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Conserved domains on  [gi|157824018|ref|NP_001101364|]
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ethanolamine kinase 1 [Rattus norvegicus]

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 ...
49-351 2.22e-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: 410.82  E-value: 2.22e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824018  49 VTLQLFTDGITNKLIACYV-GDTMDDVVLVRIYGNKTELLVDRDEEVKSFRVLQAHGCAPQLYCTFNNGLCYEFIQGEAL 127
Cdd:cd05157    1 IKVKRITGGITNALYKVTYpSGDTPKTVLVRIYGPGTELLIDRDRELRILQLLSRAGIGPKLYGRFENGRVEEFLPGRTL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824018 128 DPQHVCNPAIFRLIARQLAKIHAIHAHNGW--IPKSNLWLKMGKYFSLIPTGFADEDiNKRFLSEIPSPQLLQEEMTWMK 205
Cdd:cd05157   81 TPEDLRDPKISRLIARRLAELHSIVPLGEIegKKKPILWTTIRKWLDLAPEVFEDEK-NKEKKLEKVDLERLRKELEWLE 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824018 206 EILSSL-GSPVVLCHNDLLCKNIIYNEKQGDVQFIDYEYSGYNYLAYDIGNHFNEFAGVSDV-DYSLYPDRELQGQWLRS 283
Cdd:cd05157  160 KWLESLeKSPIVFCHNDLLYGNILYNEDDDSVTFIDFEYAGPNPRAFDIANHFCEWAGFYCVlDYSRYPTKEEQRNFLRA 239
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 157824018 284 YLEAYKEYKGfGSDVTEKEVETLFIQVNQFALASHFFWGLWALIQAKYSTIEFDFLGYAIVRFNQYFK 351
Cdd:cd05157  240 YLESLDGLPG-GEEVSEEEVEKLYNEVNLFRLASHLFWGLWALIQAAISSIDFDYLGYAKERLDEYWG 306
 
Name Accession Description Interval E-value
ETNK_euk cd05157
Euykaryotic Ethanolamine kinase; ETNK catalyzes the transfer of the gamma-phosphoryl group ...
49-351 2.22e-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: 410.82  E-value: 2.22e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824018  49 VTLQLFTDGITNKLIACYV-GDTMDDVVLVRIYGNKTELLVDRDEEVKSFRVLQAHGCAPQLYCTFNNGLCYEFIQGEAL 127
Cdd:cd05157    1 IKVKRITGGITNALYKVTYpSGDTPKTVLVRIYGPGTELLIDRDRELRILQLLSRAGIGPKLYGRFENGRVEEFLPGRTL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824018 128 DPQHVCNPAIFRLIARQLAKIHAIHAHNGW--IPKSNLWLKMGKYFSLIPTGFADEDiNKRFLSEIPSPQLLQEEMTWMK 205
Cdd:cd05157   81 TPEDLRDPKISRLIARRLAELHSIVPLGEIegKKKPILWTTIRKWLDLAPEVFEDEK-NKEKKLEKVDLERLRKELEWLE 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824018 206 EILSSL-GSPVVLCHNDLLCKNIIYNEKQGDVQFIDYEYSGYNYLAYDIGNHFNEFAGVSDV-DYSLYPDRELQGQWLRS 283
Cdd:cd05157  160 KWLESLeKSPIVFCHNDLLYGNILYNEDDDSVTFIDFEYAGPNPRAFDIANHFCEWAGFYCVlDYSRYPTKEEQRNFLRA 239
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 157824018 284 YLEAYKEYKGfGSDVTEKEVETLFIQVNQFALASHFFWGLWALIQAKYSTIEFDFLGYAIVRFNQYFK 351
Cdd:cd05157  240 YLESLDGLPG-GEEVSEEEVEKLYNEVNLFRLASHLFWGLWALIQAAISSIDFDYLGYAKERLDEYWG 306
Choline_kinase pfam01633
Choline/ethanolamine kinase; Choline kinase catalyzes the committed step in the synthesis of ...
75-275 2.15e-85

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: 257.20  E-value: 2.15e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824018   75 VLVRIYGNKTELLVDRDEEVKSFRVLQAHGCAPQLYCTFNNGLCYEFIQGEALDPQHVCNPAIFRLIARQLAKIHAIHAH 154
Cdd:pfam01633   5 VLLRIYGPGTELLINREDEIVNFALLSERGLGPKLYGFFPNGRIEEFIPSRTLSTEDLRDPEISKLIAKRLAELHSLEMP 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824018  155 ngWIPKSNLWLKMGKYFSLIPTGFADEDINKRFLSEIPSPQLLQEEMTWMKEILSSLGSPVVLCHNDLLCKNIIYNEKQG 234
Cdd:pfam01633  85 --GKKSPSLWKTMRKWLSLLKNLGAPESVNKSEQLKSINLEDLEKEINKLEKWLELLDSPIVFCHNDLQSGNILLLNETK 162
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 157824018  235 DVQFIDYEYSGYNYLAYDIGNHFNEFAGV-------SDVDYSLYPDRE 275
Cdd:pfam01633 163 RLVLIDFEYASYNYRGFDIANHFCEWAGDyhdptpfFKCDYSLYPTRE 210
PLN02421 PLN02421
phosphotransferase, alcohol group as acceptor/kinase
57-359 2.54e-84

phosphotransferase, alcohol group as acceptor/kinase


Pssm-ID: 215231 [Multi-domain]  Cd Length: 330  Bit Score: 258.90  E-value: 2.54e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824018  57 GITNKLIACYV-GDTMDDV-VLVRIYGNKTELLVDRDEEVKSFRVLQAHGCAPQLYCTFNNGLCYEFIQGEALDPQHVCN 134
Cdd:PLN02421  25 GITNLLLKVSVkEENGNEVsVTVRLFGPNTDYVIDRERELQAIKYLSAAGFGAKLLGVFGNGMIQSFINARTLTPSDMRK 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824018 135 PAIFRLIARQLAKIHAIHahngwIPKSN---LWLKMGKYFSLIPTgFADEDINKRFLSEIPSPQLLQEEMTWMKEILSSL 211
Cdd:PLN02421 105 PKVAAEIAKELRRLHQVE-----IPGSKepqLWNDIFKFYEKAST-VKFEDPEKQKKYETISFEELRDEIVELKEITDSL 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824018 212 GSPVVLCHNDLLCKNIIYNEKQGDVQFIDYEYSGYNYLAYDIGNHFNEFAGVsDVDYSLYPDRELQGQWLRSYLEAYKEY 291
Cdd:PLN02421 179 KAPVVFAHNDLLSGNLMLNEDEGKLYFIDFEYGSYSYRGYDIGNHFNEYAGF-DCDYSLYPSKEEQYHFFRHYLRPDDPE 257
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 157824018 292 KgfgsdVTEKEVETLFIQVNQFALASHFFWGLWALIQAKYSTIEFDFLGYAIVRFNQYFKMKPEVTAL 359
Cdd:PLN02421 258 E-----VSDAELEELFVETNFYALASHLYWAIWAIVQAKMSPIDFDYLGYFFLRYKEYKRQKEKLLSL 320
CotS COG0510
Thiamine kinase or a related kinase [Coenzyme transport and metabolism];
195-347 4.71e-15

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


Pssm-ID: 440276 [Multi-domain]  Cd Length: 156  Bit Score: 71.74  E-value: 4.71e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824018 195 QLLQEEMTWMKEILSSLGSPVVLCHNDLLCKNIIYNEkQGDVQFIDYEYSGYNYLAYDIGNHFNEFAgvsdvdyslyPDR 274
Cdd:COG0510   29 PELLRRLEELERALAARPLPLVLCHGDLHPGNFLVTD-DGRLYLIDWEYAGLGDPAFDLAALLVEYG----------LSP 97
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157824018 275 ELQGQWLRSYleaykeykgFGSDVTEKEVEtlfiQVNQFALASHFFWGLWALIQAKYSTiEFDFLGYAIVRFN 347
Cdd:COG0510   98 EQAEELLEAY---------GFGRPTEELLR----RLRAYRALADLLWALWALVRAAQEA-NGDLLKYLLRRLE 156
spore_CotS TIGR02906
spore coat protein, CotS family; Members of this family include the spore coat proteins CotS ...
109-323 5.00e-05

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: 44.58  E-value: 5.00e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824018  109 LYCTFNNGL--CYEFIQGEALDpqhVCNPAIFRLIARQLAKIHaiHAHNGWIPKSNL-----WLKMGKYF---------- 171
Cdd:TIGR02906  62 LYVKYNGDLyvLTEWIEGRECD---FNNPIDLKKAAKGLALFH--HASKGYVPPDGSkirskLGKWPKQFekrlkelerf 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824018  172 -SLIPTGFADEDINKRFLSEIP--------SPQLLQ--EEMTWMKEILSSLGspvvLCHNDLLCKNIIYneKQGDVQFID 240
Cdd:TIGR02906 137 kKIALEKKYKDEFDKLYLKEVDyflergkkALELLNksKYYDLCKEAKKIRG----FCHQDYAYHNILL--KDNEVYVID 210
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824018  241 YEYSGYNYLAYDIGNHFNEFA---GVSDVDyslypdrelqgqWLRSYLEAYKEYkgfgSDVTEKEVETLFIqvnqFALAS 317
Cdd:TIGR02906 211 FDYCTIDLPVRDLRKLIIKLMkknGVWDLE------------KAKEIIEAYSSI----NPLSKEEKEVLYI----DLAFP 270

                  ....*.
gi 157824018  318 HFFWGL 323
Cdd:TIGR02906 271 HKFWKI 276
CHK smart00587
ZnF_C4 abd HLH domain containing kinases domain; subfamily of choline kinases
139-253 1.38e-03

ZnF_C4 abd HLH domain containing kinases domain; subfamily of choline kinases


Pssm-ID: 214734  Cd Length: 196  Bit Score: 39.24  E-value: 1.38e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824018   139 RLIARQLAKIHAIHAH-----NGWIPKS-NLWLKMGKYFSLIPTGFADEDINKRFLSEIPSP-----------QLLQEEM 201
Cdd:smart00587  26 SLVLKKLAKLHAASAVlieeeKGSYLEEfDEGLFERFKRMFSEEFIGGLENFLRELLSQPELlkveeyiekldKLLDNLE 105
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 157824018   202 TWMKEIL-SSLGSPVVLCHNDLLCKNIIY----NEKQGDVQFIDYEYSGYNYLAYDI 253
Cdd:smart00587 106 DLKKEDKePDEGEFNVLNHGDLWANNIMFkyddEGKPEDVALIDFQLSHYGSPAEDL 162
 
Name Accession Description Interval E-value
ETNK_euk cd05157
Euykaryotic Ethanolamine kinase; ETNK catalyzes the transfer of the gamma-phosphoryl group ...
49-351 2.22e-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: 410.82  E-value: 2.22e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824018  49 VTLQLFTDGITNKLIACYV-GDTMDDVVLVRIYGNKTELLVDRDEEVKSFRVLQAHGCAPQLYCTFNNGLCYEFIQGEAL 127
Cdd:cd05157    1 IKVKRITGGITNALYKVTYpSGDTPKTVLVRIYGPGTELLIDRDRELRILQLLSRAGIGPKLYGRFENGRVEEFLPGRTL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824018 128 DPQHVCNPAIFRLIARQLAKIHAIHAHNGW--IPKSNLWLKMGKYFSLIPTGFADEDiNKRFLSEIPSPQLLQEEMTWMK 205
Cdd:cd05157   81 TPEDLRDPKISRLIARRLAELHSIVPLGEIegKKKPILWTTIRKWLDLAPEVFEDEK-NKEKKLEKVDLERLRKELEWLE 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824018 206 EILSSL-GSPVVLCHNDLLCKNIIYNEKQGDVQFIDYEYSGYNYLAYDIGNHFNEFAGVSDV-DYSLYPDRELQGQWLRS 283
Cdd:cd05157  160 KWLESLeKSPIVFCHNDLLYGNILYNEDDDSVTFIDFEYAGPNPRAFDIANHFCEWAGFYCVlDYSRYPTKEEQRNFLRA 239
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 157824018 284 YLEAYKEYKGfGSDVTEKEVETLFIQVNQFALASHFFWGLWALIQAKYSTIEFDFLGYAIVRFNQYFK 351
Cdd:cd05157  240 YLESLDGLPG-GEEVSEEEVEKLYNEVNLFRLASHLFWGLWALIQAAISSIDFDYLGYAKERLDEYWG 306
Choline_kinase pfam01633
Choline/ethanolamine kinase; Choline kinase catalyzes the committed step in the synthesis of ...
75-275 2.15e-85

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: 257.20  E-value: 2.15e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824018   75 VLVRIYGNKTELLVDRDEEVKSFRVLQAHGCAPQLYCTFNNGLCYEFIQGEALDPQHVCNPAIFRLIARQLAKIHAIHAH 154
Cdd:pfam01633   5 VLLRIYGPGTELLINREDEIVNFALLSERGLGPKLYGFFPNGRIEEFIPSRTLSTEDLRDPEISKLIAKRLAELHSLEMP 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824018  155 ngWIPKSNLWLKMGKYFSLIPTGFADEDINKRFLSEIPSPQLLQEEMTWMKEILSSLGSPVVLCHNDLLCKNIIYNEKQG 234
Cdd:pfam01633  85 --GKKSPSLWKTMRKWLSLLKNLGAPESVNKSEQLKSINLEDLEKEINKLEKWLELLDSPIVFCHNDLQSGNILLLNETK 162
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 157824018  235 DVQFIDYEYSGYNYLAYDIGNHFNEFAGV-------SDVDYSLYPDRE 275
Cdd:pfam01633 163 RLVLIDFEYASYNYRGFDIANHFCEWAGDyhdptpfFKCDYSLYPTRE 210
PLN02421 PLN02421
phosphotransferase, alcohol group as acceptor/kinase
57-359 2.54e-84

phosphotransferase, alcohol group as acceptor/kinase


Pssm-ID: 215231 [Multi-domain]  Cd Length: 330  Bit Score: 258.90  E-value: 2.54e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824018  57 GITNKLIACYV-GDTMDDV-VLVRIYGNKTELLVDRDEEVKSFRVLQAHGCAPQLYCTFNNGLCYEFIQGEALDPQHVCN 134
Cdd:PLN02421  25 GITNLLLKVSVkEENGNEVsVTVRLFGPNTDYVIDRERELQAIKYLSAAGFGAKLLGVFGNGMIQSFINARTLTPSDMRK 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824018 135 PAIFRLIARQLAKIHAIHahngwIPKSN---LWLKMGKYFSLIPTgFADEDINKRFLSEIPSPQLLQEEMTWMKEILSSL 211
Cdd:PLN02421 105 PKVAAEIAKELRRLHQVE-----IPGSKepqLWNDIFKFYEKAST-VKFEDPEKQKKYETISFEELRDEIVELKEITDSL 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824018 212 GSPVVLCHNDLLCKNIIYNEKQGDVQFIDYEYSGYNYLAYDIGNHFNEFAGVsDVDYSLYPDRELQGQWLRSYLEAYKEY 291
Cdd:PLN02421 179 KAPVVFAHNDLLSGNLMLNEDEGKLYFIDFEYGSYSYRGYDIGNHFNEYAGF-DCDYSLYPSKEEQYHFFRHYLRPDDPE 257
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 157824018 292 KgfgsdVTEKEVETLFIQVNQFALASHFFWGLWALIQAKYSTIEFDFLGYAIVRFNQYFKMKPEVTAL 359
Cdd:PLN02421 258 E-----VSDAELEELFVETNFYALASHLYWAIWAIVQAKMSPIDFDYLGYFFLRYKEYKRQKEKLLSL 320
ChoK_euk cd05156
Euykaryotic Choline Kinase; ChoK catalyzes the transfer of the gamma-phosphoryl group from ATP ...
57-354 2.58e-73

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: 230.59  E-value: 2.58e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824018  57 GITNKLIACYVGDTMDDV------VLVRIYGN---KTELLVDrdEEVkSFRVLQAHGCAPQLYCTFNNGLCYEFIQGEAL 127
Cdd:cd05156    9 GLSNLLYLCSLPDGVVPVggeprkVLLRIYGQilqAEESLVT--ESV-IFALLSERGLGPKLYGIFPGGRLEEFIPSRPL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824018 128 DPQHVCNPAIFRLIARQLAKIHAIHahngwIPKSN----LWLKMGKYFS-LIPTGFADEDINKRFLSEIPSPQLLQEEMT 202
Cdd:cd05156   86 TTDELSLPEISRKIARKMARFHSLE-----MPISKepkwLFDTMERWLKeALSILFTDEPTKPSKQLELLLSYDLAKELG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824018 203 WMKEILSSLGSPVVLCHND------LLCKNIIYNEKQgDVQFIDYEYSGYNYLAYDIGNHFNEFA---------GVSdVD 267
Cdd:cd05156  161 WLRSLLESTPSPVVFCHNDlqegniLLLNGPENSEDD-KLVLIDFEYCSYNYRGFDLANHFCEWAydytvpeppYFK-IN 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824018 268 YSLYPDRELQGQWLRSYLEAYKEYKG-FGSDVTEKEVETLFIQVNQFALASHFFWGLWALIQAKYSTIEFDFLGYAIVRF 346
Cdd:cd05156  239 PENYPTREQQLHFIRAYLDEQYKDKTnDLTEERSKEEEKLLLEVNRFALASHFFWGLWSIVQAKISSIEFGYLEYAQARL 318

                 ....*...
gi 157824018 347 NQYFKMKP 354
Cdd:cd05156  319 DAYFKQKE 326
PLN02236 PLN02236
choline kinase
26-356 1.26e-58

choline kinase


Pssm-ID: 177880 [Multi-domain]  Cd Length: 344  Bit Score: 193.34  E-value: 1.26e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824018  26 EQRCRDGALSLLQHLRPHW----DPREVTLQLFTDGITNKLIAC-YVGDTMDDV--VLVRIYGNKTELLVDRDEEVKSFR 98
Cdd:PLN02236  12 SGRIPDELKRILHSLASKWgdvvDDEALQVIPLKGAMTNEVFQIkWPTKEGNLGrkVLVRIYGEGVELFFDRDDEIRTFE 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824018  99 VLQAHGCAPQLYCTFNNGLCYEFIQGEALDPQHVCNPAIFRLIARQLAKIHAIHahngwIPKSN---LWLKMGKYFSLIP 175
Cdd:PLN02236  92 CMSRHGQGPRLLGRFPNGRVEEFIHARTLSAADLRDPEISALIAAKLREFHSLD-----MPGPKnvlLWDRLRNWLKEAK 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824018 176 TGFADEDINKRFLSEipspqlLQEEMTWMKEILSSLGSPVVLCHNDLLCKNIIYNEKQGDVQFIDYEYSGYNYLAYDIGN 255
Cdd:PLN02236 167 NLCSPEEAKEFRLDS------LEDEINLLEKELSGDDQEIGFCHNDLQYGNIMIDEETRAITIIDYEYASYNPVAYDIAN 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824018 256 HFNEFAGV--SD----VDYSLYPDRELQGQWLRSYLEAYkeykgfGSDVTEKEVETLFIQVNQFALASHFFWGLWALIQA 329
Cdd:PLN02236 241 HFCEMAADyhSEtphiLDYSKYPGEEERRRFIRTYLSSS------GEEPSDEEVEQLLDDVEKYTLASHLFWGLWGIISG 314
                        330       340
                 ....*....|....*....|....*..
gi 157824018 330 KYSTIEFDFLGYAIVRFNQYFKMKPEV 356
Cdd:PLN02236 315 HVNKIDFDYMEYARQRFEQYWLRKPEL 341
ChoK-like_euk cd14021
Euykaryotic Choline Kinase and similar proteins; This group is composed of eukaryotic choline ...
57-326 3.65e-46

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: 157.04  E-value: 3.65e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824018  57 GITNKL----IACYVGDTMDDVVLVRIYGNKTELLVDRDEEVKSFRVLQAHGCAPQLYCTFNNGLCYEFIQGEALDPQHV 132
Cdd:cd14021    9 GLTNQVykvsLKDESDSLEPKKVLFRIYGKYLSTLYDREKESEVFKILSEQGLGPKLIYKFDGGRIEEYIDGRPLTTDEL 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824018 133 CNPAIFRLIARQLAKIHAIHAhngwipksnlwlkmgkyfsliptgfadedinkrflseipspqllqeemtwmkeilsslg 212
Cdd:cd14021   89 RNPSVLTSIAKLLAKFHKIKT----------------------------------------------------------- 109
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824018 213 SPVVLCHNDLLCKNIIYNEKQGDVQFIDYEYSGYNYLAYDIGNHFNEFAGVSDV--------DYSLYPDRELQGQWLRSY 284
Cdd:cd14021  110 PPVVFCHNDLQENNILLTNDQDGLRLIDFEYSGFNYRGYDIANFFNESMIDYDHpeppyfkiYKENYISEEEKRLFVSVY 189
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 157824018 285 LEAYKEYKGFGSDvtEKEVETLFIQVNQFALASHFFWGLWAL 326
Cdd:cd14021  190 LSEYLEKNVLPSL--DKLVEQFLQEVEIFTLGSHLYWGLWSI 229
PTZ00296 PTZ00296
choline kinase; Provisional
43-361 3.62e-36

choline kinase; Provisional


Pssm-ID: 240350 [Multi-domain]  Cd Length: 442  Bit Score: 136.17  E-value: 3.62e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824018  43 HWDPREVTLQLFTDGITNKLIACYVG-DTMDDV------VLVRIYGNKTELLVDRDEEVKSFRVLQAHGCAPQLYCTFNN 115
Cdd:PTZ00296 102 RFTEDDVRVNQILSGLTNQLFEVSLKeETANNYpsirrrVLFRIYGKDVDELYNPISEFEVYKTMSKYRIAPQLLNTFSG 181
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824018 116 GLCYEFIQGEALDPQHVCNPAIFRLIARQLAKIHAI----HAHNGWiPKSNLWLKMGKYFSLIPTGFADEDINKRFLSei 191
Cdd:PTZ00296 182 GRIEEWLYGDPLRIDDLKNPSILIGIANVLGKFHTLsrkrHLPEHW-DRTPCIFKMMEKWKNQLSKYKNIEKYQRDIH-- 258
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824018 192 pspQLLQEEMTWMKEI-----LSSLGSPVVLCHNDLLCKNIIYNEKqgDVQFIDYEYSGYNYLAYDIGNHFNEFAgvsdV 266
Cdd:PTZ00296 259 ---KYIKESEKFIKFMkvyskSDNLANDIVFCHNDLQENNIINTNK--CLRLIDFEYSGYNFLATDIANFFIETT----I 329
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824018 267 DYSL------------YPDRELQGQWLRSYLEAYKEYKGFGSDvtEKEVETLFIQVNQFALASHFFWGLWALI---QAKy 331
Cdd:PTZ00296 330 DYSVshypffaidkkkYISYENRKLFITAYLSNYLDKSLVVPN--PKIIDQILEAVEVQALGAHLLWGFWSIIrgyQTK- 406
                        330       340       350
                 ....*....|....*....|....*....|
gi 157824018 332 STIEFDFLGYAIVRFNQYFKMKPEVTALKM 361
Cdd:PTZ00296 407 SYNEFDFFLYAKERFKMYDEQKEYLISNNI 436
ChoK-like cd05151
Choline Kinase and similar proteins; This subfamily is composed of bacterial and eukaryotic ...
49-260 5.33e-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: 96.08  E-value: 5.33e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824018  49 VTLQLFTDGITNKliaCYVGDTMDDVVLVRIYGNKTELLVDRDEEVKSFRVLQAHGCAPQ-LYCTFNNG-LCYEFIQGEA 126
Cdd:cd05151    1 ITIEPLKGGLTNK---NYLVEVAGKKYVLRIPGAGTELLIDRENEKANSKAAAELGIAPEvIYFDPETGvKITEFIEGAT 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824018 127 LDPQHVCNPAIFRLIARQLAKIHAihahngwipksnlwlkmgkyfsliptgfadedinkrflSEIPspqllqeemtwmke 206
Cdd:cd05151   78 LLTNDFSDPENLERIAALLRKLHS--------------------------------------SPLE-------------- 105
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 157824018 207 ilsslgsPVVLCHNDLLCKNIIYNEKQgdVQFIDYEYSGYNYLAYDIGNHFNEF 260
Cdd:cd05151  106 -------DLVLCHNDLVPGNFLLDDDR--LYLIDWEYAGMNDPLFDLAALFSEN 150
CotS COG0510
Thiamine kinase or a related kinase [Coenzyme transport and metabolism];
195-347 4.71e-15

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


Pssm-ID: 440276 [Multi-domain]  Cd Length: 156  Bit Score: 71.74  E-value: 4.71e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824018 195 QLLQEEMTWMKEILSSLGSPVVLCHNDLLCKNIIYNEkQGDVQFIDYEYSGYNYLAYDIGNHFNEFAgvsdvdyslyPDR 274
Cdd:COG0510   29 PELLRRLEELERALAARPLPLVLCHGDLHPGNFLVTD-DGRLYLIDWEYAGLGDPAFDLAALLVEYG----------LSP 97
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157824018 275 ELQGQWLRSYleaykeykgFGSDVTEKEVEtlfiQVNQFALASHFFWGLWALIQAKYSTiEFDFLGYAIVRFN 347
Cdd:COG0510   98 EQAEELLEAY---------GFGRPTEELLR----RLRAYRALADLLWALWALVRAAQEA-NGDLLKYLLRRLE 156
APH pfam01636
Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance ...
50-290 2.70e-12

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: 65.99  E-value: 2.70e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824018   50 TLQLFTDGITNKliACYVGDTMDDVVLvRIYgNKTELLVDRDEEVKSFRVLQAHG----CAPQLYCTFNNGLC-----YE 120
Cdd:pfam01636   1 TLRPISSGASNR--TYLVTTGDGRYVL-RLP-PPGRAAEELRRELALLRHLAAAGvppvPRVLAGCTDAELLGlpfllME 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824018  121 FIQGEAL--DPQHVCNPAIFRLIARQLAKIHAIHAHNG---WIPKSNLwlkmgkYFSLIPTGFADEDINKRFLSEIPspQ 195
Cdd:pfam01636  77 YLPGEVLarPLLPEERGALLEALGRALARLHAVDPAALplaGRLARLL------ELLRQLEAALARLLAAELLDRLE--E 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824018  196 LLQEEMTWMKEILSSlGSPVVLCHNDLLCKNIIYNEKQGDVQFIDYEYSGYNYLAYDIGNHFNEFagvsdvdyslypDRE 275
Cdd:pfam01636 149 LEERLLAALLALLPA-ELPPVLVHGDLHPGNLLVDPGGRVSGVIDFEDAGLGDPAYDLAILLNSW------------GRE 215
                         250
                  ....*....|....*
gi 157824018  276 LQGQWLRSYLEAYKE 290
Cdd:pfam01636 216 LGAELLAAYLAAYGA 230
PTZ00384 PTZ00384
choline kinase; Provisional
37-347 3.17e-09

choline kinase; Provisional


Pssm-ID: 173576 [Multi-domain]  Cd Length: 383  Bit Score: 57.87  E-value: 3.17e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824018  37 LQHLrPHWD---PREVTLQLFTDGITNKLIACYVGDTMDDV-----VLVRIYGNKTELLVDRDEEVKSFRVLQAHGCAPQ 108
Cdd:PTZ00384  39 IRHV-PFWNnvnPEFIEIKKMNNGITNQVYQATLVDGDKDRypiksVCIKKSSTYNSLVIDNDLQYNIAKLLGDNNFGPK 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824018 109 LYCTFNNGLCYEFIQGEALDPQHVCNPAIFRLIARQLAKIHAIHAHngWIPKSnlWLKMGKYFSLIPTGFAD-EDINKRF 187
Cdd:PTZ00384 118 IIGRFGDFTIQEWVEGNTMGIDSLQNLSVLTGIASSLAKFHKRVTE--LVPKE--WDRTPMFLTKISTWSQHvERIIKKY 193
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824018 188 LSEIPSPQLLQE-EMtwMKEILS-------SLGSPVVLCHNDLLCKNIIyNEKQGdVQFIDYEYSGYNYLAYDIGNHFNE 259
Cdd:PTZ00384 194 NLDFDYNELVQNyEL--FKKILNnhlntsnSITNSVLFCHNDLFFTNIL-DFNQG-IYFIDFDFAGFNYVGWEIANFFVK 269
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824018 260 FAGVSDVD---YSLYPD-----RELQGQWLRSYLEAYKEYKGFGSDVTEKEvetlFIQ-VNQFALASHFFWGLWALIQAK 330
Cdd:PTZ00384 270 LYIVYDPPtppYFNSDDslalsEEMKTIFVSVYLSQLLGKNVLPSDDLVKE----FLQsLEIHTLGVNLFWTYWGIVMND 345
                        330       340
                 ....*....|....*....|.
gi 157824018 331 YSTIEF----DFLGYAIVRFN 347
Cdd:PTZ00384 346 KPKNELskpvKFEAYAKFQYN 366
HomoserineK_II cd05153
Type II Homoserine Kinase; This subfamily is composed of unusual homoserine kinases, from a ...
119-331 8.07e-08

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: 53.03  E-value: 8.07e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824018 119 YEFIQGEALDPQhvcNPAIFRLIARQLAKIHAI-----------HAHNGWIPksnLWLKMGKYFSLIPTGFADedinkrf 187
Cdd:cd05153   94 FPFLPGESLTTP---TPEQCRAIGAALARLHLAlagfppprpnpRGLAWWKP---LAERLKARLDLLAADDRA------- 160
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824018 188 lseipspqLLQEEMTW-MKEILSSLgsPVVLCHNDLLCKNIIYNekqGD--VQFIDYEYSGYNYLAYDIGNHFNEFAgvS 264
Cdd:cd05153  161 --------LLEDELARlQALAPSDL--PRGVIHADLFRDNVLFD---GDrlSGIIDFYDACYDPLLYDLAIALNDWC--F 225
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 157824018 265 DVDYSLYPDRelqgqwLRSYLEAYKEYKGFgsdvTEKEVETLFIqvnQFALASHFFWgLWALIQAKY 331
Cdd:cd05153  226 DDDGKLDPER------AKALLAGYQSVRPL----TEEEKAALPL---LLRAAALRFW-LSRLYDFHL 278
SrkA COG2334
Ser/Thr protein kinase RdoA involved in Cpx stress response, MazF antagonist [Signal ...
118-288 4.88e-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: 50.69  E-value: 4.88e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824018 118 CYEFIQGEALDPQhvcNPAIFRLIARQLAKIHAIHAhnGWIPKSnlwlkmgkyfsliPTGFADEDINKRFL--SEIPSP- 194
Cdd:COG2334   93 LFPFLPGRSPEEP---SPEQLEELGRLLARLHRALA--DFPRPN-------------ARDLAWWDELLERLlgPLLPDPe 154
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824018 195 --QLLQEEMTWMKEILSSLGS--PVVLCHNDLLCKNIIYNEKQGDVqFIDYEYSGYNYLAYDIGnhfnefAGVSDVdysl 270
Cdd:COG2334  155 drALLEELLDRLEARLAPLLGalPRGVIHGDLHPDNVLFDGDGVSG-LIDFDDAGYGPRLYDLA------IALNGW---- 223
                        170
                 ....*....|....*...
gi 157824018 271 yPDRELQGQWLRSYLEAY 288
Cdd:COG2334  224 -ADGPLDPARLAALLEGY 240
YcbJ COG3173
Predicted kinase, aminoglycoside phosphotransferase (APT) family [General function prediction ...
36-299 3.03e-06

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


Pssm-ID: 442406 [Multi-domain]  Cd Length: 284  Bit Score: 48.19  E-value: 3.03e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824018  36 LLQHLRPHWDpREVTLQLFTDGITNKLiacYVGDTMDDVVLvRIY--GNKTELLVDRdeEvksFRVLQA-HGCA------ 106
Cdd:COG3173   11 LLAAQLPGLA-GLPEVEPLSGGWSNLT---YRLDTGDRLVL-RRPprGLASAHDVRR--E---ARVLRAlAPRLgvpvpr 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824018 107 PQLYCTFNNGL-----CYEFIQGEALDPQ-HVCNPAIFRLIARQLAK-IHAIHAhngwIPKSNLWLKMGKyfsliPTGFA 179
Cdd:COG3173   81 PLALGEDGEVIgapfyVMEWVEGETLEDAlPDLSPAERRALARALGEfLAALHA----VDPAAAGLADGR-----PEGLE 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824018 180 ------DEDINKRFLSEIPSPQLLQEEMTWMKEILSSLGsPVVLCHNDLLCKNIIYNEKQGDVQ-FIDYEYSGYNYLAYD 252
Cdd:COG3173  152 rqlarwRAQLRRALARTDDLPALRERLAAWLAANLPEWG-PPVLVHGDLRPGNLLVDPDDGRLTaVIDWELATLGDPAAD 230
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 157824018 253 IGNHFNEFAGVSDvdysLYPDRELqgqwlrsYLEAYKEYKGFGSDVT 299
Cdd:COG3173  231 LAYLLLYWRLPDD----LLGPRAA-------FLAAYEEATGDLDDLT 266
APH_ChoK_like cd05120
Aminoglycoside 3'-phosphotransferase and Choline Kinase family; This family is composed of APH, ...
214-260 4.16e-06

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: 46.14  E-value: 4.16e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 157824018 214 PVVLCHNDLLCKNIIYNEKQGDVQFIDYEYSGYNYLAYDIGNHFNEF 260
Cdd:cd05120  110 SSVLTHGDLHPGNILVKPDGKLSGIIDWEFAGYGPPAFDYAAALRDW 156
spore_CotS TIGR02906
spore coat protein, CotS family; Members of this family include the spore coat proteins CotS ...
109-323 5.00e-05

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: 44.58  E-value: 5.00e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824018  109 LYCTFNNGL--CYEFIQGEALDpqhVCNPAIFRLIARQLAKIHaiHAHNGWIPKSNL-----WLKMGKYF---------- 171
Cdd:TIGR02906  62 LYVKYNGDLyvLTEWIEGRECD---FNNPIDLKKAAKGLALFH--HASKGYVPPDGSkirskLGKWPKQFekrlkelerf 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824018  172 -SLIPTGFADEDINKRFLSEIP--------SPQLLQ--EEMTWMKEILSSLGspvvLCHNDLLCKNIIYneKQGDVQFID 240
Cdd:TIGR02906 137 kKIALEKKYKDEFDKLYLKEVDyflergkkALELLNksKYYDLCKEAKKIRG----FCHQDYAYHNILL--KDNEVYVID 210
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824018  241 YEYSGYNYLAYDIGNHFNEFA---GVSDVDyslypdrelqgqWLRSYLEAYKEYkgfgSDVTEKEVETLFIqvnqFALAS 317
Cdd:TIGR02906 211 FDYCTIDLPVRDLRKLIIKLMkknGVWDLE------------KAKEIIEAYSSI----NPLSKEEKEVLYI----DLAFP 270

                  ....*.
gi 157824018  318 HFFWGL 323
Cdd:TIGR02906 271 HKFWKI 276
EcKL pfam02958
Ecdysteroid kinase-like family; This family includes ecdysteroid 22-kinase, an enzyme ...
127-257 8.76e-04

Ecdysteroid kinase-like family; This family includes ecdysteroid 22-kinase, an enzyme responsible for the phosphorylation of ecdysteroids (insect growth and moulting hormones) at C-22, to form physiologically inactive ecdysteroid 22-phosphates. Most insects contain 12 to 105 genes encoding this family and yet so far only one enzyme (ecdysteroid 22-kinase from Bombyx mori) has characterized substrates (2-deoxyecdysone, ecdysone, 20-hydroxyecdysone). There are good reasons to believe that this family includes kinases that act on other small molecule substrates and that they may function in detoxification processes.


Pssm-ID: 397213 [Multi-domain]  Cd Length: 293  Bit Score: 40.72  E-value: 8.76e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824018  127 LDPQHVcnpaifRLIARQLAKIHAI-------------HAHNGWIPKSNLWLKMGKYFSLIPTGFADEDInKRFLSEIPS 193
Cdd:pfam02958 111 LDLEHT------KLVLEKLAKFHAAsaalkelqpevfkQLKKGLFEEDYVNGAIKEFFEPLMETGLDAAA-EALREQLPE 183
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 157824018  194 PQLLQEEMTWMK----EILSSLGSP-----VVLCHNDLLCKNII--YNEKQG--DVQFIDYEYSGYNYLAYDIgNHF 257
Cdd:pfam02958 184 YEKYAEKLEKLKdnyfDRLLRLVEPtpgefNVLNHGDLWVNNIMfkYDDEGEpeDVILVDFQLSRYGSPAIDL-NYF 259
CotI COG5881
Spore coat protein CotI/CotS, protein kinase superfamily [Cell cycle control, cell division, ...
108-323 1.07e-03

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: 40.65  E-value: 1.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824018 108 QLYCTFNNGLCY--EFIQGEALDpqhVCNPAIFRLIARQLAKIHA----IHAHNGWIPKSNL--WLK--------MGKYF 171
Cdd:COG5881   75 KPYVKYGGKLYYltEWIEGRECD---YKNPEDLKKAAETLAEFHKaskgFEPPPGSKGRSHLgkWPErfekrleeLEKFK 151
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824018 172 SLIPTGFADEDINKRFLSEIP--------SPQLLQEE--MTWMKEILSSLGspvvLCHNDLLCKNIIYNEKqGDVQFIDY 241
Cdd:COG5881  152 KIAEKKKNKNEFDRLFLKNIDyfleqaekALELLEKSayYKLVKEAKKEGG----FCHHDYAYHNILIDED-GKIYIIDF 226
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824018 242 EYSGYNYLAYDIGNHFNEF--AGVSDVDyslypdrelqgqWLRSYLEAY-KEYKgfgsdVTEKEVETLFIqvnqFALASH 318
Cdd:COG5881  227 DYCIYDLPVHDLAKLLRRVmkRGNWDIE------------KAKEILEAYnKINP-----LSKEEIEVLLA----FLLFPQ 285

                 ....*
gi 157824018 319 FFWGL 323
Cdd:COG5881  286 KFWRL 290
CHK smart00587
ZnF_C4 abd HLH domain containing kinases domain; subfamily of choline kinases
139-253 1.38e-03

ZnF_C4 abd HLH domain containing kinases domain; subfamily of choline kinases


Pssm-ID: 214734  Cd Length: 196  Bit Score: 39.24  E-value: 1.38e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824018   139 RLIARQLAKIHAIHAH-----NGWIPKS-NLWLKMGKYFSLIPTGFADEDINKRFLSEIPSP-----------QLLQEEM 201
Cdd:smart00587  26 SLVLKKLAKLHAASAVlieeeKGSYLEEfDEGLFERFKRMFSEEFIGGLENFLRELLSQPELlkveeyiekldKLLDNLE 105
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 157824018   202 TWMKEIL-SSLGSPVVLCHNDLLCKNIIY----NEKQGDVQFIDYEYSGYNYLAYDI 253
Cdd:smart00587 106 DLKKEDKePDEGEFNVLNHGDLWANNIMFkyddEGKPEDVALIDFQLSHYGSPAEDL 162
 
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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