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Conserved domains on  [gi|189518151|ref|XP_689471|]
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ethanolamine kinase 1 isoform X1 [Danio rerio]

Protein Classification

ethanolamine kinase( domain architecture ID 10142388)

ethanolamine kinase catalyzes the transfer of the gamma-phosphoryl group from ATP to ethanolamine (Etn), the first step in the CDP-Etn pathway for the formation of the major phospholipid, phosphatidylethanolamine (PtdEtn)

CATH:  1.10.510.10
EC:  2.7.1.82
Gene Ontology:  GO:0004305|GO:0006646|GO:0005524
PubMed:  16244704

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ETNK_euk cd05157
Euykaryotic Ethanolamine kinase; ETNK catalyzes the transfer of the gamma-phosphoryl group ...
46-348 7.86e-144

Euykaryotic Ethanolamine kinase; ETNK catalyzes the transfer of the gamma-phosphoryl group from CTP to ethanolamine (Etn), the first step in the CDP-Etn pathway for the formation of the major phospholipid, phosphatidylethanolamine (PtdEtn). Unlike ChoK, ETNK shows specific activity for its substrate, and displays negligible activity towards N-methylated derivatives of Etn. The Drosophila ETNK is implicated in development and neuronal function. Mammals contain two ETNK proteins, ETNK1 and ETNK2. ETNK1 selectively increases Etn uptake and phosphorylation, as well as PtdEtn synthesis. ETNK2 is found primarily in the liver and reproductive tissues. It plays a critical role in regulating placental hemostasis to support late embryonic development. It may also have a role in testicular maturation. ETNK is part of a larger superfamily that includes the catalytic domains of other kinases, such as the typical serine/threonine/tyrosine protein kinases (PKs), RIO kinases, actin-fragmin kinase (AFK), and phosphoinositide 3-kinase (PI3K).


:

Pssm-ID: 270706 [Multi-domain]  Cd Length: 307  Bit Score: 409.28  E-value: 7.86e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189518151  46 VKMKTFTDGITNKLIGCYVGGSMQ-EVVLVRVYGNKTELFVDRENEVKSFRVLQAHRCAPRLYCTFNNGLCYEFLQGVAL 124
Cdd:cd05157    1 IKVKRITGGITNALYKVTYPSGDTpKTVLVRIYGPGTELLIDRDRELRILQLLSRAGIGPKLYGRFENGRVEEFLPGRTL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189518151 125 EPEHIRSPAIFRHIARQMAKYHAIHAHNGWV--PQSGLWLKMSKFFSLVPSHFEDPEMDQRlNNEVPSAACLRDEMIWLQ 202
Cdd:cd05157   81 TPEDLRDPKISRLIARRLAELHSIVPLGEIEgkKKPILWTTIRKWLDLAPEVFEDEKNKEK-KLEKVDLERLRKELEWLE 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189518151 203 QNLSKL-GSPVVLCHNDLLCKNIIYNQKEGNVKFIDYEYAGYNYQAFDIGNHFNEFAGLNEV-DYTLYPDRELQMQWLRA 280
Cdd:cd05157  160 KWLESLeKSPIVFCHNDLLYGNILYNEDDDSVTFIDFEYAGPNPRAFDIANHFCEWAGFYCVlDYSRYPTKEEQRNFLRA 239
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 189518151 281 YLEAYKEYKSQGSqVSNTEVELLYVQVNRFALASHFFWGLWALIQAQYSTIDFDFLGYAVLRFNQYFK 348
Cdd:cd05157  240 YLESLDGLPGGEE-VSEEEVEKLYNEVNLFRLASHLFWGLWALIQAAISSIDFDYLGYAKERLDEYWG 306
 
Name Accession Description Interval E-value
ETNK_euk cd05157
Euykaryotic Ethanolamine kinase; ETNK catalyzes the transfer of the gamma-phosphoryl group ...
46-348 7.86e-144

Euykaryotic Ethanolamine kinase; ETNK catalyzes the transfer of the gamma-phosphoryl group from CTP to ethanolamine (Etn), the first step in the CDP-Etn pathway for the formation of the major phospholipid, phosphatidylethanolamine (PtdEtn). Unlike ChoK, ETNK shows specific activity for its substrate, and displays negligible activity towards N-methylated derivatives of Etn. The Drosophila ETNK is implicated in development and neuronal function. Mammals contain two ETNK proteins, ETNK1 and ETNK2. ETNK1 selectively increases Etn uptake and phosphorylation, as well as PtdEtn synthesis. ETNK2 is found primarily in the liver and reproductive tissues. It plays a critical role in regulating placental hemostasis to support late embryonic development. It may also have a role in testicular maturation. ETNK is part of a larger superfamily that includes the catalytic domains of other kinases, such as the typical serine/threonine/tyrosine protein kinases (PKs), RIO kinases, actin-fragmin kinase (AFK), and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270706 [Multi-domain]  Cd Length: 307  Bit Score: 409.28  E-value: 7.86e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189518151  46 VKMKTFTDGITNKLIGCYVGGSMQ-EVVLVRVYGNKTELFVDRENEVKSFRVLQAHRCAPRLYCTFNNGLCYEFLQGVAL 124
Cdd:cd05157    1 IKVKRITGGITNALYKVTYPSGDTpKTVLVRIYGPGTELLIDRDRELRILQLLSRAGIGPKLYGRFENGRVEEFLPGRTL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189518151 125 EPEHIRSPAIFRHIARQMAKYHAIHAHNGWV--PQSGLWLKMSKFFSLVPSHFEDPEMDQRlNNEVPSAACLRDEMIWLQ 202
Cdd:cd05157   81 TPEDLRDPKISRLIARRLAELHSIVPLGEIEgkKKPILWTTIRKWLDLAPEVFEDEKNKEK-KLEKVDLERLRKELEWLE 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189518151 203 QNLSKL-GSPVVLCHNDLLCKNIIYNQKEGNVKFIDYEYAGYNYQAFDIGNHFNEFAGLNEV-DYTLYPDRELQMQWLRA 280
Cdd:cd05157  160 KWLESLeKSPIVFCHNDLLYGNILYNEDDDSVTFIDFEYAGPNPRAFDIANHFCEWAGFYCVlDYSRYPTKEEQRNFLRA 239
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 189518151 281 YLEAYKEYKSQGSqVSNTEVELLYVQVNRFALASHFFWGLWALIQAQYSTIDFDFLGYAVLRFNQYFK 348
Cdd:cd05157  240 YLESLDGLPGGEE-VSEEEVEKLYNEVNLFRLASHLFWGLWALIQAAISSIDFDYLGYAKERLDEYWG 306
PLN02421 PLN02421
phosphotransferase, alcohol group as acceptor/kinase
33-356 4.91e-84

phosphotransferase, alcohol group as acceptor/kinase


Pssm-ID: 215231 [Multi-domain]  Cd Length: 330  Bit Score: 258.13  E-value: 4.91e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189518151  33 LIKTLRPHWK---PSEVKMKTFTDGITNKLIGCYVGG--SMQEVVLVRVYGNKTELFVDRENEVKSFRVLQAHRCAPRLY 107
Cdd:PLN02421   1 VCKALFKGWSdldDSDFSVERISGGITNLLLKVSVKEenGNEVSVTVRLFGPNTDYVIDRERELQAIKYLSAAGFGAKLL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189518151 108 CTFNNGLCYEFLQGVALEPEHIRSPAIFRHIARQMAKYHAIHAHNGWVPQsgLWLKMSKFFSLVPS-HFEDPEMDQRLnn 186
Cdd:PLN02421  81 GVFGNGMIQSFINARTLTPSDMRKPKVAAEIAKELRRLHQVEIPGSKEPQ--LWNDIFKFYEKASTvKFEDPEKQKKY-- 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189518151 187 EVPSAACLRDEMIWLQQNLSKLGSPVVLCHNDLLCKNIIYNQKEGNVKFIDYEYAGYNYQAFDIGNHFNEFAGLnEVDYT 266
Cdd:PLN02421 157 ETISFEELRDEIVELKEITDSLKAPVVFAHNDLLSGNLMLNEDEGKLYFIDFEYGSYSYRGYDIGNHFNEYAGF-DCDYS 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189518151 267 LYPDRELQMQWLRAYLEAYKEYKsqgsqVSNTEVELLYVQVNRFALASHFFWGLWALIQAQYSTIDFDFLGYAVLRFNQY 346
Cdd:PLN02421 236 LYPSKEEQYHFFRHYLRPDDPEE-----VSDAELEELFVETNFYALASHLYWAIWAIVQAKMSPIDFDYLGYFFLRYKEY 310
                        330
                 ....*....|
gi 189518151 347 FKMKPEVMSL 356
Cdd:PLN02421 311 KRQKEKLLSL 320
Choline_kinase pfam01633
Choline/ethanolamine kinase; Choline kinase catalyzes the committed step in the synthesis of ...
69-272 6.67e-76

Choline/ethanolamine kinase; Choline kinase catalyzes the committed step in the synthesis of phosphatidylcholine by the CDP-choline pathway. This alignment covers the protein kinase portion of the protein. The divergence of this family makes it very difficult to create a model that specifically predicts choline/ethanolamine kinases only. However if [add Pfam ID here for Choline_kinase_C] is also present then it is definitely a member of this family.


Pssm-ID: 396278 [Multi-domain]  Cd Length: 211  Bit Score: 232.93  E-value: 6.67e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189518151   69 QEVVLVRVYGNKTELFVDRENEVKSFRVLQAHRCAPRLYCTFNNGLCYEFLQGVALEPEHIRSPAIFRHIARQMAKYHAI 148
Cdd:pfam01633   2 PRKVLLRIYGPGTELLINREDEIVNFALLSERGLGPKLYGFFPNGRIEEFIPSRTLSTEDLRDPEISKLIAKRLAELHSL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189518151  149 HAHngWVPQSGLWLKMSKFFSLVPSHFEDPEMDQRLNNEVPSAACLRDEMIWLQQNLSKLGSPVVLCHNDLLCKNIIYNQ 228
Cdd:pfam01633  82 EMP--GKKSPSLWKTMRKWLSLLKNLGAPESVNKSEQLKSINLEDLEKEINKLEKWLELLDSPIVFCHNDLQSGNILLLN 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 189518151  229 KEGNVKFIDYEYAGYNYQAFDIGNHFNEFAG-------LNEVDYTLYPDRE 272
Cdd:pfam01633 160 ETKRLVLIDFEYASYNYRGFDIANHFCEWAGdyhdptpFFKCDYSLYPTRE 210
CotS COG0510
Thiamine kinase or a related kinase [Coenzyme transport and metabolism];
194-344 4.55e-17

Thiamine kinase or a related kinase [Coenzyme transport and metabolism];


Pssm-ID: 440276 [Multi-domain]  Cd Length: 156  Bit Score: 77.51  E-value: 4.55e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189518151 194 LRDEMIWLQQNLSKLGSPVVLCHNDLLCKNIIYnQKEGNVKFIDYEYAGYNYQAFDIGNHFNEFAglnevdytlyPDREL 273
Cdd:COG0510   31 LLRRLEELERALAARPLPLVLCHGDLHPGNFLV-TDDGRLYLIDWEYAGLGDPAFDLAALLVEYG----------LSPEQ 99
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 189518151 274 QMQWLRAYLEAYKEyksqgsqvsntevELLYVQVNRFALASHFFWGLWALIQAQYSTiDFDFLGYAVLRFN 344
Cdd:COG0510  100 AEELLEAYGFGRPT-------------EELLRRLRAYRALADLLWALWALVRAAQEA-NGDLLKYLLRRLE 156
spore_CotS TIGR02906
spore coat protein, CotS family; Members of this family include the spore coat proteins CotS ...
106-320 1.77e-03

spore coat protein, CotS family; Members of this family include the spore coat proteins CotS and YtaA from Bacillus subtilis and, from other endospore-forming bacteria, homologs that are more closely related to these two than to the spore coat proteins YutH and YsxE. The CotS family is more broadly distributed than YutH or YsxE, but still is not universal among spore-formers. [Cellular processes, Sporulation and germination]


Pssm-ID: 131952 [Multi-domain]  Cd Length: 313  Bit Score: 39.96  E-value: 1.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189518151  106 LYCTFNNGL--CYEFLQGVALE---PEHIRSpaifrhIARQMAKYHaiHAHNGWVPQSGL--------WLK--------M 164
Cdd:TIGR02906  62 LYVKYNGDLyvLTEWIEGRECDfnnPIDLKK------AAKGLALFH--HASKGYVPPDGSkirsklgkWPKqfekrlkeL 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189518151  165 SKFFSLVPSHFEDPEMDQRLNNEVpsaaclrDEMI-----------------WLQQNLSKLGspvvLCHNDLLCKNIIYn 227
Cdd:TIGR02906 134 ERFKKIALEKKYKDEFDKLYLKEV-------DYFLergkkalellnkskyydLCKEAKKIRG----FCHQDYAYHNILL- 201
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189518151  228 qKEGNVKFIDYEYAGYNYQAFDIGNHfnefagLNEVDYTLYpdrELQMQWLRAYLEAYkeykSQGSQVSNTEVELLYVqv 307
Cdd:TIGR02906 202 -KDNEVYVIDFDYCTIDLPVRDLRKL------IIKLMKKNG---VWDLEKAKEIIEAY----SSINPLSKEEKEVLYI-- 265
                         250
                  ....*....|...
gi 189518151  308 nrFALASHFFWGL 320
Cdd:TIGR02906 266 --DLAFPHKFWKI 276
 
Name Accession Description Interval E-value
ETNK_euk cd05157
Euykaryotic Ethanolamine kinase; ETNK catalyzes the transfer of the gamma-phosphoryl group ...
46-348 7.86e-144

Euykaryotic Ethanolamine kinase; ETNK catalyzes the transfer of the gamma-phosphoryl group from CTP to ethanolamine (Etn), the first step in the CDP-Etn pathway for the formation of the major phospholipid, phosphatidylethanolamine (PtdEtn). Unlike ChoK, ETNK shows specific activity for its substrate, and displays negligible activity towards N-methylated derivatives of Etn. The Drosophila ETNK is implicated in development and neuronal function. Mammals contain two ETNK proteins, ETNK1 and ETNK2. ETNK1 selectively increases Etn uptake and phosphorylation, as well as PtdEtn synthesis. ETNK2 is found primarily in the liver and reproductive tissues. It plays a critical role in regulating placental hemostasis to support late embryonic development. It may also have a role in testicular maturation. ETNK is part of a larger superfamily that includes the catalytic domains of other kinases, such as the typical serine/threonine/tyrosine protein kinases (PKs), RIO kinases, actin-fragmin kinase (AFK), and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270706 [Multi-domain]  Cd Length: 307  Bit Score: 409.28  E-value: 7.86e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189518151  46 VKMKTFTDGITNKLIGCYVGGSMQ-EVVLVRVYGNKTELFVDRENEVKSFRVLQAHRCAPRLYCTFNNGLCYEFLQGVAL 124
Cdd:cd05157    1 IKVKRITGGITNALYKVTYPSGDTpKTVLVRIYGPGTELLIDRDRELRILQLLSRAGIGPKLYGRFENGRVEEFLPGRTL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189518151 125 EPEHIRSPAIFRHIARQMAKYHAIHAHNGWV--PQSGLWLKMSKFFSLVPSHFEDPEMDQRlNNEVPSAACLRDEMIWLQ 202
Cdd:cd05157   81 TPEDLRDPKISRLIARRLAELHSIVPLGEIEgkKKPILWTTIRKWLDLAPEVFEDEKNKEK-KLEKVDLERLRKELEWLE 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189518151 203 QNLSKL-GSPVVLCHNDLLCKNIIYNQKEGNVKFIDYEYAGYNYQAFDIGNHFNEFAGLNEV-DYTLYPDRELQMQWLRA 280
Cdd:cd05157  160 KWLESLeKSPIVFCHNDLLYGNILYNEDDDSVTFIDFEYAGPNPRAFDIANHFCEWAGFYCVlDYSRYPTKEEQRNFLRA 239
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 189518151 281 YLEAYKEYKSQGSqVSNTEVELLYVQVNRFALASHFFWGLWALIQAQYSTIDFDFLGYAVLRFNQYFK 348
Cdd:cd05157  240 YLESLDGLPGGEE-VSEEEVEKLYNEVNLFRLASHLFWGLWALIQAAISSIDFDYLGYAKERLDEYWG 306
PLN02421 PLN02421
phosphotransferase, alcohol group as acceptor/kinase
33-356 4.91e-84

phosphotransferase, alcohol group as acceptor/kinase


Pssm-ID: 215231 [Multi-domain]  Cd Length: 330  Bit Score: 258.13  E-value: 4.91e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189518151  33 LIKTLRPHWK---PSEVKMKTFTDGITNKLIGCYVGG--SMQEVVLVRVYGNKTELFVDRENEVKSFRVLQAHRCAPRLY 107
Cdd:PLN02421   1 VCKALFKGWSdldDSDFSVERISGGITNLLLKVSVKEenGNEVSVTVRLFGPNTDYVIDRERELQAIKYLSAAGFGAKLL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189518151 108 CTFNNGLCYEFLQGVALEPEHIRSPAIFRHIARQMAKYHAIHAHNGWVPQsgLWLKMSKFFSLVPS-HFEDPEMDQRLnn 186
Cdd:PLN02421  81 GVFGNGMIQSFINARTLTPSDMRKPKVAAEIAKELRRLHQVEIPGSKEPQ--LWNDIFKFYEKASTvKFEDPEKQKKY-- 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189518151 187 EVPSAACLRDEMIWLQQNLSKLGSPVVLCHNDLLCKNIIYNQKEGNVKFIDYEYAGYNYQAFDIGNHFNEFAGLnEVDYT 266
Cdd:PLN02421 157 ETISFEELRDEIVELKEITDSLKAPVVFAHNDLLSGNLMLNEDEGKLYFIDFEYGSYSYRGYDIGNHFNEYAGF-DCDYS 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189518151 267 LYPDRELQMQWLRAYLEAYKEYKsqgsqVSNTEVELLYVQVNRFALASHFFWGLWALIQAQYSTIDFDFLGYAVLRFNQY 346
Cdd:PLN02421 236 LYPSKEEQYHFFRHYLRPDDPEE-----VSDAELEELFVETNFYALASHLYWAIWAIVQAKMSPIDFDYLGYFFLRYKEY 310
                        330
                 ....*....|
gi 189518151 347 FKMKPEVMSL 356
Cdd:PLN02421 311 KRQKEKLLSL 320
Choline_kinase pfam01633
Choline/ethanolamine kinase; Choline kinase catalyzes the committed step in the synthesis of ...
69-272 6.67e-76

Choline/ethanolamine kinase; Choline kinase catalyzes the committed step in the synthesis of phosphatidylcholine by the CDP-choline pathway. This alignment covers the protein kinase portion of the protein. The divergence of this family makes it very difficult to create a model that specifically predicts choline/ethanolamine kinases only. However if [add Pfam ID here for Choline_kinase_C] is also present then it is definitely a member of this family.


Pssm-ID: 396278 [Multi-domain]  Cd Length: 211  Bit Score: 232.93  E-value: 6.67e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189518151   69 QEVVLVRVYGNKTELFVDRENEVKSFRVLQAHRCAPRLYCTFNNGLCYEFLQGVALEPEHIRSPAIFRHIARQMAKYHAI 148
Cdd:pfam01633   2 PRKVLLRIYGPGTELLINREDEIVNFALLSERGLGPKLYGFFPNGRIEEFIPSRTLSTEDLRDPEISKLIAKRLAELHSL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189518151  149 HAHngWVPQSGLWLKMSKFFSLVPSHFEDPEMDQRLNNEVPSAACLRDEMIWLQQNLSKLGSPVVLCHNDLLCKNIIYNQ 228
Cdd:pfam01633  82 EMP--GKKSPSLWKTMRKWLSLLKNLGAPESVNKSEQLKSINLEDLEKEINKLEKWLELLDSPIVFCHNDLQSGNILLLN 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 189518151  229 KEGNVKFIDYEYAGYNYQAFDIGNHFNEFAG-------LNEVDYTLYPDRE 272
Cdd:pfam01633 160 ETKRLVLIDFEYASYNYRGFDIANHFCEWAGdyhdptpFFKCDYSLYPTRE 210
ChoK_euk cd05156
Euykaryotic Choline Kinase; ChoK catalyzes the transfer of the gamma-phosphoryl group from ATP ...
46-351 1.14e-66

Euykaryotic Choline Kinase; ChoK catalyzes the transfer of the gamma-phosphoryl group from ATP (or CTP) to its substrate, choline, producing phosphorylcholine (PCho), a precursor to the biosynthesis of two major membrane phospholipids, phosphatidylcholine (PC) and sphingomyelin (SM). Although choline is the preferred substrate, ChoK also shows substantial activity towards ethanolamine and its N-methylated derivatives. ChoK plays an important role in cell signaling pathways and the regulation of cell growth. Along with PCho, it is involved in malignant transformation through Ras oncogenes in various human cancers such as breast, lung, colon, prostate, neuroblastoma, and hepatic lymphoma. In mammalian cells, there are three ChoK isoforms (A-1, A-2, and B) which are active in homo- or heterodimeric forms. The ChoK subfamily is part of a larger superfamily that includes the catalytic domains of other kinases, such as the typical serine/threonine/tyrosine protein kinases (PKs), RIO kinases, actin-fragmin kinase (AFK), and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270705 [Multi-domain]  Cd Length: 326  Bit Score: 213.26  E-value: 1.14e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189518151  46 VKMKTFTDGITNKLIGC------YVGGSMQEVVLVRVYGNKTELFVDRENEVKSFRVLQAHRCAPRLYCTFNNGLCYEFL 119
Cdd:cd05156    1 FGIKTITGGLSNLLYLCslpdgvVPVGGEPRKVLLRIYGQILQAEESLVTESVIFALLSERGLGPKLYGIFPGGRLEEFI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189518151 120 QGVALEPEHIRSPAIFRHIARQMAKYHAIHahngwVPQS----GLWLKMSKFFSLVPSH-FEDPEMDQRLNNEVPSAACL 194
Cdd:cd05156   81 PSRPLTTDELSLPEISRKIARKMARFHSLE-----MPISkepkWLFDTMERWLKEALSIlFTDEPTKPSKQLELLLSYDL 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189518151 195 RDEMIWLQQNLSKLGSPVVLCHNDLLCKNII-----YNQKEGNVKFIDYEYAGYNYQAFDIGNHFNEFAglneVDYT--- 266
Cdd:cd05156  156 AKELGWLRSLLESTPSPVVFCHNDLQEGNILllngpENSEDDKLVLIDFEYCSYNYRGFDLANHFCEWA----YDYTvpe 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189518151 267 ---------LYPDRELQMQWLRAYLEAYKEYKSQGSQvSNTEVEL--LYVQVNRFALASHFFWGLWALIQAQYSTIDFDF 335
Cdd:cd05156  232 ppyfkinpeNYPTREQQLHFIRAYLDEQYKDKTNDLT-EERSKEEekLLLEVNRFALASHFFWGLWSIVQAKISSIEFGY 310
                        330
                 ....*....|....*.
gi 189518151 336 LGYAVLRFNQYFKMKP 351
Cdd:cd05156  311 LEYAQARLDAYFKQKE 326
PLN02236 PLN02236
choline kinase
72-355 3.36e-63

choline kinase


Pssm-ID: 177880 [Multi-domain]  Cd Length: 344  Bit Score: 204.89  E-value: 3.36e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189518151  72 VLVRVYGNKTELFVDRENEVKSFRVLQAHRCAPRLYCTFNNGLCYEFLQGVALEPEHIRSPAIFRHIARQMAKYHAIHah 151
Cdd:PLN02236  68 VLVRIYGEGVELFFDRDDEIRTFECMSRHGQGPRLLGRFPNGRVEEFIHARTLSAADLRDPEISALIAAKLREFHSLD-- 145
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189518151 152 ngwVPQSG---LWLKMSKFFSLVPSHFEDPEMDQ-RLNnevpsaaCLRDEMIWLQQNLSKLGSPVVLCHNDLLCKNIIYN 227
Cdd:PLN02236 146 ---MPGPKnvlLWDRLRNWLKEAKNLCSPEEAKEfRLD-------SLEDEINLLEKELSGDDQEIGFCHNDLQYGNIMID 215
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189518151 228 QKEGNVKFIDYEYAGYNYQAFDIGNHFNEFAG------LNEVDYTLYPDRELQMQWLRAYLEaykeykSQGSQVSNTEVE 301
Cdd:PLN02236 216 EETRAITIIDYEYASYNPVAYDIANHFCEMAAdyhsetPHILDYSKYPGEEERRRFIRTYLS------SSGEEPSDEEVE 289
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 189518151 302 LLYVQVNRFALASHFFWGLWALIQAQYSTIDFDFLGYAVLRFNQYFKMKPEVMS 355
Cdd:PLN02236 290 QLLDDVEKYTLASHLFWGLWGIISGHVNKIDFDYMEYARQRFEQYWLRKPELLG 343
ChoK-like_euk cd14021
Euykaryotic Choline Kinase and similar proteins; This group is composed of eukaryotic choline ...
49-323 4.13e-48

Euykaryotic Choline Kinase and similar proteins; This group is composed of eukaryotic choline kinase, ethanolamine kinase, and similar proteins. ChoK catalyzes the transfer of the gamma-phosphoryl group from ATP (or CTP) to its substrate, choline, producing phosphorylcholine (PCho), a precursor to the biosynthesis of two major membrane phospholipids, phosphatidylcholine (PC), and sphingomyelin (SM). Although choline is the preferred substrate, ChoK also shows substantial activity towards ethanolamine and its N-methylated derivatives. ETNK catalyzes the transfer of the gamma-phosphoryl group from CTP to ethanolamine (Etn), the first step in the CDP-Etn pathway for the formation of the major phospholipid, phosphatidylethanolamine (PtdEtn). Unlike ChoK, ETNK shows specific activity for its substrate and displays negligible activity towards N-methylated derivatives of Etn. ChoK plays an important role in cell signaling pathways and the regulation of cell growth. The ChoK subfamily is part of a larger superfamily that includes the catalytic domains of other kinases, such as the typical serine/threonine/tyrosine protein kinases (PKs), RIO kinases, actin-fragmin kinase (AFK), and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270923 [Multi-domain]  Cd Length: 229  Bit Score: 162.05  E-value: 4.13e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189518151  49 KTFTDGITNKL----IGCYVGGSMQEVVLVRVYGNKTELFVDRENEVKSFRVLQAHRCAPRLYCTFNNGLCYEFLQGVAL 124
Cdd:cd14021    4 IRILSGLTNQVykvsLKDESDSLEPKKVLFRIYGKYLSTLYDREKESEVFKILSEQGLGPKLIYKFDGGRIEEYIDGRPL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189518151 125 EPEHIRSPAIFRHIARQMAKYHAIHAhngwvpqsglwlkmskffslvpshfedpemdqrlnnevpsaaclrdemiwlqqn 204
Cdd:cd14021   84 TTDELRNPSVLTSIAKLLAKFHKIKT------------------------------------------------------ 109
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189518151 205 lsklgSPVVLCHNDLLCKNIIYNQKEGNVKFIDYEYAGYNYQAFDIGNHFNEFAGLNEV--------DYTLYPDRELQMQ 276
Cdd:cd14021  110 -----PPVVFCHNDLQENNILLTNDQDGLRLIDFEYSGFNYRGYDIANFFNESMIDYDHpeppyfkiYKENYISEEEKRL 184
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 189518151 277 WLRAYLEAYKEYKSQGSqvSNTEVELLYVQVNRFALASHFFWGLWAL 323
Cdd:cd14021  185 FVSVYLSEYLEKNVLPS--LDKLVEQFLQEVEIFTLGSHLYWGLWSI 229
PTZ00296 PTZ00296
choline kinase; Provisional
40-355 6.79e-38

choline kinase; Provisional


Pssm-ID: 240350 [Multi-domain]  Cd Length: 442  Bit Score: 140.79  E-value: 6.79e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189518151  40 HWKPSEVKMKTFTDGITNKLIGCYVGGS-------MQEVVLVRVYGNKTELFVDRENEVKSFRVLQAHRCAPRLYCTFNN 112
Cdd:PTZ00296 102 RFTEDDVRVNQILSGLTNQLFEVSLKEEtannypsIRRRVLFRIYGKDVDELYNPISEFEVYKTMSKYRIAPQLLNTFSG 181
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189518151 113 GLCYEFLQGVALEPEHIRSPAIFRHIARQMAKYHAI----HAHNGWVPQSGLWLKMSKFFSLVpSHFEDPEMDQRLNNEV 188
Cdd:PTZ00296 182 GRIEEWLYGDPLRIDDLKNPSILIGIANVLGKFHTLsrkrHLPEHWDRTPCIFKMMEKWKNQL-SKYKNIEKYQRDIHKY 260
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189518151 189 PSAACLRDEMIWLQQNLSKLGSPVVLCHNDLLCKNIIYNQKegNVKFIDYEYAGYNYQAFDIGNHFNEFAglneVDYTL- 267
Cdd:PTZ00296 261 IKESEKFIKFMKVYSKSDNLANDIVFCHNDLQENNIINTNK--CLRLIDFEYSGYNFLATDIANFFIETT----IDYSVs 334
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189518151 268 -----------YPDRELQMQWLRAYLEaykEYKSQGSQVSNTEVELLYVQ-VNRFALASHFFWGLWALIQAQY--STIDF 333
Cdd:PTZ00296 335 hypffaidkkkYISYENRKLFITAYLS---NYLDKSLVVPNPKIIDQILEaVEVQALGAHLLWGFWSIIRGYQtkSYNEF 411
                        330       340
                 ....*....|....*....|..
gi 189518151 334 DFLGYAVLRFNQYFKMKPEVMS 355
Cdd:PTZ00296 412 DFFLYAKERFKMYDEQKEYLIS 433
ChoK-like cd05151
Choline Kinase and similar proteins; This subfamily is composed of bacterial and eukaryotic ...
54-257 1.35e-24

Choline Kinase and similar proteins; This subfamily is composed of bacterial and eukaryotic choline kinases, as well as eukaryotic ethanolamine kinase. ChoK catalyzes the transfer of the gamma-phosphoryl group from ATP (or CTP) to its substrate, choline, producing phosphorylcholine (PCho), a precursor to the biosynthesis of two major membrane phospholipids, phosphatidylcholine (PC), and sphingomyelin (SM). Although choline is the preferred substrate, ChoK also shows substantial activity towards ethanolamine and its N-methylated derivatives. Bacterial ChoK is also referred to as licA protein. ETNK catalyzes the transfer of the gamma-phosphoryl group from CTP to ethanolamine (Etn), the first step in the CDP-Etn pathway for the formation of the major phospholipid, phosphatidylethanolamine (PtdEtn). Unlike ChoK, ETNK shows specific activity for its substrate and displays negligible activity towards N-methylated derivatives of Etn. ChoK plays an important role in cell signaling pathways and the regulation of cell growth. The ChoK subfamily is part of a larger superfamily that includes the catalytic domains of other kinases, such as the typical serine/threonine/tyrosine protein kinases (PKs), RIO kinases, actin-fragmin kinase (AFK), and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270700 [Multi-domain]  Cd Length: 152  Bit Score: 97.63  E-value: 1.35e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189518151  54 GITNKLIGCYVGGsmqEVVLVRVYGNKTELFVDRENEVKSFRVLQAHRCAPR-LYCTFNNG-LCYEFLQGVALEPEHIRS 131
Cdd:cd05151    9 GLTNKNYLVEVAG---KKYVLRIPGAGTELLIDRENEKANSKAAAELGIAPEvIYFDPETGvKITEFIEGATLLTNDFSD 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189518151 132 PAIFRHIARQMAKYHAIHAHngwvpqsglwlkmskffslvpshfedpemdqrlnnevpsaaclrdemiwlqqnlsklgsP 211
Cdd:cd05151   86 PENLERIAALLRKLHSSPLE-----------------------------------------------------------D 106
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 189518151 212 VVLCHNDLLCKNIIYNQkeGNVKFIDYEYAGYNYQAFDIGNHFNEF 257
Cdd:cd05151  107 LVLCHNDLVPGNFLLDD--DRLYLIDWEYAGMNDPLFDLAALFSEN 150
CotS COG0510
Thiamine kinase or a related kinase [Coenzyme transport and metabolism];
194-344 4.55e-17

Thiamine kinase or a related kinase [Coenzyme transport and metabolism];


Pssm-ID: 440276 [Multi-domain]  Cd Length: 156  Bit Score: 77.51  E-value: 4.55e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189518151 194 LRDEMIWLQQNLSKLGSPVVLCHNDLLCKNIIYnQKEGNVKFIDYEYAGYNYQAFDIGNHFNEFAglnevdytlyPDREL 273
Cdd:COG0510   31 LLRRLEELERALAARPLPLVLCHGDLHPGNFLV-TDDGRLYLIDWEYAGLGDPAFDLAALLVEYG----------LSPEQ 99
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 189518151 274 QMQWLRAYLEAYKEyksqgsqvsntevELLYVQVNRFALASHFFWGLWALIQAQYSTiDFDFLGYAVLRFN 344
Cdd:COG0510  100 AEELLEAYGFGRPT-------------EELLRRLRAYRALADLLWALWALVRAAQEA-NGDLLKYLLRRLE 156
APH pfam01636
Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance ...
63-287 1.90e-09

Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance proteins, which confer resistance to various aminoglycosides they include: aminoglycoside 3'-phosphotransferase or kanamycin kinase / neomycin-kanamycin phosphotransferase and streptomycin 3''-kinase or streptomycin 3''-phosphotransferase. The aminoglycoside phosphotransferases inactivate aminoglycoside antibiotics via phosphorylation. This family also includes homoserine kinase. This family is related to fructosamine kinase pfam03881.


Pssm-ID: 426359 [Multi-domain]  Cd Length: 239  Bit Score: 57.51  E-value: 1.90e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189518151   63 YVGGSMQEVVLvRVYgNKTELFVDRENEVKSFRVLQAHR----CAPRLYCTFNNGLC-----YEFLQGVALEPEHIR--S 131
Cdd:pfam01636  15 LVTTGDGRYVL-RLP-PPGRAAEELRRELALLRHLAAAGvppvPRVLAGCTDAELLGlpfllMEYLPGEVLARPLLPeeR 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189518151  132 PAIFRHIARQMAKYHAIHAhnGWVPQSG---LWLKMSKFFSLVPSHFEDPEMDQRLnnevpsAACLRDEMIWLQQNLsKL 208
Cdd:pfam01636  93 GALLEALGRALARLHAVDP--AALPLAGrlaRLLELLRQLEAALARLLAAELLDRL------EELEERLLAALLALL-PA 163
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 189518151  209 GSPVVLCHNDLLCKNIIYNQKEGNVKFIDYEYAGYNYQAFDIGNHFNEFaglnevdytlypDRELQMQWLRAYLEAYKE 287
Cdd:pfam01636 164 ELPPVLVHGDLHPGNLLVDPGGRVSGVIDFEDAGLGDPAYDLAILLNSW------------GRELGAELLAAYLAAYGA 230
HomoserineK_II cd05153
Type II Homoserine Kinase; This subfamily is composed of unusual homoserine kinases, from a ...
116-323 6.14e-09

Type II Homoserine Kinase; This subfamily is composed of unusual homoserine kinases, from a subset of bacteria, which have a Protein Kinase fold. These proteins do not bear any similarity to the GHMP family homoserine kinases present in most bacteria and eukaryotes. Homoserine kinase catalyzes the transfer of the gamma-phosphoryl group from ATP to L-homoserine producing L-homoserine phosphate, an intermediate in the production of the amino acids threonine, methionine, and isoleucine. The Type II homoserine kinase subfamily is part of a larger superfamily that includes the catalytic domains of other kinases, such as the typical serine/threonine/tyrosine protein kinases (PKs), RIO kinases, actin-fragmin kinase (AFK), and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270702 [Multi-domain]  Cd Length: 300  Bit Score: 56.50  E-value: 6.14e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189518151 116 YEFLQGVALEPehiRSPAIFRHIARQMAKYHaiHAHNGWVPQSGlwlkmskfFSLVPSHFED--PEMDQRLNNEVPS-AA 192
Cdd:cd05153   94 FPFLPGESLTT---PTPEQCRAIGAALARLH--LALAGFPPPRP--------NPRGLAWWKPlaERLKARLDLLAADdRA 160
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189518151 193 CLRDEMIWLQQN-LSKLgsPVVLCHNDLLCKNIIYnqKEGNVK-FIDYEYAGYNYQAFDIGNHFNEFAGLNevDYTLYPD 270
Cdd:cd05153  161 LLEDELARLQALaPSDL--PRGVIHADLFRDNVLF--DGDRLSgIIDFYDACYDPLLYDLAIALNDWCFDD--DGKLDPE 234
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 189518151 271 RelqmqwLRAYLEAYKEYKSqgsqVSNTEVELLYVQvnrFALASHFFWGLWAL 323
Cdd:cd05153  235 R------AKALLAGYQSVRP----LTEEEKAALPLL---LRAAALRFWLSRLY 274
APH_ChoK_like cd05120
Aminoglycoside 3'-phosphotransferase and Choline Kinase family; This family is composed of APH, ...
49-257 1.32e-07

Aminoglycoside 3'-phosphotransferase and Choline Kinase family; This family is composed of APH, ChoK, ethanolamine kinase (ETNK), macrolide 2'-phosphotransferase (MPH2'), an unusual homoserine kinase, and uncharacterized proteins with similarity to the N-terminal domain of acyl-CoA dehydrogenase 10 (ACAD10). The members of this family catalyze the transfer of the gamma-phosphoryl group from ATP (or CTP) to small molecule substrates such as aminoglycosides, macrolides, choline, ethanolamine, and homoserine. Phosphorylation of the antibiotics, aminoglycosides and macrolides, leads to their inactivation and to bacterial antibiotic resistance. Phosphorylation of choline, ethanolamine, and homoserine serves as precursors to the synthesis of important biological compounds, such as the major phospholipids, phosphatidylcholine and phosphatidylethanolamine and the amino acids, threonine, methionine, and isoleucine. The APH/ChoK family is part of a larger superfamily that includes the catalytic domains of other kinases, such as the typical serine/threonine/tyrosine protein kinases (PKs), RIO kinases, actin-fragmin kinase (AFK), and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270690 [Multi-domain]  Cd Length: 158  Bit Score: 50.76  E-value: 1.32e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189518151  49 KTFTDGITNKLigcYVGGSMQEVVLvRVYGNktELFVDRENEVKSFRVLQAHRC--APRLYCTFNNG----LCYEFLQGV 122
Cdd:cd05120    4 KLIKEGGDNKV---YLLGDPREYVL-KIGPP--RLKKDLEKEAAMLQLLAGKLSlpVPKVYGFGESDgweyLLMERIEGE 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189518151 123 ALEPEHIR-----SPAIFRHIARQMAKYHAIhahngwvpqsglwlkmskffslvpshfedpemdqrlnnevpsaaclrde 197
Cdd:cd05120   78 TLSEVWPRlseeeKEKIADQLAEILAALHRI------------------------------------------------- 108
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 189518151 198 miwlqqnlsklgSPVVLCHNDLLCKNIIYNQKEGNVKFIDYEYAGYNYQAFDIGNHFNEF 257
Cdd:cd05120  109 ------------DSSVLTHGDLHPGNILVKPDGKLSGIIDWEFAGYGPPAFDYAAALRDW 156
SrkA COG2334
Ser/Thr protein kinase RdoA involved in Cpx stress response, MazF antagonist [Signal ...
115-285 3.14e-07

Ser/Thr protein kinase RdoA involved in Cpx stress response, MazF antagonist [Signal transduction mechanisms]; Ser/Thr protein kinase RdoA involved in Cpx stress response, MazF antagonist is part of the Pathway/BioSystem: Threonine biosynthesis


Pssm-ID: 441905 [Multi-domain]  Cd Length: 297  Bit Score: 51.46  E-value: 3.14e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189518151 115 CYEFLQGVALEPehiRSPAIFRHIARQMAKYHAIHAhnGWVPQSGLWLKMskffslvpshfEDPEMDQRLNNEVPSA--- 191
Cdd:COG2334   93 LFPFLPGRSPEE---PSPEQLEELGRLLARLHRALA--DFPRPNARDLAW-----------WDELLERLLGPLLPDPedr 156
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189518151 192 ACLRDEMIWLQQNLSKLGS--PVVLCHNDLLCKNIIYNQkEGNVKFIDYEYAGYNYQAFDIGnhfnefaglnevdYTLY- 268
Cdd:COG2334  157 ALLEELLDRLEARLAPLLGalPRGVIHGDLHPDNVLFDG-DGVSGLIDFDDAGYGPRLYDLA-------------IALNg 222
                        170
                 ....*....|....*...
gi 189518151 269 -PDRELQMQWLRAYLEAY 285
Cdd:COG2334  223 wADGPLDPARLAALLEGY 240
YcbJ COG3173
Predicted kinase, aminoglycoside phosphotransferase (APT) family [General function prediction ...
72-287 5.88e-07

Predicted kinase, aminoglycoside phosphotransferase (APT) family [General function prediction only];


Pssm-ID: 442406 [Multi-domain]  Cd Length: 284  Bit Score: 50.50  E-value: 5.88e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189518151  72 VLVRVY--GNKTELFVDREnevksFRVLQA-HRCA----PRLYCTFNNG-------LCYEFLQGVALEPEHIR-SPAIFR 136
Cdd:COG3173   45 LVLRRPprGLASAHDVRRE-----ARVLRAlAPRLgvpvPRPLALGEDGevigapfYVMEWVEGETLEDALPDlSPAERR 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189518151 137 HIARQMAKYHA-IHAHNgwVPQSGLwlkmskfFSLVPSHFEDP------EMDQRLNNEVPSAAcLRDEMI-WLQQNLSKL 208
Cdd:COG3173  120 ALARALGEFLAaLHAVD--PAAAGL-------ADGRPEGLERQlarwraQLRRALARTDDLPA-LRERLAaWLAANLPEW 189
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189518151 209 GsPVVLCHNDLLCKNIIYNQKEGNVK-FIDYEYAGYNYQAFDIGNHFNEFAGLNEvdytLYPDRElqmqwlrAYLEAYKE 287
Cdd:COG3173  190 G-PPVLVHGDLRPGNLLVDPDDGRLTaVIDWELATLGDPAADLAYLLLYWRLPDD----LLGPRA-------AFLAAYEE 257
PTZ00384 PTZ00384
choline kinase; Provisional
212-344 9.96e-06

choline kinase; Provisional


Pssm-ID: 173576 [Multi-domain]  Cd Length: 383  Bit Score: 47.08  E-value: 9.96e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189518151 212 VVLCHNDLLCKNII-YNQkegNVKFIDYEYAGYNYQAFDIGNHFNEFAGLNEVD---YTLYPD-----RELQMQWLRAYL 282
Cdd:PTZ00384 227 VLFCHNDLFFTNILdFNQ---GIYFIDFDFAGFNYVGWEIANFFVKLYIVYDPPtppYFNSDDslalsEEMKTIFVSVYL 303
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189518151 283 eaykeykSQ--GSQV--SNTEVELLYVQVNRFALASHFFWGLWALIQA----QYSTIDFDFLGYAVLRFN 344
Cdd:PTZ00384 304 -------SQllGKNVlpSDDLVKEFLQSLEIHTLGVNLFWTYWGIVMNdkpkNELSKPVKFEAYAKFQYN 366
CotI COG5881
Spore coat protein CotI/CotS, protein kinase superfamily [Cell cycle control, cell division, ...
214-320 5.66e-04

Spore coat protein CotI/CotS, protein kinase superfamily [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 444583 [Multi-domain]  Cd Length: 331  Bit Score: 41.42  E-value: 5.66e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189518151 214 LCHNDLLCKNIIYNqKEGNVKFIDYEYAGYNYQAFDIGNHFNEFAGLNEVDytlypdrelqMQWLRAYLEAYKEYKSqgs 293
Cdd:COG5881  203 FCHHDYAYHNILID-EDGKIYIIDFDYCIYDLPVHDLAKLLRRVMKRGNWD----------IEKAKEILEAYNKINP--- 268
                         90       100
                 ....*....|....*....|....*..
gi 189518151 294 qVSNTEVELLYVqvnrFALASHFFWGL 320
Cdd:COG5881  269 -LSKEEIEVLLA----FLLFPQKFWRL 290
spore_CotS TIGR02906
spore coat protein, CotS family; Members of this family include the spore coat proteins CotS ...
106-320 1.77e-03

spore coat protein, CotS family; Members of this family include the spore coat proteins CotS and YtaA from Bacillus subtilis and, from other endospore-forming bacteria, homologs that are more closely related to these two than to the spore coat proteins YutH and YsxE. The CotS family is more broadly distributed than YutH or YsxE, but still is not universal among spore-formers. [Cellular processes, Sporulation and germination]


Pssm-ID: 131952 [Multi-domain]  Cd Length: 313  Bit Score: 39.96  E-value: 1.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189518151  106 LYCTFNNGL--CYEFLQGVALE---PEHIRSpaifrhIARQMAKYHaiHAHNGWVPQSGL--------WLK--------M 164
Cdd:TIGR02906  62 LYVKYNGDLyvLTEWIEGRECDfnnPIDLKK------AAKGLALFH--HASKGYVPPDGSkirsklgkWPKqfekrlkeL 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189518151  165 SKFFSLVPSHFEDPEMDQRLNNEVpsaaclrDEMI-----------------WLQQNLSKLGspvvLCHNDLLCKNIIYn 227
Cdd:TIGR02906 134 ERFKKIALEKKYKDEFDKLYLKEV-------DYFLergkkalellnkskyydLCKEAKKIRG----FCHQDYAYHNILL- 201
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189518151  228 qKEGNVKFIDYEYAGYNYQAFDIGNHfnefagLNEVDYTLYpdrELQMQWLRAYLEAYkeykSQGSQVSNTEVELLYVqv 307
Cdd:TIGR02906 202 -KDNEVYVIDFDYCTIDLPVRDLRKL------IIKLMKKNG---VWDLEKAKEIIEAY----SSINPLSKEEKEVLYI-- 265
                         250
                  ....*....|...
gi 189518151  308 nrFALASHFFWGL 320
Cdd:TIGR02906 266 --DLAFPHKFWKI 276
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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