved in morphogenesis, pathogenicity, and pigment formation. Cot1 plays a role in polar tip extension.The fungal NDR subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270778 [Multi-domain]  Cd Length: 377  Bit Score: 98.38  E-value: 6.93e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 248 DYRTVTInteqkvsdfydieerLGSGKFGQVfRLVEKK-TRKVWAGKFF---KAYSAKEKENIRQEISIMNCLHHPKLVQ 323
Cdd:cd05629     2 DFHTVKV---------------IGKGAFGEV-RLVQKKdTGKIYAMKTLlksEMFKKDQLAHVKAERDVLAESDSPWVVS 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 324 CVDAFEEKANIVMVLEIVSGGELFERIIDEDFeLTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGtRIKL 403
Cdd:cd05629    66 LYYSFQDAQYLYLIMEFLPGGDLMTMLIKYDT-FSEDVTRFYMAECVLAIEAVHKLGFIHRDIKPDNIL-IDRGG-HIKL 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 404 IDFGLA---RRLENAGSLKVLF---------------------------------------------GTPEFVAPEVINY 435
Cdd:cd05629   143 SDFGLStgfHKQHDSAYYQKLLqgksnknridnrnsvavdsinltmsskdqiatwkknrrlmaystvGTPDYIAPEIFLQ 222
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034633499 436 EPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTS--ATWDFDDEAfdEISDDAKDFISNLLkKDMKNRL 508
Cdd:cd05629   223 QGYGQECDWWSLGAIMFECLIGWPPFCSENSHETYRKIINwrETLYFPDDI--HLSVEAEDLIRRLI-TNAENRL 294
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
609-700 8.61e-22

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


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 90.17  E-value: 8.61e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 609 PYFSKTIRDLEVVEGSAARFDCKIEGYPDPEVVWFKDDQSI---RESRHFQIdYDEDGNCSLIISDVCGDDDAKYTCKAV 685
Cdd:cd20951     1 PEFIIRLQSHTVWEKSDAKLRVEVQGKPDPEVKWYKNGVPIdpsSIPGKYKI-ESEYGVHVLHIRRVTVEDSAVYSAVAK 79
                          90
                  ....*....|....*
gi 1034633499 686 NSLGEATCTAELIVE 700
Cdd:cd20951    80 NIHGEASSSASVVVE 94
STKc_MLK4 cd14146
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the ...
270-463 9.22e-22

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: 95.49  E-value: 9.22e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 270 LGSGKFGQVFRlvekktrKVWAGKFFKAYSAKEK---------ENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEI 340
Cdd:cd14146     2 IGVGGFGKVYR-------ATWKGQEVAVKAARQDpdedikataESVRQEAKLFSMLRHPNIIKLEGVCLEEPNLCLVMEF 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 341 VSGGELFERIIDEDFELTEREC--------IKYMRQISEGVEYIHKQGIV---HLDLKPENIMCVNKT------GTRIKL 403
Cdd:cd14146    75 ARGGTLNRALAAANAAPGPRRArripphilVNWAVQIARGMLYLHEEAVVpilHRDLKSSNILLLEKIehddicNKTLKI 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 404 IDFGLARRLENAGSLKVLfGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMG 463
Cdd:cd14146   155 TDFGLAREWHRTTKMSAA-GTYAWMAPEVIKSSLFSKGSDIWSYGVLLWELLTGEVPYRG 213
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
268-519 1.09e-21

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: 95.53  E-value: 1.09e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 268 ERLGSGKFGQVFRLVEKKTRKVWAGKFFK--AYSAKEKEN--------IRQEISIMNCLHHPKLVQCVdAFEEKANIVMV 337
Cdd:cd06629     7 ELIGKGTYGRVYLAMNATTGEMLAVKQVElpKTSSDRADSrqktvvdaLKSEIDTLKDLDHPNIVQYL-GFEETEDYFSI 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 338 -LEIVSGGELFERIidEDFELTERECIK-YMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGTrIKLIDFGLARRLEN- 414
Cdd:cd06629    86 fLEYVPGGSIGSCL--RKYGKFEEDLVRfFTRQILDGLAYLHSKGILHRDLKADNIL-VDLEGI-CKISDFGISKKSDDi 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 415 -----AGSLKvlfGTPEFVAPEVINYEPIGYAT--DMWSIGVICYILVSGLSPFmgdNDNETLA------NVTSATWDFD 481
Cdd:cd06629   162 ygnngATSMQ---GSVFWMAPEVIHSQGQGYSAkvDIWSLGCVVLEMLAGRRPW---SDDEAIAamfklgNKRSAPPVPE 235
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1034633499 482 DEafdEISDDAKDFISNLLKKDMKNRLDCTQCLQHPWL 519
Cdd:cd06629   236 DV---NLSPEALDFLNACFAIDPRDRPTAAELLSHPFL 270
PTKc_Frk_like cd05068
Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
269-473 1.29e-21

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: 95.17  E-value: 1.29e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 269 RLGSGKFGQVFRLVEKKTRKVwAGKFFKAYSAKEKENIRqEISIMNCLHHPKLVQCVDAFEEKANIVMVLEIVSGGELFE 348
Cdd:cd05068    15 KLGSGQFGEVWEGLWNNTTPV-AVKTLKPGTMDPEDFLR-EAQIMKKLRHPKLIQLYAVCTLEEPIYIITELMKHGSLLE 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 349 RIIDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGTrIKLIDFGLARRLENAGSLKVLFGTP--- 425
Cdd:cd05068    93 YLQGKGRSLQLPQLIDMAAQVASGMAYLESQNYIHRDLAARNVL-VGENNI-CKVADFGLARVIKVEDEYEAREGAKfpi 170
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1034633499 426 EFVAPEVINYEPIGYATDMWSIGVICYILVS-GLSPFMGDNDNETLANV 473
Cdd:cd05068   171 KWTAPEAANYNRFSIKSDVWSFGILLTEIVTyGRIPYPGMTNAEVLQQV 219
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
286-526 1.55e-21

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 98.55  E-value: 1.55e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 286 TRKVWAgKFFKAYSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEIVSGGELFERI---IDEDFELTEREC 362
Cdd:PTZ00267   93 KEKVVA-KFVMLNDERQAAYARSELHCLAACDHFGIVKHFDDFKSDDKLLLIMEYGSGGDLNKQIkqrLKEHLPFQEYEV 171
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 363 IKYMRQISEGVEYIHKQGIVHLDLKPENIMCVnKTGTrIKLIDFGLARRLENAGSLKV---LFGTPEFVAPEVINYEPIG 439
Cdd:PTZ00267  172 GLLFYQIVLALDEVHSRKMMHRDLKSANIFLM-PTGI-IKLGDFGFSKQYSDSVSLDVassFCGTPYYLAPELWERKRYS 249
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 440 YATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDfddeAFD-EISDDAKDFISNLLKKDMKNRLDCTQCLqHPW 518
Cdd:PTZ00267  250 KKADMWSLGVILYELLTLHRPFKGPSQREIMQQVLYGKYD----PFPcPVSSGMKALLDPLLSKNPALRPTTQQLL-HTE 324

                  ....*...
gi 1034633499 519 LMKDTKNM 526
Cdd:PTZ00267  325 FLKYVANL 332
STKc_PIM2 cd14101
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
270-520 1.84e-21

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: 94.53  E-value: 1.84e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 270 LGSGKFGQVF---RLVE--KKTRKVWAGKFFKAYSAKEKEN-IRQEISIMNCL----HHPKLVQCVDAFEEKANIVMVLE 339
Cdd:cd14101     8 LGKGGFGTVYaghRISDglQVAIKQISRNRVQQWSKLPGVNpVPNEVALLQSVgggpGHRGVIRLLDWFEIPEGFLLVLE 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 340 -IVSGGELFErIIDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKTGTrIKLIDFGLARRLENagSL 418
Cdd:cd14101    88 rPQHCQDLFD-YITERGALDESLARRFFKQVVEAVQHCHSKGVVHRDIKDENILVDLRTGD-IKLIDFGSGATLKD--SM 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 419 KVLF-GTPEFVAPEVINYEPI-GYATDMWSIGVICYILVSGLSPFMGDNDnetlanVTSATWDFDdeafDEISDDAKDFI 496
Cdd:cd14101   164 YTDFdGTRVYSPPEWILYHQYhALPATVWSLGILLYDMVCGDIPFERDTD------ILKAKPSFN----KRVSNDCRSLI 233
                         250       260
                  ....*....|....*....|....
gi 1034633499 497 SNLLKKDMKNRLDCTQCLQHPWLM 520
Cdd:cd14101   234 RSCLAYNPSDRPSLEQILLHPWMM 257
STKc_TNIK cd06637
Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs ...
264-543 1.98e-21

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: 95.17  E-value: 1.98e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 264 YDIEERLGSGKFGQVFRLVEKKTRKVWAGKFFKAySAKEKENIRQEISIMNCL-HHPKLVQCVDAFEEKA------NIVM 336
Cdd:cd06637     8 FELVELVGNGTYGQVYKGRHVKTGQLAAIKVMDV-TGDEEEEIKQEINMLKKYsHHRNIATYYGAFIKKNppgmddQLWL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 337 VLEIVSGGELFERIIDEDFELTERECIKYM-RQISEGVEYIHKQGIVHLDLKPENIMCVNKtgTRIKLIDFGLARRLE-N 414
Cdd:cd06637    87 VMEFCGAGSVTDLIKNTKGNTLKEEWIAYIcREILRGLSHLHQHKVIHRDIKGQNVLLTEN--AEVKLVDFGVSAQLDrT 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 415 AGSLKVLFGTPEFVAPEVINYE-----PIGYATDMWSIGVICYILVSGLSPFMGDNDNETL--------ANVTSATWdfd 481
Cdd:cd06637   165 VGRRNTFIGTPYWMAPEVIACDenpdaTYDFKSDLWSLGITAIEMAEGAPPLCDMHPMRALfliprnpaPRLKSKKW--- 241
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034633499 482 deafdeiSDDAKDFISNLLKKDMKNRLDCTQCLQHPWLMKDTKNMEAKKLSKDRMKKYMARR 543
Cdd:cd06637   242 -------SKKFQSFIESCLVKNHSQRPSTEQLMKHPFIRDQPNERQVRIQLKDHIDRTKKKR 296
STKc_MEKK3 cd06651
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
270-518 2.10e-21

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: 94.76  E-value: 2.10e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 270 LGSGKFGQVFRLVEKKTRKVWAGKFFK-----AYSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKA--NIVMVLEIVS 342
Cdd:cd06651    15 LGQGAFGRVYLCYDVDTGRELAAKQVQfdpesPETSKEVSALECEIQLLKNLQHERIVQYYGCLRDRAekTLTIFMEYMP 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 343 GGELFERIIDEDfELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMcvNKTGTRIKLIDFGLARRLE----NAGSL 418
Cdd:cd06651    95 GGSVKDQLKAYG-ALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANIL--RDSAGNVKLGDFGASKRLQticmSGTGI 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 419 KVLFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMgdnDNETLANVTS-ATWDFDDEAFDEISDDAKDFIS 497
Cdd:cd06651   172 RSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWA---EYEAMAAIFKiATQPTNPQLPSHISEHARDFLG 248
                         250       260
                  ....*....|....*....|.
gi 1034633499 498 NLLkKDMKNRLDCTQCLQHPW 518
Cdd:cd06651   249 CIF-VEARHRPSAEELLRHPF 268
STKc_MLK3 cd14147
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the ...
266-463 2.34e-21

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: 94.33  E-value: 2.34e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 266 IEERLGSGKFGQVFRlvekktrKVWAGKFFKAYSAKEK---------ENIRQEISIMNCLHHPKLVQCVDAFEEKANIVM 336
Cdd:cd14147     7 LEEVIGIGGFGKVYR-------GSWRGELVAVKAARQDpdedisvtaESVRQEARLFAMLAHPNIIALKAVCLEEPNLCL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 337 VLEIVSGGELFERIIDEdfELTERECIKYMRQISEGVEYIHKQGIV---HLDLKPENIMCV---------NKTgtrIKLI 404
Cdd:cd14147    80 VMEYAAGGPLSRALAGR--RVPPHVLVNWAVQIARGMHYLHCEALVpviHRDLKSNNILLLqpienddmeHKT---LKIT 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1034633499 405 DFGLARRLENAGSLKVLfGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMG 463
Cdd:cd14147   155 DFGLAREWHKTTQMSAA-GTYAWMAPEVIKASTFSKGSDVWSFGVLLWELLTGEVPYRG 212
STKc_PAK5 cd06658
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the ...
269-519 2.59e-21

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: 94.72  E-value: 2.59e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 269 RLGSGKFGQVFRLVEKKTRKVWAGKFFKAYSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEIVSGGELFE 348
Cdd:cd06658    29 KIGEGSTGIVCIATEKHTGKQVAVKKMDLRKQQRRELLFNEVVIMRDYHHENVVDMYNSYLVGDELWVVMEFLEGGALTD 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 349 RIIDEDF--ELTERECIKYMRQISegveYIHKQGIVHLDLKPENIMCVnkTGTRIKLIDFGL-ARRLENAGSLKVLFGTP 425
Cdd:cd06658   109 IVTHTRMneEQIATVCLSVLRALS----YLHNQGVIHRDIKSDSILLT--SDGRIKLSDFGFcAQVSKEVPKRKSLVGTP 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 426 EFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDFDDEAfDEISDDAKDFISNLLKKDMK 505
Cdd:cd06658   183 YWMAPEVISRLPYGTEVDIWSLGIMVIEMIDGEPPYFNEPPLQAMRRIRDNLPPRVKDS-HKVSSVLRGFLDLMLVREPS 261
                         250
                  ....*....|....
gi 1034633499 506 NRLDCTQCLQHPWL 519
Cdd:cd06658   262 QRATAQELLQHPFL 275
STKc_NIK cd13991
Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs ...
267-461 2.64e-21

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: 94.11  E-value: 2.64e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 267 EERLGSGKFGQVFRLVEKKT------RKVwAGKFFKAysakekenirQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEI 340
Cdd:cd13991    11 QLRIGRGSFGEVHRMEDKQTgfqcavKKV-RLEVFRA----------EELMACAGLTSPRVVPLYGAVREGPWVNIFMDL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 341 VSGGELfERIIDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGTRIKLIDFGLARRLENAGSLKV 420
Cdd:cd13991    80 KEGGSL-GQLIKEQGCLPEDRALHYLGQALEGLEYLHSRKILHGDVKADNVL-LSSDGSDAFLCDFGHAECLDPDGLGKS 157
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1034633499 421 LF------GTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPF 461
Cdd:cd13991   158 LFtgdyipGTETHMAPEVVLGKPCDAKVDVWSSCCMMLHMLNGCHPW 204
STKc_MAP4K4_6_N cd06636
N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase ...
264-519 3.81e-21

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: 94.30  E-value: 3.81e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 264 YDIEERLGSGKFGQVFRLVEKKTRKVWAGKFFKAySAKEKENIRQEISIMNCL-HHPKLVQCVDAFEEKA------NIVM 336
Cdd:cd06636    18 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDV-TEDEEEEIKLEINMLKKYsHHRNIATYYGAFIKKSppghddQLWL 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 337 VLEIVSGGELFERIIDEDFELTERECIKYM-RQISEGVEYIHKQGIVHLDLKPENIMCVNKtgTRIKLIDFGLARRLE-N 414
Cdd:cd06636    97 VMEFCGAGSVTDLVKNTKGNALKEDWIAYIcREILRGLAHLHAHKVIHRDIKGQNVLLTEN--AEVKLVDFGVSAQLDrT 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 415 AGSLKVLFGTPEFVAPEVINYE-----PIGYATDMWSIGVICYILVSGLSPFMGDNDNETL--------ANVTSATWdfd 481
Cdd:cd06636   175 VGRRNTFIGTPYWMAPEVIACDenpdaTYDYRSDIWSLGITAIEMAEGAPPLCDMHPMRALfliprnppPKLKSKKW--- 251
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1034633499 482 deafdeiSDDAKDFISNLLKKDMKNRLDCTQCLQHPWL 519
Cdd:cd06636   252 -------SKKFIDFIEGCLVKNYLSRPSTEQLLKHPFI 282
STKc_NDR1 cd05628
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 1; STKs catalyze ...
270-496 3.90e-21

Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NDR1 (also called STK38) plays a role in proper centrosome duplication. It is highly expressed in thymus, muscle, lung and spleen. It is not an essential protein because mice deficient of NDR1 remain viable and fertile. However, these mice develop T-cell lymphomas and appear to be hypersenstive to carcinogenic treatment. NDR1 appears to also act as a tumor suppressor. NDR kinase contains an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Like many other AGC kinases, NDR kinase requires phosphorylation at two sites, the activation loop (A-loop) and the hydrophobic motif (HM), for activity. The NDR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270777 [Multi-domain]  Cd Length: 376  Bit Score: 95.88  E-value: 3.90e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 270 LGSGKFGQVfRLVEKK-TRKVWAGKFFKAYSAKEKE---NIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEIVSGGE 345
Cdd:cd05628     9 IGRGAFGEV-RLVQKKdTGHVYAMKILRKADMLEKEqvgHIRAERDILVEADSLWVVKMFYSFQDKLNLYLIMEFLPGGD 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 346 LFERIIDEDfELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKtgTRIKLIDFGLARRLENA---------- 415
Cdd:cd05628    88 MMTLLMKKD-TLTEEETQFYIAETVLAIDSIHQLGFIHRDIKPDNLLLDSK--GHVKLSDFGLCTGLKKAhrtefyrnln 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 416 GSLKVLF--------------------------GTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNET 469
Cdd:cd05628   165 HSLPSDFtfqnmnskrkaetwkrnrrqlafstvGTPDYIAPEVFMQTGYNKLCDWWSLGVIMYEMLIGYPPFCSETPQET 244
                         250       260
                  ....*....|....*....|....*....
gi 1034633499 470 LANVTS--ATWDFDDEAfdEISDDAKDFI 496
Cdd:cd05628   245 YKKVMNwkETLIFPPEV--PISEKAKDLI 271
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
264-516 3.95e-21

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: 93.90  E-value: 3.95e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 264 YDIEERLGSGKFGQVFRLVEKKTRKVWAGKFFKAYSAKEKENIRQEISIMNCLHHPKLVQCVD-AFEEKAN----IVMVL 338
Cdd:cd13986     2 YRIQRLLGEGGFSFVYLVEDLSTGRLYALKKILCHSKEDVKEAMREIENYRLFNHPNILRLLDsQIVKEAGgkkeVYLLL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 339 EIVSGGEL---FERIIDEDFELTERECIKYMRQISEGVEYIHKQGIV---HLDLKPENIMcVNKTGTRIkLIDFG----- 407
Cdd:cd13986    82 PYYKRGSLqdeIERRLVKGTFFPEDRILHIFLGICRGLKAMHEPELVpyaHRDIKPGNVL-LSEDDEPI-LMDLGsmnpa 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 408 --------LARRLENAGSLKvlfGTPEFVAPEVINYEP---IGYATDMWSIGVICYILVSGLSPF---MGDNDNETLAnV 473
Cdd:cd13986   160 rieiegrrEALALQDWAAEH---CTMPYRAPELFDVKShctIDEKTDIWSLGCTLYALMYGESPFeriFQKGDSLALA-V 235
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1034633499 474 TSATWDFDDEAfdEISDDAKDFISNLLKKDMKNRLDCTQCLQH 516
Cdd:cd13986   236 LSGNYSFPDNS--RYSEELHQLVKSMLVVNPAERPSIDDLLSR 276
STKc_Pho85 cd07836
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; ...
268-518 4.07e-21

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: 94.08  E-value: 4.07e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 268 ERLGSGKFGQVFRLVEKKTRKVWAGKFFK--AYSAKEKENIRqEISIMNCLHHPKLVQCVDAFEEKANIVMVLEIVSGGe 345
Cdd:cd07836     6 EKLGEGTYATVYKGRNRTTGEIVALKEIHldAEEGTPSTAIR-EISLMKELKHENIVRLHDVIHTENKLMLVFEYMDKD- 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 346 lFERIID---EDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGtRIKLIDFGLARRlenagslkvlF 422
Cdd:cd07836    84 -LKKYMDthgVRGALDPNTVKSFTYQLLKGIAFCHENRVLHRDLKPQNLL-INKRG-ELKLADFGLARA----------F 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 423 GTP------EFV-----APEVInyepIG---YAT--DMWSIGVICYILVSGLSPFMGDNDNETLANV-------TSATW- 478
Cdd:cd07836   151 GIPvntfsnEVVtlwyrAPDVL----LGsrtYSTsiDIWSVGCIMAEMITGRPLFPGTNNEDQLLKIfrimgtpTESTWp 226
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1034633499 479 ----------DFDDEA-------FDEISDDAKDFISNLLKKDMKNRLDCTQCLQHPW 518
Cdd:cd07836   227 gisqlpeykpTFPRYPpqdlqqlFPHADPLGIDLLHRLLQLNPELRISAHDALQHPW 283
STKc_MOK cd07831
Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs ...
264-518 4.37e-21

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: 93.88  E-value: 4.37e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 264 YDIEERLGSGKFGQVFRLVEKKTRKVWAGKFFKA-YSAKEKENIRQEISIMNCL-HHPKLVQCVDA-FEEKAN-IVMVLE 339
Cdd:cd07831     1 YKILGKIGEGTFSEVLKAQSRKTGKYYAIKCMKKhFKSLEQVNNLREIQALRRLsPHPNILRLIEVlFDRKTGrLALVFE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 340 IVSGgELFERIIDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKTgtrIKLIDFGLARRLENAGSLK 419
Cdd:cd07831    81 LMDM-NLYELIKGRKRPLPEKRVKNYMYQLLKSLDHMHRNGIFHRDIKPENILIKDDI---LKLADFGSCRGIYSKPPYT 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 420 VLFGTPEFVAPEVI----NYepiGYATDMWSIGVICYILVSgLSP-FMGDNDNETLA---NV---------------TSA 476
Cdd:cd07831   157 EYISTRWYRAPECLltdgYY---GPKMDIWAVGCVFFEILS-LFPlFPGTNELDQIAkihDVlgtpdaevlkkfrksRHM 232
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1034633499 477 TWDFDDEAFDEI-------SDDAKDFISNLLKKDMKNRLDCTQCLQHPW 518
Cdd:cd07831   233 NYNFPSKKGTGLrkllpnaSAEGLDLLKKLLAYDPDERITAKQALRHPY 281
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
264-519 4.94e-21

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: 93.39  E-value: 4.94e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 264 YDIEERLGSGKFGQVFRLVEKKTRKVWAGKFFKAYSAKE---KENIRQEISIMNCLHHPKLVQCVDAFE---EKANIVMv 337
Cdd:cd14164     2 YTLGTTIGEGSFSKVKLATSQKYCCKVAIKIVDRRRASPdfvQKFLPRELSILRRVNHPNIVQMFECIEvanGRLYIVM- 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 338 leivsggELFERIIDEDFELTERECIKYMR----QISEGVEYIHKQGIVHLDLKPENIMcVNKTGTRIKLIDFGLARRLE 413
Cdd:cd14164    81 -------EAAATDLLQKIQEVHHIPKDLARdmfaQMVGAVNYLHDMNIVHRDLKCENIL-LSADDRKIKIADFGFARFVE 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 414 NAGSLKVLF-GTPEFVAPEVIN---YEPIGYatDMWSIGVICYILVSGLSPFMGDNDNET---------LANVtsatwdf 480
Cdd:cd14164   153 DYPELSTTFcGSRAYTPPEVILgtpYDPKKY--DVWSLGVVLYVMVTGTMPFDETNVRRLrlqqrgvlyPSGV------- 223
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1034633499 481 ddeafdEISDDAKDFISNLLKKDMKNRLDCTQCLQHPWL 519
Cdd:cd14164   224 ------ALEEPCRALIRTLLQFNPSTRPSIQQVAGNSWL 256
STKc_CDKL1_4 cd07847
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; ...
262-518 5.50e-21

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: 93.59  E-value: 5.50e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 262 DFYDIEERLGSGKFGQVFRLVEKKTRKVWAGKFFKAysAKEKENIRQ----EISIMNCLHHPKLVQCVDAFEEKANIVMV 337
Cdd:cd07847     1 EKYEKLSKIGEGSYGVVFKCRNRETGQIVAIKKFVE--SEDDPVIKKialrEIRMLKQLKHPNLVNLIEVFRRKRKLHLV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 338 LEIVSGGELFE-----RIIDEDfelterECIKYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGtRIKLIDFGLARRL 412
Cdd:cd07847    79 FEYCDHTVLNEleknpRGVPEH------LIKKIIWQTLQAVNFCHKHNCIHRDVKPENIL-ITKQG-QIKLCDFGFARIL 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 413 ENAGSLKVLF-GTPEFVAPEVI----NYEPigyATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDFD------ 481
Cdd:cd07847   151 TGPGDDYTDYvATRWYRAPELLvgdtQYGP---PVDVWAIGCVFAELLTGQPLWPGKSDVDQLYLIRKTLGDLIprhqqi 227
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1034633499 482 ---------------------DEAFDEISDDAKDFISNLLKKDMKNRLDCTQCLQHPW 518
Cdd:cd07847   228 fstnqffkglsipepetreplESKFPNISSPALSFLKGCLQMDPTERLSCEELLEHPY 285
STKc_MAP3K12_13 cd14059
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase ...
270-461 5.53e-21

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: 92.56  E-value: 5.53e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 270 LGSGKFGQVFRlvekktrkvwaGKFFKAYSAKEKENIRQEISI--MNCLHHPKLVQCVDAFEEKANIVMVLEIVSGGELF 347
Cdd:cd14059     1 LGSGAQGAVFL-----------GKFRGEEVAVKKVRDEKETDIkhLRKLNHPNIIKFKGVCTQAPCYCILMEYCPYGQLY 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 348 ErIIDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKTgtRIKLIDFGLARRLeNAGSLKVLF-GTPE 426
Cdd:cd14059    70 E-VLRAGREITPSLLVDWSKQIASGMNYLHLHKIIHRDLKSPNVLVTYND--VLKISDFGTSKEL-SEKSTKMSFaGTVA 145
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1034633499 427 FVAPEVINYEPIGYATDMWSIGVICYILVSGLSPF 461
Cdd:cd14059   146 WMAPEVIRNEPCSEKVDIWSFGVVLWELLTGEIPY 180
PKc_PBS2_like cd06622
Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
268-522 5.85e-21

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: 93.76  E-value: 5.85e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 268 ERLGSGKFGQVFRLVEKKTRKVWAGKFFKAYSAKEKEN-IRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEIVSGGEL 346
Cdd:cd06622     7 DELGKGNYGSVYKVLHRPTGVTMAMKEIRLELDESKFNqIIMELDILHKAVSPYIVDFYGAFFIEGAVYMCMEYMDAGSL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 347 fERIIDEDFELT---ERECIKYMRQISEGVEYIHKQ-GIVHLDLKPENIMCvNKTGTrIKLIDFGLARRLEnAGSLKVLF 422
Cdd:cd06622    87 -DKLYAGGVATEgipEDVLRRITYAVVKGLKFLKEEhNIIHRDVKPTNVLV-NGNGQ-VKLCDFGVSGNLV-ASLAKTNI 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 423 GTPEFVAPEVINYE-PIGYAT-----DMWSIGVICYILVSGLSPFmgdnDNETLANV---TSATWDFDDEAF-DEISDDA 492
Cdd:cd06622   163 GCQSYMAPERIKSGgPNQNPTytvqsDVWSLGLSILEMALGRYPY----PPETYANIfaqLSAIVDGDPPTLpSGYSDDA 238
                         250       260       270
                  ....*....|....*....|....*....|
gi 1034633499 493 KDFISNLLKKDMKNRLDCTQCLQHPWLMKD 522
Cdd:cd06622   239 QDFVAKCLNKIPNRRPTYAQLLEHPWLVKY 268
STKc_aPKC cd05588
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the ...
270-468 6.29e-21

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: 94.41  E-value: 6.29e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 270 LGSGKFGQVFRLVEKKTRKVWAGKFFKAYSAKEKENI---RQEISIMNCL-HHPKLVQCVDAFEEKANIVMVLEIVSGGE 345
Cdd:cd05588     3 IGRGSYAKVLMVELKKTKRIYAMKVIKKELVNDDEDIdwvQTEKHVFETAsNHPFLVGLHSCFQTESRLFFVIEFVNGGD 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 346 LFERIiDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGtRIKLIDFGLARRLENAGSLKVLF-GT 424
Cdd:cd05588    83 LMFHM-QRQRRLPEEHARFYSAEISLALNFLHEKGIIYRDLKLDNVL-LDSEG-HIKLTDYGMCKEGLRPGDTTSTFcGT 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1034633499 425 PEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPF--MGDNDNE 468
Cdd:cd05588   160 PNYIAPEILRGEDYGFSVDWWALGVLMFEMLAGRSPFdiVGSSDNP 205
STKc_MLK2 cd14148
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the ...
270-461 7.28e-21

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: 92.74  E-value: 7.28e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 270 LGSGKFGQVFRlvekktrKVWAGKFFKAYSAKEK---------ENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEI 340
Cdd:cd14148     2 IGVGGFGKVYK-------GLWRGEEVAVKAARQDpdediavtaENVRQEARLFWMLQHPNIIALRGVCLNPPHLCLVMEY 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 341 VSGGELFERIIDEdfELTERECIKYMRQISEGVEYIHKQGIV---HLDLKPENIMCVNK------TGTRIKLIDFGLARR 411
Cdd:cd14148    75 ARGGALNRALAGK--KVPPHVLVNWAVQIARGMNYLHNEAIVpiiHRDLKSSNILILEPienddlSGKTLKITDFGLARE 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1034633499 412 LENAGSLKVLfGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPF 461
Cdd:cd14148   153 WHKTTKMSAA-GTYAWMAPEVIRLSLFSKSSDVWSFGVLLWELLTGEVPY 201
STKc_CDKL5 cd07848
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs ...
270-517 8.53e-21

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: 93.14  E-value: 8.53e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 270 LGSGKFGQVFRLVEKKTRKVWAGKFFKAYSAKE--KENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEIVSGGELf 347
Cdd:cd07848     9 VGEGAYGVVLKCRHKETKEIVAIKKFKDSEENEevKETTLRELKMLRTLKQENIVELKEAFRRRGKLYLVFEYVEKNML- 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 348 eRIIDEDFELTERECIK-YMRQISEGVEYIHKQGIVHLDLKPENIMCvnKTGTRIKLIDFGLARRLE--NAGSLKVLFGT 424
Cdd:cd07848    88 -ELLEEMPNGVPPEKVRsYIYQLIKAIHWCHKNDIVHRDIKPENLLI--SHNDVLKLCDFGFARNLSegSNANYTEYVAT 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 425 PEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDFDDEAFDEISDDAK----------- 493
Cdd:cd07848   165 RWYRSPELLLGAPYGKAVDMWSVGCILGELSDGQPLFPGESEIDQLFTIQKVLGPLPAEQMKLFYSNPRfhglrfpavnh 244
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1034633499 494 -----------------DFISNLLKKDMKNRLDCTQCLQHP 517
Cdd:cd07848   245 pqslerrylgilsgvllDLMKNLLKLNPTDRYLTEQCLNHP 285
PKc_YAK1 cd14212
Catalytic domain of the Dual-specificity protein kinase, YAK1; Dual-specificity PKs catalyze ...
264-465 9.21e-21

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: 93.85  E-value: 9.21e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 264 YDIEERLGSGKFGQVFRLVEKKTRKVWAGKFFK---AYSakekeniRQ---EISIMNCL---------HHpkLVQCVDAF 328
Cdd:cd14212     1 YLVLDLLGQGTFGQVVKCQDLKTNKLVAVKVLKnkpAYF-------RQamlEIAILTLLntkydpedkHH--IVRLLDHF 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 329 EEKANIVMVLEIVsGGELFERIIDEDFELTERECIK-YMRQISEGVEYIHKQGIVHLDLKPENIMCVNKTGTRIKLIDFG 407
Cdd:cd14212    72 MHHGHLCIVFELL-GVNLYELLKQNQFRGLSLQLIRkFLQQLLDALSVLKDARIIHCDLKPENILLVNLDSPEIKLIDFG 150
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1034633499 408 LArRLENAgSLKVLFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDN 465
Cdd:cd14212   151 SA-CFENY-TLYTYIQSRFYRSPEVLLGLPYSTAIDMWSLGCIAAELFLGLPLFPGNS 206
STKc_MRCK_beta cd05624
Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control ...
251-500 9.25e-21

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


Pssm-ID: 270774 [Multi-domain]  Cd Length: 409  Bit Score: 95.46  E-value: 9.25e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 251 TVTINTEQKVSDFYDIEERLGSGKFGQVFRLVEKKTRKVWAGKFFKAYSA---KEKENIRQEISIM---NC-----LHHp 319
Cdd:cd05624    61 TQLVKEMQLHRDDFEIIKVIGRGAFGEVAVVKMKNTERIYAMKILNKWEMlkrAETACFREERNVLvngDCqwittLHY- 139
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 320 klvqcvdAFEEKANIVMVLEIVSGGELFERIIDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGt 399
Cdd:cd05624   140 -------AFQDENYLYLVMDYYVGGDLLTLLSKFEDKLPEDMARFYIGEMVLAIHSIHQLHYVHRDIKPDNVL-LDMNG- 210
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 400 RIKLIDFGLARRLENAGSLK--VLFGTPEFVAPEVIN--------YEPigyATDMWSIGVICYILVSGLSPFMGDNDNET 469
Cdd:cd05624   211 HIRLADFGSCLKMNDDGTVQssVAVGTPDYISPEILQamedgmgkYGP---ECDWWSLGVCMYEMLYGETPFYAESLVET 287
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1034633499 470 LANVTSATWDFD-DEAFDEISDDAKDFISNLL 500
Cdd:cd05624   288 YGKIMNHEERFQfPSHVTDVSEEAKDLIQRLI 319
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
261-516 9.66e-21

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: 92.82  E-value: 9.66e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 261 SDFYDIEeRLGSGKFGQVFRLVEKKTRKVWAGKFFKAYSA-KEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLE 339
Cdd:cd14046     6 TDFEELQ-VLGKGAFGQVVKVRNKLDGRYYAIKKIKLRSEsKNNSRILREVMLLSRLNHQHVVRYYQAWIERANLYIQME 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 340 IVSGGELFERIIDEDFELTEReCIKYMRQISEGVEYIHKQGIVHLDLKPENIM--CVNKtgtrIKLIDFGLARRLENA-- 415
Cdd:cd14046    85 YCEKSTLRDLIDSGLFQDTDR-LWRLFRQILEGLAYIHSQGIIHRDLKPVNIFldSNGN----VKIGDFGLATSNKLNve 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 416 -----------------GSLKVLFGTPEFVAPEVINYEPIGY--ATDMWSIGVI----CYILVSGLSPFmgdndnETLAN 472
Cdd:cd14046   160 latqdinkstsaalgssGDLTGNVGTALYVAPEVQSGTKSTYneKVDMYSLGIIffemCYPFSTGMERV------QILTA 233
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1034633499 473 VTSATWDFDDEA-FDEISDDAKdFISNLLKKDMKNRLDCTQCLQH 516
Cdd:cd14046   234 LRSVSIEFPPDFdDNKHSKQAK-LIRWLLNHDPAKRPSAQELLKS 277
STKc_LIMK cd14154
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer ...
270-454 1.11e-20

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


Pssm-ID: 271056 [Multi-domain]  Cd Length: 272  Bit Score: 92.57  E-value: 1.11e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 270 LGSGKFGQVFRLVEKKTRKVWAGKFFKAYSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEIVSGGELFER 349
Cdd:cd14154     1 LGKGFFGQAIKVTHRETGEVMVMKELIRFDEEAQRNFLKEVKVMRSLDHPNVLKFIGVLYKDKKLNLITEYIPGGTLKDV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 350 IIDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENimCVNKTGTRIKLIDFGLAR-----RLENAGSLK----- 419
Cdd:cd14154    81 LKDMARPLPWAQRVRFAKDIASGMAYLHSMNIIHRDLNSHN--CLVREDKTVVVADFGLARliveeRLPSGNMSPsetlr 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1034633499 420 -----------VLFGTPEFVAPEVINYEPIGYATDMWSIG-VICYIL 454
Cdd:cd14154   159 hlkspdrkkryTVVGNPYWMAPEMLNGRSYDEKVDIFSFGiVLCEII 205
STKc_WNK3 cd14031
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze ...
264-523 1.54e-20

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


Pssm-ID: 270933 [Multi-domain]  Cd Length: 275  Bit Score: 92.09  E-value: 1.54e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 264 YDIEerLGSGKFGQVFRLVEKKT--RKVWAGKFFKAYSAKEKENIRQEISIMNCLHHPKLVQCVDAFEE----KANIVMV 337
Cdd:cd14031    14 FDIE--LGRGAFKTVYKGLDTETwvEVAWCELQDRKLTKAEQQRFKEEAEMLKGLQHPNIVRFYDSWESvlkgKKCIVLV 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 338 LEIVSGGELfeRIIDEDFELTERECIK-YMRQISEGVEYIHKQG--IVHLDLKPENIMCVNKTGTrIKLIDFGLARRLEN 414
Cdd:cd14031    92 TELMTSGTL--KTYLKRFKVMKPKVLRsWCRQILKGLQFLHTRTppIIHRDLKCDNIFITGPTGS-VKIGDLGLATLMRT 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 415 AGSlKVLFGTPEFVAPEVINyEPIGYATDMWSIGVICYILVSGLSPFMG-DNDNETLANVTSAtwdFDDEAFDEISD-DA 492
Cdd:cd14031   169 SFA-KSVIGTPEFMAPEMYE-EHYDESVDVYAFGMCMLEMATSEYPYSEcQNAAQIYRKVTSG---IKPASFNKVTDpEV 243
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1034633499 493 KDFISNLLKKDMKNRLDCTQCLQHPWLMKDT 523
Cdd:cd14031   244 KEIIEGCIRQNKSERLSIKDLLNHAFFAEDT 274
PTKc_FAK cd05056
Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the ...
268-468 1.59e-20

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: 92.10  E-value: 1.59e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 268 ERLGSGKFGQVFRLV--EKKTRKV-WAGKFFKAYSAKE-KENIRQEISIMNCLHHPKLVQCVDAFEEKAnIVMVLEIVSG 343
Cdd:cd05056    12 RCIGEGQFGDVYQGVymSPENEKIaVAVKTCKNCTSPSvREKFLQEAYIMRQFDHPHIVKLIGVITENP-VWIVMELAPL 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 344 GELFERIIDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKTGtrIKLIDFGLARRLENAGSLKVLFG 423
Cdd:cd05056    91 GELRSYLQVNKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSPDC--VKLGDFGLSRYMEDESYYKASKG 168
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1034633499 424 T-P-EFVAPEVINYEPIGYATDMWSIGVICY-ILVSGLSPFMGDNDNE 468
Cdd:cd05056   169 KlPiKWMAPESINFRRFTSASDVWMFGVCMWeILMLGVKPFQGVKNND 216
STKc_NDR2 cd05627
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 2; STKs catalyze ...
270-508 1.67e-20

Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NDR2 (also called STK38-like) plays a role in proper centrosome duplication. In addition, it is involved in regulating neuronal growth and differentiation, as well as in facilitating neurite outgrowth. NDR2 is also implicated in fear conditioning as it contributes to the coupling of neuronal morphological changes with fear-memory consolidation. NDR kinase contains an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Like many other AGC kinases, NDR kinase requires phosphorylation at two sites, the activation loop (A-loop) and the hydrophobic motif (HM), for activity. The NDR2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270776 [Multi-domain]  Cd Length: 366  Bit Score: 93.97  E-value: 1.67e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 270 LGSGKFGQVfRLVEKK-TRKVWAGKFFKAYSAKEKE---NIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEIVSGGE 345
Cdd:cd05627    10 IGRGAFGEV-RLVQKKdTGHIYAMKILRKADMLEKEqvaHIRAERDILVEADGAWVVKMFYSFQDKRNLYLIMEFLPGGD 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 346 LFERIIDEDfELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKtgTRIKLIDFGLARRLENAGSLKVL---- 421
Cdd:cd05627    89 MMTLLMKKD-TLSEEATQFYIAETVLAIDAIHQLGFIHRDIKPDNLLLDAK--GHVKLSDFGLCTGLKKAHRTEFYrnlt 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 422 --------------------------------FGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNET 469
Cdd:cd05627   166 hnppsdfsfqnmnskrkaetwkknrrqlaystVGTPDYIAPEVFMQTGYNKLCDWWSLGVIMYEMLIGYPPFCSETPQET 245
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1034633499 470 LANVTS--ATWDFDDEAfdEISDDAKDFISNLLkKDMKNRL 508
Cdd:cd05627   246 YRKVMNwkETLVFPPEV--PISEKAKDLILRFC-TDAENRI 283
STKc_ERK5 cd07855
Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; ...
259-521 1.70e-20

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: 93.20  E-value: 1.70e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 259 KVSDFYDIEERLGSGKFGQVFRLVEKKTRKVWAGKffKAYSAKE-----KENIRqEISIMNCLHHPKLVQCVDAFEEKA- 332
Cdd:cd07855     2 DVGDRYEPIETIGSGAYGVVCSAIDTKSGQKVAIK--KIPNAFDvvttaKRTLR-ELKILRHFKHDNIIAIRDILRPKVp 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 333 -----NIVMVLEIVSGGelFERIIDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGTrIKLIDFG 407
Cdd:cd07855    79 yadfkDVYVVLDLMESD--LHHIIHSDQPLTLEHIRYFLYQLLRGLKYIHSANVIHRDLKPSNLL-VNENCE-LKIGDFG 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 408 LARRLENAGSLKVLFGTpEFV------APEVINYEPiGY--ATDMWSIGVI-------------------CYILVSGLSP 460
Cdd:cd07855   155 MARGLCTSPEEHKYFMT-EYVatrwyrAPELMLSLP-EYtqAIDMWSVGCIfaemlgrrqlfpgknyvhqLQLILTVLGT 232
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034633499 461 FMGDNDNET-----------LANVTSATWdfdDEAFDEISDDAKDFISNLLKKDMKNRLDCTQCLQHPWLMK 521
Cdd:cd07855   233 PSQAVINAIgadrvrryiqnLPNKQPVPW---ETLYPKADQQALDLLSQMLRFDPSERITVAEALQHPFLAK 301
PTZ00426 PTZ00426
cAMP-dependent protein kinase catalytic subunit; Provisional
257-519 1.75e-20

cAMP-dependent protein kinase catalytic subunit; Provisional


Pssm-ID: 173616 [Multi-domain]  Cd Length: 340  Bit Score: 93.51  E-value: 1.75e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 257 EQKVSDFYDIEErLGSGKFGQVF--RLVEKKTRKVWAGKFFKAYSAKEKE--NIRQEISIMNCLHHPKLVQCVDAFEEKA 332
Cdd:PTZ00426   26 KMKYEDFNFIRT-LGTGSFGRVIlaTYKNEDFPPVAIKRFEKSKIIKQKQvdHVFSERKILNYINHPFCVNLYGSFKDES 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 333 NIVMVLEIVSGGELFERIIDEDFELTERECIkYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGTrIKLIDFGLARRL 412
Cdd:PTZ00426  105 YLYLVLEFVIGGEFFTFLRRNKRFPNDVGCF-YAAQIVLIFEYLQSLNIVYRDLKPENLL-LDKDGF-IKMTDFGFAKVV 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 413 ENagSLKVLFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDFDdeafDEISDDA 492
Cdd:PTZ00426  182 DT--RTYTLCGTPEYIAPEILLNVGHGKAADWWTLGIFIYEILVGCPPFYANEPLLIYQKILEGIIYFP----KFLDNNC 255
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1034633499 493 KDFISNLLKKDMKNRL-----DCTQCLQHPWL 519
Cdd:PTZ00426  256 KHLMKKLLSHDLTKRYgnlkkGAQNVKEHPWF 287
PTKc_Lyn cd05072
Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the ...
268-473 2.85e-20

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: 91.26  E-value: 2.85e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 268 ERLGSGKFGQVFRLVEKKTRKVwAGKFFKAySAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEIVSGGELF 347
Cdd:cd05072    13 KKLGAGQFGEVWMGYYNNSTKV-AVKTLKP-GTMSVQAFLEEANLMKTLQHDKLVRLYAVVTKEEPIYIITEYMAKGSLL 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 348 ERI-IDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENI------MCvnktgtriKLIDFGLARRLE-NAGSLK 419
Cdd:cd05072    91 DFLkSDEGGKVLLPKLIDFSAQIAEGMAYIERKNYIHRDLRAANVlvseslMC--------KIADFGLARVIEdNEYTAR 162
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1034633499 420 VLFGTP-EFVAPEVINYEPIGYATDMWSIGVICY-ILVSGLSPFMGDNDNETLANV 473
Cdd:cd05072   163 EGAKFPiKWTAPEAINFGSFTIKSDVWSFGILLYeIVTYGKIPYPGMSNSDVMSAL 218
PTKc_Lck_Blk cd05067
Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs ...
266-473 3.33e-20

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: 91.10  E-value: 3.33e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 266 IEERLGSGKFGQVFRLVEKKTRKVwAGKFFKAYSAkEKENIRQEISIMNCLHHPKLVQcVDAFEEKANIVMVLEIVSGGE 345
Cdd:cd05067    11 LVERLGAGQFGEVWMGYYNGHTKV-AIKSLKQGSM-SPDAFLAEANLMKQLQHQRLVR-LYAVVTQEPIYIITEYMENGS 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 346 LFERI-IDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGTrIKLIDFGLARRLE-NAGSLKVLFG 423
Cdd:cd05067    88 LVDFLkTPSGIKLTINKLLDMAAQIAEGMAFIEERNYIHRDLRAANIL-VSDTLS-CKIADFGLARLIEdNEYTAREGAK 165
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1034633499 424 TP-EFVAPEVINYEPIGYATDMWSIGVICYILVS-GLSPFMGDNDNETLANV 473
Cdd:cd05067   166 FPiKWTAPEAINYGTFTIKSDVWSFGILLTEIVThGRIPYPGMTNPEVIQNL 217
STKc_aPKC_zeta cd05617
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze ...
264-510 6.84e-20

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: 92.01  E-value: 6.84e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 264 YDIEERLGSGKFGQVFRLVEKKTRKVWAGKFFKAYSAKEKENI----RQEISIMNCLHHPKLVQCVDAFEEKANIVMVLE 339
Cdd:cd05617    17 FDLIRVIGRGSYAKVLLVRLKKNDQIYAMKVVKKELVHDDEDIdwvqTEKHVFEQASSNPFLVGLHSCFQTTSRLFLVIE 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 340 IVSGGELFERIiDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGtRIKLIDFGLARRLENAGSLK 419
Cdd:cd05617    97 YVNGGDLMFHM-QRQRKLPEEHARFYAAEICIALNFLHERGIIYRDLKLDNVL-LDADG-HIKLTDYGMCKEGLGPGDTT 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 420 VLF-GTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLanvtsATWDFDDEAFDE--------ISD 490
Cdd:cd05617   174 STFcGTPNYIAPEILRGEEYGFSVDWWALGVLMFEMMAGRSPFDIITDNPDM-----NTEDYLFQVILEkpiriprfLSV 248
                         250       260
                  ....*....|....*....|
gi 1034633499 491 DAKDFISNLLKKDMKNRLDC 510
Cdd:cd05617   249 KASHVLKGFLNKDPKERLGC 268
STKc_myosinIIIB_N cd06639
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze ...
261-519 6.85e-20

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: 90.82  E-value: 6.85e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 261 SDFYDIEERLGSGKFGQVFRLVEKKTRKVWAGKFFKAYSAKEKEnIRQEISIMNCL-HHPKLVQCVDAFEEKANIV---- 335
Cdd:cd06639    21 SDTWDIIETIGKGTYGKVYKVTNKKDGSLAAVKILDPISDVDEE-IEAEYNILRSLpNHPNVVKFYGMFYKADQYVggql 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 336 -MVLEIVSGG---ELFERIIDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKTGtrIKLIDFGLARR 411
Cdd:cd06639   100 wLVLELCNGGsvtELVKGLLKCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGG--VKLVDFGVSAQ 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 412 LENAGSLK-VLFGTPEFVAPEVINYE-PIGYA----TDMWSIGVICYILVSGLSPFMGDNDNETLANV---TSATWDFDD 482
Cdd:cd06639   178 LTSARLRRnTSVGTPFWMAPEVIACEqQYDYSydarCDVWSLGITAIELADGDPPLFDMHPVKALFKIprnPPPTLLNPE 257
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1034633499 483 EAFDEISddakDFISNLLKKDMKNRLDCTQCLQHPWL 519
Cdd:cd06639   258 KWCRGFS----HFISQCLIKDFEKRPSVTHLLEHPFI 290
PKc_MKK7 cd06618
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
251-519 7.90e-20

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: 90.51  E-value: 7.90e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 251 TVTINTEQKVSDFYDIE--ERLGSGKFGQVFRLVEKKTRKVWAGK-FFKAYSAKEKENIRQEISIMnCLHH--PKLVQCV 325
Cdd:cd06618     2 YLTIDGKKYKADLNDLEnlGEIGSGTCGQVYKMRHKKTGHVMAVKqMRRSGNKEENKRILMDLDVV-LKSHdcPYIVKCY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 326 DAFEEKANIVMVLEIVS----------GGELFERIIDedfeltereciKYMRQISEGVEYI-HKQGIVHLDLKPENIMcV 394
Cdd:cd06618    81 GYFITDSDVFICMELMStcldkllkriQGPIPEDILG-----------KMTVSIVKALHYLkEKHGVIHRDVKPSNIL-L 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 395 NKTGTrIKLIDFGLARRLENAGSLKVLFGTPEFVAPEVINYEPIG-Y--ATDMWSIGVICYILVSGLSPFMG-DNDNETL 470
Cdd:cd06618   149 DESGN-VKLCDFGISGRLVDSKAKTRSAGCAAYMAPERIDPPDNPkYdiRADVWSLGISLVELATGQFPYRNcKTEFEVL 227
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1034633499 471 ANVTSatwdfDD-------EAFdeiSDDAKDFISNLLKKDMKNRLDCTQCLQHPWL 519
Cdd:cd06618   228 TKILN-----EEppslppnEGF---SPDFCSFVDLCLTKDHRYRPKYRELLQHPFI 275
STKc_MLK cd14061
Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the ...
270-463 7.99e-20

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: 89.76  E-value: 7.99e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 270 LGSGKFGQVFRlvekktrKVWAGKFFKAYSAKEK---------ENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEI 340
Cdd:cd14061     2 IGVGGFGKVYR-------GIWRGEEVAVKAARQDpdedisvtlENVRQEARLFWMLRHPNIIALRGVCLQPPNLCLVMEY 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 341 VSGGELfERIIDEDfELTERECIKYMRQISEGVEYIHKQG---IVHLDLKPENIMCVNKTGTR------IKLIDFGLARR 411
Cdd:cd14061    75 ARGGAL-NRVLAGR-KIPPHVLVDWAIQIARGMNYLHNEApvpIIHRDLKSSNILILEAIENEdlenktLKITDFGLARE 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1034633499 412 LENAGSLKVLfGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMG 463
Cdd:cd14061   153 WHKTTRMSAA-GTYAWMAPEVIKSSTFSKASDVWSYGVLLWELLTGEVPYKG 203
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
131-223 9.32e-20

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 84.47  E-value: 9.32e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 131 PDPPaGTPCASDIRSSSLTLSWyGSSYDGGSAVQSYSIEIWDSANKTWKELAT--CRSTSFNVQDLLPDHEYKFRVRAIN 208
Cdd:cd00063     1 PSPP-TNLRVTDVTSTSVTLSW-TPPEDDGGPITGYVVEYREKGSGDWKEVEVtpGSETSYTLTGLKPGTEYEFRVRAVN 78
                          90
                  ....*....|....*
gi 1034633499 209 VYGTSEPSQESELTT 223
Cdd:cd00063    79 GGGESPPSESVTVTT 93
STKc_MPK1 cd07857
Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; ...
308-519 9.57e-20

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: 90.93  E-value: 9.57e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 308 QEISIMNCLHHPKLVQcvdAFEEKANIVMV--LEIVSGG---------ELFE----RIIDEDFELTERECIKYMRQISEG 372
Cdd:cd07857    41 KKILAKRALRELKLLR---HFRGHKNITCLydMDIVFPGnfnelylyeELMEadlhQIIRSGQPLTDAHFQSFIYQILCG 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 373 VEYIHKQGIVHLDLKPENIMCvnKTGTRIKLIDFGLAR-----RLENAGSLKVLFGTPEFVAPEV-INYEPIGYATDMWS 446
Cdd:cd07857   118 LKYIHSANVLHRDLKPGNLLV--NADCELKICDFGLARgfsenPGENAGFMTEYVATRWYRAPEImLSFQSYTKAIDVWS 195
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 447 IGVICYILVSGLSPFMGDN---------------DNETLANVTSA-TWDFD-----------DEAFDEISDDAKDFISNL 499
Cdd:cd07857   196 VGCILAELLGRKPVFKGKDyvdqlnqilqvlgtpDEETLSRIGSPkAQNYIrslpnipkkpfESIFPNANPLALDLLEKL 275
                         250       260
                  ....*....|....*....|
gi 1034633499 500 LKKDMKNRLDCTQCLQHPWL 519
Cdd:cd07857   276 LAFDPTKRISVEEALEHPYL 295
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
316-465 1.33e-19

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 92.94  E-value: 1.33e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 316 LHHPKLVQCVDAFEEKAN--IVMvlEIVSGGELfERIIDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMc 393
Cdd:NF033483   64 LSHPNIVSVYDVGEDGGIpyIVM--EYVDGRTL-KDYIREHGPLSPEEAVEIMIQILSALEHAHRNGIVHRDIKPQNIL- 139
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034633499 394 VNKTGtRIKLIDFGLARRLENAgSL----KVLfGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDN 465
Cdd:NF033483  140 ITKDG-RVKVTDFGIARALSST-TMtqtnSVL-GTVHYLSPEQARGGTVDARSDIYSLGIVLYEMLTGRPPFDGDS 212
STKc_CDK12 cd07864
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs ...
262-519 1.48e-19

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: 89.86  E-value: 1.48e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 262 DFYDIEERLGSGKFGQVFRLVEKKTRKVWAGKffKAYSAKEKEN-----IRqEISIMNCLHHPKLVQ----------CVD 326
Cdd:cd07864     7 DKFDIIGIIGEGTYGQVYKAKDKDTGELVALK--KVRLDNEKEGfpitaIR-EIKILRQLNHRSVVNlkeivtdkqdALD 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 327 AFEEKANIVMVLEIVSG---GELFERIIDedfeLTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKtgTRIKL 403
Cdd:cd07864    84 FKKDKGAFYLVFEYMDHdlmGLLESGLVH----FSEDHIKSFMKQLLEGLNYCHKKNFLHRDIKCSNILLNNK--GQIKL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 404 IDFGLAR-------RLENAGSLKVLFGTPEFVAPEvinyEPIGYATDMWSIGVICYILVSGLSPFMGDNDN---ETLANV 473
Cdd:cd07864   158 ADFGLARlynseesRPYTNKVITLWYRPPELLLGE----ERYGPAIDVWSCGCILGELFTKKPIFQANQELaqlELISRL 233
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034633499 474 ----TSATWD-------FDD------------EAFDEISDDAKDFISNLLKKDMKNRLDCTQCLQHPWL 519
Cdd:cd07864   234 cgspCPAVWPdviklpyFNTmkpkkqyrrrlrEEFSFIPTPALDLLDHMLTLDPSKRCTAEQALNSPWL 302
STKc_WNK4 cd14033
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze ...
264-516 2.37e-19

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


Pssm-ID: 270935 [Multi-domain]  Cd Length: 261  Bit Score: 88.52  E-value: 2.37e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 264 YDIEerLGSGKFGQVFRLVEKKT--RKVWAGKFFKAYSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKAN----IVMV 337
Cdd:cd14033     5 FNIE--IGRGSFKTVYRGLDTETtvEVAWCELQTRKLSKGERQRFSEEVEMLKGLQHPNIVRFYDSWKSTVRghkcIILV 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 338 LEIVSGGEL---FERIIDEDFELTERecikYMRQISEGVEYIHKQG--IVHLDLKPENIMCVNKTGTrIKLIDFGLARrL 412
Cdd:cd14033    83 TELMTSGTLktyLKRFREMKLKLLQR----WSRQILKGLHFLHSRCppILHRDLKCDNIFITGPTGS-VKIGDLGLAT-L 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 413 ENAGSLKVLFGTPEFVAPEVINyEPIGYATDMWSIGVICYILVSGLSPFMG-DNDNETLANVTSAtwdFDDEAFDEIS-D 490
Cdd:cd14033   157 KRASFAKSVIGTPEFMAPEMYE-EKYDEAVDVYAFGMCILEMATSEYPYSEcQNAAQIYRKVTSG---IKPDSFYKVKvP 232
                         250       260
                  ....*....|....*....|....*.
gi 1034633499 491 DAKDFISNLLKKDMKNRLDCTQCLQH 516
Cdd:cd14033   233 ELKEIIEGCIRTDKDERFTIQDLLEH 258
STKc_TAO cd06607
Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs ...
263-521 3.06e-19

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: 87.89  E-value: 3.06e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 263 FYDIEErLGSGKFGQVFRLVEKKTRKVWAGKFFkAYSAK---EK-ENIRQEISIMNCLHHPKLVQCVDAF--EEKANIVM 336
Cdd:cd06607     3 FEDLRE-IGHGSFGAVYYARNKRTSEVVAIKKM-SYSGKqstEKwQDIIKEVKFLRQLRHPNTIEYKGCYlrEHTAWLVM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 337 VLEIVSGGELFERIIDEdfeLTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGTrIKLIDFGLARRLENAG 416
Cdd:cd06607    81 EYCLGSASDIVEVHKKP---LQEVEIAAICHGALQGLAYLHSHNRIHRDVKAGNIL-LTEPGT-VKLADFGSASLVCPAN 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 417 SLkvlFGTPEFVAPEVI------NYEpiGYAtDMWSIGVICYILVSGLSPF-----------MGDNDNETLAnvtSATWd 479
Cdd:cd06607   156 SF---VGTPYWMAPEVIlamdegQYD--GKV-DVWSLGITCIELAERKPPLfnmnamsalyhIAQNDSPTLS---SGEW- 225
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1034633499 480 fddeafdeiSDDAKDFISNLLKKDMKNRLDCTQCLQHPWLMK 521
Cdd:cd06607   226 ---------SDDFRNFVDSCLQKIPQDRPSAEDLLKHPFVTR 258
STKc_CDK2_3 cd07860
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; ...
268-518 3.13e-19

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: 88.72  E-value: 3.13e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 268 ERLGSGKFGQVFRLVEKKTRKVWAGKFFKAYSAKE---KENIRqEISIMNCLHHPKLVQCVDAFEEKANIVMVLEIVSgg 344
Cdd:cd07860     6 EKIGEGTYGVVYKARNKLTGEVVALKKIRLDTETEgvpSTAIR-EISLLKELNHPNIVKLLDVIHTENKLYLVFEFLH-- 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 345 ELFERIID--EDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGtRIKLIDFGLARrlenAGSLKVLF 422
Cdd:cd07860    83 QDLKKFMDasALTGIPLPLIKSYLFQLLQGLAFCHSHRVLHRDLKPQNLL-INTEG-AIKLADFGLAR----AFGVPVRT 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 423 GTPEFV-----APEVInyepIG---YAT--DMWSIGVICYILVSGLSPFMGDNDNE-------TLANVTSATW------- 478
Cdd:cd07860   157 YTHEVVtlwyrAPEIL----LGckyYSTavDIWSLGCIFAEMVTRRALFPGDSEIDqlfrifrTLGTPDEVVWpgvtsmp 232
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1034633499 479 DFDD-------EAFDEI----SDDAKDFISNLLKKDMKNRLDCTQCLQHPW 518
Cdd:cd07860   233 DYKPsfpkwarQDFSKVvpplDEDGRDLLSQMLHYDPNKRISAKAALAHPF 283
PTKc_Syk cd05116
Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; PTKs catalyze the ...
270-471 3.46e-19

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: 87.71  E-value: 3.46e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 270 LGSGKFGQVFR--LVEKKTRKVWAGKFFKAYSAKE--KENIRQEISIMNCLHHPKLVQCVDAFEEKaNIVMVLEIVSGGE 345
Cdd:cd05116     3 LGSGNFGTVKKgyYQMKKVVKTVAVKILKNEANDPalKDELLREANVMQQLDNPYIVRMIGICEAE-SWMLVMEMAELGP 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 346 LfERIIDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVnkTGTRIKLIDFGLARRL---ENAGSLKVLF 422
Cdd:cd05116    82 L-NKFLQKNRHVTEKNITELVHQVSMGMKYLEESNFVHRDLAARNVLLV--TQHYAKISDFGLSKALradENYYKAQTHG 158
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1034633499 423 GTP-EFVAPEVINYEPIGYATDMWSIGVICYILVS-GLSPFMGDNDNETLA 471
Cdd:cd05116   159 KWPvKWYAPECMNYYKFSSKSDVWSFGVLMWEAFSyGQKPYKGMKGNEVTQ 209
STKc_myosinIIIA_N cd06638
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze ...
250-519 3.70e-19

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: 88.53  E-value: 3.70e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 250 RTVTINTEQKVSDFYDIEERLGSGKFGQVFRLVEKKTRKVWAGKFFKAYSAKEKEnIRQEISIMNCLH-HPKLVQCVDAF 328
Cdd:cd06638     6 KTIIFDSFPDPSDTWEIIETIGKGTYGKVFKVLNKKNGSKAAVKILDPIHDIDEE-IEAEYNILKALSdHPNVVKFYGMY 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 329 EEKA-----NIVMVLEIVSGG---ELFERIIDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKTGtr 400
Cdd:cd06638    85 YKKDvkngdQLWLVLELCNGGsvtDLVKGFLKRGERMEEPIIAYILHEALMGLQHLHVNKTIHRDVKGNNILLTTEGG-- 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 401 IKLIDFGLARRLENAGSLK-VLFGTPEFVAPEVINYEPIGYAT-----DMWSIGVICYILVSGLSPFMGDNDNETLANV- 473
Cdd:cd06638   163 VKLVDFGVSAQLTSTRLRRnTSVGTPFWMAPEVIACEQQLDSTydarcDVWSLGITAIELGDGDPPLADLHPMRALFKIp 242
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1034633499 474 --------TSATWdfddeafdeiSDDAKDFISNLLKKDMKNRLDCTQCLQHPWL 519
Cdd:cd06638   243 rnppptlhQPELW----------SNEFNDFIRKCLTKDYEKRPTVSDLLQHVFI 286
STKc_LRRK cd14000
Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the ...
270-463 3.72e-19

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: 88.05  E-value: 3.72e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 270 LGSGKFGQVFR-------LVEKKTRKVWAGKFFK------------AYSAKEKENIRQEISIMNCLHHPKLVQCVDAFEE 330
Cdd:cd14000     2 LGDGGFGSVYRasykgepVAVKIFNKHTSSNFANvpadtmlrhlraTDAMKNFRLLRQELTVLSHLHHPSIVYLLGIGIH 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 331 KanIVMVLEIVSGGELfERIIDED----FELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVN---KTGTRIKL 403
Cdd:cd14000    82 P--LMLVLELAPLGSL-DHLLQQDsrsfASLGRTLQQRIALQVADGLRYLHSAMIIYRDLKSHNVLVWTlypNSAIIIKI 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034633499 404 IDFGLARRLENAGSLKVLfGTPEFVAPEVINYEPI-GYATDMWSIGVICYILVSGLSPFMG 463
Cdd:cd14000   159 ADYGISRQCCRMGAKGSE-GTPGFRAPEIARGNVIyNEKVDVFSFGMLLYEILSGGAPMVG 218
STKc_MASTL cd05610
Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like ...
273-517 3.76e-19

Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like kinase (also called greatwall kinase); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The MASTL kinases in this group carry only a catalytic domain, which contains a long insertion relative to MAST kinases. MASTL, also called greatwall kinase (Gwl), is involved in the regulation of mitotic entry, which is controlled by the coordinated activities of protein kinases and opposing protein phosphatases (PPs). The cyclin B/CDK1 complex induces entry into M-phase while PP2A-B55 shows anti-mitotic activity. MASTL/Gwl is activated downstream of cyclin B/CDK1 and indirectly inhibits PP2A-B55 by phosphorylating the small protein alpha-endosulfine (Ensa) or the cAMP-regulated phosphoprotein 19 (Arpp19), resulting in M-phase progression. Gwl kinase may also play roles in mRNA stabilization and DNA checkpoint recovery. The human MASTL gene has also been named FLJ14813; a missense mutation in FLJ14813 is associated with autosomal dominant thrombocytopenia. The MASTL kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270761 [Multi-domain]  Cd Length: 349  Bit Score: 89.55  E-value: 3.76e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 273 GKFGQVFRLVEKKTRKVWAGKFFKAYSAKEKENIRQEISIMNCLHHPKLVQCVDAF---EEKANIVMVLEIVSGGELFER 349
Cdd:cd05610    15 GAFGKVYLGRKKNNSKLYAVKVVKKADMINKNMVHQVQAERDALALSKSPFIVHLYyslQSANNVYLVMEYLIGGDVKSL 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 350 I-----IDEDFELtereciKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKtgTRIKLIDFGLA-----RRLE------ 413
Cdd:cd05610    95 LhiygyFDEEMAV------KYISEVALALDYLHRHGIIHRDLKPDNMLISNE--GHIKLTDFGLSkvtlnRELNmmdilt 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 414 ---------------------------------------NAGSLKV----LFGTPEFVAPEVINYEPIGYATDMWSIGVI 450
Cdd:cd05610   167 tpsmakpkndysrtpgqvlslisslgfntptpyrtpksvRRGAARVegerILGTPDYLAPELLLGKPHGPAVDWWALGVC 246
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034633499 451 CYILVSGLSPFMGDNDNETLANVTSAT--WDFDDEafdEISDDAKDFISNLLKKDMKNRLDCTQCLQHP 517
Cdd:cd05610   247 LFEFLTGIPPFNDETPQQVFQNILNRDipWPEGEE---ELSVNAQNAIEILLTMDPTKRAGLKELKQHP 312
STKc_PAK4 cd06657
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the ...
269-521 3.83e-19

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: 88.54  E-value: 3.83e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 269 RLGSGKFGQVFRLVEKKTRKVWAGKFFKAYSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEIVSGGELFE 348
Cdd:cd06657    27 KIGEGSTGIVCIATVKSSGKLVAVKKMDLRKQQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGALTD 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 349 riIDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKTgtRIKLIDFGLARRL-ENAGSLKVLFGTPEF 427
Cdd:cd06657   107 --IVTHTRMNEEQIAAVCLAVLKALSVLHAQGVIHRDIKSDSILLTHDG--RVKLSDFGFCAQVsKEVPRRKSLVGTPYW 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 428 VAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSaTWDFDDEAFDEISDDAKDFISNLLKKDMKNR 507
Cdd:cd06657   183 MAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIRD-NLPPKLKNLHKVSPSLKGFLDRLLVRDPAQR 261
                         250
                  ....*....|....
gi 1034633499 508 LDCTQCLQHPWLMK 521
Cdd:cd06657   262 ATAAELLKHPFLAK 275
STKc_TLK2 cd14041
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the ...
260-520 4.05e-19

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


Pssm-ID: 270943 [Multi-domain]  Cd Length: 309  Bit Score: 88.96  E-value: 4.05e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 260 VSDFYDIEERLGSGKFGQVFR---LVEKKTRKVWAGKFFKAYSAKEKENIRQ----EISIMNCLHHPKLVQCVDAFE-EK 331
Cdd:cd14041     4 LNDRYLLLHLLGRGGFSEVYKafdLTEQRYVAVKIHQLNKNWRDEKKENYHKhacrEYRIHKELDHPRIVKLYDYFSlDT 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 332 ANIVMVLEIVSGGELfERIIDEDFELTERECIKYMRQISEGVEYIH--KQGIVHLDLKPENIMCVNKTGT-RIKLIDFGL 408
Cdd:cd14041    84 DSFCTVLEYCEGNDL-DFYLKQHKLMSEKEARSIIMQIVNALKYLNeiKPPIIHYDLKPGNILLVNGTACgEIKITDFGL 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 409 ARRL--ENAGSLKVL------FGTPEFVAPE--VINYEP--IGYATDMWSIGVICYILVSGLSPFMGDNDNETL--ANVT 474
Cdd:cd14041   163 SKIMddDSYNSVDGMeltsqgAGTYWYLPPEcfVVGKEPpkISNKVDVWSVGVIFYQCLYGRKPFGHNQSQQDIlqENTI 242
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1034633499 475 SATWDFDDEAFDEISDDAKDFISNLLKKDMKNRLDCTQCLQHPWLM 520
Cdd:cd14041   243 LKATEVQFPPKPVVTPEAKAFIRRCLAYRKEDRIDVQQLACDPYLL 288
STKc_MAP4K3 cd06645
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
264-521 5.14e-19

Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase kinase kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAP4K3 plays a role in the nutrient-responsive pathway of mTOR (mammalian target of rapamycin) signaling. MAP4K3 is required in the activation of S6 kinase by amino acids and for the phosphorylation of the mTOR-regulated inhibitor of eukaryotic initiation factor 4E. mTOR regulates ribosome biogenesis and protein translation, and is frequently deregulated in cancer. MAP4Ks are involved in MAPK signaling pathways by activating a MAPK kinase kinase. Each MAPK cascade is activated either by a small GTP-binding protein or by an adaptor protein, which transmits the signal either directly to a MAP3K to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. Members of this subfamily contain an N-terminal catalytic domain and a C-terminal citron homology (CNH) regulatory domain. The MAP4K3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270812 [Multi-domain]  Cd Length: 272  Bit Score: 87.79  E-value: 5.14e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 264 YDIEERLGSGKFGQVFRLVEKKTRKVWAGKFFKAYSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEIVSG 343
Cdd:cd06645    13 FELIQRIGSGTYGDVYKARNVNTGELAAIKVIKLEPGEDFAVVQQEIIMMKDCKHSNIVAYFGSYLRRDKLWICMEFCGG 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 344 GELfERIIDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKtgTRIKLIDFGLARRLE-NAGSLKVLF 422
Cdd:cd06645    93 GSL-QDIYHVTGPLSESQIAYVSRETLQGLYYLHSKGKMHRDIKGANILLTDN--GHVKLADFGVSAQITaTIAKRKSFI 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 423 GTPEFVAPEVINYEPIG---YATDMWSIGvICYILVSGLSPFMGD-NDNETLANVTSATWD---FDDEAfdEISDDAKDF 495
Cdd:cd06645   170 GTPYWMAPEVAAVERKGgynQLCDIWAVG-ITAIELAELQPPMFDlHPMRALFLMTKSNFQppkLKDKM--KWSNSFHHF 246
                         250       260
                  ....*....|....*....|....*.
gi 1034633499 496 ISNLLKKDMKNRLDCTQCLQHPWLMK 521
Cdd:cd06645   247 VKMALTKNPKKRPTAEKLLQHPFVTQ 272
STKc_MRCK_alpha cd05623
Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 ...
264-500 7.52e-19

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


Pssm-ID: 270773 [Multi-domain]  Cd Length: 409  Bit Score: 89.69  E-value: 7.52e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 264 YDIEERLGSGKFGQVFRLVEKKTRKVWAGKFFKAYSA---KEKENIRQEISIM--------NCLHHpklvqcvdAFEEKA 332
Cdd:cd05623    74 FEILKVIGRGAFGEVAVVKLKNADKVFAMKILNKWEMlkrAETACFREERDVLvngdsqwiTTLHY--------AFQDDN 145
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 333 NIVMVLEIVSGGELFERIIDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGtRIKLIDFGLARRL 412
Cdd:cd05623   146 NLYLVMDYYVGGDLLTLLSKFEDRLPEDMARFYLAEMVLAIDSVHQLHYVHRDIKPDNIL-MDMNG-HIRLADFGSCLKL 223
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 413 ENAGSLK--VLFGTPEFVAPEVIN--------YEPigyATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDFD- 481
Cdd:cd05623   224 MEDGTVQssVAVGTPDYISPEILQamedgkgkYGP---ECDWWSLGVCMYEMLYGETPFYAESLVETYGKIMNHKERFQf 300
                         250
                  ....*....|....*....
gi 1034633499 482 DEAFDEISDDAKDFISNLL 500
Cdd:cd05623   301 PTQVTDVSENAKDLIRRLI 319
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
609-699 8.01e-19

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


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 81.86  E-value: 8.01e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 609 PYFSKTIRDLEVVEGSAARFDCKIEGYPDPEVVWFKDDQSIRESRHFQIdYDEDGNCSLIISDVCGDDDAKYTCKAVNSL 688
Cdd:cd20972     2 PQFIQKLRSQEVAEGSKVRLECRVTGNPTPVVRWFCEGKELQNSPDIQI-HQEGDLHSLIIAEAFEEDTGRYSCLATNSV 80
                          90
                  ....*....|.
gi 1034633499 689 GEATCTAELIV 699
Cdd:cd20972    81 GSDTTSAEIFV 91
STKc_CDK5 cd07839
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs ...
264-518 1.10e-18

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: 87.10  E-value: 1.10e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 264 YDIEERLGSGKFGQVFRLVEKKTRKVWAGKFFKAYSAKE--KENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEIV 341
Cdd:cd07839     2 YEKLEKIGEGTYGTVFKAKNRETHEIVALKRVRLDDDDEgvPSSALREICLLKELKHKNIVRLYDVLHSDKKLTLVFEYC 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 342 sggelferiiDEDF---------ELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGTrIKLIDFGLARRl 412
Cdd:cd07839    82 ----------DQDLkkyfdscngDIDPEIVKSFMFQLLKGLAFCHSHNVLHRDLKPQNLL-INKNGE-LKLADFGLARA- 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 413 enagslkvlFGTP------EFV-----APEVInYEPIGYAT--DMWSIGVICYILVSGLSPFMGDNDNE--------TLA 471
Cdd:cd07839   149 ---------FGIPvrcysaEVVtlwyrPPDVL-FGAKLYSTsiDMWSAGCIFAELANAGRPLFPGNDVDdqlkrifrLLG 218
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034633499 472 NVTSATW-------DFDD-----------EAFDEISDDAKDFISNLLKKDMKNRLDCTQCLQHPW 518
Cdd:cd07839   219 TPTEESWpgvsklpDYKPypmypattslvNVVPKLNSTGRDLLQNLLVCNPVQRISAEEALQHPY 283
PTKc_EphR_A2 cd05063
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the ...
256-476 1.34e-18

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: 86.18  E-value: 1.34e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 256 TEQKVsdfydieerLGSGKFGQVFRLVEK---KTRKVWAGKFFKA-YSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEK 331
Cdd:cd05063     8 TKQKV---------IGAGEFGEVFRGILKmpgRKEVAVAIKTLKPgYTEKQRQDFLSEASIMGQFSHHNIIRLEGVVTKF 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 332 ANIVMVLEIVSGGELFERIIDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTgTRIKLIDFGLARR 411
Cdd:cd05063    79 KPAMIITEYMENGALDKYLRDHDGEFSSYQLVGMLRGIAAGMKYLSDMNYVHRDLAARNIL-VNSN-LECKVSDFGLSRV 156
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034633499 412 LEN---------AGSLKVlfgtpEFVAPEVINYEPIGYATDMWSIGVICY-ILVSGLSPFMGDNDNETLANVTSA 476
Cdd:cd05063   157 LEDdpegtyttsGGKIPI-----RWTAPEAIAYRKFTSASDVWSFGIVMWeVMSFGERPYWDMSNHEVMKAINDG 226
STKc_CDK8_like cd07842
Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs ...
263-518 1.49e-18

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: 87.34  E-value: 1.49e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 263 FYDIEERLGSGKFGQVFRLVEKKTR--KVWAGKFFKAySAKEKENIRQ----EISIMNCLHHPKLVQCVDAFEEKAN--I 334
Cdd:cd07842     1 KYEIEGCIGRGTYGRVYKAKRKNGKdgKEYAIKKFKG-DKEQYTGISQsacrEIALLRELKHENVVSLVEVFLEHADksV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 335 VMVleivsggelferiidedFELTER---ECIKYMR-----------------QISEGVEYIHKQGIVHLDLKPENI--M 392
Cdd:cd07842    80 YLL-----------------FDYAEHdlwQIIKFHRqakrvsippsmvksllwQILNGIHYLHSNWVLHRDLKPANIlvM 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 393 CVNKTGTRIKLIDFGLARRLENAgsLKVLF-GTPEFV-----APEVI----NYEPigyATDMWSIGVICYILVSGLSPFM 462
Cdd:cd07842   143 GEGPERGVVKIGDLGLARLFNAP--LKPLAdLDPVVVtiwyrAPELLlgarHYTK---AIDIWAIGCIFAELLTLEPIFK 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 463 GDNDN----------------ETLANVTSATW-------------------DFDD-------EAFDEISDDAKDFISNLL 500
Cdd:cd07842   218 GREAKikksnpfqrdqlerifEVLGTPTEKDWpdikkmpeydtlksdtkasTYPNsllakwmHKHKKPDSQGFDLLRKLL 297
                         330
                  ....*....|....*...
gi 1034633499 501 KKDMKNRLDCTQCLQHPW 518
Cdd:cd07842   298 EYDPTKRITAEEALEHPY 315
STKc_SRPK cd14136
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase; STKs catalyze ...
264-519 1.51e-18

Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SRPKs phosphorylate and regulate splicing factors from the SR protein family by specifically phosphorylating multiple serine residues residing in SR/RS dipeptide motifs (also known as RS domains). Phosphorylation of the RS domains enhances interaction with transportin SR and facilitates entry of the SR proteins into the nucleus. SRPKs contain a nonconserved insert domain, within the well-conserved catalytic kinase domain, that regulates their subcellular localization. They play important roles in mediating pre-mRNA processing and mRNA maturation, as well as other cellular functions such as chromatin reorganization, cell cycle and p53 regulation, and metabolic signaling. Vertebrates contain three distinct SRPKs, called SRPK1-3. The SRPK homolog in budding yeast, Sky1p, recognizes and phosphorylates its substrate Npl3p, which lacks a classic RS domain but contains a single RS dipeptide at the C-terminus of its RGG domain. Npl3p is a shuttling heterogeneous nuclear ribonucleoprotein (hnRNP) that exports a distinct class of mRNA from the nucleus to the cytoplasm. The SRPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271038 [Multi-domain]  Cd Length: 320  Bit Score: 87.25  E-value: 1.51e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 264 YDIEERLGSGKFGQVFRLVEKKTRKVWAGKFFKaySAKE-KENIRQEISIMNCL-----HHP---KLVQCVDAFEEKAN- 333
Cdd:cd14136    12 YHVVRKLGWGHFSTVWLCWDLQNKRFVALKVVK--SAQHyTEAALDEIKLLKCVreadpKDPgreHVVQLLDDFKHTGPn 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 334 ---IVMVLEiVSGGELFERIIDEDFELTERECIK-YMRQISEGVEYIHKQ-GIVHLDLKPENI-MCVNKtgTRIKLIDFG 407
Cdd:cd14136    90 gthVCMVFE-VLGPNLLKLIKRYNYRGIPLPLVKkIARQVLQGLDYLHTKcGIIHTDIKPENVlLCISK--IEVKIADLG 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 408 larrleNAGSLKVLFG----TPEFVAPEVINYEPIGYATDMWSIGVICYILVSG---LSPFMGDN---DNETLA------ 471
Cdd:cd14136   167 ------NACWTDKHFTediqTRQYRSPEVILGAGYGTPADIWSTACMAFELATGdylFDPHSGEDysrDEDHLAliiell 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 472 ------------------------------------NVTSATWDFDDEAFDEISddakDFISNLLKKDMKNRLDCTQCLQ 515
Cdd:cd14136   241 griprsiilsgkysreffnrkgelrhisklkpwpleDVLVEKYKWSKEEAKEFA----SFLLPMLEYDPEKRATAAQCLQ 316

                  ....
gi 1034633499 516 HPWL 519
Cdd:cd14136   317 HPWL 320
PTKc_Fes_like cd05041
Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; ...
268-469 1.77e-18

Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; Fes subfamily; catalytic (c) domain. Fes subfamily members include Fes (or Fps), Fer, and similar proteins. The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K). PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Fes subfamily proteins are cytoplasmic (or nonreceptor) tyr kinases containing an N-terminal region with FCH (Fes/Fer/CIP4 homology) and coiled-coil domains, followed by a SH2 domain, and a C-terminal catalytic domain. The genes for Fes (feline sarcoma) and Fps (Fujinami poultry sarcoma) were first isolated from tumor-causing retroviruses. The viral oncogenes encode chimeric Fes proteins consisting of Gag sequences at the N-termini, resulting in unregulated tyr kinase activity. Fes and Fer kinases play roles in haematopoiesis, inflammation and immunity, growth factor signaling, cytoskeletal regulation, cell migration and adhesion, and the regulation of cell-cell interactions. Fes and Fer show redundancy in their biological functions.


Pssm-ID: 270637 [Multi-domain]  Cd Length: 251  Bit Score: 85.57  E-value: 1.77e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 268 ERLGSGKFGQVFRLVEKKTRKVWAGKFFKA-YSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEIVSGGEL 346
Cdd:cd05041     1 EKIGRGNFGDVYRGVLKPDNTEVAVKTCREtLPPDLKRKFLQEARILKQYDHPNIVKLIGVCVQKQPIMIVMELVPGGSL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 347 FERIIDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENimCVNKTGTRIKLIDFGLARRlENAGSLKVLFGTPE 426
Cdd:cd05041    81 LTFLRKKGARLTVKQLLQMCLDAAAGMEYLESKNCIHRDLAARN--CLVGENNVLKISDFGMSRE-EEDGEYTVSDGLKQ 157
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1034633499 427 ----FVAPEVINYEPIGYATDMWSIGVICY-ILVSGLSPFMGDNDNET 469
Cdd:cd05041   158 ipikWTAPEALNYGRYTSESDVWSFGILLWeIFSLGATPYPGMSNQQT 205
PTKc_EphR cd05033
Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
266-450 2.90e-18

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: 85.12  E-value: 2.90e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 266 IEERLGSGKFGQVF----RLVEKKTRKVwAGKFFKA-YSAKEKENIRQEISIMNCLHHPKLVQcVDAFEEKANIVM-VLE 339
Cdd:cd05033     8 IEKVIGGGEFGEVCsgslKLPGKKEIDV-AIKTLKSgYSDKQRLDFLTEASIMGQFDHPNVIR-LEGVVTKSRPVMiVTE 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 340 IVSGGEL--FERIIDEDFELTEreCIKYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTgTRIKLIDFGLARRLENAGS 417
Cdd:cd05033    86 YMENGSLdkFLRENDGKFTVTQ--LVGMLRGIASGMKYLSEMNYVHRDLAARNIL-VNSD-LVCKVSDFGLSRRLEDSEA 161
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1034633499 418 LKVLFG--TP-EFVAPEVINYEPIGYATDMWSIGVI 450
Cdd:cd05033   162 TYTTKGgkIPiRWTAPEAIAYRKFTSASDVWSFGIV 197
PTKc_Fes cd05084
Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the ...
268-469 2.92e-18

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: 84.98  E-value: 2.92e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 268 ERLGSGKFGQVF--RLVEKKTrKVWAGKFFKAYSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEIVSGGE 345
Cdd:cd05084     2 ERIGRGNFGEVFsgRLRADNT-PVAVKSCRETLPPDLKAKFLQEARILKQYSHPNIVRLIGVCTQKQPIYIVMELVQGGD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 346 LFERIIDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKTGtrIKLIDFGLARRLEN-----AGSLKV 420
Cdd:cd05084    81 FLTFLRTEGPRLKVKELIRMVENAAAGMEYLESKHCIHRDLAARNCLVTEKNV--LKISDFGMSREEEDgvyaaTGGMKQ 158
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1034633499 421 LfgTPEFVAPEVINYEPIGYATDMWSIGVICYILVS-GLSPFMGDNDNET 469
Cdd:cd05084   159 I--PVKWTAPEALNYGRYSSESDVWSFGILLWETFSlGAVPYANLSNQQT 206
STKc_WNK2_like cd14032
Catalytic domain of With No Lysine (WNK) 2-like Serine/Threonine kinases; STKs catalyze the ...
264-523 3.12e-18

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


Pssm-ID: 270934 [Multi-domain]  Cd Length: 266  Bit Score: 85.13  E-value: 3.12e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 264 YDIEerLGSGKFGQVFRLVEKKT--RKVWAGKFFKAYSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKAN----IVMV 337
Cdd:cd14032     5 FDIE--LGRGSFKTVYKGLDTETwvEVAWCELQDRKLTKVERQRFKEEAEMLKGLQHPNIVRFYDFWESCAKgkrcIVLV 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 338 LEIVSGGELfeRIIDEDFELTERECIK-YMRQISEGVEYIHKQG--IVHLDLKPENIMCVNKTGTrIKLIDFGLARrLEN 414
Cdd:cd14032    83 TELMTSGTL--KTYLKRFKVMKPKVLRsWCRQILKGLLFLHTRTppIIHRDLKCDNIFITGPTGS-VKIGDLGLAT-LKR 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 415 AGSLKVLFGTPEFVAPEVINyEPIGYATDMWSIGVICYILVSGLSPFmgdNDNETLANV-TSATWDFDDEAFDEISD-DA 492
Cdd:cd14032   159 ASFAKSVIGTPEFMAPEMYE-EHYDESVDVYAFGMCMLEMATSEYPY---SECQNAAQIyRKVTCGIKPASFEKVTDpEI 234
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1034633499 493 KDFISNLLKKDMKNRLDCTQCLQHPWLMKDT 523
Cdd:cd14032   235 KEIIGECICKNKEERYEIKDLLSHAFFAEDT 265
STKc_PCTAIRE3 cd07871
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer ...
268-519 3.13e-18

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: 85.83  E-value: 3.13e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 268 ERLGSGKFGQVFRLVEKKTRKVWAgkfFKAYSAKEKEN-----IRqEISIMNCLHHPKLVQCVDAFEEKANIVMVLEIVS 342
Cdd:cd07871    11 DKLGEGTYATVFKGRSKLTENLVA---LKEIRLEHEEGapctaIR-EVSLLKNLKHANIVTLHDIIHTERCLTLVFEYLD 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 343 GGelFERIIDEDFELTERECIK-YMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGtRIKLIDFGLARrlenAGSL--- 418
Cdd:cd07871    87 SD--LKQYLDNCGNLMSMHNVKiFMFQLLRGLSYCHKRKILHRDLKPQNLL-INEKG-ELKLADFGLAR----AKSVptk 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 419 --------------KVLFGTPEFVAPevinyepigyaTDMWSIGVICYILVSGLSPFMGDNDNETL-------ANVTSAT 477
Cdd:cd07871   159 tysnevvtlwyrppDVLLGSTEYSTP-----------IDMWGVGCILYEMATGRPMFPGSTVKEELhlifrllGTPTEET 227
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034633499 478 W-------DFDDEAFDE------------ISDDAKDFISNLLKKDMKNRLDCTQCLQHPWL 519
Cdd:cd07871   228 WpgvtsneEFRSYLFPQyraqplinhaprLDTDGIDLLSSLLLYETKSRISAEAALRHSYF 288
STKc_CDK10 cd07845
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs ...
269-518 3.14e-18

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: 86.27  E-value: 3.14e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 269 RLGSGKFGQVFRLVEKKTRKVWAGKffKAYSAKEKENIR----QEISIMNCLHHPklvqcvdafeekaNIVMVLEIVSGG 344
Cdd:cd07845    14 RIGEGTYGIVYRARDTTSGEIVALK--KVRMDNERDGIPisslREITLLLNLRHP-------------NIVELKEVVVGK 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 345 EL------FE-------RIIDE---DFELTERECIkyMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGTrIKLIDFGL 408
Cdd:cd07845    79 HLdsiflvMEyceqdlaSLLDNmptPFSESQVKCL--MLQLLRGLQYLHENFIIHRDLKVSNLL-LTDKGC-LKIADFGL 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 409 ARRLEN-AGSLkvlfgTPEFV-----APEVI----NYEPigyATDMWSIGVICYILVSGLSPFMGDNDNETLANV----- 473
Cdd:cd07845   155 ARTYGLpAKPM-----TPKVVtlwyrAPELLlgctTYTT---AIDMWAVGCILAELLAHKPLLPGKSEIEQLDLIiqllg 226
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034633499 474 --TSATW-DFDD------------------EAFDEISDDAKDFISNLLKKDMKNRLDCTQCLQHPW 518
Cdd:cd07845   227 tpNESIWpGFSDlplvgkftlpkqpynnlkHKFPWLSEAGLRLLNFLLMYDPKKRATAEEALESSY 292
IgI_1_Palladin_C cd05893
First C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig ...
609-699 4.58e-18

First C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of palladin. Palladin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to this family contain multiple Ig-like domains and function as scaffolds, modulating actin cytoskeleton. Palladin binds to alpha-actinin ezrin, vasodilator-stimulated phosphoprotein VASP, SPIN90 (also known as DIP or mDia interacting protein), and Src. Palladin also binds F-actin directly, via its Ig3 domain. Palladin is expressed as several alternatively spliced isoforms, having various combinations of Ig-like domains, in a cell-type-specific manner. It has been suggested that palladin's different Ig-like domains may be specialized for distinct functions. 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: 409474  Cd Length: 92  Bit Score: 79.76  E-value: 4.58e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 609 PYFSKTIRDLEVVEGSAARFDCKIEGYPDPEVVWFKDDQSIR-ESRHFQIDYDEDGNCSLIISDVCGDDDAKYTCKAVNS 687
Cdd:cd05893     1 PFFEMKLKHYKIFEGMPVTFTCRVAGNPKPKIYWFKDGKQISpKSDHYTIQRDLDGTCSLHTTASTLDDDGNYTIMAANP 80
                          90
                  ....*....|..
gi 1034633499 688 LGEATCTAELIV 699
Cdd:cd05893    81 QGRISCTGRLMV 92
PTKc_Hck cd05073
Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the ...
266-470 4.63e-18

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: 84.69  E-value: 4.63e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 266 IEERLGSGKFGQVFRLVEKKTRKVwAGKFFKAYSAkEKENIRQEISIMNCLHHPKLVQcVDAFEEKANIVMVLEIVSGGE 345
Cdd:cd05073    15 LEKKLGAGQFGEVWMATYNKHTKV-AVKTMKPGSM-SVEAFLAEANVMKTLQHDKLVK-LHAVVTKEPIYIITEFMAKGS 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 346 LFERI-IDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCvnKTGTRIKLIDFGLARRLE-NAGSLKVLFG 423
Cdd:cd05073    92 LLDFLkSDEGSKQPLPKLIDFSAQIAEGMAFIEQRNYIHRDLRAANILV--SASLVCKIADFGLARVIEdNEYTAREGAK 169
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1034633499 424 TP-EFVAPEVINYEPIGYATDMWSIGVICYILVS-GLSPFMGDNDNETL 470
Cdd:cd05073   170 FPiKWTAPEAINFGSFTIKSDVWSFGILLMEIVTyGRIPYPGMSNPEVI 218
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
301-517 5.26e-18

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: 84.33  E-value: 5.26e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 301 KEKENIRQEISIMNCLHHPKLVQ--CVDAFEEKAN----IVMVLEIVSGGELFERIIDEDFELTERECIkYMRQISEGVE 374
Cdd:cd14012    40 KQIQLLEKELESLKKLRHPNLVSylAFSIERRGRSdgwkVYLLTEYAPGGSLSELLDSVGSVPLDTARR-WTLQLLEALE 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 375 YIHKQGIVHLDLKPENIMCVNKTG-TRIKLIDFGLARRLEN---AGSLKVLFGTPeFVAPEVIN-YEPIGYATDMWSIGV 449
Cdd:cd14012   119 YLHRNGVVHKSLHAGNVLLDRDAGtGIVKLTDYSLGKTLLDmcsRGSLDEFKQTY-WLPPELAQgSKSPTRKTDVWDLGL 197
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034633499 450 ICYILVSGLSPFMgdndNETLANVTSATwdfddeafDEISDDAKDFISNLLKKDMKNRLDCTQCLQHP 517
Cdd:cd14012   198 LFLQMLFGLDVLE----KYTSPNPVLVS--------LDLSASLQDFLSKCLSLDPKKRPTALELLPHE 253
PTKc_Syk_like cd05060
Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
268-471 5.49e-18

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: 84.32  E-value: 5.49e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 268 ERLGSGKFGQVFR--LVEKKTRKV-WAGKFFKA-YSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKAnIVMVLEIVSG 343
Cdd:cd05060     1 KELGHGNFGSVRKgvYLMKSGKEVeVAVKTLKQeHEKAGKKEFLREASVMAQLDHPCIVRLIGVCKGEP-LMLVMELAPL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 344 GELFERIIDeDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKTGTRIKliDFGLARRLeNAGSLKVLFG 423
Cdd:cd05060    80 GPLLKYLKK-RREIPVSDLKELAHQVAMGMAYLESKHFVHRDLAARNVLLVNRHQAKIS--DFGMSRAL-GAGSDYYRAT 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1034633499 424 T----P-EFVAPEVINYEPIGYATDMWSIGVICYILVS-GLSPFMGDNDNETLA 471
Cdd:cd05060   156 TagrwPlKWYAPECINYGKFSSKSDVWSYGVTLWEAFSyGAKPYGEMKGPEVIA 209
I-set pfam07679
Immunoglobulin I-set domain;
38-127 5.85e-18

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 79.22  E-value: 5.85e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499  38 PQIIQFPEDQKVRAGESVELFGKVTGTQPITCTWMKFRKQIQESEHMKVENSENGSKLTILAARQEHCGCYTLLVENKLG 117
Cdd:pfam07679   1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAG 80
                          90
                  ....*....|
gi 1034633499 118 SRQAQVNLTV 127
Cdd:pfam07679  81 EAEASAELTV 90
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
616-699 6.08e-18

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: 79.09  E-value: 6.08e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499  616 RDLEVVEGSAARFDCKIEGYPDPEVVWFKDDQS-IRESRHFQIDYDeDGNCSLIISDVCGDDDAKYTCKAVNSLGEATCT 694
Cdd:smart00410   2 PSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKlLAESGRFSVSRS-GSTSTLTISNVTPEDSGTYTCAATNSSGSASSG 80

                   ....*
gi 1034633499  695 AELIV 699
Cdd:smart00410  81 TTLTV 85
STKc_CdkB_plant cd07837
Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; ...
262-518 6.68e-18

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: 84.89  E-value: 6.68e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 262 DFYDIEERLGSGKFGQVFRLVEKKTRKVWAGKffKAYSAKEKENIR----QEISIMNCLHH-PKLVQ--CVDAFEE--KA 332
Cdd:cd07837     1 DAYEKLEKIGEGTYGKVYKARDKNTGKLVALK--KTRLEMEEEGVPstalREVSLLQMLSQsIYIVRllDVEHVEEngKP 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 333 NIVMVLEIVSGGelFERIID-----EDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGTRIKLIDFG 407
Cdd:cd07837    79 LLYLVFEYLDTD--LKKFIDsygrgPHNPLPAKTIQSFMYQLCKGVAHCHSHGVMHRDLKPQNLL-VDKQKGLLKIADLG 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 408 LARrlenAGSLKVLFGTPEFV-----APEVInyepIG---YAT--DMWSIGVICYILVSGLSPFMGDNDNETLANV---- 473
Cdd:cd07837   156 LGR----AFTIPIKSYTHEIVtlwyrAPEVL----LGsthYSTpvDMWSVGCIFAEMSRKQPLFPGDSELQQLLHIfrll 227
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034633499 474 ---TSATW-------DFDD----------EAFDEISDDAKDFISNLLKKDMKNRLDCTQCLQHPW 518
Cdd:cd07837   228 gtpNEEVWpgvsklrDWHEypqwkpqdlsRAVPDLEPEGVDLLTKMLAYDPAKRISAKAALQHPY 292
STKc_LIMK1 cd14221
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the ...
270-454 7.34e-18

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: 84.24  E-value: 7.34e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 270 LGSGKFGQVFRLVEKKTRKVWAGKFFKAYSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEIVSGGELFER 349
Cdd:cd14221     1 LGKGCFGQAIKVTHRETGEVMVMKELIRFDEETQRTFLKEVKVMRCLEHPNVLKFIGVLYKDKRLNFITEYIKGGTLRGI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 350 IIDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENimCVNKTGTRIKLIDFGLARRL-------ENAGSLK--- 419
Cdd:cd14221    81 IKSMDSHYPWSQRVSFAKDIASGMAYLHSMNIIHRDLNSHN--CLVRENKSVVVADFGLARLMvdektqpEGLRSLKkpd 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1034633499 420 -----VLFGTPEFVAPEVINYEPIGYATDMWSIG-VICYIL 454
Cdd:cd14221   159 rkkryTVVGNPYWMAPEMINGRSYDEKVDVFSFGiVLCEII 199
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
270-514 8.28e-18

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: 84.25  E-value: 8.28e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 270 LGSGKFGQVFRLVEKKTRKVWAGKFFKAYSAKEKENIRQEISIMNCLHHPKLVQ---CVDAFEEKAnivMVLEIVSGGEL 346
Cdd:cd14066     1 IGSGGFGTVYKGVLENGTVVAVKRLNEMNCAASKKEFLTELEMLGRLRHPNLVRllgYCLESDEKL---LVYEYMPNGSL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 347 FERI--IDEDFELTERECIKYMRQISEGVEYIHKQG---IVHLDLKPENIMCVNktGTRIKLIDFGLARRLENAGSLKV- 420
Cdd:cd14066    78 EDRLhcHKGSPPLPWPQRLKIAKGIARGLEYLHEECpppIIHGDIKSSNILLDE--DFEPKLTDFGLARLIPPSESVSKt 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 421 --LFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTsatwdfdDEAFDEISDDAKDFISN 498
Cdd:cd14066   156 saVKGTIGYLAPEYIRTGRVSTKSDVYSFGVVLLELLTGKPAVDENRENASRKDLV-------EWVESKGKEELEDILDK 228
                         250
                  ....*....|....*.
gi 1034633499 499 LLKKDMKNRLDCTQCL 514
Cdd:cd14066   229 RLVDDDGVEEEEVEAL 244
STKc_p38gamma cd07880
Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase ...
249-508 9.02e-18

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: 85.39  E-value: 9.02e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 249 YRTVTINTEQKVSDFYDIEERLGSGKFGQVFRLVEKKT-RKVWAGKFFKAYSAK--EKENIRqEISIMNCLHHPKLVQCV 325
Cdd:cd07880     2 YRQEVNKTIWEVPDRYRDLKQVGSGAYGTVCSALDRRTgAKVAIKKLYRPFQSElfAKRAYR-ELRLLKHMKHENVIGLL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 326 DAFEEKANI--------VMVLEIVSGGELFERiidedfELTERECIKYM-RQISEGVEYIHKQGIVHLDLKPENiMCVNK 396
Cdd:cd07880    81 DVFTPDLSLdrfhdfylVMPFMGTDLGKLMKH------EKLSEDRIQFLvYQMLKGLKYIHAAGIIHRDLKPGN-LAVNE 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 397 TgTRIKLIDFGLARRLENAGSLKVLfgTPEFVAPEVI-NYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTS 475
Cdd:cd07880   154 D-CELKILDFGLARQTDSEMTGYVV--TRWYRAPEVIlNWMHYTQTVDIWSVGCIMAEMLTGKPLFKGHDHLDQLMEIMK 230
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1034633499 476 ATWDFDDEAFDEI-SDDAKDFISNL---LKKDMKNRL 508
Cdd:cd07880   231 VTGTPSKEFVQKLqSEDAKNYVKKLprfRKKDFRSLL 267
PK_TRB1 cd14023
Pseudokinase domain of Tribbles Homolog 1; The pseudokinase domain shows similarity to protein ...
307-519 9.58e-18

Pseudokinase domain of Tribbles Homolog 1; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. TRB1 interacts directly with the mitogen activated protein kinase (MAPK) kinase MKK4, an activator of JNK. It regulates vascular smooth muscle cell proliferation and chemotaxis through the JNK signaling pathway. It is found to be down-regulated in human acute myeloid leukaemia (AML) and may play a role in the pathogenesis of the disease. It has also been identified as a potential biomarker for antibody-mediated allograft failure. TRB1 is one of three Tribbles Homolog (TRB) proteins present in vertebrates that are encoded by three separate genes. TRB proteins interact with many proteins involved in signalling pathways. They play scaffold-like regulatory functions and affect many cellular processes such as mitosis, apoptosis, and gene expression. The TRB1 subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270925 [Multi-domain]  Cd Length: 242  Bit Score: 83.17  E-value: 9.58e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 307 RQEISIMNCLHHPKLVQC----VDAFEEK----------ANIVMVLEIVSGGELFERIIDEDF-----------ELTERE 361
Cdd:cd14023     6 REHVYRALQLHSGAELQCkvfpLKHYQDKirpyiqlpshRNITGIVEVILGDTKAYVFFEKDFgdmhsyvrsckRLREEE 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 362 CIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKTGTRIKLIDFGLARRL-ENAGSLKVLFGTPEFVAPEVINYEPI-- 438
Cdd:cd14023    86 AARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSDEERTQLRLESLEDTHIMkGEDDALSDKHGCPAYVSPEILNTTGTys 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 439 GYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDFDdeafDEISDDAKDFISNLLKKDMKNRLDCTQCLQHPW 518
Cdd:cd14023   166 GKSADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQFCIP----DHVSPKARCLIRSLLRREPSERLTAPEILLHPW 241

                  .
gi 1034633499 519 L 519
Cdd:cd14023   242 F 242
STKc_TLK1 cd14040
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the ...
270-520 1.02e-17

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


Pssm-ID: 270942 [Multi-domain]  Cd Length: 299  Bit Score: 84.34  E-value: 1.02e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 270 LGSGKFGQVFR---LVEKKTRKVWAGKFFKAYSAKEKENIRQ----EISIMNCLHHPKLVQCVDAFE-EKANIVMVLEIV 341
Cdd:cd14040    14 LGRGGFSEVYKafdLYEQRYAAVKIHQLNKSWRDEKKENYHKhacrEYRIHKELDHPRIVKLYDYFSlDTDTFCTVLEYC 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 342 SGGELfERIIDEDFELTERECIKYMRQISEGVEYIH--KQGIVHLDLKPENIMCVNKTGT-RIKLIDFGLARRLENAGS- 417
Cdd:cd14040    94 EGNDL-DFYLKQHKLMSEKEARSIVMQIVNALRYLNeiKPPIIHYDLKPGNILLVDGTACgEIKITDFGLSKIMDDDSYg 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 418 ------LKVLFGTPEFVAPE--VINYEP--IGYATDMWSIGVICYILVSGLSPFMGDNDNETL--ANVTSATWDFDDEAF 485
Cdd:cd14040   173 vdgmdlTSQGAGTYWYLPPEcfVVGKEPpkISNKVDVWSVGVIFFQCLYGRKPFGHNQSQQDIlqENTILKATEVQFPVK 252
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1034633499 486 DEISDDAKDFISNLLKKDMKNRLDCTQCLQHPWLM 520
Cdd:cd14040   253 PVVSNEAKAFIRRCLAYRKEDRFDVHQLASDPYLL 287
STKc_TAO3 cd06633
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze ...
263-522 1.38e-17

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: 84.32  E-value: 1.38e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 263 FYDIEErLGSGKFGQVFRLVEKKTRKVWAGKFFkAYSAKEK----ENIRQEISIMNCLHHPKLVQCVDAF--EEKANIVM 336
Cdd:cd06633    23 FVDLHE-IGHGSFGAVYFATNSHTNEVVAIKKM-SYSGKQTnekwQDIIKEVKFLQQLKHPNTIEYKGCYlkDHTAWLVM 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 337 VLEIVSGGELFERiidEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGtRIKLIDFGLARRLENAG 416
Cdd:cd06633   101 EYCLGSASDLLEV---HKKPLQEVEIAAITHGALQGLAYLHSHNMIHRDIKAGNIL-LTEPG-QVKLADFGSASIASPAN 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 417 SlkvLFGTPEFVAPEVI------NYEPigyATDMWSIGVICYILVSGLSPFMGDNDNETLANVtsATWDFDDEAFDEISD 490
Cdd:cd06633   176 S---FVGTPYWMAPEVIlamdegQYDG---KVDIWSLGITCIELAERKPPLFNMNAMSALYHI--AQNDSPTLQSNEWTD 247
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1034633499 491 DAKDFISNLLKKDMKNRLDCTQCLQHPWLMKD 522
Cdd:cd06633   248 SFRGFVDYCLQKIPQERPSSAELLRHDFVRRE 279
STKc_SHIK cd13974
Catalytic domain of the Serine/Threonine kinase, SINK-homologous inhibitory kinase; STKs ...
357-516 1.44e-17

Catalytic domain of the Serine/Threonine kinase, SINK-homologous inhibitory kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SHIK, also referred to as STK40 or LYK4, is a cytoplasmic and nuclear protein that is involved in the negative regulation of NF-kappaB- and p53-mediated transcription. It was identified as a protein related to SINK, a p65-interacting protein that inhibits p65 phosphorylation by the catalytic subunit of PKA, thereby inhibiting transcriptional competence of NF-kappaB. The SHIK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270876 [Multi-domain]  Cd Length: 290  Bit Score: 83.61  E-value: 1.44e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 357 LTERECIKYMRQISEGVEYIHKQGIVHLDLKPENiMCVNKTGTRIKLIDFGLARRLENAGS-LKVLFGTPEFVAPEVINY 435
Cdd:cd13974   129 LSEREALVIFYDVVRVVEALHKKNIVHRDLKLGN-MVLNKRTRKITITNFCLGKHLVSEDDlLKDQRGSPAYISPDVLSG 207
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 436 EP-IGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDFDDEAfdEISDDAKDFISNLLKKDMKNRLDCTQCL 514
Cdd:cd13974   208 KPyLGKPSDMWALGVVLFTMLYGQFPFYDSIPQELFRKIKAAEYTIPEDG--RVSENTVCLIRKLLVLNPQKRLTASEVL 285

                  ..
gi 1034633499 515 QH 516
Cdd:cd13974   286 DS 287
STKc_p38beta cd07878
Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase ...
249-521 1.48e-17

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: 84.72  E-value: 1.48e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 249 YRTVTINTEQKVSDFYDIEERLGSGKFGQVFRLVEKKTR-KVWAGKFFKAY-SAKEKENIRQEISIMNCLHHPKLVQCVD 326
Cdd:cd07878     2 YRQELNKTVWEVPERYQNLTPVGSGAYGSVCSAYDTRLRqKVAVKKLSRPFqSLIHARRTYRELRLLKHMKHENVIGLLD 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 327 AFE-----EKANIVMVLEIVSGGEL-----FERIIDEDFELterecikYMRQISEGVEYIHKQGIVHLDLKPENImCVNK 396
Cdd:cd07878    82 VFTpatsiENFNEVYLVTNLMGADLnnivkCQKLSDEHVQF-------LIYQLLRGLKYIHSAGIIHRDLKPSNV-AVNE 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 397 TgTRIKLIDFGLARRLENAGSLKVlfGTPEFVAPEV-INYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTS 475
Cdd:cd07878   154 D-CELRILDFGLARQADDEMTGYV--ATRWYRAPEImLNWMHYNQTVDIWSVGCIMAELLKGKALFPGNDYIDQLKRIME 230
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034633499 476 ATWDFDDEAFDEISDD---------------------------AKDFISNLLKKDMKNRLDCTQCLQHPWLMK 521
Cdd:cd07878   231 VVGTPSPEVLKKISSEharkyiqslphmpqqdlkkifrganplAIDLLEKMLVLDSDKRISASEALAHPYFSQ 303
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
262-518 1.52e-17

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 83.71  E-value: 1.52e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 262 DFYDIEERLGSGKFGQVFRLVEKKTRKVWAGKffKAYSAKEKENIR----QEISIMNCLHHPKLVQCVDAFEEKANIVMV 337
Cdd:PLN00009    2 DQYEKVEKIGEGTYGVVYKARDRVTNETIALK--KIRLEQEDEGVPstaiREISLLKEMQHGNIVRLQDVVHSEKRLYLV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 338 LEIVSGGelFERIIDE--DFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKTGTrIKLIDFGLARrlenA 415
Cdd:PLN00009   80 FEYLDLD--LKKHMDSspDFAKNPRLIKTYLYQILRGIAYCHSHRVLHRDLKPQNLLIDRRTNA-LKLADFGLAR----A 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 416 GSLKVLFGTPEFV-----APEVInyepIG---YAT--DMWSIGVICYILVSGLSPFMGDNDNETLANV-------TSATW 478
Cdd:PLN00009  153 FGIPVRTFTHEVVtlwyrAPEIL----LGsrhYSTpvDIWSVGCIFAEMVNQKPLFPGDSEIDELFKIfrilgtpNEETW 228
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1034633499 479 -------DFDDeAFDE------------ISDDAKDFISNLLKKDMKNRLDCTQCLQHPW 518
Cdd:PLN00009  229 pgvtslpDYKS-AFPKwppkdlatvvptLEPAGVDLLSKMLRLDPSKRITARAALEHEY 286
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
270-463 1.67e-17

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: 82.89  E-value: 1.67e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 270 LGSGKFGQVfRLVEKKTRKVW-AGKFFKAY--SAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEIVSGG-- 344
Cdd:cd13978     1 LGSGGFGTV-SKARHVSWFGMvAIKCLHSSpnCIEERKALLKEAEKMERARHSYVLPLLGVCVERRSLGLVMEYMENGsl 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 345 -ELFERIIdEDFELTERecIKYMRQISEGVEYIH--KQGIVHLDLKPENIMCVNKtgTRIKLIDFGLAR------RLENA 415
Cdd:cd13978    80 kSLLEREI-QDVPWSLR--FRIIHEIALGMNFLHnmDPPLLHHDLKPENILLDNH--FHVKISDFGLSKlgmksiSANRR 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1034633499 416 GSLKVLFGTPEFVAPEviNYEPIGY----ATDMWSIGVICYILVSGLSPFMG 463
Cdd:cd13978   155 RGTENLGGTPIYMAPE--AFDDFNKkptsKSDVYSFAIVIWAVLTRKEPFEN 204
PTKc_Fer cd05085
Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; ...
268-463 1.70e-17

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: 82.75  E-value: 1.70e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 268 ERLGSGKFGQVFRLVEKKTRKVWAGKFFKAYSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEIVSGGELF 347
Cdd:cd05085     2 ELLGKGNFGEVYKGTLKDKTPVAVKTCKEDLPQELKIKFLSEARILKQYDHPNIVKLIGVCTQRQPIYIVMELVPGGDFL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 348 ERIIDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENimCVNKTGTRIKLIDFGLARRlENAG--SLKVLFGTP 425
Cdd:cd05085    82 SFLRKKKDELKTKQLVKFSLDAAAGMAYLESKNCIHRDLAARN--CLVGENNALKISDFGMSRQ-EDDGvySSSGLKQIP 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1034633499 426 -EFVAPEVINYEPIGYATDMWSIGVICYILVS-GLSPFMG 463
Cdd:cd05085   159 iKWTAPEALNYGRYSSESDVWSFGILLWETFSlGVCPYPG 198
PTKc_Src_Fyn_like cd14203
Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
269-473 1.96e-17

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: 82.66  E-value: 1.96e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 269 RLGSGKFGQVFRLVEKKTRKVwAGKFFKAySAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKAnIVMVLEIVSGGELFE 348
Cdd:cd14203     2 KLGQGCFGEVWMGTWNGTTKV-AIKTLKP-GTMSPEAFLEEAQIMKKLRHDKLVQLYAVVSEEP-IYIVTEFMSKGSLLD 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 349 RIIDEDFE-LTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNktGTRIKLIDFGLARRLE-NAGSLKVLFGTP- 425
Cdd:cd14203    79 FLKDGEGKyLKLPQLVDMAAQIASGMAYIERMNYIHRDLRAANILVGD--NLVCKIADFGLARLIEdNEYTARQGAKFPi 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1034633499 426 EFVAPEVINYEPIGYATDMWSIGV-ICYILVSGLSPFMGDNDNETLANV 473
Cdd:cd14203   157 KWTAPEAALYGRFTIKSDVWSFGIlLTELVTKGRVPYPGMNNREVLEQV 205
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
300-450 2.16e-17

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


Pssm-ID: 274846 [Multi-domain]  Cd Length: 1266  Bit Score: 86.82  E-value: 2.16e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499  300 AKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVM-VLEIVSGGELFERIIDEDfELTERECIKYMRQISEGVEYIHK 378
Cdd:TIGR03903   19 EHQRARFRRETALCARLYHPNIVALLDSGEAPPGLLFaVFEYVPGRTLREVLAADG-ALPAGETGRLMLQVLDALACAHN 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499  379 QGIVHLDLKPENIMCVNKTGTR-IKLIDFGLARRLENAGSLKVL--------FGTPEFVAPEVINYEPIGYATDMWSIGV 449
Cdd:TIGR03903   98 QGIVHRDLKPQNIMVSQTGVRPhAKVLDFGIGTLLPGVRDADVAtltrttevLGTPTYCAPEQLRGEPVTPNSDLYAWGL 177

                   .
gi 1034633499  450 I 450
Cdd:TIGR03903  178 I 178
STKc_NAK_like cd14037
Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze ...
266-520 2.42e-17

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


Pssm-ID: 270939 [Multi-domain]  Cd Length: 277  Bit Score: 82.72  E-value: 2.42e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 266 IEERLGSGKFGQVFRLVEKKTRKVWAGKFFKAYSAKEKENIRQEISIM-NCLHHPKLVQCVD--AFEEKANI--VMVL-E 339
Cdd:cd14037     7 IEKYLAEGGFAHVYLVKTSNGGNRAALKRVYVNDEHDLNVCKREIEIMkRLSGHKNIVGYIDssANRSGNGVyeVLLLmE 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 340 IVSGGELF----ERIideDFELTERECIKYMRQISEGVEYIH--KQGIVHLDLKPENIMCVnkTGTRIKLIDFGLA---- 409
Cdd:cd14037    87 YCKGGGVIdlmnQRL---QTGLTESEILKIFCDVCEAVAAMHylKPPLIHRDLKVENVLIS--DSGNYKLCDFGSAttki 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 410 RRLENAGSLKVL------FGTPEFVAPEVINY---EPIGYATDMWSIGVICYILVSGLSPFmgdNDNETLAnVTSATWDF 480
Cdd:cd14037   162 LPPQTKQGVTYVeedikkYTTLQYRAPEMIDLyrgKPITEKSDIWALGCLLYKLCFYTTPF---EESGQLA-ILNGNFTF 237
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1034633499 481 DDeaFDEISDDAKDFISNLLKKDMKNRLDCTQCLQHPWLM 520
Cdd:cd14037   238 PD--NSRYSKRLHKLIRYMLEEDPEKRPNIYQVSYEAFEL 275
STKc_A-Raf cd14150
Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) ...
268-470 2.56e-17

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: 82.37  E-value: 2.56e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 268 ERLGSGKFGQVFRlvekktrKVWAG----KFFKAY--SAKEKENIRQEISIMNCLHHPKLVQCVdAFEEKANIVMVLEIV 341
Cdd:cd14150     6 KRIGTGSFGTVFR-------GKWHGdvavKILKVTepTPEQLQAFKNEMQVLRKTRHVNILLFM-GFMTRPNFAIITQWC 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 342 SGGELFER--IIDEDFELTERecIKYMRQISEGVEYIHKQGIVHLDLKPENIMCvnKTGTRIKLIDFGLA---RRLENAG 416
Cdd:cd14150    78 EGSSLYRHlhVTETRFDTMQL--IDVARQTAQGMDYLHAKNIIHRDLKSNNIFL--HEGLTVKIGDFGLAtvkTRWSGSQ 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1034633499 417 SLKVLFGTPEFVAPEVINYE---PIGYATDMWSIGVICYILVSGLSPFMGDNDNETL 470
Cdd:cd14150   154 QVEQPSGSILWMAPEVIRMQdtnPYSFQSDVYAYGVVLYELMSGTLPYSNINNRDQI 210
PTKc_Fyn cd05070
Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the ...
266-473 2.64e-17

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: 82.81  E-value: 2.64e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 266 IEERLGSGKFGQVFRLVEKKTRKVwAGKFFKAySAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKAnIVMVLEIVSGGE 345
Cdd:cd05070    13 LIKRLGNGQFGEVWMGTWNGNTKV-AIKTLKP-GTMSPESFLEEAQIMKKLKHDKLVQLYAVVSEEP-IYIVTEYMSKGS 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 346 LFERIID-EDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNktGTRIKLIDFGLARRLE-NAGSLKVLFG 423
Cdd:cd05070    90 LLDFLKDgEGRALKLPNLVDMAAQVAAGMAYIERMNYIHRDLRSANILVGN--GLICKIADFGLARLIEdNEYTARQGAK 167
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1034633499 424 TP-EFVAPEVINYEPIGYATDMWSIGVICYILVS-GLSPFMGDNDNETLANV 473
Cdd:cd05070   168 FPiKWTAPEAALYGRFTIKSDVWSFGILLTELVTkGRVPYPGMNNREVLEQV 219
STKc_PCTAIRE_like cd07844
Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
264-519 3.00e-17

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


Pssm-ID: 270835 [Multi-domain]  Cd Length: 286  Bit Score: 82.81  E-value: 3.00e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 264 YDIEERLGSGKFGQVFRLVEKKTRKVWAgkfFKAYSAKEKEN-----IRqEISIMNCLHHpklvqcvdafeekANIVMVL 338
Cdd:cd07844     2 YKKLDKLGEGSYATVYKGRSKLTGQLVA---LKEIRLEHEEGapftaIR-EASLLKDLKH-------------ANIVTLH 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 339 EIVSGGELFERIidedFELTERECIKYMR----------------QISEGVEYIHKQGIVHLDLKPENIMcVNKTGtRIK 402
Cdd:cd07844    65 DIIHTKKTLTLV----FEYLDTDLKQYMDdcggglsmhnvrlflfQLLRGLAYCHQRRVLHRDLKPQNLL-ISERG-ELK 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 403 LIDFGLARrlenAGSLKVLFGTPEFVA-----PEVInyepIG---YAT--DMWSIGVICYILVSGLSPFMGDNDNE---- 468
Cdd:cd07844   139 LADFGLAR----AKSVPSKTYSNEVVTlwyrpPDVL----LGsteYSTslDMWGVGCIFYEMATGRPLFPGSTDVEdqlh 210
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034633499 469 ----TLANVTSATW-------DFDDEAF---------------DEISdDAKDFISNLLKKDMKNRLDCTQCLQHPWL 519
Cdd:cd07844   211 kifrVLGTPTEETWpgvssnpEFKPYSFpfypprplinhaprlDRIP-HGEELALKFLQYEPKKRISAAEAMKHPYF 286
STKc_MLTK cd14060
Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated ...
271-463 3.30e-17

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: 81.54  E-value: 3.30e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 271 GSGKFGQVFRlvekktrKVWAGKFfKAYSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEIVSGGELFERI 350
Cdd:cd14060     2 GGGSFGSVYR-------AIWVSQD-KEVAVKKLLKIEKEAEILSVLSHRNIIQFYGAILEAPNYGIVTEYASYGSLFDYL 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 351 IDEDFELTE-RECIKYMRQISEGVEYIHKQG---IVHLDLKPENI-MCVNKTgtrIKLIDFGlARRLENAGSLKVLFGTP 425
Cdd:cd14060    74 NSNESEEMDmDQIMTWATDIAKGMHYLHMEApvkVIHRDLKSRNVvIAADGV---LKICDFG-ASRFHSHTTHMSLVGTF 149
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1034633499 426 EFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMG 463
Cdd:cd14060   150 PWMAPEVIQSLPVSETCDTYSYGVVLWEMLTREVPFKG 187
STKc_HIPK3 cd14229
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 3; ...
264-450 3.63e-17

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: 83.15  E-value: 3.63e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 264 YDIEERLGSGKFGQVFRLVEKKTRKVWAGKFFKAYSAKEKENiRQEISIMNCLHHPK-----LVQCVDAFEEKANIVMVL 338
Cdd:cd14229     2 YEVLDFLGRGTFGQVVKCWKRGTNEIVAVKILKNHPSYARQG-QIEVGILARLSNENadefnFVRAYECFQHRNHTCLVF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 339 EIVSGgELFERIIDEDFELTERECIK-YMRQISEGVEYIHKQGIVHLDLKPENIMCVN--KTGTRIKLIDFGLARRLENA 415
Cdd:cd14229    81 EMLEQ-NLYDFLKQNKFSPLPLKVIRpILQQVATALKKLKSLGLIHADLKPENIMLVDpvRQPYRVKVIDFGSASHVSKT 159
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1034633499 416 gSLKVLFGTPEFVAPEVINYEPIGYATDMWSIGVI 450
Cdd:cd14229   160 -VCSTYLQSRYYRAPEIILGLPFCEAIDMWSLGCV 193
STKc_HIPK1 cd14228
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 1; ...
248-474 4.12e-17

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: 83.60  E-value: 4.12e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 248 DYRTVTINTEQKVSDFYDIEERLGSGKFGQVFRLVEKKTRKVWAGKFFKAYSAKEKENiRQEISIMNCLHHPK-----LV 322
Cdd:cd14228     1 DYQLVQHEILCSMTNSYEVLEFLGRGTFGQVAKCWKRSTKEIVAIKILKNHPSYARQG-QIEVSILSRLSSENadeynFV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 323 QCVDAFEEKANIVMVLEIVSGgELFERIIDEDFELTERECIK-YMRQISEGVEYIHKQGIVHLDLKPENIMCVN--KTGT 399
Cdd:cd14228    80 RSYECFQHKNHTCLVFEMLEQ-NLYDFLKQNKFSPLPLKYIRpILQQVATALMKLKSLGLIHADLKPENIMLVDpvRQPY 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034633499 400 RIKLIDFGLARRLENAgSLKVLFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVT 474
Cdd:cd14228   159 RVKVIDFGSASHVSKA-VCSTYLQSRYYRAPEIILGLPFCEAIDMWSLGCVIAELFLGWPLYPGASEYDQIRYIS 232
STKc_EIF2AK1_HRI cd14049
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
256-515 4.62e-17

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: 82.17  E-value: 4.62e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 256 TEQKVSDFYDIEeRLGSGKFGQVFRLVEKKTRKVWAGK--FFKAYSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKAN 333
Cdd:cd14049     1 TSRYLNEFEEIA-RLGKGGYGKVYKVRNKLDGQYYAIKkiLIKKVTKRDCMKVLREVKVLAGLQHPNIVGYHTAWMEHVQ 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 334 IVMVLEI-VSGGELFERIIDEDFELTERE-------------CIKYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGT 399
Cdd:cd14049    80 LMLYIQMqLCELSLWDWIVERNKRPCEEEfksapytpvdvdvTTKILQQLLEGVTYIHSMGIVHRDLKPRNIF-LHGSDI 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 400 RIKLIDFGLARRLENAGSLKVL-------------FGTPEFVAPEVINYEPIGYATDMWSIGVicyILVSGLSPFMGDND 466
Cdd:cd14049   159 HVRIGDFGLACPDILQDGNDSTtmsrlnglthtsgVGTCLYAAPEQLEGSHYDFKSDMYSIGV---ILLELFQPFGTEME 235
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1034633499 467 N-ETLANVTSATWdfdDEAFDEISDDAKDFISNLLKKDMKNRLDCTQCLQ 515
Cdd:cd14049   236 RaEVLTQLRNGQI---PKSLCKRWPVQAKYIKLLTSTEPSERPSASQLLE 282
STKc_LRRK2 cd14068
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze ...
270-457 5.59e-17

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


Pssm-ID: 270970 [Multi-domain]  Cd Length: 252  Bit Score: 81.15  E-value: 5.59e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 270 LGSGKFGQVFRLVEKKTRKvwAGKFFKAYSAKEKenIRQEISIMNCLHHPKLVQCVDAfeEKANIVMVLEIVSGGELFER 349
Cdd:cd14068     2 LGDGGFGSVYRAVYRGEDV--AVKIFNKHTSFRL--LRQELVVLSHLHHPSLVALLAA--GTAPRMLVMELAPKGSLDAL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 350 IIDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVN-KTGTRI--KLIDFGLARRLENAGsLKVLFGTPE 426
Cdd:cd14068    76 LQQDNASLTRTLQHRIALHVADGLRYLHSAMIIYRDLKPHNVLLFTlYPNCAIiaKIADYGIAQYCCRMG-IKTSEGTPG 154
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1034633499 427 FVAPEVINYEPI-GYATDMWSIGVICYILVSG 457
Cdd:cd14068   155 FRAPEVARGNVIyNQQADVYSFGLLLYDILTC 186
STKc_MAP4K5 cd06646
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
264-464 5.78e-17

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: 81.61  E-value: 5.78e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 264 YDIEERLGSGKFGQVFRLVEKKTRKVWAGKFFKAYSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEIVSG 343
Cdd:cd06646    11 YELIQRVGSGTYGDVYKARNLHTGELAAVKIIKLEPGDDFSLIQQEIFMVKECKHCNIVAYFGSYLSREKLWICMEYCGG 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 344 GELfERIIDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKTGtrIKLIDFGLARRL-ENAGSLKVLF 422
Cdd:cd06646    91 GSL-QDIYHVTGPLSELQIAYVCRETLQGLAYLHSKGKMHRDIKGANILLTDNGD--VKLADFGVAAKItATIAKRKSFI 167
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1034633499 423 GTPEFVAPEVINYEPIG---YATDMWSIGvICYILVSGLSPFMGD 464
Cdd:cd06646   168 GTPYWMAPEVAAVEKNGgynQLCDIWAVG-ITAIELAELQPPMFD 211
STKc_p38delta cd07879
Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase ...
249-542 5.92e-17

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: 83.03  E-value: 5.92e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 249 YRTVTINTEQKVSDFYDIEERLGSGKFGQVFRLVEKKT-RKVWAGKFFKAYSAK--EKENIRqEISIMNCLHHPKLVQCV 325
Cdd:cd07879     2 YREEVNKTVWELPERYTSLKQVGSGAYGSVCSAIDKRTgEKVAIKKLSRPFQSEifAKRAYR-ELTLLKHMQHENVIGLL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 326 DAFEEKAN--------IVMV-----LEIVSGGELFEriidedfelterECIKYM-RQISEGVEYIHKQGIVHLDLKPENi 391
Cdd:cd07879    81 DVFTSAVSgdefqdfyLVMPymqtdLQKIMGHPLSE------------DKVQYLvYQMLCGLKYIHSAGIIHRDLKPGN- 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 392 MCVNKTgTRIKLIDFGLARRLENAGSLKVLfgTPEFVAPEVI-NYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETL 470
Cdd:cd07879   148 LAVNED-CELKILDFGLARHADAEMTGYVV--TRWYRAPEVIlNWMHYNQTVDIWSVGCIMAEMLTGKTLFKGKDYLDQL 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 471 ANVTSATW----DF----DDEA-------------------FDEISDDAKDFISNLLKKDMKNRLDCTQCLQHPWL--MK 521
Cdd:cd07879   225 TQILKVTGvpgpEFvqklEDKAaksyikslpkyprkdfstlFPKASPQAVDLLEKMLELDVDKRLTATEALEHPYFdsFR 304
                         330       340       350
                  ....*....|....*....|....*....|.
gi 1034633499 522 DTK----------NMEAKKLSKDRMKKYMAR 542
Cdd:cd07879   305 DADeeteqqpyddSLENEKLSVDEWKKHIYK 335
PKc_TESK cd14155
Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; ...
270-454 6.10e-17

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: 80.98  E-value: 6.10e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 270 LGSGKFGQVFRLVEKKTRKVWAGKFFKaySAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEIVSGGELfER 349
Cdd:cd14155     1 IGSGFFSEVYKVRHRTSGQVMALKMNT--LSSNRANMLREVQLMNRLSHPNILRFMGVCVHQGQLHALTEYINGGNL-EQ 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 350 IIDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKTGTRIKLI-DFGLARRLENAGS----LKVLfGT 424
Cdd:cd14155    78 LLDSNEPLSWTVRVKLALDIARGLSYLHSKGIFHRDLTSKNCLIKRDENGYTAVVgDFGLAEKIPDYSDgkekLAVV-GS 156
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1034633499 425 PEFVAPEVINYEPIGYATDMWSIGVI-CYIL 454
Cdd:cd14155   157 PYWMAPEVLRGEPYNEKADVFSYGIIlCEII 187
STKc_beta_ARK cd05606
Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs ...
270-518 6.53e-17

Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The beta-ARK group is composed of GRK2, GRK3, and similar proteins. GRK2 and GRK3 are both widely expressed in many tissues, although GRK2 is present at higher levels. They contain an N-terminal RGS homology (RH) domain, a central catalytic domain, and C-terminal pleckstrin homology (PH) domain that mediates PIP2 and G protein betagamma-subunit translocation to the membrane. GRK2 (also called beta-ARK or beta-ARK1) is important in regulating several cardiac receptor responses. It plays a role in cardiac development and in hypertension. Deletion of GRK2 in mice results in embryonic lethality, caused by hypoplasia of the ventricular myocardium. GRK2 also plays important roles in the liver (as a regulator of portal blood pressure), in immune cells, and in the nervous system. Altered GRK2 expression has been reported in several disorders including major depression, schizophrenia, bipolar disorder, and Parkinsonism. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The beta-ARK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270757 [Multi-domain]  Cd Length: 279  Bit Score: 81.72  E-value: 6.53e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 270 LGSGKFGQVFRLVEKKTRKVWAGKFFKAYSAKEKE------NIRQEISIMNCLHHPKLVQCVD-AFEEKANIVMVLEIVS 342
Cdd:cd05606     2 IGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQgetlalNERIMLSLVSTGGDCPFIVCMTyAFQTPDKLCFILDLMN 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 343 GGELFERIIDEDFeLTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGtRIKLIDFGLA----RRLENAGsl 418
Cdd:cd05606    82 GGDLHYHLSQHGV-FSEAEMRFYAAEVILGLEHMHNRFIVYRDLKPANIL-LDEHG-HVRISDLGLAcdfsKKKPHAS-- 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 419 kvlFGTPEFVAPEVINyEPIGY--ATDMWSIGVICYILVSGLSPFMGDNDNETLAnVTSATWDFDDEAFDEISDDAKDFI 496
Cdd:cd05606   157 ---VGTHGYMAPEVLQ-KGVAYdsSADWFSLGCMLYKLLKGHSPFRQHKTKDKHE-IDRMTLTMNVELPDSFSPELKSLL 231
                         250       260
                  ....*....|....*....|....*..
gi 1034633499 497 SNLLKKDMKNRLDC-----TQCLQHPW 518
Cdd:cd05606   232 EGLLQRDVSKRLGClgrgaTEVKEHPF 258
PTKc_Zap-70 cd05115
Catalytic domain of the Protein Tyrosine Kinase, Zeta-chain-associated protein of 70kDa; PTKs ...
267-449 7.65e-17

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: 81.15  E-value: 7.65e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 267 EERLGSGKFGQVFRLVEKKTRKVW--AGKFFKAYSAKE-KENIRQEISIMNCLHHPKLVQCVDAFEEKAnIVMVLEIVSG 343
Cdd:cd05115     9 EVELGSGNFGCVKKGVYKMRKKQIdvAIKVLKQGNEKAvRDEMMREAQIMHQLDNPYIVRMIGVCEAEA-LMLVMEMASG 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 344 GELFERIIDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKTGTRIKliDFGLARRL---ENAGSLKV 420
Cdd:cd05115    88 GPLNKFLSGKKDEITVSNVVELMHQVSMGMKYLEEKNFVHRDLAARNVLLVNQHYAKIS--DFGLSKALgadDSYYKARS 165
                         170       180       190
                  ....*....|....*....|....*....|
gi 1034633499 421 LFGTP-EFVAPEVINYEPIGYATDMWSIGV 449
Cdd:cd05115   166 AGKWPlKWYAPECINFRKFSSRSDVWSYGV 195
STKc_IRAK4 cd14158
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; ...
269-507 7.82e-17

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: 81.39  E-value: 7.82e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 269 RLGSGKFGQVFRLVEKKTrKVWAGKFF---KAYSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEIVSGGE 345
Cdd:cd14158    22 KLGEGGFGVVFKGYINDK-NVAVKKLAamvDISTEDLTKQFEQEIQVMAKCQHENLVELLGYSCDGPQLCLVYTYMPNGS 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 346 LFERI--IDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCvnKTGTRIKLIDFGLARRLEnAGSL----K 419
Cdd:cd14158   101 LLDRLacLNDTPPLSWHMRCKIAQGTANGINYLHENNHIHRDIKSANILL--DETFVPKISDFGLARASE-KFSQtimtE 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 420 VLFGTPEFVAPEVINYEpIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDFDDEAFDEISDDAKDFISNL 499
Cdd:cd14158   178 RIVGTTAYMAPEALRGE-ITPKSDIFSFGVVLLEIITGLPPVDENRDPQLLLDIKEEIEDEEKTIEDYVDKKMGDWDSTS 256
                         250
                  ....*....|....*...
gi 1034633499 500 LKK----------DMKNR 507
Cdd:cd14158   257 IEAmysvasqclnDKKNR 274
STKc_p38alpha cd07877
Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase ...
249-499 8.04e-17

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: 82.39  E-value: 8.04e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 249 YRTVTINTEQKVSDFYDIEERLGSGKFGQVFRLVEKKTR-KVWAGKFFKAY-SAKEKENIRQEISIMNCLHHPKLVQCVD 326
Cdd:cd07877     4 YRQELNKTIWEVPERYQNLSPVGSGAYGSVCAAFDTKTGlRVAVKKLSRPFqSIIHAKRTYRELRLLKHMKHENVIGLLD 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 327 AFE-----EKANIVMVLEIVSGGELFEriIDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENiMCVNKTgTRI 401
Cdd:cd07877    84 VFTparslEEFNDVYLVTHLMGADLNN--IVKCQKLTDDHVQFLIYQILRGLKYIHSADIIHRDLKPSN-LAVNED-CEL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 402 KLIDFGLARRLENAGSLKVlfGTPEFVAPEV-INYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDF 480
Cdd:cd07877   160 KILDFGLARHTDDEMTGYV--ATRWYRAPEImLNWMHYNQTVDIWSVGCIMAELLTGRTLFPGTDHIDQLKLILRLVGTP 237
                         250       260
                  ....*....|....*....|
gi 1034633499 481 DDEAFDEI-SDDAKDFISNL 499
Cdd:cd07877   238 GAELLKKIsSESARNYIQSL 257
PTKc_EphR_B cd05065
Catalytic domain of the Protein Tyrosine Kinases, Class EphB Ephrin Receptors; PTKs catalyze ...
263-472 8.07e-17

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


Pssm-ID: 173638 [Multi-domain]  Cd Length: 269  Bit Score: 81.07  E-value: 8.07e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 263 FYDIEERLGSGKFGQVFR----LVEKKTRKVwAGKFFKA-YSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMV 337
Cdd:cd05065     5 CVKIEEVIGAGEFGEVCRgrlkLPGKREIFV-AIKTLKSgYTEKQRRDFLSEASIMGQFDHPNIIHLEGVVTKSRPVMII 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 338 LEIVSGGELFERIIDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMcVNkTGTRIKLIDFGLARRLENAGS 417
Cdd:cd05065    84 TEFMENGALDSFLRQNDGQFTVIQLVGMLRGIAAGMKYLSEMNYVHRDLAARNIL-VN-SNLVCKVSDFGLSRFLEDDTS 161
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034633499 418 LKVLFGT-----P-EFVAPEVINYEPIGYATDMWSIGVICYILVS-GLSPFMgDNDNETLAN 472
Cdd:cd05065   162 DPTYTSSlggkiPiRWTAPEAIAYRKFTSASDVWSYGIVMWEVMSyGERPYW-DMSNQDVIN 222
PTKc_Ror cd05048
Catalytic Domain of the Protein Tyrosine Kinases, Receptor tyrosine kinase-like Orphan ...
268-468 8.59e-17

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: 81.27  E-value: 8.59e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 268 ERLGSGKFGQVFR--LV----EKKTRKVwAGKFFKAY-SAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEI 340
Cdd:cd05048    11 EELGEGAFGKVYKgeLLgpssEESAISV-AIKTLKENaSPKTQQDFRREAELMSDLQHPNIVCLLGVCTKEQPQCMLFEY 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 341 VSGGELFERII-------------DEDFE--LTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKtGTRIKLID 405
Cdd:cd05048    90 MAHGDLHEFLVrhsphsdvgvssdDDGTAssLDQSDFLHIAIQIAAGMEYLSSHHYVHRDLAARNCL-VGD-GLTVKISD 167
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034633499 406 FGLARRLENAGSLKVLFGTP---EFVAPEVINYEPIGYATDMWSIGVICYILVS-GLSPFMGDNDNE 468
Cdd:cd05048   168 FGLSRDIYSSDYYRVQSKSLlpvRWMPPEAILYGKFTTESDVWSFGVVLWEIFSyGLQPYYGYSNQE 234
STKc_HIPK2 cd14227
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 2; ...
248-474 1.24e-16

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: 82.06  E-value: 1.24e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 248 DYRTVTINTEQKVSDFYDIEERLGSGKFGQVFRLVEKKTRKVWAGKFFKAYSAKEKENiRQEISIMNCLHHP-----KLV 322
Cdd:cd14227     1 DYQLVQHEVLCSMTNTYEVLEFLGRGTFGQVVKCWKRGTNEIVAIKILKNHPSYARQG-QIEVSILARLSTEsaddyNFV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 323 QCVDAFEEKANIVMVLEIVSGgELFERIIDEDFELTERECIK-YMRQISEGVEYIHKQGIVHLDLKPENIMCVN--KTGT 399
Cdd:cd14227    80 RAYECFQHKNHTCLVFEMLEQ-NLYDFLKQNKFSPLPLKYIRpILQQVATALMKLKSLGLIHADLKPENIMLVDpsRQPY 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034633499 400 RIKLIDFGLARRLENAgSLKVLFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVT 474
Cdd:cd14227   159 RVKVIDFGSASHVSKA-VCSTYLQSRYYRAPEIILGLPFCEAIDMWSLGCVIAELFLGWPLYPGASEYDQIRYIS 232
PTZ00283 PTZ00283
serine/threonine protein kinase; Provisional
256-517 1.30e-16

serine/threonine protein kinase; Provisional


Pssm-ID: 240344 [Multi-domain]  Cd Length: 496  Bit Score: 83.38  E-value: 1.30e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 256 TEQKVSDFYDIEERLGSGKFGQVfrLVEKKTR--KVWAGKF--FKAYSAKEKENIRQEIS-IMNClHHPKLVQCVDAF-- 328
Cdd:PTZ00283   26 TAKEQAKKYWISRVLGSGATGTV--LCAKRVSdgEPFAVKVvdMEGMSEADKNRAQAEVCcLLNC-DFFSIVKCHEDFak 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 329 ------EEKANIVMVLEIVSGGELFERIIDE---DFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIM-CVNKTg 398
Cdd:PTZ00283  103 kdprnpENVLMIALVLDYANAGDLRQEIKSRaktNRTFREHEAGLLFIQVLLAVHHVHSKHMIHRDIKSANILlCSNGL- 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 399 trIKLIDFGLARRLENAGSLKV---LFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTS 475
Cdd:PTZ00283  182 --VKLGDFGFSKMYAATVSDDVgrtFCGTPYYVAPEIWRRKPYSKKADMFSLGVLLYELLTLKRPFDGENMEEVMHKTLA 259
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1034633499 476 ATWdfdDEAFDEISDDAKDFISNLLKKDMKNRLDCTQCLQHP 517
Cdd:PTZ00283  260 GRY---DPLPPSISPEMQEIVTALLSSDPKRRPSSSKLLNMP 298
STKc_CDK4 cd07863
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs ...
264-519 1.34e-16

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: 80.78  E-value: 1.34e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 264 YDIEERLGSGKFGQVFrlvekKTRKVWAGKFFKAYSAKEKENirQEISIMNCLHHPKLVQCVDAFEEkANIVMVLEIVSG 343
Cdd:cd07863     2 YEPVAEIGVGAYGTVY-----KARDPHSGHFVALKSVRVQTN--EDGLPLSTVREVALLKRLEAFDH-PNIVRLMDVCAT 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 344 GE---------LFERIiDEDFEL---------TERECIK-YMRQISEGVEYIHKQGIVHLDLKPENIMCVnkTGTRIKLI 404
Cdd:cd07863    74 SRtdretkvtlVFEHV-DQDLRTyldkvpppgLPAETIKdLMRQFLRGLDFLHANCIVHRDLKPENILVT--SGGQVKLA 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 405 DFGLARRLENAGSLKVLFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANV-------TSAT 477
Cdd:cd07863   151 DFGLARIYSCQMALTPVVVTLWYRAPEVLLQSTYATPVDMWSVGCIFAEMFRRKPLFCGNSEADQLGKIfdliglpPEDD 230
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1034633499 478 WDFD----------------DEAFDEISDDAKDFISNLLKKDMKNRLDCTQCLQHPWL 519
Cdd:cd07863   231 WPRDvtlprgafsprgprpvQSVVPEIEESGAQLLLEMLTFNPHKRISAFRALQHPFF 288
PTKc_EphR_A cd05066
Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors; PTKs catalyze ...
266-466 1.95e-16

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: 79.91  E-value: 1.95e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 266 IEERLGSGKFGQV----FRLVEKKTRKVwAGKFFKA-YSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEI 340
Cdd:cd05066     8 IEKVIGAGEFGEVcsgrLKLPGKREIPV-AIKTLKAgYTEKQRRDFLSEASIMGQFDHPNIIHLEGVVTRSKPVMIVTEY 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 341 VSGGELFERIIDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMcVNkTGTRIKLIDFGLARRLEN------ 414
Cdd:cd05066    87 MENGSLDAFLRKHDGQFTVIQLVGMLRGIASGMKYLSDMGYVHRDLAARNIL-VN-SNLVCKVSDFGLSRVLEDdpeaay 164
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1034633499 415 ---AGSLKVlfgtpEFVAPEVINYEPIGYATDMWSIGVICYILVS-GLSPF--MGDND 466
Cdd:cd05066   165 ttrGGKIPI-----RWTAPEAIAYRKFTSASDVWSYGIVMWEVMSyGERPYweMSNQD 217
STKc_PCTAIRE1 cd07873
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer ...
268-519 1.98e-16

Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PCTAIRE-1 is expressed ubiquitously and is localized in the cytoplasm. Its kinase activity is cell cycle dependent and peaks at the S and G2 phases. PCTAIRE-1 is highly expressed in the brain and may play a role in regulating neurite outgrowth. It can also associate with Trap (Tudor repeat associator with PCTAIRE-2), a physiological partner of PCTAIRE-2; with p11, a small dimeric protein with similarity to S100; and with 14-3-3 proteins, mediators of phosphorylation-dependent interactions in many different proteins. PCTAIRE-1 shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PCTAIRE-1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270854 [Multi-domain]  Cd Length: 297  Bit Score: 80.43  E-value: 1.98e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 268 ERLGSGKFGQVFRLVEKKTRKVWAgkfFKAYSAKEKEN-----IRqEISIMNCLHHPKLVQCVDAFEEKANIVMVLEIVS 342
Cdd:cd07873     8 DKLGEGTYATVYKGRSKLTDNLVA---LKEIRLEHEEGapctaIR-EVSLLKDLKHANIVTLHDIIHTEKSLTLVFEYLD 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 343 GGelFERIIDEDFELTERECIK-YMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGtRIKLIDFGLARrlenAGSLKVL 421
Cdd:cd07873    84 KD--LKQYLDDCGNSINMHNVKlFLFQLLRGLAYCHRRKVLHRDLKPQNLL-INERG-ELKLADFGLAR----AKSIPTK 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 422 FGTPEFVA----PEVINYEPIGYAT--DMWSIGVICYILVSGLSPFMGDNDNETLANV-------TSATWD--FDDEAFD 486
Cdd:cd07873   156 TYSNEVVTlwyrPPDILLGSTDYSTqiDMWGVGCIFYEMSTGRPLFPGSTVEEQLHFIfrilgtpTEETWPgiLSNEEFK 235
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1034633499 487 -----------------EISDDAKDFISNLLKKDMKNRLDCTQCLQHPWL 519
Cdd:cd07873   236 synypkyradalhnhapRLDSDGADLLSKLLQFEGRKRISAEEAMKHPYF 285
STKc_WNK1 cd14030
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze ...
236-523 2.03e-16

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


Pssm-ID: 270932 [Multi-domain]  Cd Length: 289  Bit Score: 80.48  E-value: 2.03e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 236 EVSDDDEKEPEVDYRTVTINTEQKVSDFyDIEerLGSGKFGQVFRLVEKKT--RKVWAGKFFKAYSAKEKENIRQEISIM 313
Cdd:cd14030     2 ERNKQQDEIEELETKAVG*SPDGRFLKF-DIE--IGRGSFKTVYKGLDTETtvEVAWCELQDRKLSKSERQRFKEEAGML 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 314 NCLHHPKLVQCVDAFEE----KANIVMVLEIVSGGELfeRIIDEDFELTERECIK-YMRQISEGVEYIHKQG--IVHLDL 386
Cdd:cd14030    79 KGLQHPNIVRFYDSWEStvkgKKCIVLVTELMTSGTL--KTYLKRFKVMKIKVLRsWCRQILKGLQFLHTRTppIIHRDL 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 387 KPENIMCVNKTGTrIKLIDFGLARrLENAGSLKVLFGTPEFVAPEVINyEPIGYATDMWSIGVICYILVSGLSPFMG-DN 465
Cdd:cd14030   157 KCDNIFITGPTGS-VKIGDLGLAT-LKRASFAKSVIGTPEFMAPEMYE-EKYDESVDVYAFGMCMLEMATSEYPYSEcQN 233
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 466 DNETLANVTSAT--WDFDDEAFDEIsddaKDFISNLLKKDMKNRLDCTQCLQHPWLMKDT 523
Cdd:cd14030   234 AAQIYRRVTSGVkpASFDKVAIPEV----KEIIEGCIRQNKDERYAIKDLLNHAFFQEET 289
PTKc_Ror1 cd05090
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
268-473 2.28e-16

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: 80.06  E-value: 2.28e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 268 ERLGSGKFGQVFR----LVEKKTRKVWAGKFFKAYSAKEKEN-IRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEIVS 342
Cdd:cd05090    11 EELGECAFGKIYKghlyLPGMDHAQLVAIKTLKDYNNPQQWNeFQQEASLMTELHHPNIVCLLGVVTQEQPVCMLFEFMN 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 343 GGELFERII------------DED----FELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKtgTRIKLIDF 406
Cdd:cd05090    91 QGDLHEFLImrsphsdvgcssDEDgtvkSSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILVGEQ--LHVKISDL 168
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034633499 407 GLARRLENAGSLKVLFGT--P-EFVAPEVINYEPIGYATDMWSIGVICYILVS-GLSPFMGDNDNETLANV 473
Cdd:cd05090   169 GLSREIYSSDYYRVQNKSllPiRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSfGLQPYYGFSNQEVIEMV 239
PKc_MKK5 cd06619
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
267-528 3.06e-16

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: 79.54  E-value: 3.06e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 267 EERLGSGKFGQVFRLVEKKTRKVWAGKFFKAYSAKE-KENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEIVSGGE 345
Cdd:cd06619     6 QEILGHGNGGTVYKAYHLLTRRILAVKVIPLDITVElQKQIMSELEILYKCDSPYIIGFYGAFFVENRISICTEFMDGGS 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 346 LferiiDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENiMCVNKTGtRIKLIDFGLARRLENAGSlKVLFGTP 425
Cdd:cd06619    86 L-----DVYRKIPEHVLGRIAVAVVKGLTYLWSLKILHRDVKPSN-MLVNTRG-QVKLCDFGVSTQLVNSIA-KTYVGTN 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 426 EFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNE-TLANVTSATWDFDDEA----FDEISDDAKDFISNLL 500
Cdd:cd06619   158 AYMAPERISGEQYGIHSDVWSLGISFMELALGRFPYPQIQKNQgSLMPLQLLQCIVDEDPpvlpVGQFSEKFVHFITQCM 237
                         250       260
                  ....*....|....*....|....*....
gi 1034633499 501 KKDMKNRLDCTQCLQHPWL-MKDTKNMEA 528
Cdd:cd06619   238 RKQPKERPAPENLMDHPFIvQYNDGNAEV 266
PKc_DYRK4 cd14225
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
264-471 3.57e-16

Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and -Regulated Kinase 4; 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. DYRK4 is a testis-specific kinase with restricted expression to postmeiotic spermatids. It may function during spermiogenesis, however, it is not required for male fertility. DYRK4 has also been detected in a human teratocarcinoma cell line induced to produce postmitotic neurons. It may have a role in neuronal differentiation. DYRKs autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. They play important roles in cell proliferation, differentiation, survival, and development. The DYRK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271127 [Multi-domain]  Cd Length: 341  Bit Score: 80.52  E-value: 3.57e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 264 YDIEERLGSGKFGQVFRLVEKKTRKVWAGKFFKaysaKEKENIRQ---EISIMNCLHHP------KLVQCVDAFEEKANI 334
Cdd:cd14225    45 YEILEVIGKGSFGQVVKALDHKTNEHVAIKIIR----NKKRFHHQalvEVKILDALRRKdrdnshNVIHMKEYFYFRNHL 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 335 VMVLEIVsGGELFERIIDEDF-----ELTERECIKYMRQIsegvEYIHKQGIVHLDLKPENIMCVNKTGTRIKLIDFGlA 409
Cdd:cd14225   121 CITFELL-GMNLYELIKKNNFqgfslSLIRRFAISLLQCL----RLLYRERIIHCDLKPENILLRQRGQSSIKVIDFG-S 194
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034633499 410 RRLENAGSLKVL---FgtpeFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLA 471
Cdd:cd14225   195 SCYEHQRVYTYIqsrF----YRSPEVILGLPYSMAIDMWSLGCILAELYTGYPLFPGENEVEQLA 255
STKc_MAPK4_6 cd07854
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also ...
264-519 3.62e-16

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: 80.59  E-value: 3.62e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 264 YDIEER------LGSGKFGQVFRLVEKKT-RKVWAGKFFKAYSAKEKENIRqEISIMNCLHHPKLVQCVDAF-------- 328
Cdd:cd07854     1 FDLGSRymdlrpLGCGSNGLVFSAVDSDCdKRVAVKKIVLTDPQSVKHALR-EIKIIRRLDHDNIVKVYEVLgpsgsdlt 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 329 EEKANIVMVLEIVSGGELFE---RIIDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGTRIKLID 405
Cdd:cd07854    80 EDVGSLTELNSVYIVQEYMEtdlANVLEQGPLSEEHARLFMYQLLRGLKYIHSANVLHRDLKPANVF-INTEDLVLKIGD 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 406 FGLARRL----ENAGSLKVLFGTPEFVAPEVInYEPIGY--ATDMWSIGVICYILVSGLSPFMGDND------------- 466
Cdd:cd07854   159 FGLARIVdphySHKGYLSEGLVTKWYRSPRLL-LSPNNYtkAIDMWAAGCIFAEMLTGKPLFAGAHEleqmqlilesvpv 237
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034633499 467 ------NETL----ANVTSATWDFDD---EAFDEISDDAKDFISNLLKKDMKNRLDCTQCLQHPWL 519
Cdd:cd07854   238 vreedrNELLnvipSFVRNDGGEPRRplrDLLPGVNPEALDFLEQILTFNPMDRLTAEEALMHPYM 303
PTKc_Csk_like cd05039
Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
268-450 3.65e-16

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: 78.93  E-value: 3.65e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 268 ERLGSGKFGQVFrLVEKKTRKVwAGKFFKAySAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEIVSGGELF 347
Cdd:cd05039    12 ELIGKGEFGDVM-LGDYRGQKV-AVKCLKD-DSTAAQAFLAEASVMTTLRHPNLVQLLGVVLEGNGLYIVTEYMAKGSLV 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 348 ERIIDEDFELTEREC-IKYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGTrIKLIDFGLARRLE---NAGSLKVlfg 423
Cdd:cd05039    89 DYLRSRGRAVITRKDqLGFALDVCEGMEYLESKKFVHRDLAARNVL-VSEDNV-AKVSDFGLAKEASsnqDGGKLPI--- 163
                         170       180
                  ....*....|....*....|....*..
gi 1034633499 424 tpEFVAPEVINYEPIGYATDMWSIGVI 450
Cdd:cd05039   164 --KWTAPEALREKKFSTKSDVWSFGIL 188
PKc_DYRK2_3 cd14224
Catalytic domain of the protein kinases, Dual-specificity tYrosine-phosphorylated and ...
264-471 3.97e-16

Catalytic domain of the protein kinases, Dual-specificity tYrosine-phosphorylated and -Regulated Kinases 2 and 3; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. This subfamily is composed of DYRK2 and DYRK3, and similar proteins. Drosophila DYRK2 interacts and phosphorylates the chromatin remodelling factor, SNR1 (Snf5-related 1), and also interacts with the essential chromatin component, trithorax. It may play a role in chromatin remodelling. Vertebrate DYRK2 phosphorylates and regulates the tumor suppressor p53 to induce apoptosis in response to DNA damage. It can also phosphorylate the transcription factor, nuclear factor of activated T cells (NFAT). DYRK2 is overexpressed in lung adenocarcinoma and esophageal carcinomas, and is a predictor for favorable prognosis in lung adenocarcinoma. DYRK3, also called regulatory erythroid kinase (REDK), is highly expressed in erythroid cells and the testis, and is also present in adult kidney and liver. It promotes cell survival by phosphorylating and activating SIRT1, an NAD(+)-dependent protein deacetylase, which promotes p53 deacetylation, resulting in the inhibition of apoptosis. DYRKs autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. The DYRK2/3 subfamily is part of a larger superfamily that includes the catalytic domains of other S/T kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271126 [Multi-domain]  Cd Length: 380  Bit Score: 80.95  E-value: 3.97e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 264 YDIEERLGSGKFGQVFRLVEKKTRKVWAGKFFKaysaKEKENIRQ---EISImncLHHPK---------LVQCVDAFEEK 331
Cdd:cd14224    67 YEVLKVIGKGSFGQVVKAYDHKTHQHVALKMVR----NEKRFHRQaaeEIRI---LEHLKkqdkdntmnVIHMLESFTFR 139
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 332 ANIVMVLEIVSGgELFERIIDEDFELTERECI-KYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKTGTRIKLIDFGlAR 410
Cdd:cd14224   140 NHICMTFELLSM-NLYELIKKNKFQGFSLQLVrKFAHSILQCLDALHRNKIIHCDLKPENILLKQQGRSGIKVIDFG-SS 217
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034633499 411 RLENAgSLKVLFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLA 471
Cdd:cd14224   218 CYEHQ-RIYTYIQSRFYRAPEVILGARYGMPIDMWSFGCILAELLTGYPLFPGEDEGDQLA 277
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
608-686 4.72e-16

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 73.37  E-value: 4.72e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034633499 608 KPYFSKTIRDLEVVEGSAARFDCKIEGYPDPEVVWFKDDQSIRESRHfQIDYDEDGNCSLIISDVCGDDDAKYTCKAVN 686
Cdd:pfam13927   1 KPVITVSPSSVTVREGETVTLTCEATGSPPPTITWYKNGEPISSGST-RSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
270-407 5.69e-16

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: 75.17  E-value: 5.69e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 270 LGSGKFGQVFRLVEKKTRKVWAGKFFKAYSAKEKENIRQEISIMNCL--HHPKLVQCVDAFEEKANIVMVLEIVSGGELF 347
Cdd:cd13968     1 MGEGASAKVFWAEGECTTIGVAVKIGDDVNNEEGEDLESEMDILRRLkgLELNIPKVLVTEDVDGPNILLMELVKGGTLI 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 348 ERIIDEdfELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGTrIKLIDFG 407
Cdd:cd13968    81 AYTQEE--ELDEKDVESIMYQLAECMRLLHSFHLIHRDLNNDNIL-LSEDGN-VKLIDFG 136
STKc_CK1 cd14016
Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the ...
264-425 5.90e-16

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


Pssm-ID: 270918 [Multi-domain]  Cd Length: 266  Bit Score: 78.65  E-value: 5.90e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 264 YDIEERLGSGKFGQVFRLVEKKTRKVWAGKFFKaySAKEKENIRQEISIMNCLHH----PKLVQCvdaFEEKANIVMVLE 339
Cdd:cd14016     2 YKLVKKIGSGSFGEVYLGIDLKTGEEVAIKIEK--KDSKHPQLEYEAKVYKLLQGgpgiPRLYWF---GQEGDYNVMVMD 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 340 IVsGGELferiidED-FELTERE-CIKY----MRQISEGVEYIHKQGIVHLDLKPENIMC-VNKTGTRIKLIDFGLARRL 412
Cdd:cd14016    77 LL-GPSL------EDlFNKCGRKfSLKTvlmlADQMISRLEYLHSKGYIHRDIKPENFLMgLGKNSNKVYLIDFGLAKKY 149
                         170       180
                  ....*....|....*....|.
gi 1034633499 413 ENAGSL--------KVLFGTP 425
Cdd:cd14016   150 RDPRTGkhipyregKSLTGTA 170
STKc_HIPK cd14211
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase; STKs ...
264-450 7.07e-16

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: 79.41  E-value: 7.07e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 264 YDIEERLGSGKFGQVFRLVEKKTRKVWAGKFFKAYSAKEKEnIRQEISIMNCLHHPK-----LVQCVDAFEEKANIVMVL 338
Cdd:cd14211     1 YEVLEFLGRGTFGQVVKCWKRGTNEIVAIKILKNHPSYARQ-GQIEVSILSRLSQENadefnFVRAYECFQHKNHTCLVF 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 339 EIVSGgELFERIIDEDFELTERECIK-YMRQISEGVEYIHKQGIVHLDLKPENIMCVNKTGT--RIKLIDFGLARRLENA 415
Cdd:cd14211    80 EMLEQ-NLYDFLKQNKFSPLPLKYIRpILQQVLTALLKLKSLGLIHADLKPENIMLVDPVRQpyRVKVIDFGSASHVSKA 158
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1034633499 416 GSLKVLfGTPEFVAPEVINYEPIGYATDMWSIGVI 450
Cdd:cd14211   159 VCSTYL-QSRYYRAPEIILGLPFCEAIDMWSLGCV 192
STKc_GRK3 cd05633
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs ...
264-510 7.15e-16

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK3, also called beta-adrenergic receptor kinase 2 (beta-ARK2), is widely expressed in many tissues. It is involved in modulating the cholinergic response of airway smooth muscles, and also plays a role in dopamine receptor regulation. GRK3-deficient mice show a lack of olfactory receptor desensitization and altered regulation of the M2 muscarinic airway. GRK3 promoter polymorphisms may also be associated with bipolar disorder. GRK3 contains an N-terminal RGS homology (RH) domain, a central catalytic domain, and C-terminal pleckstrin homology (PH) domain that mediates PIP2 and G protein betagamma-subunit translocation to the membrane. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270781 [Multi-domain]  Cd Length: 346  Bit Score: 79.72  E-value: 7.15e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 264 YDIEERLGSGKFGQVFRLVEKKTRKVWAGKFFKAYSAKEKE------NIRQEISIMNCLHHPKLVQCVDAFEEKANIVMV 337
Cdd:cd05633     7 FSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQgetlalNERIMLSLVSTGDCPFIVCMTYAFHTPDKLCFI 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 338 LEIVSGGELFERIIDEDFeLTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKTGTRIKliDFGLARRLENAGS 417
Cdd:cd05633    87 LDLMNGGDLHYHLSQHGV-FSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHVRIS--DLGLACDFSKKKP 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 418 lKVLFGTPEFVAPEVINyEPIGY--ATDMWSIGVICYILVSGLSPFMgDNDNETLANVTSATWDFDDEAFDEISDDAKDF 495
Cdd:cd05633   164 -HASVGTHGYMAPEVLQ-KGTAYdsSADWFSLGCMLFKLLRGHSPFR-QHKTKDKHEIDRMTLTVNVELPDSFSPELKSL 240
                         250
                  ....*....|....*
gi 1034633499 496 ISNLLKKDMKNRLDC 510
Cdd:cd05633   241 LEGLLQRDVSKRLGC 255
STKc_LATS2 cd05626
Catalytic domain of the Protein Serine/Threonine Kinase, Large Tumor Suppressor 2; STKs ...
270-499 7.67e-16

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


Pssm-ID: 173715 [Multi-domain]  Cd Length: 381  Bit Score: 80.06  E-value: 7.67e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 270 LGSGKFGQVFRLVEKKTRKVWAGKFFK---AYSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEIVSGGEL 346
Cdd:cd05626     9 LGIGAFGEVCLACKVDTHALYAMKTLRkkdVLNRNQVAHVKAERDILAEADNEWVVKLYYSFQDKDNLYFVMDYIPGGDM 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 347 FERIIDEDFeLTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGtRIKLIDFGL------------------ 408
Cdd:cd05626    89 MSLLIRMEV-FPEVLARFYIAELTLAIESVHKMGFIHRDIKPDNIL-IDLDG-HIKLTDFGLctgfrwthnskyyqkgsh 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 409 ------------------------------ARRLENAGSLKVLFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGL 458
Cdd:cd05626   166 irqdsmepsdlwddvsncrcgdrlktleqrATKQHQRCLAHSLVGTPNYIAPEVLLRKGYTQLCDWWSVGVILFEMLVGQ 245
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1034633499 459 SPFMGDNDNETLANVTSATWDFDDEAFDEISDDAKDFISNL 499
Cdd:cd05626   246 PPFLAPTPTETQLKVINWENTLHIPPQVKLSPEAVDLITKL 286
STKc_LIMK2 cd14222
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the ...
270-454 7.92e-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: 78.45  E-value: 7.92e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 270 LGSGKFGQVFRLVEKKTRKVWAGKFFKAYSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEIVSGGELFER 349
Cdd:cd14222     1 LGKGFFGQAIKVTHKATGKVMVMKELIRCDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKRLNLLTEFIEGGTLKDF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 350 IIDEDFeLTERECIKYMRQISEGVEYIHKQGIVHLDLKPENimCVNKTGTRIKLIDFGLARRL---------ENAGSLKV 420
Cdd:cd14222    81 LRADDP-FPWQQKVSFAKGIASGMAYLHSMSIIHRDLNSHN--CLIKLDKTVVVADFGLSRLIveekkkpppDKPTTKKR 157
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1034633499 421 LF------------GTPEFVAPEVINYEPIGYATDMWSIG-VICYIL 454
Cdd:cd14222   158 TLrkndrkkrytvvGNPYWMAPEMLNGKSYDEKVDIFSFGiVLCEII 204
STKc_ERK1_2_like cd07849
Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine ...
260-538 1.01e-15

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


Pssm-ID: 270839 [Multi-domain]  Cd Length: 336  Bit Score: 78.89  E-value: 1.01e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 260 VSDFYDIEERLGSGKFGQVFRLVEKKTRKVWAgkfFKAYSAKEKENIRQ----EISIMNCLHHPKL-----VQCVDAFEE 330
Cdd:cd07849     3 VGPRYQNLSYIGEGAYGMVCSAVHKPTGQKVA---IKKISPFEHQTYCLrtlrEIKILLRFKHENIigildIQRPPTFES 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 331 KANIVMVLEIVSGgELFERIIDEDfeLTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTgTRIKLIDFGLAR 410
Cdd:cd07849    80 FKDVYIVQELMET-DLYKLIKTQH--LSNDHIQYFLYQILRGLKYIHSANVLHRDLKPSNLL-LNTN-CDLKICDFGLAR 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 411 ----RLENAGSLKVLFGTPEFVAPEV-INYEPIGYATDMWSIGVICYILVSGL--------------------SPFMGDN 465
Cdd:cd07849   155 iadpEHDHTGFLTEYVATRWYRAPEImLNSKGYTKAIDIWSVGCILAEMLSNRplfpgkdylhqlnlilgilgTPSQEDL 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 466 DN----------ETLANVTSATWdfdDEAFDEISDDAKDFISNLLKKDMKNRLDCTQCLQHPWL-------------MKD 522
Cdd:cd07849   235 NCiislkarnyiKSLPFKPKVPW---NKLFPNADPKALDLLDKMLTFNPHKRITVEEALAHPYLeqyhdpsdepvaeEPF 311
                         330
                  ....*....|....*..
gi 1034633499 523 TKNMEAK-KLSKDRMKK 538
Cdd:cd07849   312 PFDMELFdDLPKEKLKE 328
IgI_1_Titin_Z1z2-like cd20974
First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and ...
609-699 1.03e-15

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


Pssm-ID: 409566 [Multi-domain]  Cd Length: 93  Bit Score: 72.77  E-value: 1.03e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 609 PYFSKTIRDLEVVEGSAARFDCKIEGYPDPEVVWFKDDQSIRESR--HFQIDYdEDGNCSLIISDVCGDDDAKYTCKAVN 686
Cdd:cd20974     1 PVFTQPLQSVVVLEGSTATFEAHVSGKPVPEVSWFRDGQVISTSTlpGVQISF-SDGRAKLSIPAVTKANSGRYSLTATN 79
                          90
                  ....*....|...
gi 1034633499 687 SLGEATCTAELIV 699
Cdd:cd20974    80 GSGQATSTAELLV 92
PTKc_Itk cd05112
Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs ...
268-475 1.19e-15

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: 77.30  E-value: 1.19e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 268 ERLGSGKFGQVFRLVEKKTRKVwAGKFFKAySAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEIVSGGELF 347
Cdd:cd05112    10 QEIGSGQFGLVHLGYWLNKDKV-AIKTIRE-GAMSEEDFIEEAEVMMKLSHPKLVQLYGVCLEQAPICLVFEFMEHGCLS 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 348 ERIIDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENimCVNKTGTRIKLIDFGLARRL---ENAGSLKVLFGT 424
Cdd:cd05112    88 DYLRTQRGLFSAETLLGMCLDVCEGMAYLEEASVIHRDLAARN--CLVGENQVVKVSDFGMTRFVlddQYTSSTGTKFPV 165
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1034633499 425 pEFVAPEVINYEPIGYATDMWSIGVICYILVS-GLSPFMGDNDNETLANVTS 475
Cdd:cd05112   166 -KWSSPEVFSFSRYSSKSDVWSFGVLMWEVFSeGKIPYENRSNSEVVEDINA 216
STKc_CDK9 cd07865
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs ...
264-518 1.30e-15

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: 78.18  E-value: 1.30e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 264 YDIEERLGSGKFGQVFRLVEKKTRKVWAGKFFKAYSAKEKENIR--QEISIMNCLHHPKLVQCVDAFEEKAN-------- 333
Cdd:cd07865    14 YEKLAKIGQGTFGEVFKARHRKTGQIVALKKVLMENEKEGFPITalREIKILQLLKHENVVNLIEICRTKATpynrykgs 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 334 IVMVLEIVS---GGELFERIIDedFELTErecIK-YMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGTrIKLIDFGLA 409
Cdd:cd07865    94 IYLVFEFCEhdlAGLLSNKNVK--FTLSE---IKkVMKMLLNGLYYIHRNKILHRDMKAANIL-ITKDGV-LKLADFGLA 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 410 RRL-------ENAGSLKVLfgTPEFVAPEVI----NYEPigyATDMWSIGVICYILVSgLSPFM-GDNDNETLA------ 471
Cdd:cd07865   167 RAFslaknsqPNRYTNRVV--TLWYRPPELLlgerDYGP---PIDMWGAGCIMAEMWT-RSPIMqGNTEQHQLTlisqlc 240
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034633499 472 -NVTSATW-DFDD-EAFDEI-------------------SDDAKDFISNLLKKDMKNRLDCTQCLQHPW 518
Cdd:cd07865   241 gSITPEVWpGVDKlELFKKMelpqgqkrkvkerlkpyvkDPYALDLIDKLLVLDPAKRIDADTALNHDF 309
STKc_C-Raf cd14149
Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) ...
266-470 1.44e-15

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: 77.76  E-value: 1.44e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 266 IEERLGSGKFGQVFRlveKKTRKVWAGKFFKAY--SAKEKENIRQEISIMNCLHHPKLVQCVdAFEEKANIVMVLEIVSG 343
Cdd:cd14149    16 LSTRIGSGSFGTVYK---GKWHGDVAVKILKVVdpTPEQFQAFRNEVAVLRKTRHVNILLFM-GYMTKDNLAIVTQWCEG 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 344 GELFERIIDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCvnKTGTRIKLIDFGLA---RRLENAGSLKV 420
Cdd:cd14149    92 SSLYKHLHVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFL--HEGLTVKIGDFGLAtvkSRWSGSQQVEQ 169
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1034633499 421 LFGTPEFVAPEVINYE---PIGYATDMWSIGVICYILVSGLSPFMGDNDNETL 470
Cdd:cd14149   170 PTGSILWMAPEVIRMQdnnPFSFQSDVYSYGIVLYELMTGELPYSHINNRDQI 222
STKc_MAP3K8 cd13995
Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) ...
273-462 1.52e-15

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: 76.97  E-value: 1.52e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 273 GKFGQVFRLVEKKTRKVWAGKFFKAYSAKEkenirQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEIVSGGELFERIiD 352
Cdd:cd13995    15 GAFGKVYLAQDTKTKKRMACKLIPVEQFKP-----SDVEIQACFRHENIAELYGALLWEETVHLFMEAGEGGSVLEKL-E 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 353 EDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNktgTRIKLIDFGLARRL-ENAGSLKVLFGTPEFVAPE 431
Cdd:cd13995    89 SCGPMREFEIIWVTKHVLKGLDFLHSKNIIHHDIKPSNIVFMS---TKAVLVDFGLSVQMtEDVYVPKDLRGTEIYMSPE 165
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1034633499 432 VINYEPIGYATDMWSIGVICYILVSGLSPFM 462
Cdd:cd13995   166 VILCRGHNTKADIYSLGATIIHMQTGSPPWV 196
STKc_TAK1 cd14058
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated ...
270-461 1.79e-15

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: 76.71  E-value: 1.79e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 270 LGSGKFGQVFRLVEKKtrKVWAGKFFKAYSakEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEIVSGGELFER 349
Cdd:cd14058     1 VGRGSFGVVCKARWRN--QIVAVKIIESES--EKKAFEVEVRQLSRVDHPNIIKLYGACSNQKPVCLVMEYAEGGSLYNV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 350 I--IDEDFELTERECIKYMRQISEGVEYIHK---QGIVHLDLKPENIMCVNKtGTRIKLIDFGLARRLENagSLKVLFGT 424
Cdd:cd14058    77 LhgKEPKPIYTAAHAMSWALQCAKGVAYLHSmkpKALIHRDLKPPNLLLTNG-GTVLKICDFGTACDIST--HMTNNKGS 153
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1034633499 425 PEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPF 461
Cdd:cd14058   154 AAWMAPEVFEGSKYSEKCDVFSWGIILWEVITRRKPF 190
STKc_TAO1 cd06635
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze ...
243-563 2.31e-15

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: 77.78  E-value: 2.31e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 243 KEPEVDYRTVTINTEQKVSDFYDIeerlGSGKFGQVFRLVEKKTRKVWAGKFFkAYSAKEK----ENIRQEISIMNCLHH 318
Cdd:cd06635    10 KDPDIAELFFKEDPEKLFSDLREI----GHGSFGAVYFARDVRTSEVVAIKKM-SYSGKQSnekwQDIIKEVKFLQRIKH 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 319 PKLVQCVDAF--EEKANIVMVLEIVSGGELFERiidEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMcVNK 396
Cdd:cd06635    85 PNSIEYKGCYlrEHTAWLVMEYCLGSASDLLEV---HKKPLQEIEIAAITHGALQGLAYLHSHNMIHRDIKAGNIL-LTE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 397 TGtRIKLIDFGLARRLENAGSlkvLFGTPEFVAPEVINYEPIGY---ATDMWSIGVICYILVSGLSPFMGDNDNETLANV 473
Cdd:cd06635   161 PG-QVKLADFGSASIASPANS---FVGTPYWMAPEVILAMDEGQydgKVDVWSLGITCIELAERKPPLFNMNAMSALYHI 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 474 tsATWDFDDEAFDEISDDAKDFISNLLKKDMKNRLDCTQCLQHPWLMKDTKNMEAKKLSkdrmkkymarrkwQKTGNAVR 553
Cdd:cd06635   237 --AQNESPTLQSNEWSDYFRNFVDSCLQKIPQDRPTSEELLKHMFVLRERPETVLIDLI-------------QRTKDAVR 301
                         330
                  ....*....|
gi 1034633499 554 AIGRLSSMAM 563
Cdd:cd06635   302 ELDNLQYRKM 311
PTKc_Btk_Bmx cd05113
Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow ...
270-475 2.67e-15

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: 76.46  E-value: 2.67e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 270 LGSGKFGqVFRLVEKKTRKVWAGKFFKAYSAKEKENIrQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEIVSGGELFER 349
Cdd:cd05113    12 LGTGQFG-VVKYGKWRGQYDVAIKMIKEGSMSEDEFI-EEAKVMMNLSHEKLVQLYGVCTKQRPIFIITEYMANGCLLNY 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 350 IIDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGTrIKLIDFGLARRL---ENAGSLKVLFGTpE 426
Cdd:cd05113    90 LREMRKRFQTQQLLEMCKDVCEAMEYLESKQFLHRDLAARNCL-VNDQGV-VKVSDFGLSRYVlddEYTSSVGSKFPV-R 166
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1034633499 427 FVAPEVINYEPIGYATDMWSIGVICYILVS-GLSPFMGDNDNETLANVTS 475
Cdd:cd05113   167 WSPPEVLMYSKFSSKSDVWAFGVLMWEVYSlGKMPYERFTNSETVEHVSQ 216
STKc_B-Raf cd14151
Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) ...
268-470 3.06e-15

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: 76.64  E-value: 3.06e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 268 ERLGSGKFGQVFRlvekktrKVWAGKF------FKAYSAKEKENIRQEISIMNCLHHPKLVQCVdAFEEKANIVMVLEIV 341
Cdd:cd14151    14 QRIGSGSFGTVYK-------GKWHGDVavkmlnVTAPTPQQLQAFKNEVGVLRKTRHVNILLFM-GYSTKPQLAIVTQWC 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 342 SGGELFER--IIDEDFELteRECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCvnKTGTRIKLIDFGLA---RRLENAG 416
Cdd:cd14151    86 EGSSLYHHlhIIETKFEM--IKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFL--HEDLTVKIGDFGLAtvkSRWSGSH 161
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1034633499 417 SLKVLFGTPEFVAPEVINYE---PIGYATDMWSIGVICYILVSGLSPFMGDNDNETL 470
Cdd:cd14151   162 QFEQLSGSILWMAPEVIRMQdknPYSFQSDVYAFGIVLYELMTGQLPYSNINNRDQI 218
PTKc_Jak2_rpt2 cd14205
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the ...
268-456 3.26e-15

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: 76.59  E-value: 3.26e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 268 ERLGSGKFGQV----FRLVEKKTRKVWAGKFFKAYSAKEKENIRQEISIMNCLHHPKLVQ----CVDAfeEKANIVMVLE 339
Cdd:cd14205    10 QQLGKGNFGSVemcrYDPLQDNTGEVVAVKKLQHSTEEHLRDFEREIEILKSLQHDNIVKykgvCYSA--GRRNLRLIME 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 340 IVSGGELFERIIDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKtgTRIKLIDFGLARRL---ENAG 416
Cdd:cd14205    88 YLPYGSLRDYLQKHKERIDHIKLLQYTSQICKGMEYLGTKRYIHRDLATRNILVENE--NRVKIGDFGLTKVLpqdKEYY 165
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1034633499 417 SLKVLFGTPEF-VAPEVINYEPIGYATDMWSIGVICYILVS 456
Cdd:cd14205   166 KVKEPGESPIFwYAPESLTESKFSVASDVWSFGVVLYELFT 206
STKc_TDY_MAPK cd07859
Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; ...
264-503 4.58e-15

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: 77.13  E-value: 4.58e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 264 YDIEERLGSGKFGQVFRLVEKKTR-KVWAGKFFKAYS-AKEKENIRQEISIMNCLHHPKLVQCVDAF-----EEKANIVM 336
Cdd:cd07859     2 YKIQEVIGKGSYGVVCSAIDTHTGeKVAIKKINDVFEhVSDATRILREIKLLRLLRHPDIVEIKHIMlppsrREFKDIYV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 337 VLEIVSGGelFERIIDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCvnKTGTRIKLIDFGLARRLENAG 416
Cdd:cd07859    82 VFELMESD--LHQVIKANDDLTPEHHQFFLYQLLRALKYIHTANVFHRDLKPKNILA--NADCKLKICDFGLARVAFNDT 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 417 SLKVLF----GTPEFVAPEVI-----NYEPigyATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDFDDEAFDE 487
Cdd:cd07859   158 PTAIFWtdyvATRWYRAPELCgsffsKYTP---AIDIWSIGCIFAEVLTGKPLFPGKNVVHQLDLITDLLGTPSPETISR 234
                         250
                  ....*....|....*..
gi 1034633499 488 ISDD-AKDFISNLLKKD 503
Cdd:cd07859   235 VRNEkARRYLSSMRKKQ 251
STKc_PFTAIRE1 cd07869
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer ...
261-519 4.72e-15

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: 76.66  E-value: 4.72e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 261 SDFYDIEERLGSGKFGQVFRLVEKKTRKVWAgkfFKAYSAKEKENIR----QEISIMNCLHHPKLVQCVDAFEEKANIVM 336
Cdd:cd07869     4 ADSYEKLEKLGEGSYATVYKGKSKVNGKLVA---LKVIRLQEEEGTPftaiREASLLKGLKHANIVLLHDIIHTKETLTL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 337 VLEIVSGgELFERIIDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGtRIKLIDFGLARrlenAG 416
Cdd:cd07869    81 VFEYVHT-DLCQYMDKHPGGLHPENVKLFLFQLLRGLSYIHQRYILHRDLKPQNLL-ISDTG-ELKLADFGLAR----AK 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 417 SLKVLFGTPEFVA----PEVINYEPIGYAT--DMWSIGVICYILVSGLSPFMGDNDNE--------TLANVTSATW---- 478
Cdd:cd07869   154 SVPSHTYSNEVVTlwyrPPDVLLGSTEYSTclDMWGVGCIFVEMIQGVAAFPGMKDIQdqleriflVLGTPNEDTWpgvh 233
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1034633499 479 ---DFDDEAFDEIS--------------DDAKDFISNLLKKDMKNRLDCTQCLQHPWL 519
Cdd:cd07869   234 slpHFKPERFTLYSpknlrqawnklsyvNHAEDLASKLLQCFPKNRLSAQAALSHEYF 291
PTKc_Wee1a cd14138
Catalytic domain of the Protein Tyrosine Kinase, Wee1a; PTKs catalyze the transfer of the ...
261-466 7.56e-15

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


Pssm-ID: 271040 [Multi-domain]  Cd Length: 276  Bit Score: 75.44  E-value: 7.56e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 261 SDFYDIEeRLGSGKFGQVFRLVEKKTRKVWAGKFFK---AYSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMV 337
Cdd:cd14138     5 TEFHELE-KIGSGEFGSVFKCVKRLDGCIYAIKRSKkplAGSVDEQNALREVYAHAVLGQHSHVVRYYSAWAEDDHMLIQ 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 338 LEIVSGGELFErIIDEDFE----LTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKT---------------G 398
Cdd:cd14138    84 NEYCNGGSLAD-AISENYRimsyFTEPELKDLLLQVARGLKYIHSMSLVHMDIKPSNIFISRTSipnaaseegdedewaS 162
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034633499 399 TRI--KLIDFGLARRLENAgslKVLFGTPEFVAPEVI--NYEPIGYAtDMWSIG--VICyilVSGLSPFMGDND 466
Cdd:cd14138   163 NKVifKIGDLGHVTRVSSP---QVEEGDSRFLANEVLqeNYTHLPKA-DIFALAltVVC---AAGAEPLPTNGD 229
PKc_DYRK1 cd14226
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
258-471 8.00e-15

Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and -Regulated Kinase 1; 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. Mammals contain two types of DYRK1 proteins, DYRK1A and DYRK1B. DYRK1A was previously called minibrain kinase homolog (MNBH) or dual-specificity YAK1-related kinase. It phosphorylates various substrates and is involved in many cellular events. It phosphorylates and inhibits the transcription factors, nuclear factor of activated T cells (NFAT) and forkhead in rhabdomyosarcoma (FKHR). It regulates neuronal differentiation by targetting CREB (cAMP response element-binding protein). It also targets many endocytic proteins including dynamin and amphiphysin and may play a role in the endocytic pathway. The gene encoding DYRK1A is located in the DSCR (Down syndrome critical region) of human chromosome 21 and DYRK1A has been implicated in the pathogenesis of DS. DYRK1B, also called minibrain-related kinase (MIRK), is highly expressed in muscle and plays a critical role in muscle differentiation by regulating transcription, cell motility, survival, and cell cycle progression. It is overexpressed in many solid tumors where it acts as a tumor survival factor. DYRKs autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. The DYRK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271128 [Multi-domain]  Cd Length: 339  Bit Score: 76.20  E-value: 8.00e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 258 QKVSDFYDIEERLGSGKFGQVFRLVEKKTRKVWAGKFFK---AYSAKEKENIRQeISIMNclHHP-----KLVQCVDAFE 329
Cdd:cd14226     9 EKWMDRYEIDSLIGKGSFGQVVKAYDHVEQEWVAIKIIKnkkAFLNQAQIEVRL-LELMN--KHDtenkyYIVRLKRHFM 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 330 EKANIVMVLEIVSGgELFERIIDEDFE-----LTEreciKYMRQISEGVEYIHKQ--GIVHLDLKPENIMCVNKTGTRIK 402
Cdd:cd14226    86 FRNHLCLVFELLSY-NLYDLLRNTNFRgvslnLTR----KFAQQLCTALLFLSTPelSIIHCDLKPENILLCNPKRSAIK 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034633499 403 LIDFGLARRLENA--GSLKVLFgtpeFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLA 471
Cdd:cd14226   161 IIDFGSSCQLGQRiyQYIQSRF----YRSPEVLLGLPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMN 227
PTKc_Abl cd05052
Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase; PTKs catalyze the transfer of ...
266-463 8.15e-15

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: 75.15  E-value: 8.15e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 266 IEERLGSGKFGQVFRLVEKKTRKVWAGKFFKAYSAKEKENIRqEISIMNCLHHPKLVQCVDAFEEKANIVMVLEIVSGGE 345
Cdd:cd05052    10 MKHKLGGGQYGEVYEGVWKKYNLTVAVKTLKEDTMEVEEFLK-EAAVMKEIKHPNLVQLLGVCTREPPFYIITEFMPYGN 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 346 LFERIIDEDFELTERECIKYM-RQISEGVEYIHKQGIVHLDLKPENimCVNKTGTRIKLIDFGLARRLEN------AGSL 418
Cdd:cd05052    89 LLDYLRECNREELNAVVLLYMaTQIASAMEYLEKKNFIHRDLAARN--CLVGENHLVKVADFGLSRLMTGdtytahAGAK 166
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1034633499 419 KVLfgtpEFVAPEVINYEPIGYATDMWSIGVICY-ILVSGLSPFMG 463
Cdd:cd05052   167 FPI----KWTAPESLAYNKFSIKSDVWAFGVLLWeIATYGMSPYPG 208
PTKc_Jak_rpt2 cd05038
Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily ...
270-456 8.70e-15

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


Pssm-ID: 270634 [Multi-domain]  Cd Length: 284  Bit Score: 75.50  E-value: 8.70e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 270 LGSGKFGQV----FRLVEKKTRKVWAGKFFKAySAKEK--ENIRQEISIMNCLHHPKLVQ----CVDAFEEKANIVMvlE 339
Cdd:cd05038    12 LGEGHFGSVelcrYDPLGDNTGEQVAVKSLQP-SGEEQhmSDFKREIEILRTLDHEYIVKykgvCESPGRRSLRLIM--E 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 340 IVSGGELFERIIDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKtgTRIKLIDFGLARRL-ENAGSL 418
Cdd:cd05038    89 YLPSGSLRDYLQRHRDQIDLKRLLLFASQICKGMEYLGSQRYIHRDLAARNILVESE--DLVKISDFGLAKVLpEDKEYY 166
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1034633499 419 KV--LFGTPEF-VAPEVINYEPIGYATDMWSIGVICYILVS 456
Cdd:cd05038   167 YVkePGESPIFwYAPECLRESRFSSASDVWSFGVTLYELFT 207
STKc_GRK2 cd14223
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs ...
264-510 1.09e-14

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: 75.85  E-value: 1.09e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 264 YDIEERLGSGKFGQVFRLVEKKTRKVWAGKFFKAYSAKEKE------NIRQEISIMNCLHHPKLVQCVDAFEEKANIVMV 337
Cdd:cd14223     2 FSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQgetlalNERIMLSLVSTGDCPFIVCMSYAFHTPDKLSFI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 338 LEIVSGGELFERIIDEDFeLTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGtRIKLIDFGLARRLENAGS 417
Cdd:cd14223    82 LDLMNGGDLHYHLSQHGV-FSEAEMRFYAAEIILGLEHMHSRFVVYRDLKPANIL-LDEFG-HVRISDLGLACDFSKKKP 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 418 lKVLFGTPEFVAPEVINyEPIGY--ATDMWSIGVICYILVSGLSPFMgDNDNETLANVTSATWDFDDEAFDEISDDAKDF 495
Cdd:cd14223   159 -HASVGTHGYMAPEVLQ-KGVAYdsSADWFSLGCMLFKLLRGHSPFR-QHKTKDKHEIDRMTLTMAVELPDSFSPELRSL 235
                         250
                  ....*....|....*
gi 1034633499 496 ISNLLKKDMKNRLDC 510
Cdd:cd14223   236 LEGLLQRDVNRRLGC 250
PTKc_Ack_like cd05040
Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs ...
268-473 1.11e-14

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: 74.69  E-value: 1.11e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 268 ERLGSGKFGQVFRLV----EKKTRKVwAGKFFKAYSAKEKENI---RQEISIMNCLHHPKLVQCVDAFEEKAnIVMVLEI 340
Cdd:cd05040     1 EKLGDGSFGVVRRGEwttpSGKVIQV-AVKCLKSDVLSQPNAMddfLKEVNAMHSLDHPNLIRLYGVVLSSP-LMMVTEL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 341 VSGGELFERIIDE-DFELTERECiKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKtgTRIKLIDFGLARRLEN----- 414
Cdd:cd05040    79 APLGSLLDRLRKDqGHFLISTLC-DYAVQIANGMAYLESKRFIHRDLAARNILLASK--DKVKIGDFGLMRALPQnedhy 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034633499 415 --AGSLKVLFGtpeFVAPEVINYEPIGYATDMWSIGVICYILVS-GLSPFMGDNDNETLANV 473
Cdd:cd05040   156 vmQEHRKVPFA---WCAPESLKTRKFSHASDVWMFGVTLWEMFTyGEEPWLGLNGSQILEKI 214
PTKc_Ror2 cd05091
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
268-470 1.19e-14

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: 75.05  E-value: 1.19e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 268 ERLGSGKFGQVFR------LVEKKTRKVWAGKFFKAYSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEIV 341
Cdd:cd05091    12 EELGEDRFGKVYKghlfgtAPGEQTQAVAIKTLKDKAEGPLREEFRHEAMLRSRLQHPNIVCLLGVVTKEQPMSMIFSYC 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 342 SGGELFERII-----------DED----FELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKTGtrIKLIDF 406
Cdd:cd05091    92 SHGDLHEFLVmrsphsdvgstDDDktvkSTLEPADFLHIVTQIAAGMEYLSSHHVVHKDLATRNVLVFDKLN--VKISDL 169
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034633499 407 GLARRLENAGSLKVLFGTP---EFVAPEVINYEPIGYATDMWSIGVICYILVS-GLSPFMGDNDNETL 470
Cdd:cd05091   170 GLFREVYAADYYKLMGNSLlpiRWMSPEAIMYGKFSIDSDIWSYGVVLWEVFSyGLQPYCGYSNQDVI 237
PK_TRB2 cd14022
Pseudokinase domain of Tribbles Homolog 2; The pseudokinase domain shows similarity to protein ...
327-519 1.19e-14

Pseudokinase domain of Tribbles Homolog 2; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. TRB2 binds and negatively regulates the mitogen activated protein kinase (MAPK) kinases, MKK7 and MEK1, which are activators of the MAPKs, ERK and JNK. It controls the activation of inflammatory monocytes, which is essential in innate immune responses and the pathogenesis of inflammatory diseases such as atherosclerosis. TRB2 expression is down-regulated in human acute myeloid leukaemia (AML), which may lead to enhanced cell survival and pathogenesis of the disease. TRB2 is one of three Tribbles Homolog (TRB) proteins present in vertebrates that are encoded by three separate genes. TRB proteins interact with many proteins involved in signalling pathways. They play scaffold-like regulatory functions and affect many cellular processes such as mitosis, apoptosis, and gene expression. The TRB2 subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270924 [Multi-domain]  Cd Length: 242  Bit Score: 74.30  E-value: 1.19e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 327 AFEEKANIVMVLEIVSGGE----LFER-------IIDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVN 395
Cdd:cd14022    40 CLPAHSNINQITEIILGETkayvFFERsygdmhsFVRTCKKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFVFKD 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 396 KTGTRIKLidfglaRRLENA-------GSLKVLFGTPEFVAPEVIN----YEpiGYATDMWSIGVICYILVSGLSPFMGD 464
Cdd:cd14022   120 EERTRVKL------ESLEDAyilrghdDSLSDKHGCPAYVSPEILNtsgsYS--GKAADVWSLGVMLYTMLVGRYPFHDI 191
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1034633499 465 NDNETLANVTSATWDFDdeafDEISDDAKDFISNLLKKDMKNRLDCTQCLQHPWL 519
Cdd:cd14022   192 EPSSLFSKIRRGQFNIP----ETLSPKAKCLIRSILRREPSERLTSQEILDHPWF 242
PTKc_Trk cd05049
Catalytic domain of the Protein Tyrosine Kinases, Tropomyosin Related Kinases; PTKs catalyze ...
268-477 1.46e-14

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: 74.81  E-value: 1.46e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 268 ERLGSGKFGQVFR-----LVEKKTRKVWAGKFFK-AYSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEIV 341
Cdd:cd05049    11 RELGEGAFGKVFLgecynLEPEQDKMLVAVKTLKdASSPDARKDFEREAELLTNLQHENIVKFYGVCTEGDPLLMVFEYM 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 342 SGGEL--FERIIDED-----------FELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENimCVNKTGTRIKLIDFGL 408
Cdd:cd05049    91 EHGDLnkFLRSHGPDaaflasedsapGELTLSQLLHIAVQIASGMVYLASQHFVHRDLATRN--CLVGTNLVVKIGDFGM 168
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034633499 409 AR--------RLENAGSLKVlfgtpEFVAPEVINYEPIGYATDMWSIGVICY-ILVSGLSPFMGDNDNETLANVTSAT 477
Cdd:cd05049   169 SRdiystdyyRVGGHTMLPI-----RWMPPESILYRKFTTESDVWSFGVVLWeIFTYGKQPWFQLSNTEVIECITQGR 241
fn3 pfam00041
Fibronectin type III domain;
133-216 1.60e-14

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 69.37  E-value: 1.60e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 133 PPAGTPCASDIRSSSLTLSWYGSSyDGGSAVQSYSIEIWD-SANKTWKELATCRST-SFNVQDLLPDHEYKFRVRAINVY 210
Cdd:pfam00041   1 SAPSNLTVTDVTSTSLTVSWTPPP-DGNGPITGYEVEYRPkNSGEPWNEITVPGTTtSVTLTGLKPGTEYEVRVQAVNGG 79

                  ....*.
gi 1034633499 211 GTSEPS 216
Cdd:pfam00041  80 GEGPPS 85
PTKc_Wee1 cd14051
Catalytic domain of the Protein Tyrosine Kinase, Wee1; PTKs catalyze the transfer of the ...
268-391 1.65e-14

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


Pssm-ID: 270953 [Multi-domain]  Cd Length: 275  Bit Score: 74.36  E-value: 1.65e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 268 ERLGSGKFGQVFRLVE---------KKTRKVWAGkffkaySAKEKENIRqEISIMNCL-HHPKLVQCVDAFEEKANIVMV 337
Cdd:cd14051     6 EKIGSGEFGSVYKCINrldgcvyaiKKSKKPVAG------SVDEQNALN-EVYAHAVLgKHPHVVRYYSAWAEDDHMIIQ 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1034633499 338 LEIVSGGELFERIID---EDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENI 391
Cdd:cd14051    79 NEYCNGGSLADAISEnekAGERFSEAELKDLLLQVAQGLKYIHSQNLVHMDIKPGNI 135
STKc_SRPK3 cd14218
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase 3; STKs ...
264-519 1.83e-14

Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SRPK3 is highly expressed in the heart and skeletal muscles, and is controlled by a muscle-specific enhancer that is regulated by MEF2. It may play an important role in muscle development. SRPKs phosphorylate and regulate splicing factors from the SR protein family by specifically phosphorylating multiple serine residues residing in SR/RS dipeptide motifs (also known as RS domains). Phosphorylation of the RS domains enhances interaction with transportin SR and facilitates entry of the SR proteins into the nucleus. SRPKs contain a nonconserved insert domain, within the well-conserved catalytic kinase domain, that regulates their subcellular localization. The SRPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271120 [Multi-domain]  Cd Length: 365  Bit Score: 75.44  E-value: 1.83e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 264 YDIEERLGSGKFGQVFRLVEKKTRKVWAGKFFKAySAKEKENIRQEISIMNCLHH-----PK---LVQCVDAFE----EK 331
Cdd:cd14218    12 YHVVRKLGWGHFSTVWLCWDIQRKRFVALKVVKS-AVHYTETAVDEIKLLKCVRDsdpsdPKretIVQLIDDFKisgvNG 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 332 ANIVMVLEIVsGGELFERIIDEDFELTERECIK-YMRQISEGVEYIH-KQGIVHLDLKPENI-MCVNKTGTRI------- 401
Cdd:cd14218    91 VHVCMVLEVL-GHQLLKWIIKSNYQGLPLPCVKsILRQVLQGLDYLHtKCKIIHTDIKPENIlMCVDEGYVRRlaaeati 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 402 -----------KLIDFGLARRL------ENAGSLKVLFG-----------------TPEFVAPEVINYEPIGYATDMWSI 447
Cdd:cd14218   170 wqqagapppsgSSVSFGASDFLvnplepQNADKIRVKIAdlgnacwvhkhftediqTRQYRALEVLIGAEYGTPADIWST 249
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 448 GVICYILVSG---LSPFMGDN---DNETLANVTSATWD----------FDDEAFD------------------------- 486
Cdd:cd14218   250 ACMAFELATGdylFEPHSGEDytrDEDHIAHIVELLGDipphfalsgrYSREYFNrrgelrhiknlkhwglyevlvekye 329
                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 1034633499 487 ---EISDDAKDFISNLLKKDMKNRLDCTQCLQHPWL 519
Cdd:cd14218   330 wplEQAAQFTDFLLPMMEFLPEKRATAAQCLQHPWL 365
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
108-247 2.49e-14

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 76.58  E-value: 2.49e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 108 YTLLVENKLG----SRQAQVnLTVVDKPDPPAG-TpcASDIRSSSLTLSWYGSSydgGSAVQSYSIEIWDSANKTWKELA 182
Cdd:COG3401   207 YRVAATDTGGesapSNEVSV-TTPTTPPSAPTGlT--ATADTPGSVTLSWDPVT---ESDATGYRVYRSNSGDGPFTKVA 280
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034633499 183 TCRSTSFNVQDLLPDHEYKFRVRAINVYGT-SEPSQESELTTVGEKPEEPKDeVEVSDDDEKEPEV 247
Cdd:COG3401   281 TVTTTSYTDTGLTNGTTYYYRVTAVDAAGNeSAPSNVVSVTTDLTPPAAPSG-LTATAVGSSSITL 345
PTKc_Tie1 cd05089
Catalytic domain of the Protein Tyrosine Kinase, Tie1; Protein Tyrosine Kinase (PTK) family; ...
267-463 3.02e-14

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: 73.88  E-value: 3.02e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 267 EERLGSGKFGQVFR-LVEKKTRKVWAG-KFFKAY-SAKEKENIRQEISIMNCL-HHPKLVQCVDAFEEKANIVMVLEIVS 342
Cdd:cd05089     7 EDVIGEGNFGQVIKaMIKKDGLKMNAAiKMLKEFaSENDHRDFAGELEVLCKLgHHPNIINLLGACENRGYLYIAIEYAP 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 343 GGELFE-----RIIDED----------FELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKTGTRIKliDFG 407
Cdd:cd05089    87 YGNLLDflrksRVLETDpafakehgtaSTLTSQQLLQFASDVAKGMQYLSEKQFIHRDLAARNVLVGENLVSKIA--DFG 164
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034633499 408 LARRLE-----NAGSLKVlfgtpEFVAPEVINYEPIGYATDMWSIGVICYILVS-GLSPFMG 463
Cdd:cd05089   165 LSRGEEvyvkkTMGRLPV-----RWMAIESLNYSVYTTKSDVWSFGVLLWEIVSlGGTPYCG 221
PTKc_Tec_Rlk cd05114
Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular ...
270-474 3.30e-14

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: 73.36  E-value: 3.30e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 270 LGSGKFGqVFRLVEKKTRKVWAGKFFKAYSAKEKENIrQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEIVSGGELFER 349
Cdd:cd05114    12 LGSGLFG-VVRLGKWRAQYKVAIKAIREGAMSEEDFI-EEAKVMMKLTHPKLVQLYGVCTQQKPIYIVTEFMENGCLLNY 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 350 IIDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGTrIKLIDFGLARRL---ENAGSLKVLFGTpE 426
Cdd:cd05114    90 LRQRRGKLSRDMLLSMCQDVCEGMEYLERNNFIHRDLAARNCL-VNDTGV-VKVSDFGMTRYVlddQYTSSSGAKFPV-K 166
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1034633499 427 FVAPEVINYEPIGYATDMWSIGVICY-ILVSGLSPFMGDNDNETLANVT 474
Cdd:cd05114   167 WSPPEVFNYSKFSSKSDVWSFGVLMWeVFTEGKMPFESKSNYEVVEMVS 215
PK_TRB cd13976
Pseudokinase domain of Tribbles Homolog proteins; The pseudokinase domain shows similarity to ...
333-519 3.35e-14

Pseudokinase domain of Tribbles Homolog proteins; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. Tribbles Homolog (TRB) proteins interact with many proteins involved in signaling pathways. They play scaffold-like regulatory functions and affect many cellular processes such as mitosis, apoptosis, differentiation, and gene expression. TRB proteins bind to the middle kinase in mitogen activated protein kinase (MAPK) signaling cascades, MAPK kinases. They regulate the activity of MAPK kinases, and thus, affect MAPK signaling. In Drosophila, Tribbles regulates String, the ortholog of mammalian Cdc25, during morphogenesis. String is implicated in the progression of mitosis during embryonic development. Vertebrates contain three TRB proteins encoded by three separate genes: Tribbles-1 (TRB1 or TRIB1), Tribbles-2 (TRB2 or TRIB2), and Tribbles-3 (TRB3 or TRIB3). The TRB subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270878 [Multi-domain]  Cd Length: 242  Bit Score: 72.85  E-value: 3.35e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 333 NIVMVLEIVSGGELFERIIDEDFE-----------LTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKTGTRI 401
Cdd:cd13976    46 NISGVHEVIAGETKAYVFFERDHGdlhsyvrsrkrLREPEAARLFRQIASAVAHCHRNGIVLRDLKLRKFVFADEERTKL 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 402 KLidfglaRRLENA-------GSLKVLFGTPEFVAPEVIN----YEpiGYATDMWSIGVICYILVSGLSPFMgDNDNETL 470
Cdd:cd13976   126 RL------ESLEDAvilegedDSLSDKHGCPAYVSPEILNsgatYS--GKAADVWSLGVILYTMLVGRYPFH-DSEPASL 196
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1034633499 471 ANVTSATwdfddeAF---DEISDDAKDFISNLLKKDMKNRLDCTQCLQHPWL 519
Cdd:cd13976   197 FAKIRRG------QFaipETLSPRARCLIRSLLRREPSERLTAEDILLHPWL 242
STKc_JNK2 cd07876
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the ...
308-519 3.51e-14

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: 74.68  E-value: 3.51e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 308 QEISIMNCLHHPKLVQCVDAF------EEKANIVMVLEIVSGGelFERIIDEDFELTERECIKYmrQISEGVEYIHKQGI 381
Cdd:cd07876    69 RELVLLKCVNHKNIISLLNVFtpqkslEEFQDVYLVMELMDAN--LCQVIHMELDHERMSYLLY--QMLCGIKHLHSAGI 144
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 382 VHLDLKPENImcVNKTGTRIKLIDFGLARRLENAGSLKVLFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPF 461
Cdd:cd07876   145 IHRDLKPSNI--VVKSDCTLKILDFGLARTACTNFMMTPYVVTRYYRAPEVILGMGYKENVDIWSVGCIMGELVKGSVIF 222
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 462 MG----DNDNETLANVTSATWDFDDE------------------AFDEISDD----------------AKDFISNLLKKD 503
Cdd:cd07876   223 QGtdhiDQWNKVIEQLGTPSAEFMNRlqptvrnyvenrpqypgiSFEELFPDwifpseserdklktsqARDLLSKMLVID 302
                         250
                  ....*....|....*.
gi 1034633499 504 MKNRLDCTQCLQHPWL 519
Cdd:cd07876   303 PDKRISVDEALRHPYI 318
STKc_Sty1_Hog1 cd07856
Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases ...
270-519 4.36e-14

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: 74.15  E-value: 4.36e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 270 LGSGKFGQVFRLVEKKT-RKVWAGKFFKAYS--AKEKENIRqEISIMNCLHHPKLVQCVDAF-EEKANIVMVLEIVsgGE 345
Cdd:cd07856    18 VGMGAFGLVCSARDQLTgQNVAVKKIMKPFStpVLAKRTYR-ELKLLKHLRHENIISLSDIFiSPLEDIYFVTELL--GT 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 346 LFERIIDEdfELTERECIKY-MRQISEGVEYIHKQGIVHLDLKPENIMcVNKTgTRIKLIDFGLARRLENAGSLKVlfGT 424
Cdd:cd07856    95 DLHRLLTS--RPLEKQFIQYfLYQILRGLKYVHSAGVIHRDLKPSNIL-VNEN-CDLKICDFGLARIQDPQMTGYV--ST 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 425 PEFVAPEV-INYEPIGYATDMWSIGVICYILVSG---------------LSPFMGDNDNETLANVTSA-TWDFDD----- 482
Cdd:cd07856   169 RYYRAPEImLTWQKYDVEVDIWSAGCIFAEMLEGkplfpgkdhvnqfsiITELLGTPPDDVINTICSEnTLRFVQslpkr 248
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1034633499 483 ------EAFDEISDDAKDFISNLLKKDMKNRLDCTQCLQHPWL 519
Cdd:cd07856   249 ervpfsEKFKNADPDAIDLLEKMLVFDPKKRISAAEALAHPYL 291
STKc_CDK6 cd07862
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs ...
264-473 4.62e-14

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: 73.53  E-value: 4.62e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 264 YDIEERLGSGKFGQVFRLVEKKTrkvwAGKF--FKAYSAKEKE------NIRqEISIMNCLH---HPKLVQCVDA----- 327
Cdd:cd07862     3 YECVAEIGEGAYGKVFKARDLKN----GGRFvaLKRVRVQTGEegmplsTIR-EVAVLRHLEtfeHPNVVRLFDVctvsr 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 328 FEEKANIVMVLEIVSGG--ELFERIIDEDfelTERECIK-YMRQISEGVEYIHKQGIVHLDLKPENIMCVnkTGTRIKLI 404
Cdd:cd07862    78 TDRETKLTLVFEHVDQDltTYLDKVPEPG---VPTETIKdMMFQLLRGLDFLHSHRVVHRDLKPQNILVT--SSGQIKLA 152
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034633499 405 DFGLARRLENAGSLKVLFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANV 473
Cdd:cd07862   153 DFGLARIYSFQMALTSVVVTLWYRAPEVLLQSSYATPVDLWSVGCIFAEMFRRKPLFRGSSDVDQLGKI 221
STKc_JNK cd07850
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the ...
308-519 4.90e-14

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: 73.99  E-value: 4.90e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 308 QEISIMNCLHHPKLVQCVDAF------EEKANIVMVLEIVSGGelFERIIDEDFElteRECIKYM-RQISEGVEYIHKQG 380
Cdd:cd07850    48 RELVLMKLVNHKNIIGLLNVFtpqkslEEFQDVYLVMELMDAN--LCQVIQMDLD---HERMSYLlYQMLCGIKHLHSAG 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 381 IVHLDLKPENImcVNKTGTRIKLIDFGLARrleNAGSLKVLfgTPEFV-----APEVInyEPIGYA--TDMWSIGVICYI 453
Cdd:cd07850   123 IIHRDLKPSNI--VVKSDCTLKILDFGLAR---TAGTSFMM--TPYVVtryyrAPEVI--LGMGYKenVDIWSVGCIMGE 193
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 454 LVSGLSPFMG----DNDNETLANVTSATWDFDDE------------------AFDEISDD-----------------AKD 494
Cdd:cd07850   194 MIRGTVLFPGtdhiDQWNKIIEQLGTPSDEFMSRlqptvrnyvenrpkyagySFEELFPDvlfppdseehnklkasqARD 273
                         250       260
                  ....*....|....*....|....*
gi 1034633499 495 FISNLLKKDMKNRLDCTQCLQHPWL 519
Cdd:cd07850   274 LLSKMLVIDPEKRISVDDALQHPYI 298
STKc_LATS1 cd05625
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor 1; STKs catalyze the ...
270-501 5.18e-14

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


Pssm-ID: 270775 [Multi-domain]  Cd Length: 382  Bit Score: 74.31  E-value: 5.18e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 270 LGSGKFGQVFRLVEKKTRKVWAGKFFKAYSA---KEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEIVSGGEL 346
Cdd:cd05625     9 LGIGAFGEVCLARKVDTKALYATKTLRKKDVllrNQVAHVKAERDILAEADNEWVVRLYYSFQDKDNLYFVMDYIPGGDM 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 347 FERIIDEDFeLTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGtRIKLIDFGL------------------ 408
Cdd:cd05625    89 MSLLIRMGV-FPEDLARFYIAELTCAVESVHKMGFIHRDIKPDNIL-IDRDG-HIKLTDFGLctgfrwthdskyyqsgdh 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 409 ------------------------------ARRLENAGSLKVLFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGL 458
Cdd:cd05625   166 lrqdsmdfsnewgdpencrcgdrlkplerrAARQHQRCLAHSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILFEMLVGQ 245
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1034633499 459 SPFMGDNDNETLANVTSATWDFDDEAFDEISDDAKDFISNLLK 501
Cdd:cd05625   246 PPFLAQTPLETQMKVINWQTSLHIPPQAKLSPEASDLIIKLCR 288
PTKc_Tec_like cd05059
Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
268-473 5.23e-14

Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Tec-like subfamily is composed of Tec, Btk, Bmx (Etk), Itk (Tsk, Emt), Rlk (Txk), and similar proteins. They are cytoplasmic (or nonreceptor) PTKs with similarity to Src kinases in that they contain Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Unlike Src kinases, most Tec subfamily members except Rlk also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. In addition, some members contain the Tec homology (TH) domain, which contains proline-rich and zinc-binding regions. Tec kinases form the second largest subfamily of nonreceptor PTKs and are expressed mainly by haematopoietic cells, although Tec and Bmx are also found in endothelial cells. B-cells express Btk and Tec, while T-cells express Itk, Txk, and Tec. Collectively, Tec kinases are expressed in a variety of myeloid cells such as mast cells, platelets, macrophages, and dendritic cells. Each Tec kinase shows a distinct cell-type pattern of expression. Tec kinases play important roles in the development, differentiation, maturation, regulation, survival, and function of B-cells and T-cells. Mutations in Btk cause the severe B-cell immunodeficiency, X-linked agammaglobulinaemia (XLA). The Tec-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173637 [Multi-domain]  Cd Length: 256  Bit Score: 72.48  E-value: 5.23e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 268 ERLGSGKFGQVFRLVEKKTRKVwAGKFFKAYSAKEKENIrQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEIVSGGELF 347
Cdd:cd05059    10 KELGSGQFGVVHLGKWRGKIDV-AIKMIKEGSMSEDDFI-EEAKVMMKLSHPKLVQLYGVCTKQRPIFIVTEYMANGCLL 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 348 ERIIDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGTrIKLIDFGLARRL---ENAGSlkvlFGT 424
Cdd:cd05059    88 NYLRERRGKFQTEQLLEMCKDVCEAMEYLESNGFIHRDLAARNCL-VGEQNV-VKVSDFGLARYVlddEYTSS----VGT 161
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1034633499 425 P---EFVAPEVINYEPIGYATDMWSIGVICY-ILVSGLSPFMGDNDNETLANV 473
Cdd:cd05059   162 KfpvKWSPPEVFMYSKFSSKSDVWSFGVLMWeVFSEGKMPYERFSNSEVVEHI 214
STKc_TAO2 cd06634
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze ...
263-547 5.47e-14

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


Pssm-ID: 270804 [Multi-domain]  Cd Length: 308  Bit Score: 73.52  E-value: 5.47e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 263 FYDIEErLGSGKFGQVFRLVEKKTRKVWAGKFFkAYSAKEK----ENIRQEISIMNCLHHPKLVQCVDAF--EEKANIVM 336
Cdd:cd06634    17 FSDLRE-IGHGSFGAVYFARDVRNNEVVAIKKM-SYSGKQSnekwQDIIKEVKFLQKLRHPNTIEYRGCYlrEHTAWLVM 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 337 VLEIVSGGELFERiidEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGtRIKLIDFGLARRLENAG 416
Cdd:cd06634    95 EYCLGSASDLLEV---HKKPLQEVEIAAITHGALQGLAYLHSHNMIHRDVKAGNIL-LTEPG-LVKLGDFGSASIMAPAN 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 417 SlkvLFGTPEFVAPEVINYEPIGY---ATDMWSIGVICYILVSGLSPFMGDNDNETLANVT--------SATWdfddeaf 485
Cdd:cd06634   170 S---FVGTPYWMAPEVILAMDEGQydgKVDVWSLGITCIELAERKPPLFNMNAMSALYHIAqnespalqSGHW------- 239
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034633499 486 deiSDDAKDFISNLLKKDMKNRLDCTQCLQHPWLMKD---TKNMEAKKLSKDRMKKY--MARRKWQK 547
Cdd:cd06634   240 ---SEYFRNFVDSCLQKIPQDRPTSDVLLKHRFLLRErppTVIMDLIQRTKDAVRELdnLQYRKMKK 303
PKc_MEK cd06615
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
261-521 6.17e-14

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: 73.24  E-value: 6.17e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 261 SDFYDIEErLGSGKFGQVFRLVEKKTRKVWAGKFFKAysaKEKENIRQEI-SIMNCLHH---PKLVQCVDAFEEKANIVM 336
Cdd:cd06615     1 DDFEKLGE-LGAGNGGVVTKVLHRPSGLIMARKLIHL---EIKPAIRNQIiRELKVLHEcnsPYIVGFYGAFYSDGEISI 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 337 VLEIVSGGELfERIIDEDFELTERECIKYMRQISEGVEYIH-KQGIVHLDLKPENIMcVNKTGtRIKLIDFGLARRLENa 415
Cdd:cd06615    77 CMEHMDGGSL-DQVLKKAGRIPENILGKISIAVLRGLTYLReKHKIMHRDVKPSNIL-VNSRG-EIKLCDFGVSGQLID- 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 416 gSLKVLF-GTPEFVAPEVINYEPIGYATDMWSIGVICYILVSG-----------LSPFMGDNDN--ETLANVTSATWDFD 481
Cdd:cd06615   153 -SMANSFvGTRSYMSPERLQGTHYTVQSDIWSLGLSLVEMAIGrypipppdakeLEAMFGRPVSegEAKESHRPVSGHPP 231
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034633499 482 D--------EAFDEI-------------SDDAKDFISNLLKKDMKNRLDCTQCLQHPWLMK 521
Cdd:cd06615   232 DsprpmaifELLDYIvnepppklpsgafSDEFQDFVDKCLKKNPKERADLKELTKHPFIKR 292
IgI_2_Palladin_C cd20990
Second C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig ...
609-699 6.19e-14

Second C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of palladin. Palladin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to this family contain multiple Ig-like domains and function as scaffolds, modulating actin cytoskeleton. Palladin binds to alpha-actinin ezrin, vasodilator-stimulated phosphoprotein VASP, SPIN90 (also known as DIP or mDia interacting protein), and Src. Palladin also binds F-actin directly, via its Ig3 domain. Palladin is expressed as several alternatively spliced isoforms, having various combinations of Ig-like domains, in a cell-type-specific manner. It has been suggested that palladin's different Ig-like domains may be specialized for distinct functions. 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: 409582  Cd Length: 91  Bit Score: 67.82  E-value: 6.19e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 609 PYFSKTIRDLEVVEGSAARFDCKIEGYPDPEVVWFKDDQSIRESRHFQIDYDEDGNCSLIISDVCGDDDAKYTCKAVNSL 688
Cdd:cd20990     1 PHFLQAPGDLTVQEGKLCRMDCKVSGLPTPDLSWQLDGKPIRPDSAHKMLVRENGVHSLIIEPVTSRDAGIYTCIATNRA 80
                          90
                  ....*....|.
gi 1034633499 689 GEATCTAELIV 699
Cdd:cd20990    81 GQNSFNLELVV 91
PTKc_EGFR_like cd05057
Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs ...
270-463 6.37e-14

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: 72.83  E-value: 6.37e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 270 LGSGKFGQVFR---LVEKKTRKV-WAGKFFK-AYSAKEKENIRQEISIMNCLHHPKLVQ--CVDAFEEkanIVMVLEIVS 342
Cdd:cd05057    15 LGSGAFGTVYKgvwIPEGEKVKIpVAIKVLReETGPKANEEILDEAYVMASVDHPHLVRllGICLSSQ---VQLITQLMP 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 343 GGELFERIIDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCvnKTGTRIKLIDFGLARRLE-NAGSLKVL 421
Cdd:cd05057    92 LGCLLDYVRNHRDNIGSQLLLNWCVQIAKGMSYLEEKRLVHRDLAARNVLV--KTPNHVKITDFGLAKLLDvDEKEYHAE 169
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1034633499 422 FG-TP-EFVAPEVINYEPIGYATDMWSIGVICY-ILVSGLSPFMG 463
Cdd:cd05057   170 GGkVPiKWMALESIQYRIYTHKSDVWSYGVTVWeLMTFGAKPYEG 214
IgI_4_MYLK-like cd20976
Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a ...
609-699 6.53e-14

Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain from smooth muscle myosin light chain kinase (MYLK) and similar domains. 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 this group shows that the fourth Ig-like domain from myosin light chain kinase lacks this strand and thus 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: 409568 [Multi-domain]  Cd Length: 90  Bit Score: 67.66  E-value: 6.53e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 609 PYFSKTIRDLEVVEGSAARFDCKIEGYPDPEVVWFKDDQSIR-ESRHFQIDYdedGNCSLIISDVCGDDDAKYTCKAVNS 687
Cdd:cd20976     2 PSFSSVPKDLEAVEGQDFVAQCSARGKPVPRITWIRNAQPLQyAADRSTCEA---GVGELHIQDVLPEDHGTYTCLAKNA 78
                          90
                  ....*....|..
gi 1034633499 688 LGEATCTAELIV 699
Cdd:cd20976    79 AGQVSCSAWVTV 90
PKc_MEK1 cd06650
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
257-449 9.37e-14

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: 72.78  E-value: 9.37e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 257 EQKVSDFYDIEErLGSGKFGQVFRLVEKKTRKVWAGKFFKAYSAKEKEN-IRQEISIMNCLHHPKLVQCVDAFEEKANIV 335
Cdd:cd06650     1 ELKDDDFEKISE-LGAGNGGVVFKVSHKPSGLVMARKLIHLEIKPAIRNqIIRELQVLHECNSPYIVGFYGAFYSDGEIS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 336 MVLEIVSGGELfERIIDEDFELTERECIKYMRQISEGVEYI-HKQGIVHLDLKPENIMcVNKTGtRIKLIDFGLARRLEN 414
Cdd:cd06650    80 ICMEHMDGGSL-DQVLKKAGRIPEQILGKVSIAVIKGLTYLrEKHKIMHRDVKPSNIL-VNSRG-EIKLCDFGVSGQLID 156
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1034633499 415 AGSlKVLFGTPEFVAPEVINYEPIGYATDMWSIGV 449
Cdd:cd06650   157 SMA-NSFVGTRSYMSPERLQGTHYSVQSDIWSMGL 190
PTKc_c-ros cd05044
Catalytic domain of the Protein Tyrosine Kinase, C-ros; PTKs catalyze the transfer of the ...
270-475 1.08e-13

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: 71.68  E-value: 1.08e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 270 LGSGKFGQVFRLVEKKT-------RKVWAGKFFKAYSAKEKENIRQEISIMNCLHHPKLVQ----CVDAfeekANIVMVL 338
Cdd:cd05044     3 LGSGAFGEVFEGTAKDIlgdgsgeTKVAVKTLRKGATDQEKAEFLKEAHLMSNFKHPNILKllgvCLDN----DPQYIIL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 339 EIVSGGELFERIIDEDFE------LTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKTGTR--IKLIDFGLAR 410
Cdd:cd05044    79 ELMEGGDLLSYLRAARPTaftpplLTLKDLLSICVDVAKGCVYLEDMHFVHRDLAARNCLVSSKDYRErvVKIGDFGLAR 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034633499 411 --------RLENAGSLKVLFGTPEFVAPEVINYEpigyaTDMWSIGVICY-ILVSGLSPFMGDNDNETLANVTS 475
Cdd:cd05044   159 diykndyyRKEGEGLLPVRWMAPESLVDGVFTTQ-----SDVWAFGVLMWeILTLGQQPYPARNNLEVLHFVRA 227
PTKc_Yes cd05069
Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the ...
266-473 1.10e-13

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


Pssm-ID: 270654 [Multi-domain]  Cd Length: 279  Bit Score: 72.03  E-value: 1.10e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 266 IEERLGSGKFGQVFRLVEKKTRKVwAGKFFKAySAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKAnIVMVLEIVSGGE 345
Cdd:cd05069    16 LDVKLGQGCFGEVWMGTWNGTTKV-AIKTLKP-GTMMPEAFLQEAQIMKKLRHDKLVPLYAVVSEEP-IYIVTEFMGKGS 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 346 LFERIIDEDFE-LTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKTGTRIKliDFGLARRLE-NAGSLKVLFG 423
Cdd:cd05069    93 LLDFLKEGDGKyLKLPQLVDMAAQIADGMAYIERMNYIHRDLRAANILVGDNLVCKIA--DFGLARLIEdNEYTARQGAK 170
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1034633499 424 TP-EFVAPEVINYEPIGYATDMWSIGVICYILVS-GLSPFMGDNDNETLANV 473
Cdd:cd05069   171 FPiKWTAPEAALYGRFTIKSDVWSFGILLTELVTkGRVPYPGMVNREVLEQV 222
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
626-692 1.22e-13

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: 66.20  E-value: 1.22e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034633499 626 ARFDCKIEGYPDPEVVWFKDDQSIRESRHFQIdYDEDGNCSLIISDVCGDDDAKYTCKAVNSLGEAT 692
Cdd:cd00096     1 VTLTCSASGNPPPTITWYKNGKPLPPSSRDSR-RSELGNGTLTISNVTLEDSGTYTCVASNSAGGSA 66
STKc_PIM1 cd14100
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
321-466 1.64e-13

Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) kinase 1; 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 isoforms resulting from alternative translation initiation sites. PIM1 is the founding member of the PIM subfamily. It is involved in regulating cell growth, differentiation, and apoptosis. It promotes cancer development when overexpressed by inhibiting apoptosis, promoting cell proliferation, and promoting genomic instability. The PIM1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271002 [Multi-domain]  Cd Length: 254  Bit Score: 71.15  E-value: 1.64e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 321 LVQCVDAFEEKANIVMVLE---IVSggELFErIIDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKT 397
Cdd:cd14100    67 VIRLLDWFERPDSFVLVLErpePVQ--DLFD-FITERGALPEELARSFFRQVLEAVRHCHNCGVLHRDIKDENILIDLNT 143
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034633499 398 GtRIKLIDFGLARRLENagSLKVLF-GTPEFVAPEVINYEPI-GYATDMWSIGVICYILVSGLSPFMGDND 466
Cdd:cd14100   144 G-ELKLIDFGSGALLKD--TVYTDFdGTRVYSPPEWIRFHRYhGRSAAVWSLGILLYDMVCGDIPFEHDEE 211
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
131-213 1.66e-13

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 66.48  E-value: 1.66e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499  131 PDPPaGTPCASDIRSSSLTLSWYGSSYDGG-SAVQSYSIEIWDSANKTWKELATCRSTSFNVQDLLPDHEYKFRVRAINV 209
Cdd:smart00060   1 PSPP-SNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNG 79

                   ....
gi 1034633499  210 YGTS 213
Cdd:smart00060  80 AGEG 83
PTKc_Tie cd05047
Catalytic domain of Tie Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
270-463 1.71e-13

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: 71.23  E-value: 1.71e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 270 LGSGKFGQVFRLVEKK--TRKVWAGKFFKAYSAK-EKENIRQEISIMNCL-HHPKLVQCVDAFEEKANIVMVLEIVSGGE 345
Cdd:cd05047     3 IGEGNFGQVLKARIKKdgLRMDAAIKRMKEYASKdDHRDFAGELEVLCKLgHHPNIINLLGACEHRGYLYLAIEYAPHGN 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 346 LFE-----RIIDED----------FELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKTGTRIKliDFGLAR 410
Cdd:cd05047    83 LLDflrksRVLETDpafaianstaSTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIA--DFGLSR 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1034633499 411 RLE-----NAGSLKVlfgtpEFVAPEVINYEPIGYATDMWSIGVICYILVS-GLSPFMG 463
Cdd:cd05047   161 GQEvyvkkTMGRLPV-----RWMAIESLNYSVYTTNSDVWSYGVLLWEIVSlGGTPYCG 214
PTKc_TrkB cd05093
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase B; PTKs catalyze ...
266-474 1.85e-13

Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase B; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. TrkB is a receptor PTK (RTK) containing an extracellular region with arrays of leucine-rich motifs flanked by two cysteine-rich clusters followed by two immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. Binding of TrkB to its ligands, brain-derived neurotrophic factor (BDNF) or neurotrophin 4 (NT4), results in receptor oligomerization and activation of the catalytic domain. TrkB is broadly expressed in the nervous system and in some non-neural tissues. It plays important roles in cell proliferation, differentiation, and survival. BDNF/Trk signaling plays a key role in regulating activity-dependent synaptic plasticity. TrkB also contributes to protection against gp120-induced neuronal cell death. TrkB overexpression is associated with poor prognosis in neuroblastoma (NB) and other human cancers. It acts as a suppressor of anoikis (detachment-induced apoptosis) and contributes to tumor metastasis. The TrkB subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270675 [Multi-domain]  Cd Length: 288  Bit Score: 71.61  E-value: 1.85e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 266 IEERLGSGKFGQVF-----RLVEKKTRKVWAGKFFKAYSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEI 340
Cdd:cd05093     9 LKRELGEGAFGKVFlaecyNLCPEQDKILVAVKTLKDASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEY 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 341 VSGGEL--FERIIDED----------FELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENimCVNKTGTRIKLIDFGL 408
Cdd:cd05093    89 MKHGDLnkFLRAHGPDavlmaegnrpAELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRN--CLVGENLLVKIGDFGM 166
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 409 ARRLENAGSLKVLFGTP---EFVAPEVINYEPIGYATDMWSIGVICY-ILVSGLSPFMGDNDNETLANVT 474
Cdd:cd05093   167 SRDVYSTDYYRVGGHTMlpiRWMPPESIMYRKFTTESDVWSLGVVLWeIFTYGKQPWYQLSNNEVIECIT 236
STKc_LRRK1 cd14067
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze ...
307-463 1.92e-13

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: 71.15  E-value: 1.92e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 307 RQEISIMNCLHHPKLVQCVD--------AFEEK--ANIVMVLEIVSGGELFeriIDEDFELTERecIKYmrQISEGVEYI 376
Cdd:cd14067    58 RQEASMLHSLQHPCIVYLIGisihplcfALELAplGSLNTVLEENHKGSSF---MPLGHMLTFK--IAY--QIAAGLAYL 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 377 HKQGIVHLDLKPENIMCVN---KTGTRIKLIDFGLARRLENAGSLKVLfGTPEFVAPEV---INYEPigyATDMWSIGVI 450
Cdd:cd14067   131 HKKNIIFCDLKSDNILVWSldvQEHINIKLSDYGISRQSFHEGALGVE-GTPGYQAPEIrprIVYDE---KVDMFSYGMV 206
                         170
                  ....*....|...
gi 1034633499 451 CYILVSGLSPFMG 463
Cdd:cd14067   207 LYELLSGQRPSLG 219
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
48-127 2.28e-13

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 65.69  E-value: 2.28e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499  48 KVRAGESVELFGKVTGTQPITCTWMKFRKQIQESEHMKVENSENGSKLTILAARQEHCGCYTLLVENKLGSRQAQVNLTV 127
Cdd:cd05748     3 VVRAGESLRLDIPIKGRPTPTVTWSKDGQPLKETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINVKV 82
PTKc_Jak3_rpt2 cd05081
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the ...
267-454 3.11e-13

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: 70.69  E-value: 3.11e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 267 EER-------LGSGKFGQV----FRLVEKKTRKVWAGKFFKAYSAKEKENIRQEISIMNCLHHPKLVQ----CVDAFEEK 331
Cdd:cd05081     2 EERhlkyisqLGKGNFGSVelcrYDPLGDNTGALVAVKQLQHSGPDQQRDFQREIQILKALHSDFIVKyrgvSYGPGRRS 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 332 ANIVMvlEIVSGGELFERIIDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCvnKTGTRIKLIDFGLARR 411
Cdd:cd05081    82 LRLVM--EYLPSGCLRDFLQRHRARLDASRLLLYSSQICKGMEYLGSRRCVHRDLAARNILV--ESEAHVKIADFGLAKL 157
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1034633499 412 LENAGSLKVLF---GTPEF-VAPEVINYEPIGYATDMWSIGVICYIL 454
Cdd:cd05081   158 LPLDKDYYVVRepgQSPIFwYAPESLSDNIFSRQSDVWSFGVVLYEL 204
PK_KSR cd14063
Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to ...
265-465 3.13e-13

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: 70.46  E-value: 3.13e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 265 DIEERLGSGKFGQVFRlvekktrKVWAG----KFFKA-YSAKEK-ENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVL 338
Cdd:cd14063     3 EIKEVIGKGRFGRVHR-------GRWHGdvaiKLLNIdYLNEEQlEAFKEEVAAYKNTRHDNLVLFMGACMDPPHLAIVT 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 339 EIVSGGELFERIID--EDFELTERECIKymRQISEGVEYIHKQGIVHLDLKPENIMCVNKtgtRIKLIDFGL--ARRLEN 414
Cdd:cd14063    76 SLCKGRTLYSLIHErkEKFDFNKTVQIA--QQICQGMGYLHAKGIIHKDLKSKNIFLENG---RVVITDFGLfsLSGLLQ 150
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034633499 415 AG----SLKVLFGTPEFVAPEVI----------NYEPIGYATDMWSIGVICYILVSGLSPFMGDN 465
Cdd:cd14063   151 PGrredTLVIPNGWLCYLAPEIIralspdldfeESLPFTKASDVYAFGTVWYELLAGRWPFKEQP 215
PKc_MKK3_6 cd06617
Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase ...
262-517 3.32e-13

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: 70.53  E-value: 3.32e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 262 DFYDIEErLGSGKFGQVFRLVEKKTRKVWAGKFFKA-YSAKEKENIRQEISI-MNCLHHPKLVQCVDAFEEKANIVMVLE 339
Cdd:cd06617     2 DLEVIEE-LGRGAYGVVDKMRHVPTGTIMAVKRIRAtVNSQEQKRLLMDLDIsMRSVDCPYTVTFYGALFREGDVWICME 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 340 IV--SGGELFERIIDEDFELTERECIKYMRQISEGVEYIHKQ-GIVHLDLKPENIMcVNKTGtRIKLIDFGLARRLENAG 416
Cdd:cd06617    81 VMdtSLDKFYKKVYDKGLTIPEDILGKIAVSIVKALEYLHSKlSVIHRDVKPSNVL-INRNG-QVKLCDFGISGYLVDSV 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 417 SLKVLFGTPEFVAPEVINYE--PIGY--ATDMWSIGVICYILVSGLSPFmgdnDN-----ETLANV---TSATwdFDDEA 484
Cdd:cd06617   159 AKTIDAGCKPYMAPERINPElnQKGYdvKSDVWSLGITMIELATGRFPY----DSwktpfQQLKQVveePSPQ--LPAEK 232
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1034633499 485 FdeiSDDAKDFISNLLKKDMKNRLDCTQCLQHP 517
Cdd:cd06617   233 F---SPEFQDFVNKCLKKNYKERPNYPELLQHP 262
STKc_Raf cd14062
Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) ...
270-468 3.41e-13

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: 70.11  E-value: 3.41e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 270 LGSGKFGQVFR-----LVEKKTRKVwagkffKAYSAKEKENIRQEISIMNCLHHPKLVQCVdAFEEKANIVMVLEIVSGG 344
Cdd:cd14062     1 IGSGSFGTVYKgrwhgDVAVKKLNV------TDPTPSQLQAFKNEVAVLRKTRHVNILLFM-GYMTKPQLAIVTQWCEGS 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 345 ELFERI--IDEDFELTEreCIKYMRQISEGVEYIHKQGIVHLDLKPENIMCvnKTGTRIKLIDFGLA---RRLENAGSLK 419
Cdd:cd14062    74 SLYKHLhvLETKFEMLQ--LIDIARQTAQGMDYLHAKNIIHRDLKSNNIFL--HEDLTVKIGDFGLAtvkTRWSGSQQFE 149
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1034633499 420 VLFGTPEFVAPEVI---NYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNE 468
Cdd:cd14062   150 QPTGSILWMAPEVIrmqDENPYSFQSDVYAFGIVLYELLTGQLPYSHINNRD 201
PTKc_Src cd05071
Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the ...
266-473 3.86e-13

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: 70.49  E-value: 3.86e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 266 IEERLGSGKFGQVFRLVEKKTRKVwAGKFFKAySAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKAnIVMVLEIVSGGE 345
Cdd:cd05071    13 LEVKLGQGCFGEVWMGTWNGTTRV-AIKTLKP-GTMSPEAFLQEAQVMKKLRHEKLVQLYAVVSEEP-IYIVTEYMSKGS 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 346 LFERIIDEDFE-LTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMcvnkTGTRI--KLIDFGLARRLE-NAGSLKVL 421
Cdd:cd05071    90 LLDFLKGEMGKyLRLPQLVDMAAQIASGMAYVERMNYVHRDLRAANIL----VGENLvcKVADFGLARLIEdNEYTARQG 165
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1034633499 422 FGTP-EFVAPEVINYEPIGYATDMWSIGVICYILVS-GLSPFMGDNDNETLANV 473
Cdd:cd05071   166 AKFPiKWTAPEAALYGRFTIKSDVWSFGILLTELTTkGRVPYPGMVNREVLDQV 219
PK_SCY1_like cd14011
Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein ...
293-519 4.63e-13

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: 70.43  E-value: 4.63e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 293 KFFKAYSAKEKENI----RQEISIMNCLHHPKLVQCVDAFEE-KANIVMVLEIV--SGGELFERIIDE--------DFEL 357
Cdd:cd14011    32 KQLEEYSKRDREQIlellKRGVKQLTRLRHPRILTVQHPLEEsRESLAFATEPVfaSLANVLGERDNMpspppelqDYKL 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 358 TEREcIKY-MRQISEGVEYIH-KQGIVHLDLKPENIMcVNKTGTrIKLIDFGLARRLENAGSLKVLFG------------ 423
Cdd:cd14011   112 YDVE-IKYgLLQISEALSFLHnDVKLVHGNICPESVV-INSNGE-WKLAGFDFCISSEQATDQFPYFReydpnlpplaqp 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 424 TPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDF-DDEAFDEISDDAKDFISNLLKK 502
Cdd:cd14011   189 NLNYLAPEYILSKTCDPASDMFSLGVLIYAIYNKGKPLFDCVNNLLSYKKNSNQLRQlSLSLLEKVPEELRDHVKTLLNV 268
                         250
                  ....*....|....*..
gi 1034633499 503 DMKNRLDCTQCLQHPWL 519
Cdd:cd14011   269 TPEVRPDAEQLSKIPFF 285
PKc_TNNI3K cd14064
Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; ...
270-461 4.79e-13

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: 69.48  E-value: 4.79e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 270 LGSGKFGQVFRlvEKKTRKVWAGKFFKA--YSAK-EKENIRQEISIMNCLHHPKLVQCVDA-FEEKANIVMVLEIVSGGE 345
Cdd:cd14064     1 IGSGSFGKVYK--GRCRNKIVAIKRYRAntYCSKsDVDMFCREVSILCRLNHPCVIQFVGAcLDDPSQFAIVTQYVSGGS 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 346 LF------ERIIDEDFELTerecikYMRQISEGVEYIHK--QGIVHLDLKPENIMcVNKTGtRIKLIDFGLARRLE--NA 415
Cdd:cd14064    79 LFsllheqKRVIDLQSKLI------IAVDVAKGMEYLHNltQPIIHRDLNSHNIL-LYEDG-HAVVADFGESRFLQslDE 150
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1034633499 416 GSLKVLFGTPEFVAPEVINyEPIGYA--TDMWSIGVICYILVSGLSPF 461
Cdd:cd14064   151 DNMTKQPGNLRWMAPEVFT-QCTRYSikADVFSYALCLWELLTGEIPF 197
STKc_EIF2AK3_PERK cd14048
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
264-462 5.11e-13

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: 69.90  E-value: 5.11e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 264 YDIEERLGSGKFGQVFRLVEKKTRKVWAGKFFK-AYSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKAN--------- 333
Cdd:cd14048     8 FEPIQCLGRGGFGVVFEAKNKVDDCNYAVKRIRlPNNELAREKVLREVRALAKLDHPGIVRYFNAWLERPPegwqekmde 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 334 ----IVMVLeivSGGELFERIIDEDFELTERE---CIKYMRQISEGVEYIHKQGIVHLDLKPENIM-CVNKTgtrIKLID 405
Cdd:cd14048    88 vylyIQMQL---CRKENLKDWMNRRCTMESRElfvCLNIFKQIASAVEYLHSKGLIHRDLKPSNVFfSLDDV---VKVGD 161
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 406 FGLARRL-ENAGSLKVL------------FGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFM 462
Cdd:cd14048   162 FGLVTAMdQGEPEQTVLtpmpayakhtgqVGTRLYMSPEQIHGNQYSEKVDIFALGLILFELIYSFSTQM 231
STKc_TEY_MAPK cd07858
Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; ...
349-519 5.95e-13

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


Pssm-ID: 143363 [Multi-domain]  Cd Length: 337  Bit Score: 70.48  E-value: 5.95e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 349 RIIDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMcVNkTGTRIKLIDFGLARrlenAGSLKVLFGTPEFV 428
Cdd:cd07858    97 QIIRSSQTLSDDHCQYFLYQLLRGLKYIHSANVLHRDLKPSNLL-LN-ANCDLKICDFGLAR----TTSEKGDFMTEYVV 170
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 429 -----APEVI-NYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDFDDEAFDEI-SDDAKDFISN--- 498
Cdd:cd07858   171 trwyrAPELLlNCSEYTTAIDVWSVGCIFAELLGRKPLFPGKDYVHQLKLITELLGSPSEEDLGFIrNEKARRYIRSlpy 250
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1034633499 499 -------------------LLKK----DMKNRLDCTQCLQHPWL 519
Cdd:cd07858   251 tprqsfarlfphanplaidLLEKmlvfDPSKRITVEEALAHPYL 294
STKc_PIM3 cd14102
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
321-519 6.15e-13

Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) kinase 3; 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). PIM3 can inhibit apoptosis and promote cell survival and protein translation, therefore, it can enhance the proliferation of normal and cancer cells. Mice deficient with PIM3 show minimal effects, suggesting that PIM3 msy not be essential. Since its expression is enhanced in several cancers, it may make a good molecular target for cancer drugs. The PIM3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271004 [Multi-domain]  Cd Length: 253  Bit Score: 69.21  E-value: 6.15e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 321 LVQCVDAFEEKANIVMVLEIVS-GGELFErIIDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKTGt 399
Cdd:cd14102    66 VIKLLDWYERPDGFLIVMERPEpVKDLFD-FITEKGALDEDTARGFFRQVLEAVRHCYSCGVVHRDIKDENLLVDLRTG- 143
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 400 RIKLIDFGLARRLENagSLKVLF-GTPEFVAPEVINYEPI-GYATDMWSIGVICYILVSGLSPFmgDNDNETLANVTSAT 477
Cdd:cd14102   144 ELKLIDFGSGALLKD--TVYTDFdGTRVYSPPEWIRYHRYhGRSATVWSLGVLLYDMVCGDIPF--EQDEEILRGRLYFR 219
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1034633499 478 wdfddeafDEISDDAKDFISNLLKKDMKNRLDCTQCLQHPWL 519
Cdd:cd14102   220 --------RRVSPECQQLIKWCLSLRPSDRPTLEQIFDHPWM 253
STKc_PFTAIRE2 cd07870
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer ...
268-519 6.69e-13

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: 69.99  E-value: 6.69e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 268 ERLGSGKFGQVFRLVEKKTRKVWAgkfFKAYSAKEKENIR----QEISIMNCLHHPKLVQCVDAFEEKANIVMVLEIVSG 343
Cdd:cd07870     6 EKLGEGSYATVYKGISRINGQLVA---LKVISMKTEEGVPftaiREASLLKGLKHANIVLLHDIIHTKETLTFVFEYMHT 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 344 gELFERIIDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGtRIKLIDFGLARrlenAGSLKVLFG 423
Cdd:cd07870    83 -DLAQYMIQHPGGLHPYNVRLFMFQLLRGLAYIHGQHILHRDLKPQNLL-ISYLG-ELKLADFGLAR----AKSIPSQTY 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 424 TPEFVA-----PEVInYEPIGYAT--DMWSIGVICYILVSGLSPFMGDNDN--------ETLANVTSATW-------DFD 481
Cdd:cd07870   156 SSEVVTlwyrpPDVL-LGATDYSSalDIWGAGCIFIEMLQGQPAFPGVSDVfeqlekiwTVLGVPTEDTWpgvsklpNYK 234
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1034633499 482 DEAF------------DEISD--DAKDFISNLLKKDMKNRLDCTQCLQHPWL 519
Cdd:cd07870   235 PEWFlpckpqqlrvvwKRLSRppKAEDLASQMLMMFPKDRISAQDALLHPYF 286
PTZ00036 PTZ00036
glycogen synthase kinase; Provisional
226-519 7.18e-13

glycogen synthase kinase; Provisional


Pssm-ID: 173333 [Multi-domain]  Cd Length: 440  Bit Score: 71.22  E-value: 7.18e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 226 EKPEEPKDEVEVSDDDEK-EPEVDYRTVTINTEQKVSDFYDIEERLGSGKFGQVFRLVEKKTRKVWAGKffKAYSAKEKE 304
Cdd:PTZ00036   29 EMNDKKLDEEERSHNNNAgEDEDEEKMIDNDINRSPNKSYKLGNIIGNGSFGVVYEAICIDTSEKVAIK--KVLQDPQYK 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 305 NirQEISIMNCLHHPKLV--------QCVDAFEEKA--NIVMvleivsggELFERIIDEDFELTERE-------CIK-YM 366
Cdd:PTZ00036  107 N--RELLIMKNLNHINIIflkdyyytECFKKNEKNIflNVVM--------EFIPQTVHKYMKHYARNnhalplfLVKlYS 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 367 RQISEGVEYIHKQGIVHLDLKPENIMCVNKTGTrIKLIDFGLARRLEnAGSLKVLFGTPEFV-APEVInYEPIGYAT--D 443
Cdd:PTZ00036  177 YQLCRALAYIHSKFICHRDLKPQNLLIDPNTHT-LKLCDFGSAKNLL-AGQRSVSYICSRFYrAPELM-LGATNYTThiD 253
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 444 MWSIGVICYILVSGLSPFMGDNDNETLANVT----SATWD--------FDDEAFDEIS-------------DDAKDFISN 498
Cdd:PTZ00036  254 LWSLGCIIAEMILGYPIFSGQSSVDQLVRIIqvlgTPTEDqlkemnpnYADIKFPDVKpkdlkkvfpkgtpDDAINFISQ 333
                         330       340
                  ....*....|....*....|.
gi 1034633499 499 LLKKDMKNRLDCTQCLQHPWL 519
Cdd:PTZ00036  334 FLKYEPLKRLNPIEALADPFF 354
PTKc_HER4 cd05110
Catalytic domain of the Protein Tyrosine Kinase, HER4; PTKs catalyze the transfer of the ...
270-463 7.41e-13

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: 70.10  E-value: 7.41e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 270 LGSGKFGQVFRLV---EKKTRKVWAGKFFKAYSAKEKENIR--QEISIMNCLHHPKLVQCVDAFEEkANIVMVLEIVSGG 344
Cdd:cd05110    15 LGSGAFGTVYKGIwvpEGETVKIPVAIKILNETTGPKANVEfmDEALIMASMDHPHLVRLLGVCLS-PTIQLVTQLMPHG 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 345 ELFERIIDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCvnKTGTRIKLIDFGLARRLE--------NAG 416
Cdd:cd05110    94 CLLDYVHEHKDNIGSQLLLNWCVQIAKGMMYLEERRLVHRDLAARNVLV--KSPNHVKITDFGLARLLEgdekeynaDGG 171
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1034633499 417 SLKVlfgtpEFVAPEVINYEPIGYATDMWSIGVICYILVS-GLSPFMG 463
Cdd:cd05110   172 KMPI-----KWMALECIHYRKFTHQSDVWSYGVTIWELMTfGGKPYDG 214
STKc_RIP1 cd14027
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze ...
270-461 8.07e-13

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: 69.07  E-value: 8.07e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 270 LGSGKFGQVFRLVEKKTRKVWAGKFFKAYSAKE-KENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEIVSGGELFE 348
Cdd:cd14027     1 LDSGGFGKVSLCFHRTQGLVVLKTVYTGPNCIEhNEALLEEGKMMNRLRHSRVVKLLGVILEEGKYSLVMEYMEKGNLMH 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 349 RIIDEDFELTEREciKYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTgTRIKLIDFGLA--------------RRLEN 414
Cdd:cd14027    81 VLKKVSVPLSVKG--RIILEIIEGMAYLHGKGVIHKDLKPENIL-VDND-FHIKIADLGLAsfkmwskltkeehnEQREV 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1034633499 415 AGSLKVLFGTPEFVAPE---VINYEPIgYATDMWSIGVICYILVSGLSPF 461
Cdd:cd14027   157 DGTAKKNAGTLYYMAPEhlnDVNAKPT-EKSDVYSFAIVLWAIFANKEPY 205
STKc_JNK1 cd07875
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the ...
308-519 9.73e-13

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: 70.46  E-value: 9.73e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 308 QEISIMNCLHHPKLVQCVDAF------EEKANIVMVLEIVSGgELFERIideDFELTERECIKYMRQISEGVEYIHKQGI 381
Cdd:cd07875    72 RELVLMKCVNHKNIIGLLNVFtpqkslEEFQDVYIVMELMDA-NLCQVI---QMELDHERMSYLLYQMLCGIKHLHSAGI 147
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 382 VHLDLKPENImcVNKTGTRIKLIDFGLARRLENAGSLKVLFGTPEFVAPEVInyEPIGYA--TDMWSIGVICYILVSGLS 459
Cdd:cd07875   148 IHRDLKPSNI--VVKSDCTLKILDFGLARTAGTSFMMTPYVVTRYYRAPEVI--LGMGYKenVDIWSVGCIMGEMIKGGV 223
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 460 PFMG----DNDNETLANVTSATWDF----------------------------------DDEAFDEISDDAKDFISNLLK 501
Cdd:cd07875   224 LFPGtdhiDQWNKVIEQLGTPCPEFmkklqptvrtyvenrpkyagysfeklfpdvlfpaDSEHNKLKASQARDLLSKMLV 303
                         250
                  ....*....|....*...
gi 1034633499 502 KDMKNRLDCTQCLQHPWL 519
Cdd:cd07875   304 IDASKRISVDEALQHPYI 321
STKc_JNK3 cd07874
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the ...
308-519 9.76e-13

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: 70.12  E-value: 9.76e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 308 QEISIMNCLHHPKLVQCVDAF------EEKANIVMVLEIVSGgELFERIideDFELTERECIKYMRQISEGVEYIHKQGI 381
Cdd:cd07874    65 RELVLMKCVNHKNIISLLNVFtpqkslEEFQDVYLVMELMDA-NLCQVI---QMELDHERMSYLLYQMLCGIKHLHSAGI 140
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 382 VHLDLKPENImcVNKTGTRIKLIDFGLARRLENAGSLKVLFGTPEFVAPEVInyEPIGYA--TDMWSIGVICYILVSGLS 459
Cdd:cd07874   141 IHRDLKPSNI--VVKSDCTLKILDFGLARTAGTSFMMTPYVVTRYYRAPEVI--LGMGYKenVDIWSVGCIMGEMVRHKI 216
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 460 PFMG----DNDNETLANVTSATWDF----------------------------------DDEAFDEISDDAKDFISNLLK 501
Cdd:cd07874   217 LFPGrdyiDQWNKVIEQLGTPCPEFmkklqptvrnyvenrpkyagltfpklfpdslfpaDSEHNKLKASQARDLLSKMLV 296
                         250
                  ....*....|....*...
gi 1034633499 502 KDMKNRLDCTQCLQHPWL 519
Cdd:cd07874   297 IDPAKRISVDEALQHPYI 314
PKc_CLK1_4 cd14213
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases 1 and 4; ...
264-471 9.98e-13

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: 69.88  E-value: 9.98e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 264 YDIEERLGSGKFGQVFRLVEKKTR-KVWAGKFFKAYSaKEKENIRQEISI------MNCLHHPKLVQCVDAFEEKANIVM 336
Cdd:cd14213    14 YEIVDTLGEGAFGKVVECIDHKMGgMHVAVKIVKNVD-RYREAARSEIQVlehlntTDPNSTFRCVQMLEWFDHHGHVCI 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 337 VLEIVsGGELFERIIDEDFELTERECIKYMR-QISEGVEYIHKQGIVHLDLKPENIMCVNK-----------------TG 398
Cdd:cd14213    93 VFELL-GLSTYDFIKENSFLPFPIDHIRNMAyQICKSVNFLHHNKLTHTDLKPENILFVQSdyvvkynpkmkrdertlKN 171
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034633499 399 TRIKLIDFGLARRLENAGSlkVLFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLA 471
Cdd:cd14213   172 PDIKVVDFGSATYDDEHHS--TLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVFQTHDSKEHLA 242
STKc_NLK cd07853
Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer ...
365-519 1.47e-12

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: 69.77  E-value: 1.47e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 365 YMRQISEGVEYIHKQGIVHLDLKPENIMcVNkTGTRIKLIDFGLARRLENAGSLKVlfgTPEFV-----APEVINYEP-I 438
Cdd:cd07853   108 FLYQILRGLKYLHSAGILHRDIKPGNLL-VN-SNCVLKICDFGLARVEEPDESKHM---TQEVVtqyyrAPEILMGSRhY 182
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 439 GYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDFDDEAF----------------------------DEISD 490
Cdd:cd07853   183 TSAVDIWSVGCIFAELLGRRILFQAQSPIQQLDLITDLLGTPSLEAMrsacegarahilrgphkppslpvlytlsSQATH 262
                         170       180
                  ....*....|....*....|....*....
gi 1034633499 491 DAKDFISNLLKKDMKNRLDCTQCLQHPWL 519
Cdd:cd07853   263 EAVHLLCRMLVFDPDKRISAADALAHPYL 291
PTKc_Wee1b cd14139
Catalytic domain of the Protein Tyrosine Kinase, Wee1b; PTKs catalyze the transfer of the ...
268-396 1.56e-12

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


Pssm-ID: 271041 [Multi-domain]  Cd Length: 274  Bit Score: 68.42  E-value: 1.56e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 268 ERLGSGKFGQVFRLVEKKTRKVWAGKFFK---AYSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEIVSGG 344
Cdd:cd14139     6 EKIGVGEFGSVYKCIKRLDGCVYAIKRSMrpfAGSSNEQLALHEVYAHAVLGHHPHVVRYYSAWAEDDHMIIQNEYCNGG 85
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1034633499 345 ELfERIIDEDFEL----TERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNK 396
Cdd:cd14139    86 SL-QDAISENTKSgnhfEEPELKDILLQVSMGLKYIHNSGLVHLDIKPSNIFICHK 140
PTKc_Jak1_rpt2 cd05079
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the ...
270-456 1.76e-12

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: 68.42  E-value: 1.76e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 270 LGSGKFGQV----FRLVEKKTRKVWAGKFFKAYSAKEK-ENIRQEISIMNCLHHPKLVQ----CVDafEEKANIVMVLEI 340
Cdd:cd05079    12 LGEGHFGKVelcrYDPEGDNTGEQVAVKSLKPESGGNHiADLKKEIEILRNLYHENIVKykgiCTE--DGGNGIKLIMEF 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 341 VSGGELFERIIDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKtgTRIKLIDFGLARRLENAG---S 417
Cdd:cd05079    90 LPSGSLKEYLPRNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESE--HQVKIGDFGLTKAIETDKeyyT 167
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1034633499 418 LKVLFGTPEF-VAPEVINYEPIGYATDMWSIGVICYILVS 456
Cdd:cd05079   168 VKDDLDSPVFwYAPECLIQSKFYIASDVWSFGVTLYELLT 207
PKc_MEK2 cd06649
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
257-460 2.68e-12

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: 68.54  E-value: 2.68e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 257 EQKVSDFYDIEErLGSGKFGQVFRLVEKKTRKVWAGKFFK-AYSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIV 335
Cdd:cd06649     1 ELKDDDFERISE-LGAGNGGVVTKVQHKPSGLIMARKLIHlEIKPAIRNQIIRELQVLHECNSPYIVGFYGAFYSDGEIS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 336 MVLEIVSGGELfERIIDEDFELTERECIKYMRQISEGVEYI-HKQGIVHLDLKPENIMcVNKTGtRIKLIDFGLARRLEN 414
Cdd:cd06649    80 ICMEHMDGGSL-DQVLKEAKRIPEEILGKVSIAVLRGLAYLrEKHQIMHRDVKPSNIL-VNSRG-EIKLCDFGVSGQLID 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1034633499 415 AGSlKVLFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSP 460
Cdd:cd06649   157 SMA-NSFVGTRSYMSPERLQGTHYSVQSDIWSMGLSLVELAIGRYP 201
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
44-127 2.99e-12

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: 62.91  E-value: 2.99e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499   44 PEDQKVRAGESVELFGKVTGTQPITCTWMKFRKQ-IQESEHMKVENSENGSKLTILAARQEHCGCYTLLVENKLGSRQAQ 122
Cdd:smart00410   1 PPSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKlLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSG 80

                   ....*
gi 1034633499  123 VNLTV 127
Cdd:smart00410  81 TTLTV 85
IgI_LRIG1-like cd05763
Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like ...
611-699 4.10e-12

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


Pssm-ID: 409420 [Multi-domain]  Cd Length: 91  Bit Score: 62.64  E-value: 4.10e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 611 FSKTIRDLEVVEGSAARFDCKIEGYPDPEVVWFKDD----QSIRESR-HFQIDYDEdgncsLIISDVCGDDDAKYTCKAV 685
Cdd:cd05763     2 FTKTPHDITIRAGSTARLECAATGHPTPQIAWQKDGgtdfPAARERRmHVMPEDDV-----FFIVDVKIEDTGVYSCTAQ 76
                          90
                  ....*....|....
gi 1034633499 686 NSLGEATCTAELIV 699
Cdd:cd05763    77 NSAGSISANATLTV 90
PTKc_Tyk2_rpt2 cd05080
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze ...
270-460 5.18e-12

Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tyk2 is widely expressed in many tissues. It is involved in signaling via the cytokine receptors IFN-alphabeta, IL-6, IL-10, IL-12, IL-13, and IL-23. It mediates cell surface urokinase receptor (uPAR) signaling and plays a role in modulating vascular smooth muscle cell (VSMC) functional behavior in response to injury. Tyk2 is also important in dendritic cell function and T helper (Th)1 cell differentiation. A homozygous mutation of Tyk2 was found in a patient with hyper-IgE syndrome (HIES), a primary immunodeficiency characterized by recurrent skin abscesses, pneumonia, and elevated serum IgE. This suggests that Tyk2 may play important roles in multiple cytokine signaling involved in innate and adaptive immunity. Tyk2 is a member of the Janus kinase (Jak) subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase catalytic domain. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). The Tyk2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270664 [Multi-domain]  Cd Length: 283  Bit Score: 67.23  E-value: 5.18e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 270 LGSGKFGQV----FRLVEKKTRKVWAGKFFKA-YSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKAN--IVMVLEIVS 342
Cdd:cd05080    12 LGEGHFGKVslycYDPTNDGTGEMVAVKALKAdCGPQHRSGWKQEIDILKTLYHENIVKYKGCCSEQGGksLQLIMEYVP 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 343 GGELFERIIDEDFELTEreCIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKtgTRIKLIDFGLAR---------RLE 413
Cdd:cd05080    92 LGSLRDYLPKHSIGLAQ--LLLFAQQICEGMAYLHSQHYIHRDLAARNVLLDND--RLVKIGDFGLAKavpegheyyRVR 167
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1034633499 414 NAGSLKVLfgtpeFVAPEVINYEPIGYATDMWSIGVICYILV----SGLSP 460
Cdd:cd05080   168 EDGDSPVF-----WYAPECLKEYKFYYASDVWSFGVTLYELLthcdSSQSP 213
PKc_CLK2 cd14215
Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 2; Dual-specificity ...
264-471 7.24e-12

Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 2; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. CLK2 plays a role in hepatic insulin signaling and glucose metabolism. It is induced by the insulin/Akt pathway as part of the hepatic refeeding reponse, and it directly phosphorylates the SR domain of PGC-1alpha, which results in decreased gluconeogenic gene expression and glucose output. 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 CLK2 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: 271117 [Multi-domain]  Cd Length: 330  Bit Score: 67.35  E-value: 7.24e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 264 YDIEERLGSGKFGQVFRLVE-KKTRKVWAGKFFKAYSaKEKENIRQEISIMNCLHHPK------LVQCVDAFEEKANIVM 336
Cdd:cd14215    14 YEIVSTLGEGTFGRVVQCIDhRRGGARVALKIIKNVE-KYKEAARLEINVLEKINEKDpenknlCVQMFDWFDYHGHMCI 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 337 VLEIVsGGELFERIIDEDFELTERECIKYMR-QISEGVEYIHKQGIVHLDLKPENIMCVNK-----------------TG 398
Cdd:cd14215    93 SFELL-GLSTFDFLKENNYLPYPIHQVRHMAfQVCQAVKFLHDNKLTHTDLKPENILFVNSdyeltynlekkrdersvKS 171
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034633499 399 TRIKLIDFGLARRLENAGSlkVLFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLA 471
Cdd:cd14215   172 TAIRVVDFGSATFDHEHHS--TIVSTRHYRAPEVILELGWSQPCDVWSIGCIIFEYYVGFTLFQTHDNREHLA 242
STKc_PCTAIRE2 cd07872
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer ...
268-470 1.21e-11

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: 66.17  E-value: 1.21e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 268 ERLGSGKFGQVFRLVEKKTRKVWAgkfFKAYSAKEKEN-----IRqEISIMNCLHHPKLVQCVDAFEEKANIVMVLEIVS 342
Cdd:cd07872    12 EKLGEGTYATVFKGRSKLTENLVA---LKEIRLEHEEGapctaIR-EVSLLKDLKHANIVTLHDIVHTDKSLTLVFEYLD 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 343 GGelFERIIDEDFELTERECIK-YMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGtRIKLIDFGLARrlenAGSLKVL 421
Cdd:cd07872    88 KD--LKQYMDDCGNIMSMHNVKiFLYQILRGLAYCHRRKVLHRDLKPQNLL-INERG-ELKLADFGLAR----AKSVPTK 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1034633499 422 FGTPEFVA-----PEVInyepIG---YAT--DMWSIGVICYILVSGLSPFMGDNDNETL 470
Cdd:cd07872   160 TYSNEVVTlwyrpPDVL----LGsseYSTqiDMWGVGCIFFEMASGRPLFPGSTVEDEL 214
IgI_3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
617-699 1.50e-11

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


Pssm-ID: 409390 [Multi-domain]  Cd Length: 83  Bit Score: 60.87  E-value: 1.50e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 617 DLEVVEGSAARFDCKIEGYPDPEVVWFKDDQSIRESRhFQIDYDEdgncSLIISDVCGDDDAKYTCKAVNSLGEATCTAE 696
Cdd:cd05725     6 NQVVLVDDSAEFQCEVGGDPVPTVRWRKEDGELPKGR-YEILDDH----SLKIRKVTAGDMGSYTCVAENMVGKIEASAT 80

                  ...
gi 1034633499 697 LIV 699
Cdd:cd05725    81 LTV 83
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
620-699 1.53e-11

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 60.68  E-value: 1.53e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 620 VVEGSAARFDCKIEGYPDPEVVWFKDDQSIRESRHFQIDYDEDgNCSLIISDVCGDDDAKYTCKAVNSLGEATCTAELIV 699
Cdd:cd05748     4 VRAGESLRLDIPIKGRPTPTVTWSKDGQPLKETGRVQIETTAS-STSLVIKNAKRSDSGKYTLTLKNSAGEKSATINVKV 82
PTKc_TrkA cd05092
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase A; PTKs catalyze ...
270-474 1.72e-11

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: 65.37  E-value: 1.72e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 270 LGSGKFGQVF-----RLVEKKTRKVWAGKFFKAYSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEIVSGG 344
Cdd:cd05092    13 LGEGAFGKVFlaechNLLPEQDKMLVAVKALKEATESARQDFQREAELLTVLQHQHIVRFYGVCTEGEPLIMVFEYMRHG 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 345 EL--FER-------IIDED-----FELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENimCVNKTGTRIKLIDFGLAR 410
Cdd:cd05092    93 DLnrFLRshgpdakILDGGegqapGQLTLGQMLQIASQIASGMVYLASLHFVHRDLATRN--CLVGQGLVVKIGDFGMSR 170
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034633499 411 RLENAGSLKVLFGT--P-EFVAPEVINYEPIGYATDMWSIGVICY-ILVSGLSPFMGDNDNETLANVT 474
Cdd:cd05092   171 DIYSTDYYRVGGRTmlPiRWMPPESILYRKFTTESDIWSFGVVLWeIFTYGKQPWYQLSNTEAIECIT 238
STKc_RIP4_like cd14025
Catalytic domain of the Serine/Threonine kinases, Receptor Interacting Protein 4 and similar ...
268-466 2.01e-11

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


Pssm-ID: 270927 [Multi-domain]  Cd Length: 267  Bit Score: 65.21  E-value: 2.01e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 268 ERLGSGKFGQVFRlVEKKTRKVW-AGKFFKAY--SAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMvlEIVSGG 344
Cdd:cd14025     2 EKVGSGGFGQVYK-VRHKHWKTWlAIKCPPSLhvDDSERMELLEEAKKMEMAKFRHILPVYGICSEPVGLVM--EYMETG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 345 ELFERIIDEDFELTERECIKYmrQISEGVEYIH--KQGIVHLDLKPENIMCvnKTGTRIKLIDFGLARRLENAGSLKV-- 420
Cdd:cd14025    79 SLEKLLASEPLPWELRFRIIH--ETAVGMNFLHcmKPPLLHLDLKPANILL--DAHYHVKISDFGLAKWNGLSHSHDLsr 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1034633499 421 --LFGTPEFVAPEVI--NYEPIGYATDMWSIGVICYILVSGLSPFMGDND 466
Cdd:cd14025   155 dgLRGTIAYLPPERFkeKNRCPDTKHDVYSFAIVIWGILTQKKPFAGENN 204
STKc_GAK cd14036
Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs ...
266-461 2.04e-11

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: 65.22  E-value: 2.04e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 266 IEERLGSGKFGQVFRLVEKKTRKVWAGKFFKAYSAKEKENIRQEISIMNCLH-HPKLVQCVDAF----EEK----ANIVM 336
Cdd:cd14036     4 IKRVIAEGGFAFVYEAQDVGTGKEYALKRLLSNEEEKNKAIIQEINFMKKLSgHPNIVQFCSAAsigkEESdqgqAEYLL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 337 VLEIVSGGEL-FERIIDEDFELTERECIKYMRQISEGVEYIHKQG--IVHLDLKPENIMCVNKtGTrIKLIDFGLA---- 409
Cdd:cd14036    84 LTELCKGQLVdFVKKVEAPGPFSPDTVLKIFYQTCRAVQHMHKQSppIIHRDLKIENLLIGNQ-GQ-IKLCDFGSAttea 161
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034633499 410 -----------RRLENAGSLKVLfgTPEFVAPEVI----NYePIGYATDMWSIGVICYILVSGLSPF 461
Cdd:cd14036   162 hypdyswsaqkRSLVEDEITRNT--TPMYRTPEMIdlysNY-PIGEKQDIWALGCILYLLCFRKHPF 225
IgI_Myotilin_C cd05892
C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily ...
609-699 2.35e-11

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


Pssm-ID: 409473  Cd Length: 92  Bit Score: 60.55  E-value: 2.35e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 609 PYFSKTIRDLEVVEGSAARFDCKIEGYPDPEVVWFKDDQSIR-ESRHFQIDYDEDGNCSLIISDVCGDDDAKYTCKAVNS 687
Cdd:cd05892     1 PMFIQKPQNKKVLEGDPVRLECQISAIPPPQIFWKKNNEMLQyNTDRISLYQDNCGRICLLIQNANKKDAGWYTVSAVNE 80
                          90
                  ....*....|..
gi 1034633499 688 LGEATCTAELIV 699
Cdd:cd05892    81 AGVVSCNARLDV 92
PTKc_RET cd05045
Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs ...
270-463 2.37e-11

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: 65.37  E-value: 2.37e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 270 LGSGKFGQV-----FRLVEKKTRKVWAGKFFK-AYSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLE---- 339
Cdd:cd05045     8 LGEGEFGKVvkataFRLKGRAGYTTVAVKMLKeNASSSELRDLLSEFNLLKQVNHPHVIKLYGACSQDGPLLLIVEyaky 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 340 -----------------IVSGGELFERIIDEDFE--LTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNktGTR 400
Cdd:cd05045    88 gslrsflresrkvgpsyLGSDGNRNSSYLDNPDEraLTMGDLISFAWQISRGMQYLAEMKLVHRDLAARNVLVAE--GRK 165
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034633499 401 IKLIDFGLARRL-ENAGSLKVLFG-TP-EFVAPEVINYEPIGYATDMWSIGVICYILVS-GLSPFMG 463
Cdd:cd05045   166 MKISDFGLSRDVyEEDSYVKRSKGrIPvKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTlGGNPYPG 232
PTKc_PDGFR cd05055
Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; ...
270-463 2.93e-11

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: 65.20  E-value: 2.93e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 270 LGSGKFGQV-----FRLVEKKTRKVWAGKFFKAYS-AKEKENIRQEISIMNCL-HHPKLVQCVDAFEEKANIVMVLEIVS 342
Cdd:cd05055    43 LGAGAFGKVveataYGLSKSDAVMKVAVKMLKPTAhSSEREALMSELKIMSHLgNHENIVNLLGACTIGGPILVITEYCC 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 343 GGEL--FERIIDEDFeLTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNktGTRIKLIDFGLARRLENAGSLKV 420
Cdd:cd05055   123 YGDLlnFLRRKRESF-LTLEDLLSFSYQVAKGMAFLASKNCIHRDLAARNVLLTH--GKIVKICDFGLARDIMNDSNYVV 199
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1034633499 421 ---LFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVS-GLSPFMG 463
Cdd:cd05055   200 kgnARLPVKWMAPESIFNCVYTFESDVWSYGILLWEIFSlGSNPYPG 246
IgI_2_Robo cd05724
Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
616-699 3.81e-11

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


Pssm-ID: 409389 [Multi-domain]  Cd Length: 87  Bit Score: 59.72  E-value: 3.81e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 616 RDLEVVEGSAARFDCKI-EGYPDPEVVWFKDDQSIRE-SRHFQIdyDEDGNcsLIISDVCGDDDAKYTCKAVNSLGE-AT 692
Cdd:cd05724     5 SDTQVAVGEMAVLECSPpRGHPEPTVSWRKDGQPLNLdNERVRI--VDDGN--LLIAEARKSDEGTYKCVATNMVGErES 80

                  ....*..
gi 1034633499 693 CTAELIV 699
Cdd:cd05724    81 RAARLSV 87
STKc_PRP4 cd14135
Catalytic domain of the Serine/Threonine Kinase, Pre-mRNA-Processing factor 4; STKs catalyze ...
365-470 4.21e-11

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: 64.94  E-value: 4.21e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 365 YMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGTRIKLIDFGLArrlENAGSLKVlfgTPEFV-----APEVINYEPIG 439
Cdd:cd14135   110 YAQQLFLALKHLKKCNILHADIKPDNIL-VNEKKNTLKLCDFGSA---SDIGENEI---TPYLVsrfyrAPEIILGLPYD 182
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1034633499 440 YATDMWSIGVICYILVSGLSPFMGDNDNETL 470
Cdd:cd14135   183 YPIDMWSVGCTLYELYTGKILFPGKTNNHML 213
IgI_M-protein_C cd05891
C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily ...
620-692 4.47e-11

C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of M-protein (also known as myomesin-2). M-protein is a structural protein localized to the M-band, a transverse structure in the center of the sarcomere, and is a candidate for M-band bridges. M-protein is modular consisting mainly of repetitive IG-like and fibronectin type III (FnIII) domains and has a muscle-type specific expression pattern. M-protein is present in fast fibers.


Pssm-ID: 143299  Cd Length: 92  Bit Score: 59.54  E-value: 4.47e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034633499 620 VVEGSAARFDCKIEGYPDPEVVWFKDDQSIRESRHFQIDYDEDGNCSLIISDVCGDDDAKYTCKAVNSLGEAT 692
Cdd:cd05891    13 IMEGKTLNLTCTVFGNPDPEVIWFKNDQDIELSEHYSVKLEQGKYASLTIKGVTSEDSGKYSINVKNKYGGET 85
PK_TRB3 cd14024
Pseudokinase domain of Tribbles Homolog 3; The pseudokinase domain shows similarity to protein ...
356-519 4.72e-11

Pseudokinase domain of Tribbles Homolog 3; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. TRB3 binds and regulates ATF4, p65/RelA, and PKB (or Akt). It negatively regulates ATF4-mediated gene expression including that of CHOP (C/EBP homologous protein) and HO-1, which are both involved in modulating apoptosis. It also inhibits insulin-mediated phosphorylation of PKB and is a possible determinant of insulin resistance and related disorders. In osteoarthritic chondrocytes where it inhibits insulin-like growth factor 1-mediated cell survival, TRB3 is overexpressed, resulting in increased cell death. TRB3 is one of three Tribbles Homolog (TRB) proteins present in vertebrates that are encoded by three separate genes. TRB proteins interact with many proteins involved in signalling pathways. They play scaffold-like regulatory functions and affect many cellular processes such as mitosis, apoptosis, and gene expression. The TRB3 subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270926 [Multi-domain]  Cd Length: 242  Bit Score: 63.36  E-value: 4.72e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 356 ELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKTGTRIKLIDFGLARRLE-NAGSLKVLFGTPEFVAPEVIN 434
Cdd:cd14024    80 RLSEDEARGLFTQMARAVAHCHQHGVILRDLKLRRFVFTDELRTKLVLVNLEDSCPLNgDDDSLTDKHGCPAYVGPEILS 159
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 435 --YEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDFDdeafDEISDDAKDFISNLLKKDMKNRLDCTQ 512
Cdd:cd14024   160 srRSYSGKAADVWSLGVCLYTMLLGRYPFQDTEPAALFAKIRRGAFSLP----AWLSPGARCLVSCMLRRSPAERLKASE 235

                  ....*..
gi 1034633499 513 CLQHPWL 519
Cdd:cd14024   236 ILLHPWL 242
PTKc_Csk cd05082
Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the ...
266-461 5.30e-11

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: 63.46  E-value: 5.30e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 266 IEERLGSGKFGQVFrLVEKKTRKVwAGKFFKAYSAKEKenIRQEISIMNCLHHPKLVQCVDAF-EEKANIVMVLEIVSGG 344
Cdd:cd05082    10 LLQTIGKGEFGDVM-LGDYRGNKV-AVKCIKNDATAQA--FLAEASVMTQLRHSNLVQLLGVIvEEKGGLYIVTEYMAKG 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 345 ELFERIIDEDFELTEREC-IKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKTGTRIKliDFGL---ARRLENAGSLKV 420
Cdd:cd05082    86 SLVDYLRSRGRSVLGGDClLKFSLDVCEAMEYLEGNNFVHRDLAARNVLVSEDNVAKVS--DFGLtkeASSTQDTGKLPV 163
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1034633499 421 lfgtpEFVAPEVINYEPIGYATDMWSIGVICYILVS-GLSPF 461
Cdd:cd05082   164 -----KWTAPEALREKKFSTKSDVWSFGILLWEIYSfGRVPY 200
STKc_TGFbR_I cd14056
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta family Type ...
268-454 5.35e-11

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: 64.22  E-value: 5.35e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 268 ERLGSGKFGQVfRLVEKKTRKVwAGKFFkaYSAKEKENIR-QEISIMNCLHHPKLVQCV--DAFEEKAN--IVMVLEIVS 342
Cdd:cd14056     1 KTIGKGRYGEV-WLGKYRGEKV-AVKIF--SSRDEDSWFReTEIYQTVMLRHENILGFIaaDIKSTGSWtqLWLITEYHE 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 343 GGELFERIIDEdfELTERECIKYMRQISEGVEYIH--------KQGIVHLDLKPENIMcVNKTGTrIKLIDFGLARRLEN 414
Cdd:cd14056    77 HGSLYDYLQRN--TLDTEEALRLAYSAASGLAHLHteivgtqgKPAIAHRDLKSKNIL-VKRDGT-CCIADLGLAVRYDS 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1034633499 415 -AGSLKVLF----GTPEFVAPEVINyEPIGY-------ATDMWSIG-VICYIL 454
Cdd:cd14056   153 dTNTIDIPPnprvGTKRYMAPEVLD-DSINPksfesfkMADIYSFGlVLWEIA 204
PTKc_TrkC cd05094
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase C; PTKs catalyze ...
266-474 7.89e-11

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: 63.49  E-value: 7.89e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 266 IEERLGSGKFGQVF-----RLVEKKTRKVWAGKFFKAYSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEI 340
Cdd:cd05094     9 LKRELGEGAFGKVFlaecyNLSPTKDKMLVAVKTLKDPTLAARKDFQREAELLTNLQHDHIVKFYGVCGDGDPLIMVFEY 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 341 VSGGEL--FERIIDEDF-------------ELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENimCVNKTGTRIKLID 405
Cdd:cd05094    89 MKHGDLnkFLRAHGPDAmilvdgqprqakgELGLSQMLHIATQIASGMVYLASQHFVHRDLATRN--CLVGANLLVKIGD 166
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034633499 406 FGLARRLENAGSLKVLFGTP---EFVAPEVINYEPIGYATDMWSIGVICY-ILVSGLSPFMGDNDNETLANVT 474
Cdd:cd05094   167 FGMSRDVYSTDYYRVGGHTMlpiRWMPPESIMYRKFTTESDVWSFGVILWeIFTYGKQPWFQLSNTEVIECIT 239
PKc_MKK4 cd06616
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
261-517 8.41e-11

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: 63.54  E-value: 8.41e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 261 SDFYDIEErLGSGKFGQVFRLVEKKTRKVWAGKFFKAYS-AKEKENIRQEI-SIM---NClhhPKLVQCVDA-FEE-KAN 333
Cdd:cd06616     6 EDLKDLGE-IGRGAFGTVNKMLHKPSGTIMAVKRIRSTVdEKEQKRLLMDLdVVMrssDC---PYIVKFYGAlFREgDCW 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 334 IVMVLEIVSGGELFERIID-EDFELTERECIKYMRQISEGVEYIHKQ-GIVHLDLKPENIMcVNKTGTrIKLIDFGLARR 411
Cdd:cd06616    82 ICMELMDISLDKFYKYVYEvLDSVIPEEILGKIAVATVKALNYLKEElKIIHRDVKPSNIL-LDRNGN-IKLCDFGISGQ 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 412 LENAGSLKVLFGTPEFVAPEVINYEPI--GY--ATDMWSIGVICYILVSGLSPFMG-DNDNETLANVTSA---TWDFDDE 483
Cdd:cd06616   160 LVDSIAKTRDAGCRPYMAPERIDPSASrdGYdvRSDVWSLGITLYEVATGKFPYPKwNSVFDQLTQVVKGdppILSNSEE 239
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1034633499 484 AfdEISDDAKDFISNLLKKDMKNRLDCTQCLQHP 517
Cdd:cd06616   240 R--EFSPSFVNFVNLCLIKDESKRPKYKELLKHP 271
PHA03207 PHA03207
serine/threonine kinase US3; Provisional
208-452 8.64e-11

serine/threonine kinase US3; Provisional


Pssm-ID: 165473 [Multi-domain]  Cd Length: 392  Bit Score: 64.48  E-value: 8.64e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 208 NVYGTSEPSQESELTTVGEKPEEPKDEVEVSDDDEKEPEvDYRTVTiNTEQKVSDFYDIEERLGSGKFGQVF---RLVEK 284
Cdd:PHA03207   40 DKFDDCDELGDSDDVTHATDYDADEESLSPQTDVCQEPC-ETTSSS-DPASVVRMQYNILSSLTPGSEGEVFvctKHGDE 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 285 KTRKVwagkFFKAYSAKEkeNIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEIVSGgELFErIIDEDFELTERECIK 364
Cdd:PHA03207  118 QRKKV----IVKAVTGGK--TPGREIDILKTISHRAIINLIHAYRWKSTVCMVMPKYKC-DLFT-YVDRSGPLPLEQAIT 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 365 YMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGTRIkLIDFGLARRLENAGSLKVLF---GTPEFVAPEVINYEPIGYA 441
Cdd:PHA03207  190 IQRRLLEALAYLHGRGIIHRDVKTENIF-LDEPENAV-LGDFGAACKLDAHPDTPQCYgwsGTLETNSPELLALDPYCAK 267
                         250
                  ....*....|.
gi 1034633499 442 TDMWSIGVICY 452
Cdd:PHA03207  268 TDIWSAGLVLF 278
PTKc_ALK_LTK cd05036
Catalytic domain of the Protein Tyrosine Kinases, Anaplastic Lymphoma Kinase and Leukocyte ...
270-475 1.01e-10

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: 63.18  E-value: 1.01e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 270 LGSGKFGQVFRLV------EKKTRKVwAGKFFKAYSAKEKEN-IRQEISIMNCLHHPKLVQCVD-AFEEKANIVmVLEIV 341
Cdd:cd05036    14 LGQGAFGEVYEGTvsgmpgDPSPLQV-AVKTLPELCSEQDEMdFLMEALIMSKFNHPNIVRCIGvCFQRLPRFI-LLELM 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 342 SGGEL--FER----IIDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKTGTRI-KLIDFGLARRLEN 414
Cdd:cd05036    92 AGGDLksFLRenrpRPEQPSSLTMLDLLQLAQDVAKGCRYLEENHFIHRDIAARNCLLTCKGPGRVaKIGDFGMARDIYR 171
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 415 A--------GSLKVLFGTPEFVAPEVINYEpigyaTDMWSIGVICYILVS-GLSPFMGDNDNETLANVTS 475
Cdd:cd05036   172 AdyyrkggkAMLPVKWMPPEAFLDGIFTSK-----TDVWSFGVLLWEIFSlGYMPYPGKSNQEVMEFVTS 236
PTKc_Tyro3 cd05074
Catalytic domain of the Protein Tyrosine Kinase, Tyro3; PTKs catalyze the transfer of the ...
270-468 1.05e-10

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: 63.01  E-value: 1.05e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 270 LGSGKFGQV----FRLVEKKTRKVwAGKFFKA--YSAKEKENIRQEISIMNCLHHPKLVQCVDAF-----EEKANIVMV- 337
Cdd:cd05074    17 LGKGEFGSVreaqLKSEDGSFQKV-AVKMLKAdiFSSSDIEEFLREAACMKEFDHPNVIKLIGVSlrsraKGRLPIPMVi 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 338 LEIVSGGEL-----FERIIDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGTrIKLIDFGLARRL 412
Cdd:cd05074    96 LPFMKHGDLhtfllMSRIGEEPFTLPLQTLVRFMIDIASGMEYLSSKNFIHRDLAARNCM-LNENMT-VCVADFGLSKKI 173
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034633499 413 EN--------AGSLKVLFGTPEFVAPEVINYEpigyaTDMWSIGVICY-ILVSGLSPFMGDNDNE 468
Cdd:cd05074   174 YSgdyyrqgcASKLPVKWLALESLADNVYTTH-----SDVWAFGVTMWeIMTRGQTPYAGVENSE 233
IgI_APEG-1_like cd20975
Immunoglobulin-like domain of human Aortic Preferentially Expressed Protein-1 (APEG-1) and ...
609-699 1.09e-10

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


Pssm-ID: 409567  Cd Length: 91  Bit Score: 58.64  E-value: 1.09e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 609 PYFSKTIRDLEVVEGSAARFDCKIEGYPDPEVVWFKDDQSIRESRHFQIDYDEDGNCSLIISDVCGDDDAKYTCKAVNSL 688
Cdd:cd20975     1 PTFKVSLMDQSVREGQDVIMSIRVQGEPKPVVSWLRNRQPVRPDQRRFAEEAEGGLCRLRILAAERGDAGFYTCKAVNEY 80
                          90
                  ....*....|.
gi 1034633499 689 GEATCTAELIV 699
Cdd:cd20975    81 GARQCEARLEV 91
pknD PRK13184
serine/threonine-protein kinase PknD;
264-461 1.51e-10

serine/threonine-protein kinase PknD;


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 64.79  E-value: 1.51e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 264 YDIEERLGSGKFGQVFRLVEKK-TRKVWAGKFFKAYSAKE--KENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEI 340
Cdd:PRK13184    4 YDIIRLIGKGGMGEVYLAYDPVcSRRVALKKIREDLSENPllKKRFLREAKIAADLIHPGIVPVYSICSDGDPVYYTMPY 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 341 VSG---GELFERIIDEDF---ELTERECIK-YMR---QISEGVEYIHKQGIVHLDLKPENIMcVNKTGtRIKLIDFGLAR 410
Cdd:PRK13184   84 IEGytlKSLLKSVWQKESlskELAEKTSVGaFLSifhKICATIEYVHSKGVLHRDLKPDNIL-LGLFG-EVVILDWGAAI 161
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 411 RL----ENAGSLKV---------------LFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPF 461
Cdd:PRK13184  162 FKkleeEDLLDIDVdernicyssmtipgkIVGTPDYMAPERLLGVPASESTDIYALGVILYQMLTLSFPY 231
PHA03210 PHA03210
serine/threonine kinase US3; Provisional
239-456 1.68e-10

serine/threonine kinase US3; Provisional


Pssm-ID: 165476 [Multi-domain]  Cd Length: 501  Bit Score: 63.94  E-value: 1.68e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 239 DDDEKEPEVDYRTVTINTEQKVSD----FYDIEERLGSGKFGQVF-----RLV--EKKTRKVWAGKFFKAYS----AKEK 303
Cdd:PHA03210  121 DFDEAPPDAAGPVPLAQAKLKHDDeflaHFRVIDDLPAGAFGKIFicalrASTeeAEARRGVNSTNQGKPKCerliAKRV 200
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 304 EN-------IRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEIVSGgELFERIIDEDFELTERECIK----YMRQISEG 372
Cdd:PHA03210  201 KAgsraaiqLENEILALGRLNHENILKIEEILRSEANTYMITQKYDF-DLYSFMYDEAFDWKDRPLLKqtraIMKQLLCA 279
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 373 VEYIHKQGIVHLDLKPENIMcVNKTGTrIKLIDFGLARRLENAgslKVLF-----GTPEFVAPEVINYEPIGYATDMWSI 447
Cdd:PHA03210  280 VEYIHDKKLIHRDIKLENIF-LNCDGK-IVLGDFGTAMPFEKE---REAFdygwvGTVATNSPEILAGDGYCEITDIWSC 354

                  ....*....
gi 1034633499 448 GVICYILVS 456
Cdd:PHA03210  355 GLILLDMLS 363
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
126-269 1.70e-10

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 64.25  E-value: 1.70e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 126 TVVDKPDPPAG-TpcASDIRSSSLTLSWYGSSydgGSAVQSYSIEIWDSANKTWKELA-TCRSTSFNVQDLLPDHEYKFR 203
Cdd:COG3401   322 TDLTPPAAPSGlT--ATAVGSSSITLSWTASS---DADVTGYNVYRSTSGGGTYTKIAeTVTTTSYTDTGLTPGTTYYYK 396
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034633499 204 VRAINVYGT-SEPSQESELTTV----GEKPEEPKDEVEVSDDDEKEPEVDYRTVTINTEQKVSDFYDIEER 269
Cdd:COG3401   397 VTAVDAAGNeSAPSEEVSATTAsaasGESLTASVDAVPLTDVAGATAAASAASNPGVSAAVLADGGDTGNA 467
PK_GC cd13992
Pseudokinase domain of membrane Guanylate Cyclase receptors; The pseudokinase domain shows ...
299-479 1.75e-10

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: 62.41  E-value: 1.75e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 299 SAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEIVSGGELFERIIDEDFELTERECIKYMRQISEGVEYIHK 378
Cdd:cd13992    36 SRTEKRTILQELNQLKELVHDNLNKFIGICINPPNIAVVTEYCTRGSLQDVLLNREIKMDWMFKSSFIKDIVKGMNYLHS 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 379 QGI-VHLDLKPENimCVNKTGTRIKLIDFGLARRLENAGSLKvLFGTPE-----FVAPEVINYEPIGY----ATDMWSIG 448
Cdd:cd13992   116 SSIgYHGRLKSSN--CLVDSRWVVKLTDFGLRNLLEEQTNHQ-LDEDAQhkkllWTAPELLRGSLLEVrgtqKGDVYSFA 192
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1034633499 449 VICYILVSGLSPFMGDNDNETLANVTSATWD 479
Cdd:cd13992   193 IILYEILFRSDPFALEREVAIVEKVISGGNK 223
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
37-114 2.10e-10

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 57.19  E-value: 2.10e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034633499  37 PPQIIQFPEDQKVRAGESVELFGKVTGTQPITCTWMKFRKQIQESEHMKVENSENGSKLTILAARQEHCGCYTLLVEN 114
Cdd:pfam13927   1 KPVITVSPSSVTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
PHA03209 PHA03209
serine/threonine kinase US3; Provisional
233-452 2.15e-10

serine/threonine kinase US3; Provisional


Pssm-ID: 177557 [Multi-domain]  Cd Length: 357  Bit Score: 62.97  E-value: 2.15e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 233 DEVEVSDDDE-KEPEVDYRTVTINTEQK----VSDF-YDIEERLGSGKFGQVF---RLVEKKTRKVWAGkffkaysakEK 303
Cdd:PHA03209   31 GDLEYSDDDSaSESDDDDDDGLIPTKQKarevVASLgYTVIKTLTPGSEGRVFvatKPGQPDPVVLKIG---------QK 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 304 ENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEIVSGgELFERIIDEDFELTERECIKYMRQISEGVEYIHKQGIVH 383
Cdd:PHA03209  102 GTTLIEAMLLQNVNHPSVIRMKDTLVSGAITCMVLPHYSS-DLYTYLTKRSRPLPIDQALIIEKQILEGLRYLHAQRIIH 180
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034633499 384 LDLKPENIMcVNKTGTrIKLIDFGLARRLENAGSLKVLFGTPEFVAPEVINYEPIGYATDMWSIGVICY 452
Cdd:PHA03209  181 RDVKTENIF-INDVDQ-VCIGDLGAAQFPVVAPAFLGLAGTVETNAPEVLARDKYNSKADIWSAGIVLF 247
PKc_CLK3 cd14214
Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 3; Dual-specificity ...
256-470 2.25e-10

Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 3; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. CLK3 is predominantly expressed in mature spermatozoa, and might play a role in the fertilization process. 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 CLK3 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: 271116 [Multi-domain]  Cd Length: 331  Bit Score: 62.72  E-value: 2.25e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 256 TEQKVSDFYDIEERLGSGKFGQVFRLVEKKTRKVWAGKFFKAYSAKEKENIRQEISIMNCLHHP---KLVQCV---DAFE 329
Cdd:cd14214     7 IGDWLQERYEIVGDLGEGTFGKVVECLDHARGKSQVALKIIRNVGKYREAARLEINVLKKIKEKdkeNKFLCVlmsDWFN 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 330 EKANIVMVLEIVsGGELFERIIDEDFELTERECIKYMR-QISEGVEYIHKQGIVHLDLKPENIMCVNK------------ 396
Cdd:cd14214    87 FHGHMCIAFELL-GKNTFEFLKENNFQPYPLPHIRHMAyQLCHALKFLHENQLTHTDLKPENILFVNSefdtlynesksc 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 397 -----TGTRIKLIDFGLARRLENAGSlkVLFGTPEFVAPEVInyEPIGYAT--DMWSIGVICYILVSGLSPFMGDNDNET 469
Cdd:cd14214   166 eeksvKNTSIRVADFGSATFDHEHHT--TIVATRHYRPPEVI--LELGWAQpcDVWSLGCILFEYYRGFTLFQTHENREH 241

                  .
gi 1034633499 470 L 470
Cdd:cd14214   242 L 242
STKc_TTBK cd14017
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase; STKs catalyze the ...
264-446 2.47e-10

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


Pssm-ID: 270919 [Multi-domain]  Cd Length: 263  Bit Score: 61.89  E-value: 2.47e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 264 YDIEERLGSGKFGQVFRLVEKKTRKVWAGKFFKAysAKEKENIRQEISIM----NCLHHPKLVQCVDafEEKAN-IVMVL 338
Cdd:cd14017     2 WKVVKKIGGGGFGEIYKVRDVVDGEEVAMKVESK--SQPKQVLKMEVAVLkklqGKPHFCRLIGCGR--TERYNyIVMTL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 339 EIVSGGELFERIIDEDFelTERECIKYMRQISEGVEYIHKQGIVHLDLKPENImCVNKTGT---RIKLIDFGLARRLENA 415
Cdd:cd14017    78 LGPNLAELRRSQPRGKF--SVSTTLRLGIQILKAIEDIHEVGFLHRDVKPSNF-AIGRGPSderTVYILDFGLARQYTNK 154
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1034633499 416 -GSLKV-------LFGTPEFVAPEVINYEPIGYATDMWS 446
Cdd:cd14017   155 dGEVERpprnaagFRGTVRYASVNAHRNKEQGRRDDLWS 193
PTKc_Tie2 cd05088
Catalytic domain of the Protein Tyrosine Kinase, Tie2; PTKs catalyze the transfer of the ...
260-463 3.41e-10

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: 61.94  E-value: 3.41e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 260 VSDFYDI--EERLGSGKFGQVFRLVEKKT--RKVWAGKFFKAYSAKEKE-NIRQEISIMNCL-HHPKLVQCVDAFEEKAN 333
Cdd:cd05088     3 VLEWNDIkfQDVIGEGNFGQVLKARIKKDglRMDAAIKRMKEYASKDDHrDFAGELEVLCKLgHHPNIINLLGACEHRGY 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 334 IVMVLEIVSGGELFE-----RIIDED----------FELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKTG 398
Cdd:cd05088    83 LYLAIEYAPHGNLLDflrksRVLETDpafaianstaSTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYV 162
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034633499 399 TRIKliDFGLARRLE-----NAGSLKVlfgtpEFVAPEVINYEPIGYATDMWSIGVICYILVS-GLSPFMG 463
Cdd:cd05088   163 AKIA--DFGLSRGQEvyvkkTMGRLPV-----RWMAIESLNYSVYTTNSDVWSYGVLLWEIVSlGGTPYCG 226
IgI_Twitchin_like cd20949
C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, ...
618-699 3.60e-10

C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, and similar domains; member of the I-set IgSF domains; The members here are composed of the C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin and similar proteins, including Caenorhabditis elegans and Aplysia californica Twitchin, Drosophila melanogaster Projectin, and similar proteins. These are very large muscle proteins containing multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains and a single kinase domain near the C-terminus. In humans these proteins are called Titin. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig-like domain of the Twitchin is a member of the I-set IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins (titin, telokin, and twitchin), the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D.


Pssm-ID: 409541 [Multi-domain]  Cd Length: 89  Bit Score: 56.96  E-value: 3.60e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 618 LEVVEGSAARFDCKIEGYPDPEVVWFKDDQSIRESRHFQIDYD--EDGncsLIISDVCGDDDAKYTCKAVNSLGEATCTA 695
Cdd:cd20949     9 TTVKEGQSATILCEVKGEPQPNVTWHFNGQPISASVADMSKYRilADG---LLINKVTQDDTGEYTCRAYQVNSIASDMQ 85

                  ....
gi 1034633499 696 ELIV 699
Cdd:cd20949    86 ERTV 89
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
613-692 3.65e-10

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: 56.82  E-value: 3.65e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 613 KTIRDLEVVEGSAARFDCKI-EGYPDPEVVWFKDDQSIRESRHFQIDYDEDGNCSLIISDVCGDDDAKYTCKAVNSLGEA 691
Cdd:pfam00047   1 SAPPTVTVLEGDSATLTCSAsTGSPGPDVTWSKEGGTLIESLKVKHDNGRTTQSSLLISNVTKEDAGTYTCVVNNPGGSA 80

                  .
gi 1034633499 692 T 692
Cdd:pfam00047  81 T 81
Ig5_Contactin cd04969
Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth ...
609-699 3.71e-10

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


Pssm-ID: 409358 [Multi-domain]  Cd Length: 89  Bit Score: 57.08  E-value: 3.71e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 609 PYFSKT-IRDLE-VVEGSAARFDCKIEGYPDPEVVWFKDDQSIRESRhfQIDYDEDGncSLIISDVCGDDDAKYTCKAVN 686
Cdd:cd04969     1 PDFELNpVKKKIlAAKGGDVIIECKPKASPKPTISWSKGTELLTNSS--RICILPDG--SLKIKNVTKSDEGKYTCFAVN 76
                          90
                  ....*....|...
gi 1034633499 687 SLGEATCTAELIV 699
Cdd:cd04969    77 FFGKANSTGSLSV 89
PTKc_EGFR cd05108
Catalytic domain of the Protein Tyrosine Kinase, Epidermal Growth Factor Receptor; PTKs ...
270-463 5.04e-10

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: 61.58  E-value: 5.04e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 270 LGSGKFGQVFRLV-----EKKTRKVWAGKFFKAYSAKEKENIRQEISIMNCLHHPKLVQ----CVdafeeKANIVMVLEI 340
Cdd:cd05108    15 LGSGAFGTVYKGLwipegEKVKIPVAIKELREATSPKANKEILDEAYVMASVDNPHVCRllgiCL-----TSTVQLITQL 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 341 VSGGELFERIIDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCvnKTGTRIKLIDFGLARRL-------- 412
Cdd:cd05108    90 MPFGCLLDYVREHKDNIGSQYLLNWCVQIAKGMNYLEDRRLVHRDLAARNVLV--KTPQHVKITDFGLAKLLgaeekeyh 167
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1034633499 413 ENAGSLKVlfgtpEFVAPEVINYEPIGYATDMWSIGVICYILVS-GLSPFMG 463
Cdd:cd05108   168 AEGGKVPI-----KWMALESILHRIYTHQSDVWSYGVTVWELMTfGSKPYDG 214
PTKc_FGFR2 cd05101
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs ...
270-463 8.10e-10

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: 60.80  E-value: 8.10e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 270 LGSGKFGQVFRL----VEKKTRK---VWAGKFFKAySAKEKE--NIRQEISIMNCL-HHPKLVQCVDAFEEKANIVMVLE 339
Cdd:cd05101    32 LGEGCFGQVVMAeavgIDKDKPKeavTVAVKMLKD-DATEKDlsDLVSEMEMMKMIgKHKNIINLLGACTQDGPLYVIVE 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 340 IVSGGELFE-----------------RIIDEdfELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKtgTRIK 402
Cdd:cd05101   111 YASKGNLREylrarrppgmeysydinRVPEE--QMTFKDLVSCTYQLARGMEYLASQKCIHRDLAARNVLVTEN--NVMK 186
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 403 LIDFGLARRLENA--------GSLKVlfgtpEFVAPEVINYEPIGYATDMWSIGVICY-ILVSGLSPFMG 463
Cdd:cd05101   187 IADFGLARDINNIdyykkttnGRLPV-----KWMAPEALFDRVYTHQSDVWSFGVLMWeIFTLGGSPYPG 251
STKc_SRPK1 cd14216
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase 1; STKs ...
264-519 8.26e-10

Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SRPK1 binds with high affinity the alternative splicing factor, SRSF1 (serine/arginine-rich splicing factor 1), and regiospecifically phosphorylates 10-12 serines in its RS domain. It plays a role in the regulation of pre-mRNA splicing, chromatin structure, and germ cell development. SRPKs phosphorylate and regulate splicing factors from the SR protein family by specifically phosphorylating multiple serine residues residing in SR/RS dipeptide motifs (also known as RS domains). Phosphorylation of the RS domains enhances interaction with transportin SR and facilitates entry of the SR proteins into the nucleus. SRPKs contain a nonconserved insert domain, within the well-conserved catalytic kinase domain, that regulates their subcellular localization. The SRPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271118 [Multi-domain]  Cd Length: 349  Bit Score: 61.20  E-value: 8.26e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 264 YDIEERLGSGKFGQVFRLVEKKTRKVWAGKFFKA---YSAKEKENIRQEISIMNC----LHHPKLVQCVDAFE----EKA 332
Cdd:cd14216    12 YHVIRKLGWGHFSTVWLSWDIQGKRFVAMKVVKSaehYTETALDEIKLLKSVRNSdpndPNREMVVQLLDDFKisgvNGT 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 333 NIVMVLEIVsGGELFERIIDEDFELTERECIK-YMRQISEGVEYIH-KQGIVHLDLKPENI-MCVNKTGTR--------- 400
Cdd:cd14216    92 HICMVFEVL-GHHLLKWIIKSNYQGLPLPCVKkIIRQVLQGLDYLHtKCRIIHTDIKPENIlLSVNEQYIRrlaaeatew 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 401 ------------------IKLIDFGLA----------RRLENAGSLKVLFGTpefvapevinyepiGYAT--DMWSIGVI 450
Cdd:cd14216   171 qrnflvnplepknaeklkVKIADLGNAcwvhkhftedIQTRQYRSLEVLIGS--------------GYNTpaDIWSTACM 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 451 CYILVSG---LSPFMGDN---DNETLANVTS----------ATWDFDDEAFDEISD------------------------ 490
Cdd:cd14216   237 AFELATGdylFEPHSGEDysrDEDHIALIIEllgkvprkliVAGKYSKEFFTKKGDlkhitklkpwglfevlvekyewsq 316
                         330       340       350
                  ....*....|....*....|....*....|...
gi 1034633499 491 -DAK---DFISNLLKKDMKNRLDCTQCLQHPWL 519
Cdd:cd14216   317 eEAAgftDFLLPMLELIPEKRATAAECLRHPWL 349
PTKc_HER2 cd05109
Catalytic domain of the Protein Tyrosine Kinase, HER2; PTKs catalyze the transfer of the ...
270-463 8.55e-10

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: 60.42  E-value: 8.55e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 270 LGSGKFGQVFRLV-----EKKTRKVWAGKFFKAYSAKEKENIRQEISIMNCLHHPKLVQ----CVdafeeKANIVMVLEI 340
Cdd:cd05109    15 LGSGAFGTVYKGIwipdgENVKIPVAIKVLRENTSPKANKEILDEAYVMAGVGSPYVCRllgiCL-----TSTVQLVTQL 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499 341 VSGGELFERIIDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCvnKTGTRIKLIDFGLARRLE------- 413
Cdd:cd05109    90 MPYGCLLDYVRENKDRIGSQDLLNWCVQIAKGMSYLEEVRLVHRDLAARNVLV--KSPNHVKITDFGLARLLDideteyh 167
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1034633499 414 -NAGSLKVlfgtpEFVAPEVINYEPIGYATDMWSIGVICYILVS-GLSPFMG 463
Cdd:cd05109   168 aDGGKVPI-----KWMALESILHRRFTHQSDVWSYGVTVWELMTfGAKPYDG 214
IgI_APEG-1_like cd20975
Immunoglobulin-like domain of human Aortic Preferentially Expressed Protein-1 (APEG-1) and ...
46-127 1.61e-07

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


Pssm-ID: 409567  Cd Length: 91  Bit Score: 49.78  E-value: 1.61e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499  46 DQKVRAGESVELFGKVTGTQPITCTWMKFRKQIQESEHMKVENSENG-SKLTILAARQEHCGCYTLLVENKLGSRQAQVN 124
Cdd:cd20975     9 DQSVREGQDVIMSIRVQGEPKPVVSWLRNRQPVRPDQRRFAEEAEGGlCRLRILAAERGDAGFYTCKAVNEYGARQCEAR 88

                  ...
gi 1034633499 125 LTV 127
Cdd:cd20975    89 LEV 91
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
55-121 1.62e-07

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: 48.86  E-value: 1.62e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034633499  55 VELFGKVTGTQPITCTWMKFRKQIQESEHMKVENSENGSKLTILAARQEHCGCYTLLVENKLGSRQA 121
Cdd:cd00096     1 VTLTCSASGNPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAGGSAS 67
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
37-118 2.27e-07

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


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 49.12  E-value: 2.27e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499  37 PPQIIQFPEDQKVRAGESVELFGKVTGTQPITCTWMKFRKQIQESEHMKVENSENGSKLTILAARQEHCGCYTLLVENKL 116
Cdd:cd20972     1 PPQFIQKLRSQEVAEGSKVRLECRVTGNPTPVVRWFCEGKELQNSPDIQIHQEGDLHSLIIAEAFEEDTGRYSCLATNSV 80

                  ..
gi 1034633499 117 GS 118
Cdd:cd20972    81 GS 82
IgI_4_MYLK-like cd20976
Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a ...
37-127 4.67e-06

Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain from smooth muscle myosin light chain kinase (MYLK) and similar domains. 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 this group shows that the fourth Ig-like domain from myosin light chain kinase lacks this strand and thus 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: 409568 [Multi-domain]  Cd Length: 90  Bit Score: 45.32  E-value: 4.67e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499  37 PPQIIQFPEDQKVRAGESVELFGKVTGTQPITCTWMKFRKQIQESEHMKVENSENGsKLTILAARQEHCGCYTLLVENKL 116
Cdd:cd20976     1 APSFSSVPKDLEAVEGQDFVAQCSARGKPVPRITWIRNAQPLQYAADRSTCEAGVG-ELHIQDVLPEDHGTYTCLAKNAA 79
                          90
                  ....*....|.
gi 1034633499 117 GSRQAQVNLTV 127
Cdd:cd20976    80 GQVSCSAWVTV 90
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
38-127 6.80e-06

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


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 44.79  E-value: 6.80e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633499  38 PQIIQFPEDQKVRAGESVELFGKVTGTQPITCTWMKFRKQIQESEHMKVENSENGS-KLTILAARQEHCGCYTLLVENKL 116
Cdd:cd05744     1 PHFLQAPGDLEVQEGRLCRFDCKVSGLPTPDLFWQLNGKPVRPDSAHKMLVRENGRhSLIIEPVTKRDAGIYTCIARNRA 80
                          90
                  ....*....|.
gi 1034633499 117 GSRQAQVNLTV 127
Cdd:cd05744    81 GENSFNAELVV 91
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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