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Conserved domains on  [gi|118443927|ref|YP_878728|]
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sensory transduction histidine kinase [Clostridium novyi NT]

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List of domain hits

Name Accession Description Interval E-value
HATPase_c cd00075
Histidine kinase-like ATPases; This family includes several ATP-binding proteins for example: ...
1528-1631 1.31e-31

Histidine kinase-like ATPases; This family includes several ATP-binding proteins for example: histidine kinase, DNA gyrase B, topoisomerases, heat shock protein HSP90, phytochrome-like ATPases and DNA mismatch repair proteins


:

Pssm-ID: 238030  Cd Length: 103  Bit Score: 121.60  E-value: 1.31e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927 1528 IERIILNLLSNAVKFTNK-GGNIFVTMKEEDNNIVISVKDDGIGIPKEKQSIIFDRFiqVDKSLSRNREGSGIGLALVKS 1606
Cdd:cd00075     1 LQQVLLNLLSNAIKHTPEgGGRITISVERDGDHLEIRVEDNGPGIPEEDLERIFERF--SDGSRSRKGGGTGLGLSIVKK 78
                          90       100
                  ....*....|....*....|....*
gi 118443927 1607 IVELHDGNITLKSKLGRGSEFIIKL 1631
Cdd:cd00075    79 LVELHGGRIEVESEPGGGTTFTITL 103
HisKA cd00082
Histidine Kinase A (dimerization/phosphoacceptor) domain; Histidine Kinase A dimers are formed ...
1404-1473 8.78e-13

Histidine Kinase A (dimerization/phosphoacceptor) domain; Histidine Kinase A dimers are formed through parallel association of 2 domains creating 4-helix bundles; usually these domains contain a conserved His residue and are activated via trans-autophosphorylation by the catalytic domain of the histidine kinase. They subsequently transfer the phosphoryl group to the Asp acceptor residue of a response regulator protein. Two-component signalling systems, consisting of a histidine protein kinase that senses a signal input and a response regulator that mediates the output, are ancient and evolutionarily conserved signaling mechanisms in prokaryotes and eukaryotes.


:

Pssm-ID: 119399  Cd Length: 65  Bit Score: 66.08  E-value: 8.78e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927 1404 EEMRTEFFANISHELRTPLNVIfsgyQMLNVLLENEDLENkEKVDKYMGTVKQNCYRLVRLINNLIDITK 1473
Cdd:cd00082     1 LQAKGEFLANVSHELRTPLTAI----RGALELLEEELLDD-EEQREYLERIREEAERLLRLINDLLDLSR 65
AAA_16 pfam13191
AAA ATPase domain; This family of domains contain a P-loop motif that is characteristic of the ...
207-395 6.10e-21

AAA ATPase domain; This family of domains contain a P-loop motif that is characteristic of the AAA superfamily.


:

Pssm-ID: 257559  Cd Length: 156  Bit Score: 92.53  E-value: 6.10e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927   207 KIYGREKEIETIMDKYHKACRGTLQCVAISGDSGMGKTIIGSEISKRIVKEGGILLSSKCkkynNNVPYYPLIectrmli 286
Cdd:pfam13191    1 RLVGREEELERLLDALERVRSGRPGLVLLTGPSGVGKTSLLRELLERLARKGGGVLSGKC----DELPYAALR------- 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927   287 nkilmedeekisylkkEILKELGSnaQIITKFVPEAEFLigkqPPLEERGFIESKSRFNMVIIRFTRIILNMKKPIAIFL 366
Cdd:pfam13191   70 ----------------QLLRELLR--QLLDELLPELELL----PPVPGLPPDDLRNRLEDLLRRLLRRLAARERPLVLVL 127
                          170       180
                   ....*....|....*....|....*....
gi 118443927   367 EDIQWLDESSLYIIRKFLLNKENKYLFIL 395
Cdd:pfam13191  128 DDLQWADEASLALLLALARLLERLPLLLV 156
FhlA COG2203
FOG: GAF domain [Signal transduction mechanisms]
1220-1378 1.01e-13

FOG: GAF domain [Signal transduction mechanisms]


:

Pssm-ID: 225113  Cd Length: 175  Bit Score: 71.16  E-value: 1.01e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927 1220 QSISGEIVLENLLKELMINLIASVEAERGCLI-LNKNNKLFIEAEGEVDdiCSVMENPI-ALEEYTKISKLLVNYVVRTK 1297
Cdd:COG2203    11 AKIAQDLDLEEILQAALELLAELLGADRGLIYlLDEDGLLDGALVAEAA--EAGLEQLIdELFGLVILPACLIGIALREG 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927 1298 KSILLDDGKcEDIVFDDKYIVD--NKVKSILCTPIIAKEKIIGIIYLENRFSSGIFNEKRLSIVELIASQAAISIENAFM 1375
Cdd:COG2203    89 RPVVVEDIL-QDPRFRDNPLVLlePPIRSYLGVPLIAQGELLGLLCVHDSEPRRQWSEEELELLEELAEQVAIAIERARL 167

                  ...
gi 118443927 1376 YEE 1378
Cdd:COG2203   168 YEE 170
STKc_MSK_N cd05583
N-terminal catalytic domain of the Protein Serine/Threonine Kinase, Mitogen and ...
33-164 3.39e-12

N-terminal catalytic domain of the Protein Serine/Threonine Kinase, Mitogen and stress-activated kinase; Serine/Threonine Kinases (STKs), Mitogen and stress-activated kinase (MSK) subfamily, N-terminal catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The MSK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. 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, 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.


:

Pssm-ID: 173674 [Multi-domain]  Cd Length: 288  Bit Score: 67.51  E-value: 3.39e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927   33 KIVDAVSEVHKEGMIYKYLNPKNIILDINGQLKLM----------ESTFMCRDINYNLRYMAPEQIGRIKKNVDFSTDHY 102
Cdd:cd05583   113 EIVLALDHLHQLGIIYRDIKLENILLDSEGHVVLTdfglskeflaEEEERAYSFCGTIEYMAPEVIRGGSGGHDKAVDWW 192
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 118443927  103 SLGVIFYRMLTGKLPIEVDDEiklsycNTNKKPVSPKKIKNTIPL------VISKIVMKLLEKDSEER 164
Cdd:cd05583   193 SLGVLTFELLTGASPFTVDGE------QNSQSEISRRILKSKPPFpktmsaEARDFIQKLLEKDPKKR 254
COG3899 COG3899
Predicted ATPase [General function prediction only]
208-1020 4.64e-104

Predicted ATPase [General function prediction only]


:

Pssm-ID: 226415 [Multi-domain]  Cd Length: 849  Bit Score: 354.01  E-value: 4.64e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927  208 IYGREKEIETIMDKYHKACRGTLQCVAISGDSGMGKTIIGSEISKRIVKEGGILLSSKCKKYNNNVPYYPLIECTRMLIN 287
Cdd:COG3899     2 LYGRETELAQLLAAFDRVSKGRGEVVLVAGESGIGKSALVNEVHKPITQQRGYFIKGKFDQFERNIPLSPLVQAFRDLMG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927  288 KILMEDEEKISYLKKEILKELGSNAQIITKFVPEAEFLIGKQPPLEERGFIESKSRFNMVIIRFTRIILNMKKPIAIFLE 367
Cdd:COG3899    82 QLLSESDTRILSWRARLLAALGENGQVIIDVIPELELIIGKRPPALELSPTAAQNRFNLAFLRFIQVFTAEEHPLVIVLE 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927  368 DIQWLDESSLYIIRKFLLNKENKY-----LFILTTLRTTDVENNKFlkeiveQDDVLNIKLESLNKYSIENLICDTLYCS 442
Cdd:COG3899   162 DLHWADSASLKLLQLLMDRIAIGAyrdneVLLLHPLRPTLGEILKS------ATNITTITLAPLSRADTNQLVAATLGCT 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927  443 KEEVKELVKFINIRTDGNPFFIKTSIESMYLNGVLKFDYTNNKWAWNMKLLKNMKIENSIFEIIIRKINQLSSDTKEILK 522
Cdd:COG3899   236 KLLPAPLLELIFEKTKGNPFFIEEFLKALYEEGLLVFNFDTGAWQCSIASLGILATTDAVVEFLAARLQKLPGTTREVLK 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927  523 LGSCIGQEFSLKCISEILNTSINVIFNNIIPAITEGVIILDEYATKNPKNKV---YRFAHSQIQMQIYDGISKEKKEKYH 599
Cdd:COG3899   316 AAACIGNRFDLDTLAALAEDSPALEAAALLDALQEGLILPLSETYRFGSNVDiatYKFLHDRVQQAAYNLIPESQRQYLH 395
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927  600 LSIGRYFYNEYSKNNLESKLFEVVNQLNKGRNLITNYDEIYKLIKLNLNIGLKEKEAGIHQLALGYFEVAYNLLEENSWE 679
Cdd:COG3899   396 LRIGQLLEQNIPEAGQEEEIFDIVNQLNAGVGLITLEEAVDELAELNLLAGRKAKLRSAYSAAISYLERGLSLLLADAWQ 475
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927  680 KDYDLTYAVNIELAECEFMNKNFEKAEELFKIILKNVKTPWETIKIYNMKVCIYTYFKQMDKAIETGINALKVLGIHISE 759
Cdd:COG3899   476 NQYLLALMLHRLAAENAYLRGQFELSESLIEVVLICAASNLDGAKVYELVIQAYTAQKQRLEAIALGQNALQLLGIAFPE 555
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927  760 KP--SFIKICCETLKFRLMKKSI---VNNNRYIIKENGIMEELKKLFFNMSFLAilyDKNLF--ILLVLKEMQINLYNTK 832
Cdd:COG3899   556 KPclAELNQAGEEINQLLGDRAIeelLNLPAMTDPDKLAALRILLNLILALFLT---APNLFplIILTIVTLSLKYGNSS 632
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927  833 SNNEIFTniNYEFLIMNLLKNYGKSYEMALNDLKKCYKKIDTIIYAKAYTVFANFMVLWSNDYNTTLDHLCKCYNICMDT 912
Cdd:COG3899   633 ESAAAYV--RYGDILNSFLGDFEKAYEFGKLALQLLEKFNAKELKSKWYLEAGVFILHWNDHLKETISLFKEGLVAGLEF 710
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927  913 GENSCAAFTLNNMITVFLMKGENLLEIKNKIKVYIDDIEKSNFDDIRDNLVLNRRIIDVLIADEENEVLSAKDYIIEREY 992
Cdd:COG3899   711 GDLEFASYLAAFYLAEAYKQGELLDDLRQENENYSEALAPFNQVISMVYSVLLIQLIFNLELKSEAEYELIEKILLESYI 790
                         810       820       830       840
                  ....*....|....*....|....*....|....*....|.
gi 118443927  993 LG-------------MYTYKIMLNYILGNYEDSIEIMKARE 1020
Cdd:COG3899   791 LPyllaaknlngigdLYLSKELLLYLFIDAEQAVKLAELAE 831
BaeS COG0642
Signal transduction histidine kinase [Signal transduction mechanisms]
1329-1639 7.70e-57

Signal transduction histidine kinase [Signal transduction mechanisms]


:

Pssm-ID: 223715 [Multi-domain]  Cd Length: 336  Bit Score: 202.68  E-value: 7.70e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927 1329 PIIAKEKIIGIIYLENRFSSGIFNEKRLSIVELIASQAAISIENAFMYEEINTLNKELKNTVDERTKLLNE-SIKYEEMR 1407
Cdd:COG0642    36 ELLLLLLLTLLAALLVALLLLLLLLRRLLRPLLLLADAANALAAGLTRLVLASLGSELASLAHALNELLERlERLLRRAK 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927 1408 TEFFANISHELRTPLNVIfsgyQMLNVLLENEDLENKEKvdkYMGTVKQNCYRLVRLINNLIDITKIDSGF-FKLNMINV 1486
Cdd:COG0642   116 REFLANISHELRTPLTAI----RGLLELLLEGLLDPQRE---LLEIIEEEAERLLRLVNDLLDLSRLEAGTkLKLLLELV 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927 1487 NIVNIVETITLSVAQYIESKGINLIFDtFIEEKTMACDVDKIERIILNLLSNAVKFTNkGGNIFVTMKEEDNNIVISVKD 1566
Cdd:COG0642   189 DLAELLEEVVRLLAPLAQEKGIELAVD-LPELPYVLGDPERLRQVLVNLLSNAIKYTP-GGEITISVRQDDEQVTISVED 266
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 118443927 1567 DGIGIPKEKQSIIFDRFIQVDKSlsrnREGSGIGLALVKSIVELHDGNITLKSKLGRGSEFIIKLPCKVLEKQ 1639
Cdd:COG0642   267 TGPGIPEEELERIFEPFFRTDKS----RSGTGLGLAIVKRIVELHGGTISVESEPGKGTTFTIRLPLAPAAAD 335
 
Name Accession Description Interval E-value
HATPase_c cd00075
Histidine kinase-like ATPases; This family includes several ATP-binding proteins for example: ...
1528-1631 1.31e-31

Histidine kinase-like ATPases; This family includes several ATP-binding proteins for example: histidine kinase, DNA gyrase B, topoisomerases, heat shock protein HSP90, phytochrome-like ATPases and DNA mismatch repair proteins


Pssm-ID: 238030  Cd Length: 103  Bit Score: 121.60  E-value: 1.31e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927 1528 IERIILNLLSNAVKFTNK-GGNIFVTMKEEDNNIVISVKDDGIGIPKEKQSIIFDRFiqVDKSLSRNREGSGIGLALVKS 1606
Cdd:cd00075     1 LQQVLLNLLSNAIKHTPEgGGRITISVERDGDHLEIRVEDNGPGIPEEDLERIFERF--SDGSRSRKGGGTGLGLSIVKK 78
                          90       100
                  ....*....|....*....|....*
gi 118443927 1607 IVELHDGNITLKSKLGRGSEFIIKL 1631
Cdd:cd00075    79 LVELHGGRIEVESEPGGGTTFTITL 103
HisKA cd00082
Histidine Kinase A (dimerization/phosphoacceptor) domain; Histidine Kinase A dimers are formed ...
1404-1473 8.78e-13

Histidine Kinase A (dimerization/phosphoacceptor) domain; Histidine Kinase A dimers are formed through parallel association of 2 domains creating 4-helix bundles; usually these domains contain a conserved His residue and are activated via trans-autophosphorylation by the catalytic domain of the histidine kinase. They subsequently transfer the phosphoryl group to the Asp acceptor residue of a response regulator protein. Two-component signalling systems, consisting of a histidine protein kinase that senses a signal input and a response regulator that mediates the output, are ancient and evolutionarily conserved signaling mechanisms in prokaryotes and eukaryotes.


Pssm-ID: 119399  Cd Length: 65  Bit Score: 66.08  E-value: 8.78e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927 1404 EEMRTEFFANISHELRTPLNVIfsgyQMLNVLLENEDLENkEKVDKYMGTVKQNCYRLVRLINNLIDITK 1473
Cdd:cd00082     1 LQAKGEFLANVSHELRTPLTAI----RGALELLEEELLDD-EEQREYLERIREEAERLLRLINDLLDLSR 65
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
1524-1632 9.20e-38

Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.


Pssm-ID: 214643  Cd Length: 111  Bit Score: 139.71  E-value: 9.20e-38
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927   1524 DVDKIERIILNLLSNAVKFTNKGGNIFVTMKEEDNNIVISVKDDGIGIPKEKQSIIFDRFIQVDKSlSRNREGSGIGLAL 1603
Cdd:smart00387    2 DPDRLRQVLSNLLDNAIKYTPEGGRITVTLERDGDHVEITVEDNGPGIPPEDLEKIFEPFFRTDKR-SRKIGGTGLGLSI 80
                            90       100
                    ....*....|....*....|....*....
gi 118443927   1604 VKSIVELHDGNITLKSKLGRGSEFIIKLP 1632
Cdd:smart00387   81 VKKLVELHGGEISVESEPGGGTTFTITLP 109
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
1524-1632 7.34e-35

Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the structurally related ATPase domains of histidine kinase, DNA gyrase B and HSP90.


Pssm-ID: 251347  Cd Length: 111  Bit Score: 131.29  E-value: 7.34e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927  1524 DVDKIERIILNLLSNAVKFTNKGGNIFVTMKEEDNNIVISVKDDGIGIPKEKQSIIFDRFIQVDKSlSRNREGSGIGLAL 1603
Cdd:pfam02518    2 DEDRLRQVLSNLLDNAIKHAPAGGEIEVTLERDGGRLRITVEDNGIGIPPEDLPKIFEPFFRTDGS-RSKVGGTGLGLSI 80
                           90       100
                   ....*....|....*....|....*....
gi 118443927  1604 VKSIVELHDGNITLKSKLGRGSEFIIKLP 1632
Cdd:pfam02518   81 VRKLVELHGGTITVESEPGGGTTFTLTLP 109
AAA_16 pfam13191
AAA ATPase domain; This family of domains contain a P-loop motif that is characteristic of the ...
207-395 6.10e-21

AAA ATPase domain; This family of domains contain a P-loop motif that is characteristic of the AAA superfamily.


Pssm-ID: 257559  Cd Length: 156  Bit Score: 92.53  E-value: 6.10e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927   207 KIYGREKEIETIMDKYHKACRGTLQCVAISGDSGMGKTIIGSEISKRIVKEGGILLSSKCkkynNNVPYYPLIectrmli 286
Cdd:pfam13191    1 RLVGREEELERLLDALERVRSGRPGLVLLTGPSGVGKTSLLRELLERLARKGGGVLSGKC----DELPYAALR------- 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927   287 nkilmedeekisylkkEILKELGSnaQIITKFVPEAEFLigkqPPLEERGFIESKSRFNMVIIRFTRIILNMKKPIAIFL 366
Cdd:pfam13191   70 ----------------QLLRELLR--QLLDELLPELELL----PPVPGLPPDDLRNRLEDLLRRLLRRLAARERPLVLVL 127
                          170       180
                   ....*....|....*....|....*....
gi 118443927   367 EDIQWLDESSLYIIRKFLLNKENKYLFIL 395
Cdd:pfam13191  128 DDLQWADEASLALLLALARLLERLPLLLV 156
FhlA COG2203
FOG: GAF domain [Signal transduction mechanisms]
1220-1378 1.01e-13

FOG: GAF domain [Signal transduction mechanisms]


Pssm-ID: 225113  Cd Length: 175  Bit Score: 71.16  E-value: 1.01e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927 1220 QSISGEIVLENLLKELMINLIASVEAERGCLI-LNKNNKLFIEAEGEVDdiCSVMENPI-ALEEYTKISKLLVNYVVRTK 1297
Cdd:COG2203    11 AKIAQDLDLEEILQAALELLAELLGADRGLIYlLDEDGLLDGALVAEAA--EAGLEQLIdELFGLVILPACLIGIALREG 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927 1298 KSILLDDGKcEDIVFDDKYIVD--NKVKSILCTPIIAKEKIIGIIYLENRFSSGIFNEKRLSIVELIASQAAISIENAFM 1375
Cdd:COG2203    89 RPVVVEDIL-QDPRFRDNPLVLlePPIRSYLGVPLIAQGELLGLLCVHDSEPRRQWSEEELELLEELAEQVAIAIERARL 167

                  ...
gi 118443927 1376 YEE 1378
Cdd:COG2203   168 YEE 170
HisKA pfam00512
His Kinase A (phospho-acceptor) domain; Dimerization and phospho-acceptor domain of histidine ...
1406-1477 1.08e-12

His Kinase A (phospho-acceptor) domain; Dimerization and phospho-acceptor domain of histidine kinases.


Pssm-ID: 249920  Cd Length: 66  Bit Score: 65.66  E-value: 1.08e-12
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 118443927  1406 MRTEFFANISHELRTPLNVIfsgyqMLNV-LLENEDLENKEKvdKYMGTVKQNCYRLVRLINNLIDITKIDSG 1477
Cdd:pfam00512    1 AKSEFLANLSHELRTPLTAI-----RGYLeLLLDTELSEEQR--EYLETILRSAERLLRLINDLLDLSRIEAG 66
GAF_2 pfam13185
GAF domain;
1228-1371 2.43e-12

GAF domain;


Pssm-ID: 257553  Cd Length: 150  Bit Score: 66.85  E-value: 2.43e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927  1228 LENLLKELMINLIASVEAERGCL-ILNKNNKLFIEAEGEVDDICSVMENPIALEEYTKISKLLVNY---VVRTKKSILLD 1303
Cdd:pfam13185    4 LEELLEAILEALLELTGSEAGFIgLLDEDGTLLLLAASGGTEELLRELAALSGELGGPPAAGAVGLgegALRTGKPVIIN 83
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 118443927  1304 DGKCEDIVFDDKYIVDNKVKSILCTPIIAKEKIIGIIYLENRfSSGIFNEKRLSIVELIASQAAISIE 1371
Cdd:pfam13185   84 DVASDPSGAGGLPAGHEGLRSFLSVPLISGGRVIGVLALGSK-EPGAFDEEDLELLELLAEQIAIAIE 150
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
1228-1380 3.16e-12

Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these domains in PDE6B result in autosomal recessive inheritance of retinitis pigmentosa.


Pssm-ID: 214500  Cd Length: 149  Bit Score: 66.25  E-value: 3.16e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927   1228 LENLLKELMINLIASVEAERGCLILNKNNKLFIEAEGEVDDICsvmenPIALEEYTKISKLLVNYVVRTKKSILLDDGKC 1307
Cdd:smart00065    2 LEELLQTILEELRQLLGADRVLIYLVDENDRGELVLVAADGLT-----LPTLGIRFPLDEGLAGRVAETGRPLNIPDVEA 76
                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 118443927   1308 EDIVFDDKYIVDNKVKSILCTPIIAKEKIIGIIYLENRFSSGIFNEKRLSIVELIASQAAISIENAFMYEEIN 1380
Cdd:smart00065   77 DPLFAEDLLGRYQGVRSFLAVPLVADGELVGVLALHNKKSPRPFTEEDEELLQALANQLAIALANAQLYEELR 149
STKc_MSK_N cd05583
N-terminal catalytic domain of the Protein Serine/Threonine Kinase, Mitogen and ...
33-164 3.39e-12

N-terminal catalytic domain of the Protein Serine/Threonine Kinase, Mitogen and stress-activated kinase; Serine/Threonine Kinases (STKs), Mitogen and stress-activated kinase (MSK) subfamily, N-terminal catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The MSK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. 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, 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.


Pssm-ID: 173674 [Multi-domain]  Cd Length: 288  Bit Score: 67.51  E-value: 3.39e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927   33 KIVDAVSEVHKEGMIYKYLNPKNIILDINGQLKLM----------ESTFMCRDINYNLRYMAPEQIGRIKKNVDFSTDHY 102
Cdd:cd05583   113 EIVLALDHLHQLGIIYRDIKLENILLDSEGHVVLTdfglskeflaEEEERAYSFCGTIEYMAPEVIRGGSGGHDKAVDWW 192
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 118443927  103 SLGVIFYRMLTGKLPIEVDDEiklsycNTNKKPVSPKKIKNTIPL------VISKIVMKLLEKDSEER 164
Cdd:cd05583   193 SLGVLTFELLTGASPFTVDGE------QNSQSEISRRILKSKPPFpktmsaEARDFIQKLLEKDPKKR 254
HisKA smart00388
His Kinase A (phosphoacceptor) domain; Dimerisation and phosphoacceptor domain of histidine ...
1406-1477 1.91e-11

His Kinase A (phosphoacceptor) domain; Dimerisation and phosphoacceptor domain of histidine kinases.


Pssm-ID: 214644  Cd Length: 66  Bit Score: 62.20  E-value: 1.91e-11
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 118443927   1406 MRTEFFANISHELRTPLNVIfsgyqMLNV-LLENEDLENKEKvdKYMGTVKQNCYRLVRLINNLIDITKIDSG 1477
Cdd:smart00388    1 AKREFLANLSHELRTPLTAI-----RGYLeLLLDTELSEEQR--EYLETILREAERLLRLINDLLDLSRIEAG 66
COG3899 COG3899
Predicted ATPase [General function prediction only]
208-1020 4.64e-104

Predicted ATPase [General function prediction only]


Pssm-ID: 226415 [Multi-domain]  Cd Length: 849  Bit Score: 354.01  E-value: 4.64e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927  208 IYGREKEIETIMDKYHKACRGTLQCVAISGDSGMGKTIIGSEISKRIVKEGGILLSSKCKKYNNNVPYYPLIECTRMLIN 287
Cdd:COG3899     2 LYGRETELAQLLAAFDRVSKGRGEVVLVAGESGIGKSALVNEVHKPITQQRGYFIKGKFDQFERNIPLSPLVQAFRDLMG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927  288 KILMEDEEKISYLKKEILKELGSNAQIITKFVPEAEFLIGKQPPLEERGFIESKSRFNMVIIRFTRIILNMKKPIAIFLE 367
Cdd:COG3899    82 QLLSESDTRILSWRARLLAALGENGQVIIDVIPELELIIGKRPPALELSPTAAQNRFNLAFLRFIQVFTAEEHPLVIVLE 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927  368 DIQWLDESSLYIIRKFLLNKENKY-----LFILTTLRTTDVENNKFlkeiveQDDVLNIKLESLNKYSIENLICDTLYCS 442
Cdd:COG3899   162 DLHWADSASLKLLQLLMDRIAIGAyrdneVLLLHPLRPTLGEILKS------ATNITTITLAPLSRADTNQLVAATLGCT 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927  443 KEEVKELVKFINIRTDGNPFFIKTSIESMYLNGVLKFDYTNNKWAWNMKLLKNMKIENSIFEIIIRKINQLSSDTKEILK 522
Cdd:COG3899   236 KLLPAPLLELIFEKTKGNPFFIEEFLKALYEEGLLVFNFDTGAWQCSIASLGILATTDAVVEFLAARLQKLPGTTREVLK 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927  523 LGSCIGQEFSLKCISEILNTSINVIFNNIIPAITEGVIILDEYATKNPKNKV---YRFAHSQIQMQIYDGISKEKKEKYH 599
Cdd:COG3899   316 AAACIGNRFDLDTLAALAEDSPALEAAALLDALQEGLILPLSETYRFGSNVDiatYKFLHDRVQQAAYNLIPESQRQYLH 395
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927  600 LSIGRYFYNEYSKNNLESKLFEVVNQLNKGRNLITNYDEIYKLIKLNLNIGLKEKEAGIHQLALGYFEVAYNLLEENSWE 679
Cdd:COG3899   396 LRIGQLLEQNIPEAGQEEEIFDIVNQLNAGVGLITLEEAVDELAELNLLAGRKAKLRSAYSAAISYLERGLSLLLADAWQ 475
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927  680 KDYDLTYAVNIELAECEFMNKNFEKAEELFKIILKNVKTPWETIKIYNMKVCIYTYFKQMDKAIETGINALKVLGIHISE 759
Cdd:COG3899   476 NQYLLALMLHRLAAENAYLRGQFELSESLIEVVLICAASNLDGAKVYELVIQAYTAQKQRLEAIALGQNALQLLGIAFPE 555
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927  760 KP--SFIKICCETLKFRLMKKSI---VNNNRYIIKENGIMEELKKLFFNMSFLAilyDKNLF--ILLVLKEMQINLYNTK 832
Cdd:COG3899   556 KPclAELNQAGEEINQLLGDRAIeelLNLPAMTDPDKLAALRILLNLILALFLT---APNLFplIILTIVTLSLKYGNSS 632
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927  833 SNNEIFTniNYEFLIMNLLKNYGKSYEMALNDLKKCYKKIDTIIYAKAYTVFANFMVLWSNDYNTTLDHLCKCYNICMDT 912
Cdd:COG3899   633 ESAAAYV--RYGDILNSFLGDFEKAYEFGKLALQLLEKFNAKELKSKWYLEAGVFILHWNDHLKETISLFKEGLVAGLEF 710
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927  913 GENSCAAFTLNNMITVFLMKGENLLEIKNKIKVYIDDIEKSNFDDIRDNLVLNRRIIDVLIADEENEVLSAKDYIIEREY 992
Cdd:COG3899   711 GDLEFASYLAAFYLAEAYKQGELLDDLRQENENYSEALAPFNQVISMVYSVLLIQLIFNLELKSEAEYELIEKILLESYI 790
                         810       820       830       840
                  ....*....|....*....|....*....|....*....|.
gi 118443927  993 LG-------------MYTYKIMLNYILGNYEDSIEIMKARE 1020
Cdd:COG3899   791 LPyllaaknlngigdLYLSKELLLYLFIDAEQAVKLAELAE 831
BaeS COG0642
Signal transduction histidine kinase [Signal transduction mechanisms]
1329-1639 7.70e-57

Signal transduction histidine kinase [Signal transduction mechanisms]


Pssm-ID: 223715 [Multi-domain]  Cd Length: 336  Bit Score: 202.68  E-value: 7.70e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927 1329 PIIAKEKIIGIIYLENRFSSGIFNEKRLSIVELIASQAAISIENAFMYEEINTLNKELKNTVDERTKLLNE-SIKYEEMR 1407
Cdd:COG0642    36 ELLLLLLLTLLAALLVALLLLLLLLRRLLRPLLLLADAANALAAGLTRLVLASLGSELASLAHALNELLERlERLLRRAK 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927 1408 TEFFANISHELRTPLNVIfsgyQMLNVLLENEDLENKEKvdkYMGTVKQNCYRLVRLINNLIDITKIDSGF-FKLNMINV 1486
Cdd:COG0642   116 REFLANISHELRTPLTAI----RGLLELLLEGLLDPQRE---LLEIIEEEAERLLRLVNDLLDLSRLEAGTkLKLLLELV 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927 1487 NIVNIVETITLSVAQYIESKGINLIFDtFIEEKTMACDVDKIERIILNLLSNAVKFTNkGGNIFVTMKEEDNNIVISVKD 1566
Cdd:COG0642   189 DLAELLEEVVRLLAPLAQEKGIELAVD-LPELPYVLGDPERLRQVLVNLLSNAIKYTP-GGEITISVRQDDEQVTISVED 266
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 118443927 1567 DGIGIPKEKQSIIFDRFIQVDKSlsrnREGSGIGLALVKSIVELHDGNITLKSKLGRGSEFIIKLPCKVLEKQ 1639
Cdd:COG0642   267 TGPGIPEEELERIFEPFFRTDKS----RSGTGLGLAIVKRIVELHGGTISVESEPGKGTTFTIRLPLAPAAAD 335
phoR_proteo TIGR02966
phosphate regulon sensor kinase PhoR; Members of this protein family are the regulatory ...
1404-1627 5.98e-47

phosphate regulon sensor kinase PhoR; Members of this protein family are the regulatory histidine kinase PhoR associated with the phosphate ABC transporter in most Proteobacteria. Related proteins from Gram-positive organisms are not included in this model. The phoR gene usually is adjacent to the response regulator phoB gene (TIGR02154) [Signal transduction, Two-component systems].


Pssm-ID: 234074 [Multi-domain]  Cd Length: 333  Bit Score: 173.55  E-value: 5.98e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927  1404 EEMRTEFFANISHELRTPLNVIfSGYqmLNVLLENEDLENKEKvDKYMGTVKQNCYRLVRLINNLIDITKIDSGFFKLNM 1483
Cdd:TIGR02966  111 EQMRRDFVANVSHELRTPLTVL-RGY--LETLADGPDEDPEEW-NRALEIMLEQSQRMQSLVEDLLTLSRLESAASPLED 186
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927  1484 INVNIVNIVETITLSVAQYIESKGINLIFDTfieekTMACDV----DKIERIILNLLSNAVKFTNKGGNIFVTMKEEDNN 1559
Cdd:TIGR02966  187 EPVDMPALLDHLRDEAEALSQGKNHQITFEI-----DGGVDVlgdeDELRSAFSNLVSNAIKYTPEGGTITVRWRRDGGG 261
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 118443927  1560 IVISVKDDGIGIPKEKQSIIFDRFIQVDKSLSRNREGSGIGLALVKSIVELHDGNITLKSKLGRGSEF 1627
Cdd:TIGR02966  262 AEFSVTDTGIGIAPEHLPRLTERFYRVDKSRSRDTGGTGLGLAIVKHVLSRHHARLEIESELGKGSTF 329
PRK15347 PRK15347
two component system sensor kinase SsrA; Provisional
1379-1632 1.44e-38

two component system sensor kinase SsrA; Provisional


Pssm-ID: 237951 [Multi-domain]  Cd Length: 921  Bit Score: 155.96  E-value: 1.44e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927 1379 INTLNK---ELKNTVDERTKLLNESIKYEEM----RTEFFANISHELRTPLNVIFSGYQmlnvLLENEDLENKEKvdKYM 1451
Cdd:PRK15347  363 LDTLNEqydTLENKVAERTQALAEAKQRAEQankrKSEHLTTISHEIRTPLNGVLGALE----LLQNTPLTAEQM--DLA 436
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927 1452 GTVKQNCYRLVRLINNLIDITKIDSGFFKLNMINVNIVNIVETITLSVAQYIESKGINLifDTFIEEK---TMACDVDKI 1528
Cdd:PRK15347  437 DTARQCTLSLLAIINNLLDFSRIESGQMTLSLEETALLPLLDQAMLTIQGPAQSKSLTL--RTFVGAHvplYLHLDSLRL 514
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927 1529 ERIILNLLSNAVKFTNKGGnIFVTMKEEDNNIVISVKDDGIGIPKEKQSIIFDRFIQVDKslsrNREGSGIGLALVKSIV 1608
Cdd:PRK15347  515 RQILVNLLGNAVKFTETGG-IRLRVKRHEQQLCFTVEDTGCGIDIQQQQQIFTPFYQADT----HSQGTGLGLTIASSLA 589
                         250       260
                  ....*....|....*....|....
gi 118443927 1609 ELHDGNITLKSKLGRGSEFIIKLP 1632
Cdd:PRK15347  590 KMMGGELTLFSTPGVGSCFSLVLP 613
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
1-165 6.23e-16

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 79.11  E-value: 6.23e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927      1 MEYYKKkGEviLEEFICNKKDMSIKEFLKNALKIVDAVSEVHKEGMIYKYLNPKNIILDINGQLKLMEstF-MCRDINYN 79
Cdd:smart00220   76 MEYCEG-GD--LFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLAD--FgLARQLDPG 150
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927     80 LR---------YMAPEQIGRikKNVDFSTDHYSLGVIFYRMLTGKLPIEVDDEIKLSYCNTNKKPVSPKKIKNTIPLVIS 150
Cdd:smart00220  151 EKlttfvgtpeYMAPEVLLG--KGYGKAVDIWSLGVILYELLTGKPPFPGDDQLLELFKKIGKPKPPFPPPEWDISPEAK 228
                           170
                    ....*....|....*
gi 118443927    151 KIVMKLLEKDSEERY 165
Cdd:smart00220  229 DLIRKLLVKDPEKRL 243
SPS1 COG0515
Serine/threonine protein kinase [General function prediction only / Signal transduction ...
1-219 8.24e-15

Serine/threonine protein kinase [General function prediction only / Signal transduction mechanisms / Transcription / DNA replication, recombination, and repair]


Pssm-ID: 223589 [Multi-domain]  Cd Length: 384  Bit Score: 77.09  E-value: 8.24e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927    1 MEYYKKKGEVILEEFICNKKDMSIKEFLKNALKIVDAVSEVHKEGMIYKYLNPKNIILDING-QLKL------------- 66
Cdd:COG0515    77 MEYVDGGSLEDLLKKIGRKGPLSESEALFILAQILSALEYLHSKGIIHRDIKPENILLDRDGrVVKLidfglakllpdpg 156
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927   67 --MESTFMCRDINYNLRYMAPEQI-GRIKKNVDFSTDHYSLGVIFYRMLTGKLPIEVDD---------EIKLSYCNTNKK 134
Cdd:COG0515   157 stSSIPALPSTSVGTPGYMAPEVLlGLSLAYASSSSDIWSLGITLYELLTGLPPFEGEKnssatsqtlKIILELPTPSLA 236
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927  135 PVSPKKIKNTIPLVISKIVMKLLEKDSEERYKSIYGIKVDLNKCYKSLIFSGEVYNFPLGERDVSDKLKFTNKIYGREKE 214
Cdd:COG0515   237 SPLSPSNPELISKAASDLLKKLLAKDPKNRLSSSSDLSHDLLAHLKLKESDLSDLLKPDDSAPLRLSLPPSLEALISSLN 316

                  ....*
gi 118443927  215 IETIM 219
Cdd:COG0515   317 SLAIS 321
pknD PRK13184
serine/threonine-protein kinase; Reviewed
23-175 3.19e-14

serine/threonine-protein kinase; Reviewed


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 76.73  E-value: 3.19e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927   23 SIKEFLKNALKIVDAVSEVHKEGMIYKYLNPKNIILDINGQL----------KLMESTFMCrDINYNLR----------- 81
Cdd:PRK13184  111 SVGAFLSIFHKICATIEYVHSKGVLHRDLKPDNILLGLFGEVvildwgaaifKKLEEEDLL-DIDVDERnicyssmtipg 189
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927   82 -------YMAPEqigRIKKN-VDFSTDHYSLGVIFYRMLTGKLPIEVDDEIKLSYCNTNKKP--VSPKKiknTIPLVISK 151
Cdd:PRK13184  190 kivgtpdYMAPE---RLLGVpASESTDIYALGVILYQMLTLSFPYRRKKGRKISYRDVILSPieVAPYR---EIPPFLSQ 263
                         170       180
                  ....*....|....*....|....
gi 118443927  152 IVMKLLEKDSEERYKSIYGIKVDL 175
Cdd:PRK13184  264 IAMKALAVDPAERYSSVQELKQDL 287
Pkinase pfam00069
Protein kinase domain;
1-165 4.30e-12

Protein kinase domain;


Pssm-ID: 249558 [Multi-domain]  Cd Length: 260  Bit Score: 66.89  E-value: 4.30e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927     1 MEYYKKkGEviLEEFICNKKDMSIKEFLKNALKIVDAVSEVHKEGMIYKYLNPKNIILDINGQLKL----MESTFMCRDI 76
Cdd:pfam00069   77 MEYCEG-GD--LFDYLSRGGPLSEDEAKKIALQILRGLEYLHSNGIIHRDLKPENILLDENGVVKIadfgLAKKLTKSSS 153
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927    77 NYN-----LRYMAPEQIgRIKKNVDFSTDHYSLGVIFYRMLTGKLP---IEVDDEIKLSYCNTNKKPVSPKKIKNTIPLV 148
Cdd:pfam00069  154 SLTtfvgtPEYMAPEVL-LGGNGYGPKVDVWSLGVILYELLTGKPPfsgESILDQLQLIRRILGPPLEFDEPKSDSGSEE 232
                          170
                   ....*....|....*..
gi 118443927   149 ISKIVMKLLEKDSEERY 165
Cdd:pfam00069  233 AKDLIKKCLNKDPSKRP 249
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
33-117 2.34e-06

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 50.20  E-value: 2.34e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927   33 KIVDAVSEVHKEGMIYKYLNPKNIILDINGQLKLMESTFMCR--DINYNL----RYMAPEQIGriKKNVDFSTDHYSLGV 106
Cdd:PTZ00263  126 ELVLAFEYLHSKDIIYRDLKPENLLLDNKGHVKVTDFGFAKKvpDRTFTLcgtpEYLAPEVIQ--SKGHGKAVDWWTMGV 203
                          90
                  ....*....|.
gi 118443927  107 IFYRMLTGKLP 117
Cdd:PTZ00263  204 LLYEFIAGYPP 214
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
29-132 6.42e-04

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 43.30  E-value: 6.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927   29 KNALKIVDAVSEVH---KEGMIYKYLNPKNIILDINGQ--LKLMESTFMCRDINYNLR--YMAPEQigRIKKNVDFSTDH 101
Cdd:PLN00113  784 KIAIGIAKALRFLHcrcSPAVVVGNLSPEKIIIDGKDEphLRLSLPGLLCTDTKCFISsaYVAPET--RETKDITEKSDI 861
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 118443927  102 YSLGVIFYRMLTGKLPIEVDDEIKLS------YCNTN 132
Cdd:PLN00113  862 YGFGLILIELLTGKSPADAEFGVHGSivewarYCYSD 898
 
Name Accession Description Interval E-value
HATPase_c cd00075
Histidine kinase-like ATPases; This family includes several ATP-binding proteins for example: ...
1528-1631 1.31e-31

Histidine kinase-like ATPases; This family includes several ATP-binding proteins for example: histidine kinase, DNA gyrase B, topoisomerases, heat shock protein HSP90, phytochrome-like ATPases and DNA mismatch repair proteins


Pssm-ID: 238030  Cd Length: 103  Bit Score: 121.60  E-value: 1.31e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927 1528 IERIILNLLSNAVKFTNK-GGNIFVTMKEEDNNIVISVKDDGIGIPKEKQSIIFDRFiqVDKSLSRNREGSGIGLALVKS 1606
Cdd:cd00075     1 LQQVLLNLLSNAIKHTPEgGGRITISVERDGDHLEIRVEDNGPGIPEEDLERIFERF--SDGSRSRKGGGTGLGLSIVKK 78
                          90       100
                  ....*....|....*....|....*
gi 118443927 1607 IVELHDGNITLKSKLGRGSEFIIKL 1631
Cdd:cd00075    79 LVELHGGRIEVESEPGGGTTFTITL 103
HisKA cd00082
Histidine Kinase A (dimerization/phosphoacceptor) domain; Histidine Kinase A dimers are formed ...
1404-1473 8.78e-13

Histidine Kinase A (dimerization/phosphoacceptor) domain; Histidine Kinase A dimers are formed through parallel association of 2 domains creating 4-helix bundles; usually these domains contain a conserved His residue and are activated via trans-autophosphorylation by the catalytic domain of the histidine kinase. They subsequently transfer the phosphoryl group to the Asp acceptor residue of a response regulator protein. Two-component signalling systems, consisting of a histidine protein kinase that senses a signal input and a response regulator that mediates the output, are ancient and evolutionarily conserved signaling mechanisms in prokaryotes and eukaryotes.


Pssm-ID: 119399  Cd Length: 65  Bit Score: 66.08  E-value: 8.78e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927 1404 EEMRTEFFANISHELRTPLNVIfsgyQMLNVLLENEDLENkEKVDKYMGTVKQNCYRLVRLINNLIDITK 1473
Cdd:cd00082     1 LQAKGEFLANVSHELRTPLTAI----RGALELLEEELLDD-EEQREYLERIREEAERLLRLINDLLDLSR 65
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
1524-1632 9.20e-38

Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.


Pssm-ID: 214643  Cd Length: 111  Bit Score: 139.71  E-value: 9.20e-38
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927   1524 DVDKIERIILNLLSNAVKFTNKGGNIFVTMKEEDNNIVISVKDDGIGIPKEKQSIIFDRFIQVDKSlSRNREGSGIGLAL 1603
Cdd:smart00387    2 DPDRLRQVLSNLLDNAIKYTPEGGRITVTLERDGDHVEITVEDNGPGIPPEDLEKIFEPFFRTDKR-SRKIGGTGLGLSI 80
                            90       100
                    ....*....|....*....|....*....
gi 118443927   1604 VKSIVELHDGNITLKSKLGRGSEFIIKLP 1632
Cdd:smart00387   81 VKKLVELHGGEISVESEPGGGTTFTITLP 109
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
1524-1632 7.34e-35

Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the structurally related ATPase domains of histidine kinase, DNA gyrase B and HSP90.


Pssm-ID: 251347  Cd Length: 111  Bit Score: 131.29  E-value: 7.34e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927  1524 DVDKIERIILNLLSNAVKFTNKGGNIFVTMKEEDNNIVISVKDDGIGIPKEKQSIIFDRFIQVDKSlSRNREGSGIGLAL 1603
Cdd:pfam02518    2 DEDRLRQVLSNLLDNAIKHAPAGGEIEVTLERDGGRLRITVEDNGIGIPPEDLPKIFEPFFRTDGS-RSKVGGTGLGLSI 80
                           90       100
                   ....*....|....*....|....*....
gi 118443927  1604 VKSIVELHDGNITLKSKLGRGSEFIIKLP 1632
Cdd:pfam02518   81 VRKLVELHGGTITVESEPGGGTTFTLTLP 109
AAA_16 pfam13191
AAA ATPase domain; This family of domains contain a P-loop motif that is characteristic of the ...
207-395 6.10e-21

AAA ATPase domain; This family of domains contain a P-loop motif that is characteristic of the AAA superfamily.


Pssm-ID: 257559  Cd Length: 156  Bit Score: 92.53  E-value: 6.10e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927   207 KIYGREKEIETIMDKYHKACRGTLQCVAISGDSGMGKTIIGSEISKRIVKEGGILLSSKCkkynNNVPYYPLIectrmli 286
Cdd:pfam13191    1 RLVGREEELERLLDALERVRSGRPGLVLLTGPSGVGKTSLLRELLERLARKGGGVLSGKC----DELPYAALR------- 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927   287 nkilmedeekisylkkEILKELGSnaQIITKFVPEAEFLigkqPPLEERGFIESKSRFNMVIIRFTRIILNMKKPIAIFL 366
Cdd:pfam13191   70 ----------------QLLRELLR--QLLDELLPELELL----PPVPGLPPDDLRNRLEDLLRRLLRRLAARERPLVLVL 127
                          170       180
                   ....*....|....*....|....*....
gi 118443927   367 EDIQWLDESSLYIIRKFLLNKENKYLFIL 395
Cdd:pfam13191  128 DDLQWADEASLALLLALARLLERLPLLLV 156
FhlA COG2203
FOG: GAF domain [Signal transduction mechanisms]
1220-1378 1.01e-13

FOG: GAF domain [Signal transduction mechanisms]


Pssm-ID: 225113  Cd Length: 175  Bit Score: 71.16  E-value: 1.01e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927 1220 QSISGEIVLENLLKELMINLIASVEAERGCLI-LNKNNKLFIEAEGEVDdiCSVMENPI-ALEEYTKISKLLVNYVVRTK 1297
Cdd:COG2203    11 AKIAQDLDLEEILQAALELLAELLGADRGLIYlLDEDGLLDGALVAEAA--EAGLEQLIdELFGLVILPACLIGIALREG 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927 1298 KSILLDDGKcEDIVFDDKYIVD--NKVKSILCTPIIAKEKIIGIIYLENRFSSGIFNEKRLSIVELIASQAAISIENAFM 1375
Cdd:COG2203    89 RPVVVEDIL-QDPRFRDNPLVLlePPIRSYLGVPLIAQGELLGLLCVHDSEPRRQWSEEELELLEELAEQVAIAIERARL 167

                  ...
gi 118443927 1376 YEE 1378
Cdd:COG2203   168 YEE 170
HisKA pfam00512
His Kinase A (phospho-acceptor) domain; Dimerization and phospho-acceptor domain of histidine ...
1406-1477 1.08e-12

His Kinase A (phospho-acceptor) domain; Dimerization and phospho-acceptor domain of histidine kinases.


Pssm-ID: 249920  Cd Length: 66  Bit Score: 65.66  E-value: 1.08e-12
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 118443927  1406 MRTEFFANISHELRTPLNVIfsgyqMLNV-LLENEDLENKEKvdKYMGTVKQNCYRLVRLINNLIDITKIDSG 1477
Cdd:pfam00512    1 AKSEFLANLSHELRTPLTAI-----RGYLeLLLDTELSEEQR--EYLETILRSAERLLRLINDLLDLSRIEAG 66
GAF_2 pfam13185
GAF domain;
1228-1371 2.43e-12

GAF domain;


Pssm-ID: 257553  Cd Length: 150  Bit Score: 66.85  E-value: 2.43e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927  1228 LENLLKELMINLIASVEAERGCL-ILNKNNKLFIEAEGEVDDICSVMENPIALEEYTKISKLLVNY---VVRTKKSILLD 1303
Cdd:pfam13185    4 LEELLEAILEALLELTGSEAGFIgLLDEDGTLLLLAASGGTEELLRELAALSGELGGPPAAGAVGLgegALRTGKPVIIN 83
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 118443927  1304 DGKCEDIVFDDKYIVDNKVKSILCTPIIAKEKIIGIIYLENRfSSGIFNEKRLSIVELIASQAAISIE 1371
Cdd:pfam13185   84 DVASDPSGAGGLPAGHEGLRSFLSVPLISGGRVIGVLALGSK-EPGAFDEEDLELLELLAEQIAIAIE 150
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
1228-1380 3.16e-12

Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these domains in PDE6B result in autosomal recessive inheritance of retinitis pigmentosa.


Pssm-ID: 214500  Cd Length: 149  Bit Score: 66.25  E-value: 3.16e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927   1228 LENLLKELMINLIASVEAERGCLILNKNNKLFIEAEGEVDDICsvmenPIALEEYTKISKLLVNYVVRTKKSILLDDGKC 1307
Cdd:smart00065    2 LEELLQTILEELRQLLGADRVLIYLVDENDRGELVLVAADGLT-----LPTLGIRFPLDEGLAGRVAETGRPLNIPDVEA 76
                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 118443927   1308 EDIVFDDKYIVDNKVKSILCTPIIAKEKIIGIIYLENRFSSGIFNEKRLSIVELIASQAAISIENAFMYEEIN 1380
Cdd:smart00065   77 DPLFAEDLLGRYQGVRSFLAVPLVADGELVGVLALHNKKSPRPFTEEDEELLQALANQLAIALANAQLYEELR 149
STKc_MSK_N cd05583
N-terminal catalytic domain of the Protein Serine/Threonine Kinase, Mitogen and ...
33-164 3.39e-12

N-terminal catalytic domain of the Protein Serine/Threonine Kinase, Mitogen and stress-activated kinase; Serine/Threonine Kinases (STKs), Mitogen and stress-activated kinase (MSK) subfamily, N-terminal catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The MSK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. 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, 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.


Pssm-ID: 173674 [Multi-domain]  Cd Length: 288  Bit Score: 67.51  E-value: 3.39e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927   33 KIVDAVSEVHKEGMIYKYLNPKNIILDINGQLKLM----------ESTFMCRDINYNLRYMAPEQIGRIKKNVDFSTDHY 102
Cdd:cd05583   113 EIVLALDHLHQLGIIYRDIKLENILLDSEGHVVLTdfglskeflaEEEERAYSFCGTIEYMAPEVIRGGSGGHDKAVDWW 192
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 118443927  103 SLGVIFYRMLTGKLPIEVDDEiklsycNTNKKPVSPKKIKNTIPL------VISKIVMKLLEKDSEER 164
Cdd:cd05583   193 SLGVLTFELLTGASPFTVDGE------QNSQSEISRRILKSKPPFpktmsaEARDFIQKLLEKDPKKR 254
STKc_AGC cd05123
Catalytic domain of AGC family Protein Serine/Threonine Kinases; Serine/Threonine Kinases ...
34-164 9.70e-12

Catalytic domain of AGC family Protein Serine/Threonine Kinases; Serine/Threonine Kinases (STKs), AGC (Protein Kinases A, G and C) family, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The AGC 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 (PI3K). 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. AGC kinases regulate many cellular processes including division, growth, survival, metabolism, motility, and differentiation. Many are implicated in the development of various human diseases.


Pssm-ID: 173660 [Multi-domain]  Cd Length: 250  Bit Score: 65.62  E-value: 9.70e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927   34 IVDAVSEVHKEGMIYKYLNPKNIILDINGQLKL---------MESTFMCRDINYNLRYMAPE--QIGRIKKNVDFstdhY 102
Cdd:cd05123   102 IVLALEYLHSLGIIYRDLKPENILLDADGHIKLtdfglakelSSEGSRTNTFCGTPEYLAPEvlLGKGYGKAVDW----W 177
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 118443927  103 SLGVIFYRMLTGKLPIEVDDEIKLSYCNTNKKPVSPKKIKNTIPLVISkivmKLLEKDSEER 164
Cdd:cd05123   178 SLGVLLYEMLTGKPPFYAEDRKEIYEKILKDPLRFPEFLSPEARDLIS----GLLQKDPTKR 235
STKc_nPKC_theta_delta cd05592
Catalytic domain of the Protein Serine/Threonine Kinases, Novel Protein Kinase C theta and ...
31-164 1.47e-11

Catalytic domain of the Protein Serine/Threonine Kinases, Novel Protein Kinase C theta and delta; Serine/Threonine Kinases (STKs), Novel Protein Kinase C (nPKC), theta and delta-like isoforms, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The nPKC subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. 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. 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.


Pssm-ID: 173683 [Multi-domain]  Cd Length: 316  Bit Score: 66.36  E-value: 1.47e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927   31 ALKIVDAVSEVHKEGMIYKYLNPKNIILDINGQLKL----MESTFMCRDINYNL-----RYMAPEQIGRIKKNvdFSTDH 101
Cdd:cd05592   102 AAEIICGLQFLHKKGIIYRDLKLDNVLLDKDGHIKIadfgMCKENMNGEGKASTfcgtpDYIAPEILKGQKYN--ESVDW 179
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 118443927  102 YSLGVIFYRMLTGKLPIEVDDEIKLSYCNTNKKPVSPKkiknTIPLVISKIVMKLLEKDSEER 164
Cdd:cd05592   180 WSFGVLLYEMLIGQSPFHGEDEDELFDSILNDRPHFPR----WISKEAKDCLSKLFERDPTKR 238
HisKA smart00388
His Kinase A (phosphoacceptor) domain; Dimerisation and phosphoacceptor domain of histidine ...
1406-1477 1.91e-11

His Kinase A (phosphoacceptor) domain; Dimerisation and phosphoacceptor domain of histidine kinases.


Pssm-ID: 214644  Cd Length: 66  Bit Score: 62.20  E-value: 1.91e-11
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 118443927   1406 MRTEFFANISHELRTPLNVIfsgyqMLNV-LLENEDLENKEKvdKYMGTVKQNCYRLVRLINNLIDITKIDSG 1477
Cdd:smart00388    1 AKREFLANLSHELRTPLTAI-----RGYLeLLLDTELSEEQR--EYLETILREAERLLRLINDLLDLSRIEAG 66
STKc_cGK_PKG cd05572
Catalytic domain of the Protein Serine/Threonine Kinase, cGMP-dependent protein kinase; Serine ...
34-164 2.28e-11

Catalytic domain of the Protein Serine/Threonine Kinase, cGMP-dependent protein kinase; Serine/Threonine Kinases (STKs), cGMP-dependent protein kinase (cGK or PKG) subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The cGK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. 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.


Pssm-ID: 173663 [Multi-domain]  Cd Length: 262  Bit Score: 64.95  E-value: 2.28e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927   34 IVDAVSEVHKEGMIYKYLNPKNIILDINGQLKLMESTFM----CRDINYNL----RYMAPEQIgrIKKNVDFSTDHYSLG 105
Cdd:cd05572   102 VVLAFEYLHNRGIIYRDLKPENLLLDSNGYVKLVDFGFAkklkSGQKTWTFcgtpEYVAPEII--LNKGYDFSVDYWSLG 179
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 118443927  106 VIFYRMLTGKLPIEVDDEIKLSYCNTNKKPVSPKKIKNTIPLVISKIVMKLLEKDSEER 164
Cdd:cd05572   180 ILLYELLTGRPPFGEDDEDPMEIYNDILKGNGKLEFPNYIDKAAKDLIKQLLRRNPEER 238
PKc cd00180
Catalytic domain of Protein Kinases; Protein Kinases (PKs), catalytic (c) domain. PKs catalyze ...
1-111 4.85e-11

Catalytic domain of Protein Kinases; Protein Kinases (PKs), catalytic (c) domain. PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. 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. PKs make up a large family of serine/threonine kinases, protein tyrosine kinases (PTKs), and dual-specificity PKs that phosphorylate both serine/threonine and tyrosine residues of target proteins. Majority of protein phosphorylation, about 95%, 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 550 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.


Pssm-ID: 173623 [Multi-domain]  Cd Length: 215  Bit Score: 63.02  E-value: 4.85e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927    1 MEYYKKKGeviLEEFIC-NKKDMSIKEFLKNALKIVDAVSEVHKEGMIYKYLNPKNIILD-INGQLKLM---------ES 69
Cdd:cd00180    70 MEYCEGGS---LKDLLKeNEGKLSEDEILRILLQILEGLEYLHSNGIIHRDLKPENILLDsDNGKVKLAdfglsklltSD 146
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 118443927   70 TFMCRDINYNLRYMAPEQIgRIKKNVDFSTDHYSLGVIFYRM 111
Cdd:cd00180   147 KSLLKTIVGTPAYMAPEVL-LGKGYYSEKSDIWSLGVILYEL 187
STKc_MSK1_N cd05613
N-terminal catalytic domain of the Protein Serine/Threonine Kinase, Mitogen and ...
33-164 8.93e-11

N-terminal catalytic domain of the Protein Serine/Threonine Kinase, Mitogen and stress-activated kinase 1; Serine/Threonine Kinases (STKs), Mitogen and stress-activated kinase (MSK) subfamily, MSK1, N-terminal catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The MSK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. 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. MSK1 plays a role in the regulation of translational control and transcriptional activation. It phosphorylates the transcription factors, CREB and NFkappaB. It also phosphorylates the nucleosomal proteins H3 and HMG-14. Increased phosphorylation of MEK1 is associated with the development of cerebral ischemic/hypoxic preconditioning.


Pssm-ID: 173704 [Multi-domain]  Cd Length: 290  Bit Score: 63.48  E-value: 8.93e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927   33 KIVDAVSEVHKEGMIYKYLNPKNIILDINGQLKLME----------STFMCRDINYNLRYMAPEQIGRIKKNVDFSTDHY 102
Cdd:cd05613   113 EIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDfglskefhedEVERAYSFCGTIEYMAPDIVRGGDGGHDKAVDWW 192
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 118443927  103 SLGVIFYRMLTGKLPIEVDDE----IKLSYCNTNKKPVSPKKIKntiPLViSKIVMKLLEKDSEER 164
Cdd:cd05613   193 SMGVLMYELLTGASPFTVDGEknsqAEISRRILKSEPPYPQEMS---ALA-KDIIQRLLMKDPKKR 254
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine kinase-like proteins; Serine ...
34-172 1.13e-10

Catalytic domain of Microtubule-associated serine/threonine kinase-like proteins; Serine/Threonine Kinases (STKs), Microtubule-associated serine/threonine (MAST) kinase subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The MAST kinase subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. The MAST kinase subfamily includes MAST kinases, MAST-like (MASTL) kinases, 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 also contains an insert relative to MAST kinases like MASTL. 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. The fungal proteins Rim15 and cek1 are involved in the regulation of meiosis and mitosis, respectively.


Pssm-ID: 173670 [Multi-domain]  Cd Length: 265  Bit Score: 62.65  E-value: 1.13e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927   34 IVDAVSEVHKEGMIYKYLNPKNIILDINGQLKLM-----------ESTFMCRDINYNLR------YMAPEQIgrIKKNVD 96
Cdd:cd05579   102 IVLALEYLHSNGIIHRDLKPDNILIDSNGHLKLTdfglskvglvrRQINLNDDEKEDKRivgtpdYIAPEVI--LGQGHS 179
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 118443927   97 FSTDHYSLGVIFYRMLTGKLPIEVDDEIKLsYCNTNKKPVSPKKIKNTIPLVISkIVMKLLEKDSEER--YKSIYGIK 172
Cdd:cd05579   180 KTVDWWSLGCILYEFLVGIPPFHGETPEEI-FQNILNGKIEWPEDVEVSDEAID-LISKLLVPDPEKRlgAKSIEEIK 255
STKc_RSK_N cd05582
N-terminal catalytic domain of the Protein Serine/Threonine Kinase, 90 kDa ribosomal protein ...
37-122 1.38e-10

N-terminal catalytic domain of the Protein Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; Serine/Threonine Kinases (STKs), 90 kDa ribosomal protein S6 kinase (RSK) subfamily, N-terminal catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The RSK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. 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.


Pssm-ID: 173673 [Multi-domain]  Cd Length: 318  Bit Score: 63.28  E-value: 1.38e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927   37 AVSEVHKEGMIYKYLNPKNIILDINGQLKLMESTFMCRDINYN---------LRYMAPEQIGRikKNVDFSTDHYSLGVI 107
Cdd:cd05582   110 ALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKESIDHEkkaysfcgtVEYMAPEVVNR--RGHTQSADWWSFGVL 187
                          90
                  ....*....|....*
gi 118443927  108 FYRMLTGKLPIEVDD 122
Cdd:cd05582   188 MFEMLTGSLPFQGKD 202
STKc_p70S6K cd05584
Catalytic domain of the Protein Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; ...
33-164 2.18e-10

Catalytic domain of the Protein Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; Serine/Threonine Kinases (STKs), 70 kDa ribosomal protein S6 kinase (p70S6K) subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. 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. 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).


Pssm-ID: 173675 [Multi-domain]  Cd Length: 323  Bit Score: 62.89  E-value: 2.18e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927   33 KIVDAVSEVHKEGMIYKYLNPKNIILDINGQLKL--------------MESTFmCRDInynlRYMAPEQIGRIKKNVDfs 98
Cdd:cd05584   108 EISLALEHLHQQGIIYRDLKPENILLDAQGHVKLtdfglckesihegtVTHTF-CGTI----EYMAPEILMRSGHGKA-- 180
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 118443927   99 TDHYSLGVIFYRMLTGKLPievddeiklsYCNTNKKPVSPK--KIKNTIPLVISK----IVMKLLEKDSEER 164
Cdd:cd05584   181 VDWWSLGALMYDMLTGAPP----------FTAENRKKTIDKilKGKLNLPPYLTPeardLLKKLLKRNPSSR 242
STKc_Yank1 cd05578
Catalytic domain of the Protein Serine/Threonine Kinase, Yank1; Serine/Threonine Kinases (STKs) ...
34-164 5.31e-10

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


Pssm-ID: 173669 [Multi-domain]  Cd Length: 258  Bit Score: 60.41  E-value: 5.31e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927   34 IVDAVSEVHKEGMIYKYLNPKNIILDINGQLKLME---STFMCRDINYNLR-----YMAPEQIgrIKKNVDFSTDHYSLG 105
Cdd:cd05578   109 IVLALEYLHSKGIIHRDIKPDNILLDEQGHVHITDfniATKVTPDTLTTSTsgtpgYMAPEVL--CRQGYSVAVDWWSLG 186
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 118443927  106 VIFYRMLTGKLPIEVDDEiKLSYCNTNKKPVSPKKIKNTIPLVISKIVMKLLEKDSEER 164
Cdd:cd05578   187 VTAYECLRGKRPYRGHSR-TIRDQIRAKQETADVLYPATWSTEAIDAINKLLERDPQKR 244
STKc_nPKC_theta cd05619
Catalytic domain of the Protein Serine/Threonine Kinase, Novel Protein Kinase C theta; Serine ...
1-177 9.97e-10

Catalytic domain of the Protein Serine/Threonine Kinase, Novel Protein Kinase C theta; Serine/Threonine Kinases (STKs), Novel Protein Kinase C (nPKC), theta isoform, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The nPKC subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. 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. 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.


Pssm-ID: 173709 [Multi-domain]  Cd Length: 316  Bit Score: 60.75  E-value: 9.97e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927    1 MEYYKKkGEVILEEFICNKKDMSIKEFLknALKIVDAVSEVHKEGMIYKYLNPKNIILDINGQLKLMESTfMCR-----D 75
Cdd:cd05619    75 MEYLNG-GDLMFHIQSCHKFDLPRATFY--AAEIICGLQFLHSKGIVYRDLKLDNILLDTDGHIKIADFG-MCKenmlgD 150
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927   76 INYNL-----RYMAPEQIgrIKKNVDFSTDHYSLGVIFYRMLTGKLPIEVDDEIKLSYCNTNKKPVSPKKIKNTiplvIS 150
Cdd:cd05619   151 AKTCTfcgtpDYIAPEIL--LGQKYNTSVDWWSFGVLLYEMLIGQSPFHGHDEEELFQSIRMDNPCYPRWLTRE----AK 224
                         170       180
                  ....*....|....*....|....*..
gi 118443927  151 KIVMKLLEKDSEERyksiYGIKVDLNK 177
Cdd:cd05619   225 DILVKLFVREPERR----LGVKGDIRQ 247
STKc_PKC cd05570
Catalytic domain of the Protein Serine/Threonine Kinase, Protein Kinase C; Serine/Threonine ...
31-164 1.12e-09

Catalytic domain of the Protein Serine/Threonine Kinase, Protein Kinase C; Serine/Threonine Kinases (STKs), Protein Kinase C (PKC) subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PKC subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. 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.


Pssm-ID: 173661 [Multi-domain]  Cd Length: 318  Bit Score: 60.47  E-value: 1.12e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927   31 ALKIVDAVSEVHKEGMIYKYLNPKNIILDINGQLKLMEstF-MCRD-INYNLR---------YMAPEQIGRIKknVDFST 99
Cdd:cd05570   102 AAEIVLGLQFLHERGIIYRDLKLDNVLLDSEGHIKIAD--FgMCKEgILGGVTtstfcgtpdYIAPEILSYQP--YGPAV 177
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 118443927  100 DHYSLGVIFYRMLTGKLPIEVDDEIKLSYCNTNKKPVSPKKIKNTiplvISKIVMKLLEKDSEER 164
Cdd:cd05570   178 DWWALGVLLYEMLAGQSPFEGDDEDELFQSILEDEVRYPRWLSKE----AKSILKSFLTKNPEKR 238
STKc_Nek cd08215
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A-related ...
1-164 1.50e-09

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A-related kinase; Serine/Threonine Kinases (STKs), Never In Mitosis gene A (NIMA)-related kinase (Nek) family, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Nek 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. 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.


Pssm-ID: 173755 [Multi-domain]  Cd Length: 258  Bit Score: 59.05  E-value: 1.50e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927    1 MEY------------YKKKGEVILEEFIcnkkdmsikefLKNALKIVDAVSEVHKEGMIYKYLNPKNIILDINGQLKL-- 66
Cdd:cd08215    78 MEYadggdlsqkikkQKKEGKPFPEEQI-----------LDWFVQLCLALKYLHSRKILHRDIKPQNIFLTSNGLVKLgd 146
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927   67 -------MESTFMCRDINYNLRYMAPEQIGRikKNVDFSTDHYSLGVIFYRMLTGKLPIEVDDEIKLSYcNTNKKPVSPk 139
Cdd:cd08215   147 fgiskvlSSTVDLAKTVVGTPYYLSPELCQN--KPYNYKSDIWSLGCVLYELCTLKHPFEGENLLELAL-KILKGQYPP- 222
                         170       180
                  ....*....|....*....|....*
gi 118443927  140 kIKNTIPLVISKIVMKLLEKDSEER 164
Cdd:cd08215   223 -IPSQYSSELRNLVSSLLQKDPEER 246
STKc_PDK1 cd05581
Catalytic domain of the Protein Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; ...
4-164 8.50e-09

Catalytic domain of the Protein Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; Serine/Threonine Kinases (STKs), Phosphoinositide-dependent kinase 1 (PDK1) subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PDK1 subfamily is part of a 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). 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. PDK1 is essential for normal embryo development and is important in regulating cell volume.


Pssm-ID: 173672 [Multi-domain]  Cd Length: 280  Bit Score: 57.20  E-value: 8.50e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927    4 YKKKGEviLEEFICNKKDMSIKEFLKNALKIVDAVSEVHKEGMIYKYLNPKNIILDINGQLKL----------------- 66
Cdd:cd05581    83 YAPNGE--LLQYIRKYGSLDEKCTRFYAAEILLALEYLHSKGIIHRDLKPENILLDKDMHIKItdfgtakvldpnsspes 160
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927   67 --MESTFMCRDINYNLR----------YMAPEQIGRikKNVDFSTDHYSLGVIFYRMLTGKLPIEVDDE-------IKLS 127
Cdd:cd05581   161 nkGDATNIDSQIEKNRRrfasfvgtaeYVSPELLNE--KPAGKSSDLWALGCIIYQMLTGKPPFRGSNEyltfqkiLKLE 238
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 118443927  128 YcntnkkpvspkKIKNTIPLVISKIVMKLLEKDSEER 164
Cdd:cd05581   239 Y-----------SFPPNFPPDAKDLIEKLLVLDPQDR 264
GAF pfam01590
GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl ...
1228-1370 9.43e-09

GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl cyclases, phytochromes, FhlA and NifA. Adenylyl and guanylyl cyclases catalyse ATP and GTP to the second messengers cAMP and cGMP, respectively, these products up-regulating catalytic activity by binding to the regulatory GAF domain(s). The opposite hydrolysis reaction is catalysed by phosphodiesterase. cGMP-dependent 3',5'-cyclic phosphodiesterase catalyses the conversion of guanosine 3',5'-cyclic phosphate to guanosine 5'-phosphate. Here too, cGMP regulates catalytic activity by GAF-domain binding. Phytochromes are regulatory photoreceptors in plants and bacteria which exist in two thermally-stable states that are reversibly inter-convertible by light: the Pr state absorbs maximally in the red region of the spectrum, while the Pfr state absorbs maximally in the far-red region. This domain is also found in FhlA (formate hydrogen lyase transcriptional activator) and NifA, a transcriptional activator which is required for activation of most Nif operons which are directly involved in nitrogen fixation. NifA interacts with sigma-54.


Pssm-ID: 250726  Cd Length: 146  Bit Score: 55.67  E-value: 9.43e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927  1228 LENLLKELMINLIASVEAERGCLILNKNNKLFIEAegevdDICSVMENPIALEEYTKISKLLVNYVVRTKKSILLDD--- 1304
Cdd:pfam01590    2 LEELLQTILEELRELLGADRVAIYLADADGLLLYL-----VAGDGLSDIPLAARGLPLGGGVVGEVIAGGNPIVVPDvqd 76
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 118443927  1305 -----GKCEDIVFDDKYIVDNKVKSILCTPIIAKEKIIGIIYLENRfSSGIFNEKRLSIVELIASQAAISI 1370
Cdd:pfam01590   77 dprfrDLTALASDLPHFLRGLGIRSCLAVPLKGGGELIGVLVLHST-SPRAFTEEELELLQALADQVAIAL 146
GAF_3 pfam13492
GAF domain;
1228-1372 1.48e-08

GAF domain;


Pssm-ID: 257816  Cd Length: 129  Bit Score: 54.76  E-value: 1.48e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927  1228 LENLLKELMINLIASVEAERGCLILNKNNKLFIEaegevddICSVMENPIALEEYTKISKLLVNYVVRTKKSILLDDGKC 1307
Cdd:pfam13492    2 PDELLERALELLAELLGADRAALYLLDEDGLELR-------LVAGSGGEPRLSESLPEDSPLAQRALEKGEPVSVPAGDN 74
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 118443927  1308 EDIvfddkyivdNKVKSILCTPIIAKEKIIGIIYLENRfSSGIFNEKRLSIVELIASQAAISIEN 1372
Cdd:pfam13492   75 RDL---------LPSESLLAVPLRAGGEVIGVLVLEST-PEEAFTPEDLELLELLASQIAIALEN 129
STKc_nPKC_delta cd05620
Catalytic domain of the Protein Serine/Threonine Kinase, Novel Protein Kinase C delta; Serine ...
31-173 1.50e-08

Catalytic domain of the Protein Serine/Threonine Kinase, Novel Protein Kinase C delta; Serine/Threonine Kinases (STKs), Novel Protein Kinase C (nPKC), delta isoform, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The nPKC subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. 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. 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.


Pssm-ID: 173710 [Multi-domain]  Cd Length: 316  Bit Score: 56.88  E-value: 1.50e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927   31 ALKIVDAVSEVHKEGMIYKYLNPKNIILDINGQLKLMESTfMCRDINYNLR----------YMAPEQIGRIKKNvdFSTD 100
Cdd:cd05620   102 AAEIVCGLQFLHSKGIIYRDLKLDNVMLDRDGHIKIADFG-MCKENVFGDNrastfcgtpdYIAPEILQGLKYT--FSVD 178
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 118443927  101 HYSLGVIFYRMLTGKLPIEVDDEIKLSYCNTNKKPVSPKKI-KNTiplviSKIVMKLLEKDSEERYKSIYGIKV 173
Cdd:cd05620   179 WWSFGVLLYEMLIGQSPFHGDDEDELFESIRVDTPHYPRWItKES-----KDILEKLFERDPTRRLGVVGNIRG 247
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, MAP/ERK kinase kinase 4; Serine ...
1-128 2.70e-08

Catalytic domain of the Protein Serine/Threonine Kinase, MAP/ERK kinase kinase 4; Serine/threonine kinases (STKs), MAP/ERK kinase kinase 4 (MEKK4) subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The MEKK4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. MEKK4 is a mitogen-activated protein kinase (MAPK) kinase kinase (MAPKKK or MKKK or MAP3K), that 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. MEKK4 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.


Pssm-ID: 132957 [Multi-domain]  Cd Length: 264  Bit Score: 55.42  E-value: 2.70e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927    1 MEYYKkkgEVILEEFICNKKDMSIKEFLKNALKIVDAVSEVHKEGMIYKYLNPKNIILDINGQLKL---------MESTF 71
Cdd:cd06626    78 MEYCS---GGTLEELLEHGRILDEHVIRVYTLQLLEGLAYLHSHGIVHRDIKPANIFLDHNGVIKLgdfgcavklKNNTT 154
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 118443927   72 MCRDINYNLR----YMAPEQIGRIKKNVDF-STDHYSLGVIFYRMLTGKLPI-EVDDEIKLSY 128
Cdd:cd06626   155 TMGEEVQSLAgtpaYMAPEVITGGKGKGHGrAADIWSLGCVVLEMATGKRPWsELDNEFQIMF 217
STKc_MSK2_N cd05614
N-terminal catalytic domain of the Protein Serine/Threonine Kinase, Mitogen and ...
33-164 3.45e-08

N-terminal catalytic domain of the Protein Serine/Threonine Kinase, Mitogen and stress-activated kinase 2; Serine/Threonine Kinases (STKs), Mitogen and stress-activated kinase (MSK) subfamily, MSK2, N-terminal catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The MSK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. 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. 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.


Pssm-ID: 173705 [Multi-domain]  Cd Length: 332  Bit Score: 56.11  E-value: 3.45e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927   33 KIVDAVSEVHKEGMIYKYLNPKNIILDINGQLKLM-------------ESTF-MCRDInynlRYMAPEQIgRIKKNVDFS 98
Cdd:cd05614   113 EIILALEHLHKLGIVYRDIKLENILLDSEGHVVLTdfglskeflseekERTYsFCGTI----EYMAPEII-RGKGGHGKA 187
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 118443927   99 TDHYSLGVIFYRMLTGKLPIEVDDEiklsycNTNKKPVSPKKIKNTIPL------VISKIVMKLLEKDSEER 164
Cdd:cd05614   188 VDWWSLGILIFELLTGASPFTLEGE------RNTQSEVSRRILKCDPPFpsfigpEAQDLLHKLLRKDPKKR 253
STKc_Sid2p_Dbf2p cd05600
Catalytic domain of Fungal Sid2p- and Dbf2p-like Protein Serine/Threonine Kinases; Serine ...
34-117 3.65e-08

Catalytic domain of Fungal Sid2p- and Dbf2p-like Protein Serine/Threonine Kinases; Serine/Threonine Kinases (STKs), ROCK- and NDR-like subfamily, fungal Sid2p- and Dbf2p-like proteins, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Sid2p- and Dbf2p-like group is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. 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.


Pssm-ID: 173691 [Multi-domain]  Cd Length: 333  Bit Score: 55.87  E-value: 3.65e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927   34 IVDAVSEVHKEGMIYKYLNPKNIILDINGQLKLMESTFMCRDINY------NLRYMAPEQIGriKKNVDFSTDHYSLGVI 107
Cdd:cd05600   110 MFEAVDALHELGYIHRDLKPENFLIDASGHIKLTDFGLSKGIVTYansvvgSPDYMAPEVLR--GKGYDFTVDYWSLGCM 187
                          90
                  ....*....|
gi 118443927  108 FYRMLTGKLP 117
Cdd:cd05600   188 LYEFLCGFPP 197
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; Serine/Threonine Kinases (STKs) ...
31-117 4.98e-08

Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; Serine/Threonine Kinases (STKs), cAMP-dependent protein kinase (PKA) subfamily, PRKX-like kinases, catalytic (c) subunit. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PKA subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. 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.


Pssm-ID: 173703 [Multi-domain]  Cd Length: 291  Bit Score: 55.14  E-value: 4.98e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927   31 ALKIVDAVSEVHKEGMIYKYLNPKNIILDINGQLKLMESTFM--CRDINYNL----RYMAPEQIGRikKNVDFSTDHYSL 104
Cdd:cd05612   107 ASEIVCALEYLHSKEIVYRDLKPENILLDKEGHIKLTDFGFAkkLRDRTWTLcgtpEYLAPEVIQS--KGHNKAVDWWAL 184
                          90
                  ....*....|...
gi 118443927  105 GVIFYRMLTGKLP 117
Cdd:cd05612   185 GILIYEMLVGYPP 197
STKc_SGK cd05575
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
31-164 8.63e-08

Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; Serine/Threonine Kinases (STKs), Serum- and Glucocorticoid-induced Kinase (SGK) subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The SGK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. There are three isoforms of SGK, named SGK1, SGK2, and SGK3 (also called cytokine-independent survival kinase CISK). 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.


Pssm-ID: 173666 [Multi-domain]  Cd Length: 323  Bit Score: 54.80  E-value: 8.63e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927   31 ALKIVDAVSEVHKEGMIYKYLNPKNIILDINGQLKLMESTFMCRDINYN---------LRYMAPEQIgrIKKNVDFSTDH 101
Cdd:cd05575   102 AAEIASALGYLHSLNIIYRDLKPENILLDSQGHVVLTDFGLCKEGIEHSkttstfcgtPEYLAPEVL--RKQPYDRTVDW 179
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 118443927  102 YSLGVIFYRMLTGKLPIEVDDEIKLsYCNTNKKPVspkKIKNTIPLVISKIVMKLLEKDSEER 164
Cdd:cd05575   180 WCLGAVLYEMLYGLPPFYSRDTAEM-YDNILNKPL---RLKPNISVSARHLLEGLLQKDRTKR 238
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; Serine/Threonine ...
33-119 1.26e-07

Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; Serine/Threonine Kinases (STKs), Microtubule-associated serine/threonine (MAST) kinase subfamily, fungal Rim15-like kinases, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The MAST kinase subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. 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.


Pssm-ID: 173702 [Multi-domain]  Cd Length: 260  Bit Score: 53.64  E-value: 1.26e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927   33 KIVDAVSEVHKEGMIYKYLNPKNIILDINGQLKLM-----ESTFMCRDINYNLRYMAPEQIgrIKKNVDFSTDHYSLGVI 107
Cdd:cd05611   105 EVVLGVEDLHQRGIIHRDIKPENLLIDQTGHLKLTdfglsRNGLENKKFVGTPDYLAPETI--LGVGDDKMSDWWSLGCV 182
                          90
                  ....*....|..
gi 118443927  108 FYRMLTGKLPIE 119
Cdd:cd05611   183 IFEFLFGYPPFH 194
STKc_nPKC_eta cd05590
Catalytic domain of the Protein Serine/Threonine Kinase, Novel Protein Kinase C eta; Serine ...
31-138 1.29e-07

Catalytic domain of the Protein Serine/Threonine Kinase, Novel Protein Kinase C eta; Serine/Threonine Kinases (STKs), Novel Protein Kinase C (nPKC), eta isoform, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The nPKC subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. 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. 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.


Pssm-ID: 173681 [Multi-domain]  Cd Length: 320  Bit Score: 54.13  E-value: 1.29e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927   31 ALKIVDAVSEVHKEGMIYKYLNPKNIILDINGQLKLMESTfMCRDINYNLR----------YMAPEQIGRIKKNVDfsTD 100
Cdd:cd05590   102 AAEITSALMFLHDKGIIYRDLKLDNVLLDHEGHCKLADFG-MCKEGIFNGKttstfcgtpdYIAPEILQEMLYGPS--VD 178
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 118443927  101 HYSLGVIFYRMLTGKLPIEVDDEIKLSYCNTNKKPVSP 138
Cdd:cd05590   179 WWAMGVLLYEMLCGHAPFEAENEDDLFEAILNDEVVYP 216
STKc_GRK cd05577
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase; ...
31-164 1.36e-07

Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase; Serine/Threonine Kinases (STKs), G protein-coupled Receptor Kinase (GRK) subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The GRK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. 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 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. They 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. GRKs play important roles in the cardiovascular, immune, respiratory, skeletal, and nervous systems.


Pssm-ID: 173668 [Multi-domain]  Cd Length: 277  Bit Score: 53.66  E-value: 1.36e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927   31 ALKIVDAVSEVHKEGMIYKYLNPKNIILDINGQLKLMESTFMCrDINYNLR---------YMAPEQIgrIKKNVDFSTDH 101
Cdd:cd05577   101 AAQIICGLEHLHQRRIVYRDLKPENVLLDDHGNVRISDLGLAV-ELKGGKKikgragtpgYMAPEVL--QGEVYDFSVDW 177
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 118443927  102 YSLGVIFYRMLTGKLPIEvddeiklsycnTNKKPVSPKKIKNTIPLVISK-----------IVMKLLEKDSEER 164
Cdd:cd05577   178 FALGCTLYEMIAGRSPFR-----------QRKEKVEKEELKRRTLEMAVEypdkfspeakdLCEALLQKDPEKR 240
STKc_CRIK cd05601
Catalytic domain of the Protein Serine/Threonine Kinase, Citron Rho-interacting kinase; Serine ...
33-150 1.68e-07

Catalytic domain of the Protein Serine/Threonine Kinase, Citron Rho-interacting kinase; Serine/Threonine Kinases (STKs), Citron Rho-interacting kinase (CRIK) subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The CRIK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. CRIK is also called citron kinase. It 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. CRIK, an effector of the small GTPase Rho, 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.


Pssm-ID: 173692 [Multi-domain]  Cd Length: 330  Bit Score: 53.67  E-value: 1.68e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927   33 KIVDAVSEVHKEGMIYKYLNPKNIILDINGQLKLME---STFMCRDINYNLR-------YMAPEQI----GRIKKNVDFS 98
Cdd:cd05601   110 ELVLAIHSVHQMGYVHRDIKPENVLIDRTGHIKLADfgsAARLTANKMVNSKlpvgtpdYIAPEVLttmnGDGKGTYGVE 189
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 118443927   99 TDHYSLGVIFYRMLTGKLPIEVDDEIK-----LSYCNTNKKPVSPKKIKNTIPLVIS 150
Cdd:cd05601   190 CDWWSLGVIAYEMIYGRSPFHEGTSAKtynniMNFQRFLKFPEDPKVSSDFLDLIQS 246
STKc_nPKC_epsilon cd05591
Catalytic domain of the Protein Serine/Threonine Kinase, Novel Protein Kinase C epsilon; ...
31-126 3.31e-07

Catalytic domain of the Protein Serine/Threonine Kinase, Novel Protein Kinase C epsilon; Serine/Threonine Kinases (STKs), Novel Protein Kinase C (nPKC), epsilon isoform, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The nPKC subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. 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. 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.


Pssm-ID: 173682 [Multi-domain]  Cd Length: 321  Bit Score: 52.93  E-value: 3.31e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927   31 ALKIVDAVSEVHKEGMIYKYLNPKNIILDINGQLKLMESTfMCRD--INYNLR--------YMAPEQIGRIKknVDFSTD 100
Cdd:cd05591   102 AAEVTLALMFLHRHGVIYRDLKLDNILLDAEGHCKLADFG-MCKEgiLNGVTTttfcgtpdYIAPEILQELE--YGPSVD 178
                          90       100
                  ....*....|....*....|....*.
gi 118443927  101 HYSLGVIFYRMLTGKLPIEVDDEIKL 126
Cdd:cd05591   179 WWALGVLMYEMMAGQPPFEADNEDDL 204
STKc_SGK2 cd05603
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
31-185 5.61e-07

Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; Serine/Threonine Kinases (STKs), Serum- and Glucocorticoid-induced Kinase (SGK) subfamily, SGK2 isoform, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The SGK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. There are three isoforms of SGK, named SGK1, SGK2, and SGK3. SGK2 shows a more restricted distribution that 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.


Pssm-ID: 173694 [Multi-domain]  Cd Length: 321  Bit Score: 52.28  E-value: 5.61e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927   31 ALKIVDAVSEVHKEGMIYKYLNPKNIILDINGQLKLME--------------STFmCRdinyNLRYMAPEQIGriKKNVD 96
Cdd:cd05603   102 AAEVASAIGYLHSLNIIYRDLKPENILLDSQGHVVLTDfglckegvepeettSTF-CG----TPEYLAPEVLR--KEPYD 174
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927   97 FSTDHYSLGVIFYRMLTGkLPIEVDDEIKLSYCNTNKKPVSPKKIKNTiplVISKIVMKLLEKDSEERyksiYGIKVDLN 176
Cdd:cd05603   175 RTVDWWCLGAVLYEMLYG-LPPFYSRDVSQMYDNILHKPLQLPGGKTV---AACDLLVGLLHKDQRRR----LGAKADFL 246

                  ....*....
gi 118443927  177 KCYKSLIFS 185
Cdd:cd05603   247 EIKNHVFFS 255
STKc_SGK1 cd05602
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
31-185 6.33e-07

Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 1; Serine/Threonine Kinases (STKs), Serum- and Glucocorticoid-induced Kinase (SGK) subfamily, SGK1 isoform, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The SGK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. There are three isoforms of SGK, named SGK1, SGK2, and SGK3. 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.


Pssm-ID: 173693 [Multi-domain]  Cd Length: 325  Bit Score: 51.94  E-value: 6.33e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927   31 ALKIVDAVSEVHKEGMIYKYLNPKNIILDINGQLKLMESTFMCRDINYN---------LRYMAPEQIGriKKNVDFSTDH 101
Cdd:cd05602   102 AAEIASALGYLHSLNIVYRDLKPENILLDSQGHIVLTDFGLCKENIEHNgttstfcgtPEYLAPEVLH--KQPYDRTVDW 179
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927  102 YSLGVIFYRMLTGKLPIEVDDEIKLsYCNTNKKPVspkKIKNTIPLVISKIVMKLLEKDSEERyksiYGIKVDLNKCYKS 181
Cdd:cd05602   180 WCLGAVLYEMLYGLPPFYSRNTAEM-YDNILNKPL---QLKPNITNSARHLLEGLLQKDRTKR----LGAKDDFMEIKNH 251

                  ....
gi 118443927  182 LIFS 185
Cdd:cd05602   252 IFFS 255
STKc_aPKC cd05588
Catalytic domain of the Protein Serine/Threonine Kinase, Atypical Protein Kinase C; Serine ...
31-164 6.68e-07

Catalytic domain of the Protein Serine/Threonine Kinase, Atypical Protein Kinase C; Serine/Threonine Kinases (STKs), Atypical Protein Kinase C (aPKC) subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The aPKC subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. 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. 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.


Pssm-ID: 173679 [Multi-domain]  Cd Length: 329  Bit Score: 51.75  E-value: 6.68e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927   31 ALKIVDAVSEVHKEGMIYKYLNPKNIILDINGQLKLMESTfMCRDinyNLR-------------YMAPEqIGRiKKNVDF 97
Cdd:cd05588   102 SAEISLALNFLHERGIIYRDLKLDNVLLDAEGHIKLTDYG-MCKE---GIRpgdttstfcgtpnYIAPE-ILR-GEDYGF 175
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 118443927   98 STDHYSLGVIFYRMLTGKLPIEVDDEIKLSYCNTN--------KKPVspkKIKNTIPLVISKIVMKLLEKDSEER 164
Cdd:cd05588   176 SVDWWALGVLMFEMMAGRSPFDIVGMSDNPDQNTEdylfqvilEKQI---RIPRSLSVKASSVLKGFLNKDPKER 247
STKc_SGK3 cd05604
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
31-185 6.83e-07

Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 3; Serine/Threonine Kinases (STKs), Serum- and Glucocorticoid-induced Kinase (SGK) subfamily, SGK3 isoform, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The SGK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. There are three isoforms of SGK, named SGK1, SGK2, and SGK3 (also called cytokine-independent survival kinase CISK). SGK3 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.


Pssm-ID: 173695 [Multi-domain]  Cd Length: 325  Bit Score: 51.93  E-value: 6.83e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927   31 ALKIVDAVSEVHKEGMIYKYLNPKNIILDINGQLKLMESTfMCR------DINYNL----RYMAPEQIGriKKNVDFSTD 100
Cdd:cd05604   102 AAEIASALGYLHSINIVYRDLKPENILLDSQGHVVLTDFG-LCKegiaqsDTTTTFcgtpEYLAPEVIR--KQPYDNTVD 178
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927  101 HYSLGVIFYRMLTGKLPIEVDDEIKLsYCNTNKKPVSpkkIKNTIPLVISKIVMKLLEKDSEERyksiYGIKVDLNKCYK 180
Cdd:cd05604   179 WWCLGAVLYEMLYGLPPFYCRDVAEM-YDNILHKPLV---LRPGASLTAWSILEELLEKDRQRR----LGAKEDFLEIQE 250

                  ....*
gi 118443927  181 SLIFS 185
Cdd:cd05604   251 HPFFE 255
STKc_GRK5 cd05632
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; ...
31-164 9.06e-07

Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; Serine/Threonine Kinases (STKs), G protein-coupled Receptor Kinase (GRK) subfamily, GRK5 isoform, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The GRK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. 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. There are seven types of GRKs, named GRK1 to GRK7. 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.


Pssm-ID: 173721 [Multi-domain]  Cd Length: 285  Bit Score: 51.13  E-value: 9.06e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927   31 ALKIVDAVSEVHKEGMIYKYLNPKNIILDINGQLKLMESTF--------MCRDINYNLRYMAPEQIGriKKNVDFSTDHY 102
Cdd:cd05632   108 AAEILCGLEDLHRENTVYRDLKPENILLDDYGHIRISDLGLavkipegeSIRGRVGTVGYMAPEVLN--NQRYTLSPDYW 185
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 118443927  103 SLGVIFYRMLTGKLPIEVDDEiKLSYCNTNKKPVSPKKIKNTIPLVISKIVMK-LLEKDSEER 164
Cdd:cd05632   186 GLGCLIYEMIEGQSPFRGRKE-KVKREEVDRRVLETEEVYSAKFSEEAKSICKmLLTKDPKQR 247
PKc_MKK3_6 cd06617
Catalytic domain of the dual-specificity Protein Kinases, MAP kinase kinases 3 and 6; Protein ...
19-164 1.23e-06

Catalytic domain of the dual-specificity Protein Kinases, MAP kinase kinases 3 and 6; Protein kinases (PKs), MAP kinase kinase 3 (MKK3) and MKK6 subfamily, catalytic (c) domain. PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. The MKK3 and MKK6 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. The mitogen-activated protein (MAP) kinase signaling pathways are important mediators of cellular responses to extracellular signals. The pathways involve a triple kinase core cascade comprising the MAP kinase (MAPK), which is phosphorylated and activated by a MAPK kinase (MAPKK or MKK), which itself is phosphorylated and activated by a MAPK kinase kinase (MAPKKK or MKKK). MKK3 and MKK6 are dual-specificity PKs that phosphorylate and activate their downstream target, p38 MAPK, on specific threonine and tyrosine residues. MKK3/6 plays 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.


Pssm-ID: 173729 [Multi-domain]  Cd Length: 283  Bit Score: 50.89  E-value: 1.23e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927   19 KKDMSIKE-FL-KNALKIVDAVSEVH-KEGMIYKYLNPKNIILDINGQLK---------LMEStfMCRDINYNLR-YMAP 85
Cdd:cd06617    95 DKGLTIPEdILgKIAVSIVKALEYLHsKLSVIHRDVKPSNVLINRNGQVKlcdfgisgyLVDS--VAKTIDAGCKpYMAP 172
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927   86 EQIG--RIKKNVDFSTDHYSLGVIFYRMLTGKLPIEvddeiklsycnTNKKPV----------SPKKIKNTIPLVISKIV 153
Cdd:cd06617   173 ERINpeLNQKGYDVKSDVWSLGITMIELATGRFPYD-----------SWKTPFqqlkqvveepSPQLPAEKFSPEFQDFV 241
                         170
                  ....*....|.
gi 118443927  154 MKLLEKDSEER 164
Cdd:cd06617   242 NKCLKKNYKER 252
STKc_GRK6 cd05630
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; ...
31-119 2.23e-06

Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; Serine/Threonine Kinases (STKs), G protein-coupled Receptor Kinase (GRK) subfamily, GRK6 isoform, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The GRK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. 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. There are seven types of GRKs, named GRK1 to GRK7. GRK6 is widely expressed in many tissues. t 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.


Pssm-ID: 173719 [Multi-domain]  Cd Length: 285  Bit Score: 50.02  E-value: 2.23e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927   31 ALKIVDAVSEVHKEGMIYKYLNPKNIILDINGQLKLME---STFMCRDINYNLR-----YMAPEQIGriKKNVDFSTDHY 102
Cdd:cd05630   108 AAEICCGLEDLHQERIVYRDLKPENILLDDHGHIRISDlglAVHVPEGQTIKGRvgtvgYMAPEVVK--NERYTFSPDWW 185
                          90
                  ....*....|....*..
gi 118443927  103 SLGVIFYRMLTGKLPIE 119
Cdd:cd05630   186 ALGCLLYEMIAGQSPFQ 202
STKc_beta_ARK cd05606
Catalytic domain of the Protein Serine/Threonine Kinase, beta-adrenergic receptor kinase; ...
31-164 2.53e-06

Catalytic domain of the Protein Serine/Threonine Kinase, beta-adrenergic receptor kinase; Serine/Threonine Kinases (STKs), G protein-coupled Receptor Kinase (GRK) subfamily, beta-adrenergic receptor kinase (beta-ARK) group, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The GRK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. 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. There are seven types of GRKs, named GRK1 to GRK7. 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.


Pssm-ID: 173697 [Multi-domain]  Cd Length: 278  Bit Score: 49.93  E-value: 2.53e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927   31 ALKIVDAVSEVHKEGMIYKYLNPKNIILDINGQLKLMESTFMCrdiNYNLR----------YMAPEQigrIKKNV--DFS 98
Cdd:cd05606   103 AAEIILGLEHMHNRFVVYRDLKPANILLDEHGHVRISDLGLAC---DFSKKkphasvgthgYMAPEV---LQKGVayDSS 176
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 118443927   99 TDHYSLGVIFYRMLTGKLPIEVDDEIKLSYCNTNKKPVSPkKIKNTIPLVISKIVMKLLEKDSEER 164
Cdd:cd05606   177 ADWFSLGCMLFKLLRGHSPFRQHKTKDKHEIDRMTLTMAV-ELPDSFSPELRSLLEGLLQRDVNRR 241
STKc_ROCK_NDR_like cd05573
Catalytic domain of ROCK- and NDR kinase-like Protein Serine/Threonine Kinases; Serine ...
34-172 2.95e-06

Catalytic domain of ROCK- and NDR kinase-like Protein Serine/Threonine Kinases; Serine/Threonine Kinases (STKs), Rho-associated coiled-coil containing protein kinase (ROCK) and Nuclear Dbf2-Related (NDR)-like kinase subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The ROCK- and NDR-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. 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.


Pssm-ID: 173664 [Multi-domain]  Cd Length: 350  Bit Score: 49.99  E-value: 2.95e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927   34 IVDAVSEVHKEGMIYKYLNPKNIILDINGQLKLM------------ESTFMCRDINYNLR-------------------- 81
Cdd:cd05573   110 LVLALDSVHKLGFIHRDIKPDNILIDADGHIKLAdfglckkmnkakDREYYLNDSHNLLFrdnvlvrrrdhkqrrvrans 189
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927   82 ------YMAPEQIgrIKKNVDFSTDHYSLGVIFYRMLTGKLPIeVDDEIKLSYcntnkkpvspKKIKN-----TIPL--V 148
Cdd:cd05573   190 tvgtpdYIAPEVL--RGTPYGLECDWWSLGVILYEMLYGFPPF-YSDTLQETY----------NKIINwkeslRFPPdpP 256
                         170       180
                  ....*....|....*....|....*..
gi 118443927  149 ISKIVMKLLEK---DSEERYKSIYGIK 172
Cdd:cd05573   257 VSPEAIDLICRllcDPEDRLGSFEEIK 283
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; Protein Kinases (PKs), STE family, catalytic ...
28-164 4.11e-06

Catalytic domain of STE family Protein Kinases; Protein Kinases (PKs), STE family, catalytic (c) domain. PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. The STE family is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine kinases (STKs), protein tyrosine kinases (PTKs), RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K). 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), MAPK kinase kinases (MAPKKKs), or MAPK kinase kinase 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.


Pssm-ID: 173659 [Multi-domain]  Cd Length: 253  Bit Score: 48.74  E-value: 4.11e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927   28 LKNALKivdAVSEVHKEGMIYKYLNPKNIILDINGQLKL--------MESTFMCRDINYNLRYMAPEQIgrIKKNVDFST 99
Cdd:cd05122   104 CKELLK---GLEYLHSNGIIHRDIKAANILLTSDGEVKLidfglsaqLSDTKARNTMVGTPYWMAPEVI--NGKPYDYKA 178
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 118443927  100 DHYSLGVIFYRMLTGKLPIEVDDEIK-LSYCNTNKKPVSPKKIKNTIPLVisKIVMKLLEKDSEER 164
Cdd:cd05122   179 DIWSLGITAIELAEGKPPYSELPPMKaLFKIATNGPPGLRNPEKWSDEFK--DFLKKCLQKNPEKR 242
STKc_RPK118_like cd05576
Catalytic domain of the Protein Serine/Threonine Kinases, RPK118 and similar proteins; Serine ...
31-115 4.29e-06

Catalytic domain of the Protein Serine/Threonine Kinases, RPK118 and similar proteins; Serine/Threonine Kinases (STKs), RPK118-like subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The RPK118-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. Members of this subfamily show similarity to human RPK118, which contains an N-terminal Phox homology (PX) domain, a Microtubule Interacting and Trafficking (MIT) domain, and a kinase domain containing a long insert. Also included in the family is human RPK60 (or ribosomal protein S6 kinase-like 1), which also contains MIT and kinase domains but lacks a PX domain. RPK118 binds sphingosine kinase, a key enzyme in the synthesis of sphingosine 1-phosphate (SPP), a lipid messenger involved in many cellular events. RPK118 may be involved in transmitting SPP-mediated signaling. RPK118 also binds the antioxidant peroxiredoxin-3 (PRDX3). RPK118 may be involved in the transport of PRDX3 from the cytoplasm to its site of function in the mitochondria.


Pssm-ID: 173667  Cd Length: 237  Bit Score: 48.69  E-value: 4.29e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927   31 ALKIVDAVSEVHKEGMIYKYLNPKNIILDINGQLKLmesTFMCR----------DINYNLrYMAPEqIGRIKKNVDfSTD 100
Cdd:cd05576    91 AAEMVVALDALHREGIVCRDLNPNNILLDDRGHIQL---TYFSRwsevedscdgEAVENM-YCAPE-VGGISEETE-ACD 164
                          90
                  ....*....|....*
gi 118443927  101 HYSLGVIFYRMLTGK 115
Cdd:cd05576   165 WWSLGAILFELLTGK 179
STKc_PKN cd05589
Catalytic domain of the Protein Serine/Threonine Kinase, Protein Kinase N; Serine/Threonine ...
42-164 5.28e-06

Catalytic domain of the Protein Serine/Threonine Kinase, Protein Kinase N; Serine/Threonine Kinases (STKs), Protein Kinase N (PKN) subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PKN subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. 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.


Pssm-ID: 173680 [Multi-domain]  Cd Length: 324  Bit Score: 48.91  E-value: 5.28e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927   42 HKEGMIYKYLNPKNIILDINGQLKLMESTFMCRDINYNLR---------YMAPEQIgrIKKNVDFSTDHYSLGVIFYRML 112
Cdd:cd05589   118 HENKIVYRDLKLDNLLLDTEGFVKIADFGLCKEGMGFGDRtstfcgtpeFLAPEVL--TETSYTRAVDWWGLGVLIYEML 195
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 118443927  113 TGKLPIEVDDEIKLSYCNTNKKPVSPKkiknTIPLVISKIVMKLLEKDSEER 164
Cdd:cd05589   196 VGESPFPGDDEEEVFDSIVNDEVRYPR----FLSREAISIMRRLLRRNPERR 243
STKc_Sck1_like cd05586
Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Protein Serine ...
33-122 5.62e-06

Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Protein Serine/Threonine Kinases; Serine/Threonine Kinases (STKs), Fission yeast Suppressor of loss of cAMP-dependent protein kinase (Sck1)-like subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Sck1-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. This subfamily is composed of fungal proteins with similarity to the Schizosaccharomyces pombe STK Sck1. 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.


Pssm-ID: 173677 [Multi-domain]  Cd Length: 330  Bit Score: 49.16  E-value: 5.62e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927   33 KIVDAVSEVHKEGMIYKYLNPKNIILDINGQLKLMESTFMCRDINYN---------LRYMAPEQIGRIK---KNVDFstd 100
Cdd:cd05586   104 ELVLALEHLHKYDIVYRDLKPENILLDATGHIALCDFGLSKANLTDNkttntfcgtTEYLAPEVLLDEKgytKHVDF--- 180
                          90       100
                  ....*....|....*....|..
gi 118443927  101 hYSLGVIFYRMLTGKLPIEVDD 122
Cdd:cd05586   181 -WSLGVLVFEMCCGWSPFYAED 201
STKc_cPKC_alpha cd05615
Catalytic domain of the Protein Serine/Threonine Kinase, Classical Protein Kinase C alpha; ...
41-126 5.79e-06

Catalytic domain of the Protein Serine/Threonine Kinase, Classical Protein Kinase C alpha; Serine/Threonine Kinases (STKs), Classical Protein Kinase C (cPKC) subfamily, alpha isoform, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The cPKC subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. 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. There are four cPKC isoforms, named alpha, betaI, betaII, and gamma. 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.


Pssm-ID: 173706 [Multi-domain]  Cd Length: 323  Bit Score: 48.84  E-value: 5.79e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927   41 VHKEGMIYKYLNPKNIILDINGQLKLMESTfMCRDINYN----------LRYMAPEQIGRikKNVDFSTDHYSLGVIFYR 110
Cdd:cd05615   117 LHRRGIIYRDLKLDNVMLDSEGHIKIADFG-MCKEHMVDgvttrtfcgtPDYIAPEIIAY--QPYGKSVDWWAYGVLLYE 193
                          90
                  ....*....|....*.
gi 118443927  111 MLTGKLPIEVDDEIKL 126
Cdd:cd05615   194 MLAGQPPFDGEDEDEL 209
STKc_aPKC_zeta cd05617
Catalytic domain of the Protein Serine/Threonine Kinase, Atypical Protein Kinase C zeta; ...
31-164 8.22e-06

Catalytic domain of the Protein Serine/Threonine Kinase, Atypical Protein Kinase C zeta; Serine/Threonine Kinases (STKs), Atypical Protein Kinase C (aPKC) subfamily, zeta isoform, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The aPKC subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. 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. There are two aPKC isoforms, zeta and iota. 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.


Pssm-ID: 173708 [Multi-domain]  Cd Length: 327  Bit Score: 48.49  E-value: 8.22e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927   31 ALKIVDAVSEVHKEGMIYKYLNPKNIILDINGQLKLMESTfMCR------DINYNL----RYMAPEQIGriKKNVDFSTD 100
Cdd:cd05617   102 AAEICIALNFLHERGIIYRDLKLDNVLLDADGHIKLTDYG-MCKeglgpgDTTSTFcgtpNYIAPEILR--GEEYGFSVD 178
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 118443927  101 HYSLGVIFYRMLTGKLPIEV-------DDEIKLSYCNTNKkpvsPKKIKNTIPLVISKIVMKLLEKDSEER 164
Cdd:cd05617   179 WWALGVLMFEMMAGRSPFDIitdnpdmNTEDYLFQVILEK----PIRIPRFLSVKASHVLKGFLNKDPKER 245
STKc_cPKC_beta cd05616
Catalytic domain of the Protein Serine/Threonine Kinase, Classical Protein Kinase C beta; ...
41-126 9.43e-06

Catalytic domain of the Protein Serine/Threonine Kinase, Classical Protein Kinase C beta; Serine/Threonine Kinases (STKs), Classical Protein Kinase C (cPKC) subfamily, beta isoforms, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The cPKC subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. 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. There are four cPKC isoforms, named alpha, betaI, betaII, and gamma. The PKC beta isoforms (I and II), generated by alternative splicing of a single gene, are preferentially activated by hyperglycemia-induced DAG 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.


Pssm-ID: 173707 [Multi-domain]  Cd Length: 323  Bit Score: 48.07  E-value: 9.43e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927   41 VHKEGMIYKYLNPKNIILDINGQLKLMESTfMCRDINYN----------LRYMAPEQIGRikKNVDFSTDHYSLGVIFYR 110
Cdd:cd05616   117 LHSKGIIYRDLKLDNVMLDSEGHIKIADFG-MCKENMWDgvttktfcgtPDYIAPEIIAY--QPYGKSVDWWAFGVLLYE 193
                          90
                  ....*....|....*.
gi 118443927  111 MLTGKLPIEVDDEIKL 126
Cdd:cd05616   194 MLAGQAPFEGEDEDEL 209
PTK_Ryk cd05043
Pseudokinase domain of Ryk (Receptor related to tyrosine kinase); Protein Tyrosine Kinase (PTK) ...
31-121 9.86e-06

Pseudokinase domain of Ryk (Receptor related to tyrosine kinase); Protein Tyrosine Kinase (PTK) family; Receptor related to tyrosine kinase (Ryk); pseudokinase domain. The PTKc (catalytic domain) family to which this subfamily belongs, 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. Ryk is a receptor tyr kinase (RTK) containing an extracellular region with two leucine-rich motifs, a transmembrane segment, and an intracellular inactive pseudokinase domain. The extracellular region of Ryk shows homology to the N-terminal domain of Wnt inhibitory factor-1 (WIF) and serves as the ligand (Wnt) binding domain of Ryk. Ryk is expressed in many different tissues both during development and in adults, suggesting a widespread function. It acts as a chemorepulsive axon guidance receptor of Wnt glycoproteins and is responsible for the establishment of axon tracts during the development of the central nervous system. In addition, studies in mice reveal that Ryk is essential in skeletal, craniofacial, and cardiac development. Thus, it appears Ryk is involved in signal transduction despite its lack of kinase activity. Ryk may function as an accessory protein that modulates the signals coming from catalytically active partner RTKs such as the Eph receptors.


Pssm-ID: 133175 [Multi-domain]  Cd Length: 280  Bit Score: 47.79  E-value: 9.86e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927   31 ALKIVDAVSEVHKEGMIYKYLNPKNIILDINGQLKLMESTfMCRDI------------NYNLRYMAPEQIgrIKKNVDFS 98
Cdd:cd05043   123 AIQIACGMSYLHKRGVIHKDIAARNCVIDEELQVKITDNA-LSRDLfpmdyhclgdneNRPVKWMALESL--VNKEYSSA 199
                          90       100
                  ....*....|....*....|....*
gi 118443927   99 TDHYSLGVIFYRMLT-GKLP-IEVD 121
Cdd:cd05043   200 SDVWSFGVLLWELMTlGQTPyVEID 224
STKc_cPKC cd05587
Catalytic domain of the Protein Serine/Threonine Kinase, Classical Protein Kinase C; Serine ...
31-141 1.01e-05

Catalytic domain of the Protein Serine/Threonine Kinase, Classical Protein Kinase C; Serine/Threonine Kinases (STKs), Classical (or Conventional) Protein Kinase C (cPKC) subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The cPKC subfamily is part of a 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). 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. cPKCs contain a calcium-binding C2 region in their regulatory domain. There are four cPKC isoforms, named alpha, betaI, betaII, and gamma. cPKCs are potent kinases for histones, myelin basic protein, and protamine. PKC-gamma is mainly expressed in neuronal tissues. It plays a role in protection from ischemia.


Pssm-ID: 173678 [Multi-domain]  Cd Length: 324  Bit Score: 48.24  E-value: 1.01e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927   31 ALKIVDAVSEVHKEGMIYKYLNPKNIILDINGQLKLMEstF-MCRDinyNL-------------RYMAPEQIgrIKKNVD 96
Cdd:cd05587   107 AAEIAIGLFFLHSKGIIYRDLKLDNVMLDAEGHIKIAD--FgMCKE---NIfggkttrtfcgtpDYIAPEII--AYQPYG 179
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 118443927   97 FSTDHYSLGVIFYRMLTGKLPIEVDDEIKLSYCNTNKKPVSPKKI 141
Cdd:cd05587   180 KSVDWWAFGVLLYEMLAGQPPFDGEDEDELFQSIMEHNVSYPKSL 224
STKc_aPKC_iota cd05618
Catalytic domain of the Protein Serine/Threonine Kinase, Atypical Protein Kinase C iota; ...
37-164 1.03e-05

Catalytic domain of the Protein Serine/Threonine Kinase, Atypical Protein Kinase C iota; Serine/Threonine Kinases (STKs), Atypical Protein Kinase C (aPKC) subfamily, iota isoform, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The aPKC subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. 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. There are two aPKC isoforms, zeta and iota. 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.


Pssm-ID: 88519 [Multi-domain]  Cd Length: 329  Bit Score: 48.13  E-value: 1.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927   37 AVSEVHKEGMIYKYLNPKNIILDINGQLKLMESTfMCRDinyNLR-------------YMAPEQIGriKKNVDFSTDHYS 103
Cdd:cd05618   108 ALNYLHERGIIYRDLKLDNVLLDSEGHIKLTDYG-MCKE---GLRpgdttstfcgtpnYIAPEILR--GEDYGFSVDWWA 181
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 118443927  104 LGVIFYRMLTGKLPIEVDDEIKLSYCNTNK---KPVSPKKIK--NTIPLVISKIVMKLLEKDSEER 164
Cdd:cd05618   182 LGVLMFEMMAGRSPFDIVGSSDNPDQNTEDylfQVILEKQIRipRSLSVKAASVLKSFLNKDPKER 247
STKc_YPK1_like cd05585
Catalytic domain of Yeast Protein Kinase 1-like Protein Serine/Threonine Kinases; Serine ...
37-164 1.08e-05

Catalytic domain of Yeast Protein Kinase 1-like Protein Serine/Threonine Kinases; Serine/Threonine Kinases (STKs), Yeast protein kinase 1 (YPK1)-like subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The YPK1-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. 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.


Pssm-ID: 173676 [Multi-domain]  Cd Length: 312  Bit Score: 48.01  E-value: 1.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927   37 AVSEVHKEGMIYKYLNPKNIILDINGQLKLMESTF----MCRDINYNL-----RYMAPEQI---GRIKknvdfSTDHYSL 104
Cdd:cd05585   105 ALENLHKFNVIYRDLKPENILLDYQGHIALCDFGLcklnMKDDDKTNTfcgtpEYLAPELLlghGYTK-----AVDWWTL 179
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927  105 GVIFYRMLTGkLPIEVDDEIKLSYcntNKKPVSPKKIKNTIPLVISKIVMKLLEKDSEER 164
Cdd:cd05585   180 GVLLYEMLTG-LPPFYDENVNEMY---RKILQEPLRFPDGFDRDAKDLLIGLLSRDPTRR 235
STKc_PKB cd05571
Catalytic domain of the Protein Serine/Threonine Kinase, Protein Kinase B; Serine/Threonine ...
33-126 1.17e-05

Catalytic domain of the Protein Serine/Threonine Kinase, Protein Kinase B; Serine/Threonine Kinases (STKs), Protein Kinase B (PKB) or Akt subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PKB subfamily is part of a 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). 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 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.


Pssm-ID: 173662 [Multi-domain]  Cd Length: 323  Bit Score: 47.88  E-value: 1.17e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927   33 KIVDAVSEVHKEGMIYKYLNPKNIILDINGQLKLMESTFMCRDINYNL---------RYMAPEqigrIKKNVDF--STDH 101
Cdd:cd05571   103 EIVSALGYLHSCDVVYRDLKLENLMLDKDGHIKITDFGLCKEGISDGAtmktfcgtpEYLAPE----VLEDNDYgrAVDW 178
                          90       100
                  ....*....|....*....|....*
gi 118443927  102 YSLGVIFYRMLTGKLPIEVDDEIKL 126
Cdd:cd05571   179 WGLGVVMYEMMCGRLPFYNQDHEKL 203
STKc_PKA cd05580
Catalytic domain of the Protein Serine/Threonine Kinase, cAMP-dependent protein kinase; Serine ...
31-165 1.27e-05

Catalytic domain of the Protein Serine/Threonine Kinase, cAMP-dependent protein kinase; Serine/Threonine Kinases (STKs), cAMP-dependent protein kinase (PKA) subfamily, catalytic (c) subunit. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PKA subfamily is part of a 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). This subfamily is composed of the cAMP-dependent proteins kinases, PKA and PRKX. The inactive PKA holoenzyme is a heterotetramer composed of two phosphorylated and active catalytic (C) 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 C 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.


Pssm-ID: 173671 [Multi-domain]  Cd Length: 290  Bit Score: 47.54  E-value: 1.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927   31 ALKIVDAVSEVHKEGMIYKYLNPKNIILDINGQLKLMESTFMCR--DINYNL----RYMAPEQIgrIKKNVDFSTDHYSL 104
Cdd:cd05580   107 AAQVVLALEYLHSLDIVYRDLKPENLLLDSDGYIKITDFGFAKRvkGRTYTLcgtpEYLAPEII--LSKGYGKAVDWWAL 184
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 118443927  105 GVIFYRMLTGKLPIEVDDEIKLsYcntnKKPVS-----PKKIKNTIPLVISkivmKLLEKDSEERY 165
Cdd:cd05580   185 GILIYEMLAGYPPFFDDNPIQI-Y----EKILEgkvrfPSFFSPDAKDLIR----NLLQVDLTKRL 241
STKc_PAK6 cd06659
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 6; Serine ...
34-164 1.32e-05

Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 6; Serine/threonine kinases (STKs), p21-activated kinase (PAK) 6, 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. PAK6 belongs to group II. Group II PAKs contain a PBD (p21-binding domain) and a C-terminal catalytic domain, but do not harbor an AID (autoinhibitory domain) or SH3 binding sites. 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.


Pssm-ID: 132990 [Multi-domain]  Cd Length: 297  Bit Score: 47.72  E-value: 1.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927   34 IVDAVSEVHKEGMIYKYLNPKNIILDINGQLKLMESTFmCRDINYNL----------RYMAPEQIGRIKKNVDfsTDHYS 103
Cdd:cd06659   126 VLQALCYLHSQGVIHRDIKSDSILLTLDGRVKLSDFGF-CAQISKDVpkrkslvgtpYWMAPEVISRTPYGTE--VDIWS 202
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 118443927  104 LGVIFYRMLTGKLPIEVDDEIKLSYCNTNKKPVSPKKIKNTIPlVISKIVMKLLEKDSEER 164
Cdd:cd06659   203 LGIMVIEMVDGEPPYFSDSPVQAMKRLRDSPPPKLKNAHKISP-VLRDFLERMLTREPQER 262
STKc_GRK4 cd05631
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; ...
31-125 1.66e-05

Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; Serine/Threonine Kinases (STKs), G protein-coupled Receptor Kinase (GRK) subfamily, GRK4 isoform, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The GRK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. 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. There are seven types of GRKs, named GRK1 to GRK7. 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. It 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.


Pssm-ID: 173720 [Multi-domain]  Cd Length: 285  Bit Score: 47.29  E-value: 1.66e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927   31 ALKIVDAVSEVHKEGMIYKYLNPKNIILDINGQLKLMESTFMC--------RDINYNLRYMAPEQIGriKKNVDFSTDHY 102
Cdd:cd05631   108 AAELCCGLEDLQRERIVYRDLKPENILLDDRGHIRISDLGLAVqipegetvRGRVGTVGYMAPEVIN--NEKYTFSPDWW 185
                          90       100       110
                  ....*....|....*....|....*....|...
gi 118443927  103 SLGVIFYRMLTGKLPI----------EVDDEIK 125
Cdd:cd05631   186 GLGCLIYEMIQGQSPFrkrkervkreEVDRRVK 218
STKc_PKB_beta cd05595
Catalytic domain of the Protein Serine/Threonine Kinase, Protein Kinase B beta; Serine ...
33-126 2.69e-05

Catalytic domain of the Protein Serine/Threonine Kinase, Protein Kinase B beta; Serine/Threonine Kinases (STKs), Protein Kinase B (PKB) or Akt subfamily, beta (or Akt2) isoform, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PKB subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. 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. 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.


Pssm-ID: 173686 [Multi-domain]  Cd Length: 323  Bit Score: 46.92  E-value: 2.69e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927   33 KIVDAVSEVHKEGMIYKYLNPKNIILDINGQLKLMESTfMCRDINYN----------LRYMAPEqigrIKKNVDF--STD 100
Cdd:cd05595   103 EIVSALEYLHSRDVVYRDIKLENLMLDKDGHIKITDFG-LCKEGISDgatmktfcgtPEYLAPE----VLEDNDYgrAVD 177
                          90       100
                  ....*....|....*....|....*.
gi 118443927  101 HYSLGVIFYRMLTGKLPIEVDDEIKL 126
Cdd:cd05595   178 WWGLGVVMYEMMCGRLPFYNQDHERL 203
STKc_GRK1 cd05608
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; ...
33-164 2.69e-05

Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; Serine/Threonine Kinases (STKs), G protein-coupled Receptor Kinase (GRK) subfamily, GRK1 isoform, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The GRK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. 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. There are seven types of GRKs, named GRK1 to GRK7. 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.


Pssm-ID: 173699 [Multi-domain]  Cd Length: 280  Bit Score: 46.38  E-value: 2.69e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927   33 KIVDAVSEVHKEGMIYKYLNPKNIILDINGQLK---------LMESTFMCRDINYNLRYMAPEQIgrIKKNVDFSTDHYS 103
Cdd:cd05608   105 QIISGLEHLHQRRIIYRDLKPENVLLDNDGNVRisdlglaveLKDGQSKTKGYAGTPGFMAPELL--QGEEYDFSVDYFA 182
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 118443927  104 LGVIFYRMLTGKLPIEVDDEIKLSYCNTNKKPVSPKKIKNTIPLVISKIVMKLLEKDSEER 164
Cdd:cd05608   183 LGVTLYEMIAARGPFRARGEKVENKELKQRILNDSVTYPDKFSPASKSFCEALLAKDPEKR 243
STKc_MAPKKK cd06606
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein Kinase ...
34-117 4.29e-05

Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase Kinase; Serine/threonine kinases (STKs), mitogen-activated protein kinase (MAPK) kinase kinase (MAPKKK) subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The MAPKKK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. 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.


Pssm-ID: 173724 [Multi-domain]  Cd Length: 260  Bit Score: 45.63  E-value: 4.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927   34 IVDAVSEVHKEGMIYKYLNPKNIILDINGQLKL-----------MESTFMCRDINYNLRYMAPEQIGRikKNVDFSTDHY 102
Cdd:cd06606   110 ILEGLAYLHSNGIVHRDIKGANILVDSDGVVKLadfgcakrlgdIETGEGTGSVRGTPYWMAPEVIRG--EEYGRAADIW 187
                          90
                  ....*....|....*
gi 118443927  103 SLGVIFYRMLTGKLP 117
Cdd:cd06606   188 SLGCTVIEMATGKPP 202
PKc_MAPKK_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity MAP kinase kinases; Protein kinases (PKs) ...
4-164 6.05e-05

Catalytic domain of fungal Byr1-like dual-specificity MAP kinase kinases; Protein kinases (PKs), MAP kinase kinase (MAPKK) subfamily, fungal Byr1-like proteins, catalytic (c) domain. PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. The MAPKK 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. The mitogen-activated protein (MAP) kinase signaling pathways are important mediators of cellular responses to extracellular signals. The pathways involve a triple kinase core cascade comprising of the MAP kinase (MAPK), which is phosphorylated and activated by a MAPK kinase (MAPKK or MKK), which itself is phosphorylated and activated by a MAPK kinase kinase (MAPKKK or MKKK). 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 MAPKKK 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.


Pssm-ID: 132951 [Multi-domain]  Cd Length: 284  Bit Score: 45.56  E-value: 6.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927    4 YKKKGEVIL-EEFI-CNKKDMSIKEFLKNALKIVDAVSEVHKEGMIYKY---------LNPKNIILDINGQLKL------ 66
Cdd:cd06620    72 FLNENNICMcMEFMdCGSLDRIYKKGGPIPVEILGKIAVAVVEGLTYLYnvhrimhrdIKPSNILVNSRGQIKLcdfgvs 151
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927   67 ------MESTFMCRDInynlrYMAPEQIGRIKKNVdfSTDHYSLGVIFYRMLTGKLPI---EVDDE--------IKLSYC 129
Cdd:cd06620   152 gelinsIADTFVGTST-----YMSPERIQGGKYTV--KSDVWSLGISIIELALGKFPFafsNIDDDgqddpmgiLDLLQQ 224
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 118443927  130 NTNKKPvsPKKIKNTIPLVISKIVMKLLEKDSEER 164
Cdd:cd06620   225 IVQEPP--PRLPSSDFPEDLRDFVDACLLKDPTER 257
STKc_ROCK cd05596
Catalytic domain of the Protein Serine/Threonine Kinase, Rho-associated coiled-coil containing ...
33-117 7.32e-05

Catalytic domain of the Protein Serine/Threonine Kinase, Rho-associated coiled-coil containing protein kinase; Serine/Threonine Kinases (STKs), Rho-associated coiled-coil containing protein kinase (ROCK) subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The ROCK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. 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.


Pssm-ID: 173687 [Multi-domain]  Cd Length: 370  Bit Score: 45.54  E-value: 7.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927   33 KIVDAVSEVHKEGMIYKYLNPKNIILDINGQLKL--------MESTFMCRDINY--NLRYMAPEQIGRIKKNVDF--STD 100
Cdd:cd05596   150 EVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLadfgtcmkMDANGMVRCDTAvgTPDYISPEVLKSQGGDGYYgrECD 229
                          90
                  ....*....|....*..
gi 118443927  101 HYSLGVIFYRMLTGKLP 117
Cdd:cd05596   230 WWSVGVFLYEMLVGDTP 246
PKc_MKK7 cd06618
Catalytic domain of the dual-specificity Protein Kinase, MAP kinase kinase 7; Protein kinases ...
35-166 1.84e-04

Catalytic domain of the dual-specificity Protein Kinase, MAP kinase kinase 7; Protein kinases (PKs), MAP kinase kinase 7 (MKK7) subfamily, catalytic (c) domain. PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. The MKK7 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. The mitogen-activated protein (MAP) kinase signaling pathways are important mediators of cellular responses to extracellular signals. The pathways involve a triple kinase core cascade comprising the MAP kinase (MAPK), which is phosphorylated and activated by a MAPK kinase (MAPKK or MKK), which itself is phosphorylated and activated by a MAPK kinase kinase (MAPKKK or MKKK). 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 (not included in this subfamily) 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.


Pssm-ID: 132949 [Multi-domain]  Cd Length: 296  Bit Score: 43.90  E-value: 1.84e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927   35 VDAVSEVH----KEGMIYKYLNPKNIILDINGQLKLMESTFMCRDINYNLR--------YMAPEQIG--RIKKNVDFSTD 100
Cdd:cd06618   121 VAIVKALHylkeKHGVIHRDVKPSNILLDASGNVKLCDFGISGRLVDSKAKtrsagcaaYMAPERIDppDPNPKYDIRAD 200
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 118443927  101 HYSLGVIFYRMLTGKLPIEVddeiklsyCNT---------NKKPVSPKKIKNTIPLVISkIVMKLLEKDSEERYK 166
Cdd:cd06618   201 VWSLGISLVELATGQFPYKN--------CKTefevltkilQEEPPSLPPNEGFSPDFCS-FVDLCLTKDHRKRPK 266
PKc_MKK4 cd06616
Catalytic domain of the dual-specificity Protein Kinase, MAP kinase kinase 4; Protein kinases ...
26-166 2.41e-04

Catalytic domain of the dual-specificity Protein Kinase, MAP kinase kinase 4; Protein kinases (PKs), MAP kinase kinase 4 (MKK4) subfamily, catalytic (c) domain. PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. The MKK4 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. The mitogen-activated protein (MAP) kinase signaling pathways are important mediators of cellular responses to extracellular signals. The pathways involve a triple kinase core cascade comprising of the MAP kinase (MAPK), which is phosphorylated and activated by a MAPK kinase (MAPKK or MKK), which itself is phosphorylated and activated by a MAPK kinase kinase (MAPKKK or MKKK). 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.


Pssm-ID: 132947 [Multi-domain]  Cd Length: 288  Bit Score: 43.51  E-value: 2.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927   26 EFLKNALKIvdavsevhkegmIYKYLNPKNIILDINGQLK---------LMESTFMCRDINYNlRYMAPEQIG-RIKKNV 95
Cdd:cd06616   121 NYLKEELKI------------IHRDVKPSNILLDRNGNIKlcdfgisgqLVDSIAKTRDAGCR-PYMAPERIDpSARDGY 187
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 118443927   96 DFSTDHYSLGVIFYRMLTGKLPIEVDDEIKLSYCNTNKKPvsPKKIKNTIPLVIS----KIVMKLLEKDSEERYK 166
Cdd:cd06616   188 DVRSDVWSLGITLYEVATGKFPYPKWNSVFDQLTQVVKGD--PPILSNSEEREFSpsfvNFINLCLIKDESKRPK 260
STKc_CNK2-like cd08530
Catalytic domain of the Protein Serine/Threonine Kinase, Chlamydomonas reinhardtii CNK2, and ...
31-164 3.18e-04

Catalytic domain of the Protein Serine/Threonine Kinase, Chlamydomonas reinhardtii CNK2, and similar domains; Serine/Threonine Kinases (STKs), Chlamydomonas reinhardtii Never In Mitosis gene A (NIMA)-related kinase 1 (CNK2)-like subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Chlamydomonas reinhardtii CNK2-like subfamily belongs to the (NIMA)-related kinase (Nek) family. The Nek family 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 protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. 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.


Pssm-ID: 173772 [Multi-domain]  Cd Length: 256  Bit Score: 43.20  E-value: 3.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927   31 ALKIVDAVSEVHKEGMIYKYLNPKNIILDINGQLKL--------MESTFMCRDINYNLrYMAPEqigrIKKN--VDFSTD 100
Cdd:cd08530   109 FIQLLRGLQALHEQKILHRDLKSANILLVANDLVKIgdlgiskvLKKNMAKTQIGTPH-YMAPE----VWKGrpYSYKSD 183
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 118443927  101 HYSLGVIFYRMLTGKLPIEVDDEIKLSY--CNTNKKPVSPKKIKNtiplvISKIVMKLLEKDSEER 164
Cdd:cd08530   184 IWSLGCLLYEMATFAPPFEARSMQDLRYkvQRGKYPPIPPIYSQD-----LQNFIRSMLQVKPKLR 244
STKc_PKB_gamma cd05593
Catalytic domain of the Protein Serine/Threonine Kinase, Protein Kinase B gamma; Serine ...
33-126 3.23e-04

Catalytic domain of the Protein Serine/Threonine Kinase, Protein Kinase B gamma; Serine/Threonine Kinases (STKs), Protein Kinase B (PKB) or Akt subfamily, gamma (or Akt3) isoform, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PKB subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. 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. 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.


Pssm-ID: 173684 [Multi-domain]  Cd Length: 328  Bit Score: 43.52  E-value: 3.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927   33 KIVDAVSEVHKEGMIYKYLNPKNIILDINGQLKLMESTfMCRDINYNL----------RYMAPEqigrIKKNVDF--STD 100
Cdd:cd05593   103 EIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFG-LCKEGITDAatmktfcgtpEYLAPE----VLEDNDYgrAVD 177
                          90       100
                  ....*....|....*....|....*.
gi 118443927  101 HYSLGVIFYRMLTGKLPIEVDDEIKL 126
Cdd:cd05593   178 WWGLGVVMYEMMCGRLPFYNQDHEKL 203
STKc_GRK7 cd05607
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; ...
33-130 3.43e-04

Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; Serine/Threonine Kinases (STKs), G protein-coupled Receptor Kinase (GRK) subfamily, GRK7 isoform, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The GRK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. 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. There are seven types of GRKs, named GRK1 to GRK7. 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.


Pssm-ID: 173698 [Multi-domain]  Cd Length: 277  Bit Score: 43.01  E-value: 3.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927   33 KIVDAVSEVHKEGMIYKYLNPKNIILDINGQLKLM---------ESTFMCRDINYNlRYMAPEQIgrIKKNVDFSTDHYS 103
Cdd:cd05607   103 QITCGILHLHSMDIVYRDMKPENVLLDDQGNCRLSdlglavelkDGKTITQRAGTN-GYMAPEIL--KEEPYSYPVDWFA 179
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 118443927  104 LGVIFYRMLTGKLPIE---------------VDDEIKLSYCN 130
Cdd:cd05607   180 MGCSIYEMVAGRTPFKdhkekvakeelkrrtLEDEVKFEHQN 221
STKc_MEKK1_plant cd06632
Catalytic domain of the Protein Serine/Threonine Kinase, Plant MAP/ERK kinase kinase 1; Serine ...
33-164 4.04e-04

Catalytic domain of the Protein Serine/Threonine Kinase, Plant MAP/ERK kinase kinase 1; Serine/threonine kinases (STKs), plant MAP/ERK kinase kinase 1 (MEKK1)-like subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The plant MEKK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. This subfamily is composed of plant mitogen-activated protein kinase (MAPK) kinase kinases (MAPKKKs or MKKKs or MAP3Ks) including Arabidopsis thaliana MEKK1 and MAPKKK3. MEKK1 is a MAPKKK that 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. 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.


Pssm-ID: 132963 [Multi-domain]  Cd Length: 258  Bit Score: 42.79  E-value: 4.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927   33 KIVDAVSEVHKEGMIYKYLNPKNIILDINGQLKL---------MESTFM--CRDINYnlrYMAPEQIGRiKKNVDFSTDH 101
Cdd:cd06632   110 QILLGLEYLHDRNTVHRDIKGANILVDTNGVVKLadfgmakqvVEFSFAksFKGSPY---WMAPEVIAQ-QGGYGLAADI 185
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 118443927  102 YSLGVIFYRMLTGKLPIEVDDEIKLSYcNTNKKPVSPkKIKNTIPLVISKIVMKLLEKDSEER 164
Cdd:cd06632   186 WSLGCTVLEMATGKPPWSQLEGVAAVF-KIGRSKELP-PIPDHLSDEAKDFILKCLQRDPSLR 246
STKc_GRK3 cd05633
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; ...
23-117 5.07e-04

Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; Serine/Threonine Kinases (STKs), G protein-coupled Receptor Kinase (GRK) subfamily, GRK3 isoform, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The GRK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. 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. There are seven types of GRKs, named GRK1 to GRK7. GRK3 (also known as beta-adrenergic receptor kinase 2) is widely expressed in many tissues. GRK3-deficient mice show a lack of olfactory receptor desensitization and altered regulation of the M2 muscarinic airway. GRK3 is involved in modulating the cholinergic response of airway smooth muscles. It also plays a role in dopamine receptor regulation. GRK3 promoter polymorphisms may be associated with bipolar disorder.


Pssm-ID: 173722 [Multi-domain]  Cd Length: 279  Bit Score: 42.68  E-value: 5.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927   23 SIKEFLKNALKIVDAVSEVHKEGMIYKYLNPKNIILDINGQLKLMESTFMCrdiNYNLR----------YMAPEQIGRiK 92
Cdd:cd05633    95 SEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHVRISDLGLAC---DFSKKkphasvgthgYMAPEVLQK-G 170
                          90       100
                  ....*....|....*....|....*
gi 118443927   93 KNVDFSTDHYSLGVIFYRMLTGKLP 117
Cdd:cd05633   171 TAYDSSADWFSLGCMLFKLLRGHSP 195
PKc_MAPKK_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity MAP kinase kinases; Protein kinases (PKs) ...
19-164 5.63e-04

Catalytic domain of fungal Pek1-like dual-specificity MAP kinase kinases; Protein kinases (PKs), MAP kinase kinase(MAPKK) subfamily, fungal Pek1-like proteins, catalytic (c) domain. PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. The MAPKK 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. The mitogen-activated protein (MAP) kinase signaling pathways are important mediators of cellular responses to extracellular signals. The pathways involve a triple kinase core cascade comprising of the MAP kinase (MAPK), which is phosphorylated and activated by a MAPK kinase (MAPKK or MKK), which itself is phosphorylated and activated by a MAPK kinase kinase (MAPKKK or MKKK). 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 the MAPK Pmk1/Spm1 and is regulated by the MAPKKK Mkh1. In baker's yeast, the pathway involves the MAPK Slt2, the MAPKKs MKK1 and MKK2, and the MAPKKK Bck1. The cell integrity MAPK cascade is activated by multiple stress conditions, and is essential in cell wall construction, morphogenesis, cytokinesis, and ion homeostasis.


Pssm-ID: 132952 [Multi-domain]  Cd Length: 287  Bit Score: 42.41  E-value: 5.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927   19 KKDMSIKEflKNALKIVDAV----SEVHKEGMIYKYLNPKNIILDINGQLKL------------MESTFMcrDINYnlrY 82
Cdd:cd06621    97 KRGGRIGE--KVLGKIAESVlkglSYLHSRKIIHRDIKPSNILLTRKGQVKLcdfgvsgelvnsLAGTFT--GTSF---Y 169
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927   83 MAPEqigRIK-KNVDFSTDHYSLGVIFYRMLTGKLPIEVDDEIK------LSYCNTNKKPVSPKKIKNTIPLV--ISKIV 153
Cdd:cd06621   170 MAPE---RIQgKPYSITSDVWSLGLTLLEVAQNRFPFPPEGEPPlgpielLSYIVNMPNPELKDEPGNGIKWSeeFKDFI 246
                         170
                  ....*....|.
gi 118443927  154 MKLLEKDSEER 164
Cdd:cd06621   247 KQCLEKDPTRR 257
STKc_PAK4 cd06657
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 4; Serine ...
32-164 5.69e-04

Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 4; Serine/threonine kinases (STKs), p21-activated kinase (PAK) 4, 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. PAK4 belongs to group II. Group II PAKs contain a PBD (p21-binding domain) and a C-terminal catalytic domain, but do not harbor an AID (autoinhibitory domain) or SH3 binding sites. 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.


Pssm-ID: 132988 [Multi-domain]  Cd Length: 292  Bit Score: 42.32  E-value: 5.69e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927   32 LKIVDAVSEVHKEGMIYKYLNPKNIILDINGQLKLMESTFmCRDINYNLR----------YMAPEQIGRIKKNVDfsTDH 101
Cdd:cd06657   123 LAVLKALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGF-CAQVSKEVPrrkslvgtpyWMAPELISRLPYGPE--VDI 199
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 118443927  102 YSLGVIFYRMLTGKLPIEVDDEIKLSYCNTNKKPVSPKKIKNTIPLvISKIVMKLLEKDSEER 164
Cdd:cd06657   200 WSLGIMVIEMVDGEPPYFNEPPLKAMKMIRDNLPPKLKNLHKVSPS-LKGFLDRLLVRDPAQR 261
STKc_GRK4_like cd05605
Catalytic domain of G protein-coupled Receptor Kinase 4-like Protein Serine/Threonine Kinases; ...
31-117 7.18e-04

Catalytic domain of G protein-coupled Receptor Kinase 4-like Protein Serine/Threonine Kinases; Serine/Threonine Kinases (STKs), G protein-coupled Receptor Kinase (GRK) subfamily, GRK4-like group, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The GRK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. 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. There are seven types of GRKs, named GRK1 to GRK7. Members of the GRK4-like group include GRK4, GRK5, GRK6, and similar GRKs. GRKs in this group 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.


Pssm-ID: 173696 [Multi-domain]  Cd Length: 285  Bit Score: 42.12  E-value: 7.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927   31 ALKIVDAVSEVHKEGMIYKYLNPKNIILDINGQLKLMESTFMCRDINYNL--------RYMAPEqigrIKKN--VDFSTD 100
Cdd:cd05605   108 AAEITCGLEDLHRERIVYRDLKPENILLDDYGHIRISDLGLAVEIPEGETirgrvgtvGYMAPE----VVKNerYTFSPD 183
                          90
                  ....*....|....*..
gi 118443927  101 HYSLGVIFYRMLTGKLP 117
Cdd:cd05605   184 WWGLGCLIYEMIEGKSP 200
STKc_PAK5 cd06658
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 5; Serine ...
32-117 8.50e-04

Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 5; Serine/threonine kinases (STKs), p21-activated kinase (PAK) 5, 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. PAK5 belongs to group II. Group II PAKs contain a PBD (p21-binding domain) and a C-terminal catalytic domain, but do not harbor an AID (autoinhibitory domain) or SH3 binding sites. 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.


Pssm-ID: 132989 [Multi-domain]  Cd Length: 292  Bit Score: 41.95  E-value: 8.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927   32 LKIVDAVSEVHKEGMIYKYLNPKNIILDINGQLKLMESTFmCRDINYNL----------RYMAPEQIGRIKKNVDfsTDH 101
Cdd:cd06658   125 LSVLRALSYLHNQGVIHRDIKSDSILLTSDGRIKLSDFGF-CAQVSKEVpkrkslvgtpYWMAPEVISRLPYGTE--VDI 201
                          90
                  ....*....|....*.
gi 118443927  102 YSLGVIFYRMLTGKLP 117
Cdd:cd06658   202 WSLGIMVIEMIDGEPP 217
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
29-118 1.12e-03

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase Kinase; Protein kinases (PKs), MAP kinase kinase (MAPKK) subfamily, catalytic (c) domain. PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. The MAPKK 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. The mitogen-activated protein (MAP) kinase signaling pathways are important mediators of cellular responses to extracellular signals. The pathways involve a triple kinase core cascade comprising the MAP kinase (MAPK), which is phosphorylated and activated by a MAPK kinase (MAPKK or MKK or MAP2K), which itself is phosphorylated and activated by a MAPK kinase kinase (MAPKKK or MKKK or MAP3K). MAPKKs are dual-specificity PKs that phosphorylate their downstream targets, MAPKs, at specific threonine and tyrosine residues. 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.


Pssm-ID: 173723 [Multi-domain]  Cd Length: 265  Bit Score: 41.53  E-value: 1.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927   29 KNALKIVDAVSEVH-KEGMIYKYLNPKNIILDINGQLKLME---STFMCRDINYNL----RYMAPEqigRIKKNV-DFST 99
Cdd:cd06605   104 KIAVAVLKGLTYLHeKHKIIHRDVKPSNILVNSRGQIKLCDfgvSGQLVNSLAKTFvgtsSYMAPE---RIQGNDySVKS 180
                          90
                  ....*....|....*....
gi 118443927  100 DHYSLGVIFYRMLTGKLPI 118
Cdd:cd06605   181 DIWSLGLSLIELATGRFPY 199
STKc_MAPKKK_Bck1_like cd06629
Catalytic domain of fungal Bck1-like MAP Kinase Kinase Kinases; Serine/threonine kinases (STKs) ...
24-164 1.21e-03

Catalytic domain of fungal Bck1-like MAP Kinase Kinase Kinases; Serine/threonine kinases (STKs), mitogen-activated protein kinase (MAPK) kinase kinase (MAPKKK) subfamily, fungal Bck1-like proteins, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The MAPKKK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. Members of this group include the MAPKKKs Saccharomyces cerevisiae Bck1 and Schizosaccharomyces pombe Mkh1, and related proteins. 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. 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.


Pssm-ID: 132960 [Multi-domain]  Cd Length: 272  Bit Score: 41.32  E-value: 1.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927   24 IKEFLKNALKivdAVSEVHKEGMIYKYLNPKNIILDINGQLKLmeSTF---------MCRDINYNLR----YMAPEQIGR 90
Cdd:cd06629   110 VRFFTEQVLE---GLAYLHSKGILHRDLKADNLLVDADGICKI--SDFgiskksddiYDNDQNMSMQgsvfWMAPEVIHS 184
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 118443927   91 IKKNVDFSTDHYSLGVIFYRMLTGKLPIEVDDEIKLSYCNTNKKPVSPkkIKNTIPLVISKIVMKLL----EKDSEER 164
Cdd:cd06629   185 YSQGYSAKVDIWSLGCVVLEMFAGRRPWSDEEAIAAMFKLGNKRSAPP--IPPDVSMNLSPVALDFLnacfTINPDNR 260
STKc_PAK_I cd06647
Catalytic domain of the Protein Serine/Threonine Kinase, Group I p21-activated kinase; Serine ...
33-182 1.44e-03

Catalytic domain of the Protein Serine/Threonine Kinase, Group I p21-activated kinase; Serine/threonine kinases (STKs), p21-activated kinase (PAK) subfamily, Group I, 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 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. PAKs from higher eukaryotes are classified into two groups (I and II), according to their biochemical and structural features. 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.


Pssm-ID: 132978 [Multi-domain]  Cd Length: 293  Bit Score: 41.04  E-value: 1.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927   33 KIVDAVSEVHKEGMIYKYLNPKNIILDINGQLKLMESTFmCRDINYNLR----------YMAPEQIGRikKNVDFSTDHY 102
Cdd:cd06647   123 ECLQALEFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGF-CAQITPEQSkrstmvgtpyWMAPEVVTR--KAYGPKVDIW 199
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927  103 SLGVIFYRMLTGKLPIEVDDEIKLSY-CNTNKKPVSPKKIKNTipLVISKIVMKLLEKDSEERYKSIYGIKVDLNKCYKS 181
Cdd:cd06647   200 SLGIMAIEMVEGEPPYLNENPLRALYlIATNGTPELQNPEKLS--AIFRDFLNRCLEMDVEKRGSAKELLQHPFLKLAKP 277

                  .
gi 118443927  182 L 182
Cdd:cd06647   278 L 278
STKc_phototropin_like cd05574
Catalytic domain of Phototropin-like Protein Serine/Threonine Kinases; Serine/Threonine ...
31-172 1.63e-03

Catalytic domain of Phototropin-like Protein Serine/Threonine Kinases; Serine/Threonine Kinases (STKs), Phototropin-like subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The phototropin-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. Included in this subfamily are plant phototropins and predominantly uncharacterized fungal STKs whose catalytic domains resemble the phototropin kinase domain. One protein from Neurospora crassa is called nrc-2. 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. Neurospora crassa nrc-2 plays a role in growth and development by controlling entry into the conidiation program.


Pssm-ID: 173665 [Multi-domain]  Cd Length: 316  Bit Score: 41.11  E-value: 1.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927   31 ALKIVDAVSEVHKEGMIYKYLNPKNIILDINGQLklMESTFmcrDINYNL------------------------------ 80
Cdd:cd05574   109 AAEVLLALEYLHLLGIVYRDLKPENILLHESGHI--MLSDF---DLSKQSdvepppvskalrkgsrrssvnsipsetfse 183
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927   81 -------------RYMAPEQI---GRikknvDFSTDHYSLGVIFYRMLTGKLPIEVDDeIKLSYCNTNKKPVS-PKKIkn 143
Cdd:cd05574   184 epsfrsnsfvgteEYIAPEVIsgdGH-----GSAVDWWTLGILLYEMLYGTTPFKGSN-RDETFSNILKKEVTfPGSP-- 255
                         170       180       190
                  ....*....|....*....|....*....|..
gi 118443927  144 TIPLVISKIVMKLLEKDSEERYKSIYG---IK 172
Cdd:cd05574   256 PVSSSARDLIRKLLVKDPSKRLGSKRGaaeIK 287
STKc_MRCK_alpha cd05623
Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control ...
33-117 1.65e-03

Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control protein 42 binding kinase alpha; Serine/Threonine Kinases (STKs), DMPK-like subfamily, DMPK-related cell division control protein 42 (Cdc42) binding kinase (MRCK) alpha isoform, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The DMPK-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. MRCK is activated via interaction with the small GTPase Cdc42. MRCK/Cdc42 signaling mediates myosin-dependent cell motility. MRCKalpha 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.


Pssm-ID: 88524 [Multi-domain]  Cd Length: 332  Bit Score: 41.20  E-value: 1.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927   33 KIVDAVSEVHKEGMIYKYLNPKNIILDINGQ---------LKLMESTFMCRDINYNL-RYMAPEQIGRI---KKNVDFST 99
Cdd:cd05623   110 EMVIAIDSVHQLHYVHRDIKPDNILMDMNGHirladfgscLKLMEDGTVQSSVAVGTpDYISPEILQAMedgKGKYGPEC 189
                          90
                  ....*....|....*...
gi 118443927  100 DHYSLGVIFYRMLTGKLP 117
Cdd:cd05623   190 DWWSLGVCMYEMLYGETP 207
STKc_Nek6 cd08228
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A-related ...
1-130 1.90e-03

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A-related kinase 6; Serine/Threonine Kinases (STKs), Never In Mitosis gene A (NIMA)-related kinase 6 (Nek6) subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Nek6 subfamily is one 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 protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. 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.


Pssm-ID: 173768 [Multi-domain]  Cd Length: 267  Bit Score: 40.78  E-value: 1.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927    1 MEYYKKKGEVILEEFIcnkkdmsikefLKNALKIVDAVSEVHKEGMIYKYLNPKNIILDINGQLKLME---------STF 71
Cdd:cd08228    93 IKYFKKQKRLIPERTV-----------WKYFVQLCSAVEHMHSRRVMHRDIKPANVFITATGVVKLGDlglgrffssKTT 161
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927   72 MCRDINYNLRYMAPEqigRIKKN-VDFSTDHYSLGVIFYRMLTGKLPIEVDDEIKLSYCN 130
Cdd:cd08228   162 AAHSLVGTPYYMSPE---RIHENgYNFKSDIWSLGCLLYEMAALQSPFYGDKMNLFSLCQ 218
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Protein Serine/Threonine Kinases; Serine/threonine ...
1-135 2.19e-03

Catalytic domain of Fungal Nak1-like Protein Serine/Threonine Kinases; Serine/threonine kinases (STKs), Nak1 subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Nak1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. This subfamily is composed of Schizosaccharomyces pombe Nak1, Saccharomyces cerevisiae Kic1p (kinase that interacts with Cdc31p) and related proteins. Nak1 (also known as 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.


Pssm-ID: 132991 [Multi-domain]  Cd Length: 277  Bit Score: 40.50  E-value: 2.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927    1 MEYYK-------KKGEVILEEFICnkkdMSIKEFLKnalkivdAVSEVHKEGMIYKYLNPKNIILDINGQLKLME----- 68
Cdd:cd06917    81 MEYAEggsvrtlMKAGPIAEKYIS----VIIREVLV-------ALKYIHKVGVIHRDIKAANILVTNTGNVKLCDfgvaa 149
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 118443927   69 ---------STFMcrDINYnlrYMAPEQIgRIKKNVDFSTDHYSLGVIFYRMLTGKLPIEVDDEIKLSYCNTNKKP 135
Cdd:cd06917   150 llnqnsskrSTFV--GTPY---WMAPEVI-TEGKYYDTKADIWSLGITIYEMATGNPPYSDVDAFRAMMLIPKSKP 219
STKc_MRCK_beta cd05624
Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control ...
33-117 3.65e-03

Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control protein 42 binding kinase beta; Serine/Threonine Kinases (STKs), DMPK-like subfamily, DMPK-related cell division control protein 42 (Cdc42) binding kinase (MRCK) beta isoform, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The DMPK-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. MRCK is activated via interaction with the small GTPase Cdc42. MRCK/Cdc42 signaling mediates myosin-dependent cell motility. MRCKbeta is expressed ubiquitously in many tissues.


Pssm-ID: 173713 [Multi-domain]  Cd Length: 331  Bit Score: 39.99  E-value: 3.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927   33 KIVDAVSEVHKEGMIYKYLNPKNIILDINGQLKLMESTfMCRDINYN-----------LRYMAPEQIGRIKKNVDF---S 98
Cdd:cd05624   110 EMVLAIHSIHQLHYVHRDIKPDNVLLDMNGHIRLADFG-SCLKMNQDgtvqssvavgtPDYISPEILQAMEDGMGKygpE 188
                          90
                  ....*....|....*....
gi 118443927   99 TDHYSLGVIFYRMLTGKLP 117
Cdd:cd05624   189 CDWWSLGVCMYEMLYGETP 207
STKc_ROCK2 cd05621
Catalytic domain of the Protein Serine/Threonine Kinase, Rho-associated coiled-coil containing ...
33-121 4.66e-03

Catalytic domain of the Protein Serine/Threonine Kinase, Rho-associated coiled-coil containing protein kinase 2; Serine/Threonine Kinases (STKs), ROCK subfamily, ROCK2 (or ROK-alpha) isoform, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The ROCK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. 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. 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.


Pssm-ID: 173711 [Multi-domain]  Cd Length: 370  Bit Score: 40.00  E-value: 4.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927   33 KIVDAVSEVHKEGMIYKYLNPKNIILDINGQLKL--------MESTFM--CRDINYNLRYMAPEQIGRIKKNVDF--STD 100
Cdd:cd05621   150 EVVLALDAIHSMGLIHRDVKPDNMLLDKHGHLKLadfgtcmkMDETGMvrCDTAVGTPDYISPEVLKSQGGDGYYgrECD 229
                          90       100
                  ....*....|....*....|.
gi 118443927  101 HYSLGVIFYRMLTGKLPIEVD 121
Cdd:cd05621   230 WWSVGVFLFEMLVGDTPFYAD 250
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A-related ...
33-164 5.03e-03

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A-related kinase 9; Serine/Threonine Kinases (STKs), Never In Mitosis gene A (NIMA)-related kinase 9 (Nek9) subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Nek9 subfamily is one 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 protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. 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.


Pssm-ID: 173761 [Multi-domain]  Cd Length: 256  Bit Score: 39.35  E-value: 5.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118443927   33 KIVDAVSEVHKEGMIYKYLNPKNIILDINGQLKL--------MESTF-MCRDINYNLRYMAPEQIGRIKKNvdFSTDHYS 103
Cdd:cd08221   109 QIVSAVSYIHKAGILHRDIKTLNIFLTKAGLIKLgdfgiskiLGSEYsMAETVVGTPYYMSPELCQGVKYN--FKSDIWA 186
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 118443927  104 LGVIFYRMLTGKLPIEVDDEIKL--SYCNTNKKPVSPKKIKNTIPLVISkivmkLLEKD