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Conserved domains on  [gi|119593981|gb|EAW73575|]
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hCG16873, isoform CRA_a [Homo sapiens]

Protein Classification

choline/ethanolamine kinase family protein( domain architecture ID 10142383)

choline/ethanolamine kinase family protein catalyzes the phosphorylation of choline and/or ethanolamine

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ChoK_euk cd05156
Euykaryotic Choline Kinase; ChoK catalyzes the transfer of the gamma-phosphoryl group from ATP ...
69-385 0e+00

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: 552.62  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593981  69 LRVYPVSGGLSNLLFRCSLPDHLPSVGEEPREVLLRLYGAILQGVDSLVLESVMFAILAERSLGPQLYGVFPEGRLEQYI 148
Cdd:cd05156    1 FGIKTITGGLSNLLYLCSLPDGVVPVGGEPRKVLLRIYGQILQAEESLVTESVIFALLSERGLGPKLYGIFPGGRLEEFI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593981 149 PSRPLKTQELREPVLSAAIATKMAQFHGMEMPFTKEPHWLFGTMERYLKQIQDLPPTGLPE-----MNLLEMYSLKDEMG 223
Cdd:cd05156   81 PSRPLTTDELSLPEISRKIARKMARFHSLEMPISKEPKWLFDTMERWLKEALSILFTDEPTkpskqLELLLSYDLAKELG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593981 224 NLRKLLESTPSPVVFCHNDIQEGNILLLSEPE--NADSLMLVDFEYSSYNYRGFDIGNHFCEWVYDYTHEEWPFYKARPT 301
Cdd:cd05156  161 WLRSLLESTPSPVVFCHNDLQEGNILLLNGPEnsEDDKLVLIDFEYCSYNYRGFDLANHFCEWAYDYTVPEPPYFKINPE 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593981 302 DYPTQEQQLHFIRHYLAEAKKGET-LSQEEQRKLEEDLLVEVSRYALASHFFWGLWSILQASMSTIEFGYLDYAQSRFQF 380
Cdd:cd05156  241 NYPTREQQLHFIRAYLDEQYKDKTnDLTEERSKEEEKLLLEVNRFALASHFFWGLWSIVQAKISSIEFGYLEYAQARLDA 320

                 ....*
gi 119593981 381 YFQQK 385
Cdd:cd05156  321 YFKQK 325
 
Name Accession Description Interval E-value
ChoK_euk cd05156
Euykaryotic Choline Kinase; ChoK catalyzes the transfer of the gamma-phosphoryl group from ATP ...
69-385 0e+00

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: 552.62  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593981  69 LRVYPVSGGLSNLLFRCSLPDHLPSVGEEPREVLLRLYGAILQGVDSLVLESVMFAILAERSLGPQLYGVFPEGRLEQYI 148
Cdd:cd05156    1 FGIKTITGGLSNLLYLCSLPDGVVPVGGEPRKVLLRIYGQILQAEESLVTESVIFALLSERGLGPKLYGIFPGGRLEEFI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593981 149 PSRPLKTQELREPVLSAAIATKMAQFHGMEMPFTKEPHWLFGTMERYLKQIQDLPPTGLPE-----MNLLEMYSLKDEMG 223
Cdd:cd05156   81 PSRPLTTDELSLPEISRKIARKMARFHSLEMPISKEPKWLFDTMERWLKEALSILFTDEPTkpskqLELLLSYDLAKELG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593981 224 NLRKLLESTPSPVVFCHNDIQEGNILLLSEPE--NADSLMLVDFEYSSYNYRGFDIGNHFCEWVYDYTHEEWPFYKARPT 301
Cdd:cd05156  161 WLRSLLESTPSPVVFCHNDLQEGNILLLNGPEnsEDDKLVLIDFEYCSYNYRGFDLANHFCEWAYDYTVPEPPYFKINPE 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593981 302 DYPTQEQQLHFIRHYLAEAKKGET-LSQEEQRKLEEDLLVEVSRYALASHFFWGLWSILQASMSTIEFGYLDYAQSRFQF 380
Cdd:cd05156  241 NYPTREQQLHFIRAYLDEQYKDKTnDLTEERSKEEEKLLLEVNRFALASHFFWGLWSIVQAKISSIEFGYLEYAQARLDA 320

                 ....*
gi 119593981 381 YFQQK 385
Cdd:cd05156  321 YFKQK 325
Choline_kinase pfam01633
Choline/ethanolamine kinase; Choline kinase catalyzes the committed step in the synthesis of ...
97-308 1.53e-93

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: 279.16  E-value: 1.53e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593981   97 EPREVLLRLYGAILQGVDSLVLESVMFAILAERSLGPQLYGVFPEGRLEQYIPSRPLKTQELREPVLSAAIATKMAQFHG 176
Cdd:pfam01633   1 SPRKVLLRIYGPGTELLINREDEIVNFALLSERGLGPKLYGFFPNGRIEEFIPSRTLSTEDLRDPEISKLIAKRLAELHS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593981  177 MEMPFTKEPhWLFGTMERYLKQIQDLP-PTGLP---EMNLLEMYSLKDEMGNLRKLLESTPSPVVFCHNDIQEGNILLLS 252
Cdd:pfam01633  81 LEMPGKKSP-SLWKTMRKWLSLLKNLGaPESVNkseQLKSINLEDLEKEINKLEKWLELLDSPIVFCHNDLQSGNILLLN 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 119593981  253 EpenADSLMLVDFEYSSYNYRGFDIGNHFCEWVYDYTHEEwPFYKARPTDYPTQEQ 308
Cdd:pfam01633 160 E---TKRLVLIDFEYASYNYRGFDIANHFCEWAGDYHDPT-PFFKCDYSLYPTREE 211
PLN02236 PLN02236
choline kinase
57-388 1.31e-76

choline kinase


Pssm-ID: 177880 [Multi-domain]  Cd Length: 344  Bit Score: 240.72  E-value: 1.31e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593981  57 LGGAWRRV-QPEELRVYPVSGGLSNLLFRCSLPDhlpSVGEEPREVLLRLYGailQGVDSLVL---ESVMFAILAERSLG 132
Cdd:PLN02236  26 LASKWGDVvDDEALQVIPLKGAMTNEVFQIKWPT---KEGNLGRKVLVRIYG---EGVELFFDrddEIRTFECMSRHGQG 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593981 133 PQLYGVFPEGRLEQYIPSRPLKTQELREPVLSAAIATKMAQFHGMEMPFTKEPHwLFGTMERYLKQIQDL-PPTglpEMN 211
Cdd:PLN02236 100 PRLLGRFPNGRVEEFIHARTLSAADLRDPEISALIAAKLREFHSLDMPGPKNVL-LWDRLRNWLKEAKNLcSPE---EAK 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593981 212 LLEMYSLKDEMGNLRKLLESTPSPVVFCHNDIQEGNILLlsePENADSLMLVDFEYSSYNYRGFDIGNHFCEWVYDYtHE 291
Cdd:PLN02236 176 EFRLDSLEDEINLLEKELSGDDQEIGFCHNDLQYGNIMI---DEETRAITIIDYEYASYNPVAYDIANHFCEMAADY-HS 251
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593981 292 EWPF---YkarpTDYPTQEQQLHFIRHYLAEAkkGETLSQEEQrkleEDLLVEVSRYALASHFFWGLWSILQASMSTIEF 368
Cdd:PLN02236 252 ETPHildY----SKYPGEEERRRFIRTYLSSS--GEEPSDEEV----EQLLDDVEKYTLASHLFWGLWGIISGHVNKIDF 321
                        330       340
                 ....*....|....*....|
gi 119593981 369 GYLDYAQSRFQFYFQQKGQL 388
Cdd:PLN02236 322 DYMEYARQRFEQYWLRKPEL 341
CotS COG0510
Thiamine kinase or a related kinase [Coenzyme transport and metabolism];
173-379 4.70e-15

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


Pssm-ID: 440276 [Multi-domain]  Cd Length: 156  Bit Score: 72.12  E-value: 4.70e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593981 173 QFHGMEMPFTKEPhwlfgtmERYLKQIQDLPPTGLPEmnllemysLKDEMGNLRKLLESTPSPVVFCHNDIQEGNILLls 252
Cdd:COG0510    1 RLHASPALLRFDL-------FARLERYLALGPRDLPE--------LLRRLEELERALAARPLPLVLCHGDLHPGNFLV-- 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593981 253 epENADSLMLVDFEYSSYNYRGFDIGNHFCEWVYDytheewpfykarptdyptQEQQLHFIRHYLAEAkkgetlsqeeqr 332
Cdd:COG0510   64 --TDDGRLYLIDWEYAGLGDPAFDLAALLVEYGLS------------------PEQAEELLEAYGFGR------------ 111
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 119593981 333 kLEEDLLVEVSRYALASHFFWGLWSILQASmSTIEFGYLDYAQSRFQ 379
Cdd:COG0510  112 -PTEELLRRLRAYRALADLLWALWALVRAA-QEANGDLLKYLLRRLE 156
spore_CotS TIGR02906
spore coat protein, CotS family; Members of this family include the spore coat proteins CotS ...
166-279 1.36e-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: 40.34  E-value: 1.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593981  166 AIATKMAQFH----GMEMPFTKEPHWLFGTM-ERYLKQIQDLpptgLPEMNLLEMYSLKDEMGNL--------------- 225
Cdd:TIGR02906  92 KAAKGLALFHhaskGYVPPDGSKIRSKLGKWpKQFEKRLKEL----ERFKKIALEKKYKDEFDKLylkevdyflergkka 167
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119593981  226 -RKLLESTPSPVV--------FCHNDIQEGNILLlsepeNADSLMLVDFEYSSYNYRGFDIGN 279
Cdd:TIGR02906 168 lELLNKSKYYDLCkeakkirgFCHQDYAYHNILL-----KDNEVYVIDFDYCTIDLPVRDLRK 225
 
Name Accession Description Interval E-value
ChoK_euk cd05156
Euykaryotic Choline Kinase; ChoK catalyzes the transfer of the gamma-phosphoryl group from ATP ...
69-385 0e+00

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: 552.62  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593981  69 LRVYPVSGGLSNLLFRCSLPDHLPSVGEEPREVLLRLYGAILQGVDSLVLESVMFAILAERSLGPQLYGVFPEGRLEQYI 148
Cdd:cd05156    1 FGIKTITGGLSNLLYLCSLPDGVVPVGGEPRKVLLRIYGQILQAEESLVTESVIFALLSERGLGPKLYGIFPGGRLEEFI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593981 149 PSRPLKTQELREPVLSAAIATKMAQFHGMEMPFTKEPHWLFGTMERYLKQIQDLPPTGLPE-----MNLLEMYSLKDEMG 223
Cdd:cd05156   81 PSRPLTTDELSLPEISRKIARKMARFHSLEMPISKEPKWLFDTMERWLKEALSILFTDEPTkpskqLELLLSYDLAKELG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593981 224 NLRKLLESTPSPVVFCHNDIQEGNILLLSEPE--NADSLMLVDFEYSSYNYRGFDIGNHFCEWVYDYTHEEWPFYKARPT 301
Cdd:cd05156  161 WLRSLLESTPSPVVFCHNDLQEGNILLLNGPEnsEDDKLVLIDFEYCSYNYRGFDLANHFCEWAYDYTVPEPPYFKINPE 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593981 302 DYPTQEQQLHFIRHYLAEAKKGET-LSQEEQRKLEEDLLVEVSRYALASHFFWGLWSILQASMSTIEFGYLDYAQSRFQF 380
Cdd:cd05156  241 NYPTREQQLHFIRAYLDEQYKDKTnDLTEERSKEEEKLLLEVNRFALASHFFWGLWSIVQAKISSIEFGYLEYAQARLDA 320

                 ....*
gi 119593981 381 YFQQK 385
Cdd:cd05156  321 YFKQK 325
ETNK_euk cd05157
Euykaryotic Ethanolamine kinase; ETNK catalyzes the transfer of the gamma-phosphoryl group ...
69-382 1.14e-105

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: 313.75  E-value: 1.14e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593981  69 LRVYPVSGGLSNLLFRCSLPDhlpsvGEEPREVLLRLYGAilqGVDSLV---LESVMFAILAERSLGPQLYGVFPEGRLE 145
Cdd:cd05157    1 IKVKRITGGITNALYKVTYPS-----GDTPKTVLVRIYGP---GTELLIdrdRELRILQLLSRAGIGPKLYGRFENGRVE 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593981 146 QYIPSRPLKTQELREPVLSAAIATKMAQFHGMEMPFTKEPHW---LFGTMERYLKQIQDLPPTGLPEMNLLEMYS---LK 219
Cdd:cd05157   73 EFLPGRTLTPEDLRDPKISRLIARRLAELHSIVPLGEIEGKKkpiLWTTIRKWLDLAPEVFEDEKNKEKKLEKVDlerLR 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593981 220 DEMGNLRKLLES-TPSPVVFCHNDIQEGNILLlsePENADSLMLVDFEYSSYNYRGFDIGNHFCEWVYDYTHEEWpfyka 298
Cdd:cd05157  153 KELEWLEKWLESlEKSPIVFCHNDLLYGNILY---NEDDDSVTFIDFEYAGPNPRAFDIANHFCEWAGFYCVLDY----- 224
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593981 299 rpTDYPTQEQQLHFIRHYLAEAKKGETLSQEEQRKLEEdLLVEVSRYALASHFFWGLWSILQASMSTIEFGYLDYAQSRF 378
Cdd:cd05157  225 --SRYPTKEEQRNFLRAYLESLDGLPGGEEVSEEEVEK-LYNEVNLFRLASHLFWGLWALIQAAISSIDFDYLGYAKERL 301

                 ....
gi 119593981 379 QFYF 382
Cdd:cd05157  302 DEYW 305
ChoK-like_euk cd14021
Euykaryotic Choline Kinase and similar proteins; This group is composed of eukaryotic choline ...
69-358 1.35e-95

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: 285.32  E-value: 1.35e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593981  69 LRVYPVSGGLSNLLFRCSLPDHLPSVgeEPREVLLRLYGAILQGVDSLVLESVMFAILAERSLGPQLYGVFPEGRLEQYI 148
Cdd:cd14021    1 ILVIRILSGLTNQVYKVSLKDESDSL--EPKKVLFRIYGKYLSTLYDREKESEVFKILSEQGLGPKLIYKFDGGRIEEYI 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593981 149 PSRPLKTQELREPVLSAAIATKMAQFHGMEMPftkephwlfgtmerylkqiqdlpptglpemnllemyslkdemgnlrkl 228
Cdd:cd14021   79 DGRPLTTDELRNPSVLTSIAKLLAKFHKIKTP------------------------------------------------ 110
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593981 229 lestpsPVVFCHNDIQEGNILLLSepeNADSLMLVDFEYSSYNYRGFDIGNHFCEWVYDYTHEEWPFYKARPTDYPTQEQ 308
Cdd:cd14021  111 ------PVVFCHNDLQENNILLTN---DQDGLRLIDFEYSGFNYRGYDIANFFNESMIDYDHPEPPYFKIYKENYISEEE 181
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 119593981 309 QLHFIRHYLAEAKkgETLSQEEQRKLEEDLLVEVSRYALASHFFWGLWSI 358
Cdd:cd14021  182 KRLFVSVYLSEYL--EKNVLPSLDKLVEQFLQEVEIFTLGSHLYWGLWSI 229
Choline_kinase pfam01633
Choline/ethanolamine kinase; Choline kinase catalyzes the committed step in the synthesis of ...
97-308 1.53e-93

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: 279.16  E-value: 1.53e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593981   97 EPREVLLRLYGAILQGVDSLVLESVMFAILAERSLGPQLYGVFPEGRLEQYIPSRPLKTQELREPVLSAAIATKMAQFHG 176
Cdd:pfam01633   1 SPRKVLLRIYGPGTELLINREDEIVNFALLSERGLGPKLYGFFPNGRIEEFIPSRTLSTEDLRDPEISKLIAKRLAELHS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593981  177 MEMPFTKEPhWLFGTMERYLKQIQDLP-PTGLP---EMNLLEMYSLKDEMGNLRKLLESTPSPVVFCHNDIQEGNILLLS 252
Cdd:pfam01633  81 LEMPGKKSP-SLWKTMRKWLSLLKNLGaPESVNkseQLKSINLEDLEKEINKLEKWLELLDSPIVFCHNDLQSGNILLLN 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 119593981  253 EpenADSLMLVDFEYSSYNYRGFDIGNHFCEWVYDYTHEEwPFYKARPTDYPTQEQ 308
Cdd:pfam01633 160 E---TKRLVLIDFEYASYNYRGFDIANHFCEWAGDYHDPT-PFFKCDYSLYPTREE 211
PLN02236 PLN02236
choline kinase
57-388 1.31e-76

choline kinase


Pssm-ID: 177880 [Multi-domain]  Cd Length: 344  Bit Score: 240.72  E-value: 1.31e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593981  57 LGGAWRRV-QPEELRVYPVSGGLSNLLFRCSLPDhlpSVGEEPREVLLRLYGailQGVDSLVL---ESVMFAILAERSLG 132
Cdd:PLN02236  26 LASKWGDVvDDEALQVIPLKGAMTNEVFQIKWPT---KEGNLGRKVLVRIYG---EGVELFFDrddEIRTFECMSRHGQG 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593981 133 PQLYGVFPEGRLEQYIPSRPLKTQELREPVLSAAIATKMAQFHGMEMPFTKEPHwLFGTMERYLKQIQDL-PPTglpEMN 211
Cdd:PLN02236 100 PRLLGRFPNGRVEEFIHARTLSAADLRDPEISALIAAKLREFHSLDMPGPKNVL-LWDRLRNWLKEAKNLcSPE---EAK 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593981 212 LLEMYSLKDEMGNLRKLLESTPSPVVFCHNDIQEGNILLlsePENADSLMLVDFEYSSYNYRGFDIGNHFCEWVYDYtHE 291
Cdd:PLN02236 176 EFRLDSLEDEINLLEKELSGDDQEIGFCHNDLQYGNIMI---DEETRAITIIDYEYASYNPVAYDIANHFCEMAADY-HS 251
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593981 292 EWPF---YkarpTDYPTQEQQLHFIRHYLAEAkkGETLSQEEQrkleEDLLVEVSRYALASHFFWGLWSILQASMSTIEF 368
Cdd:PLN02236 252 ETPHildY----SKYPGEEERRRFIRTYLSSS--GEEPSDEEV----EQLLDDVEKYTLASHLFWGLWGIISGHVNKIDF 321
                        330       340
                 ....*....|....*....|
gi 119593981 369 GYLDYAQSRFQFYFQQKGQL 388
Cdd:PLN02236 322 DYMEYARQRFEQYWLRKPEL 341
PLN02421 PLN02421
phosphotransferase, alcohol group as acceptor/kinase
53-394 8.60e-65

phosphotransferase, alcohol group as acceptor/kinase


Pssm-ID: 215231 [Multi-domain]  Cd Length: 330  Bit Score: 209.98  E-value: 8.60e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593981  53 CREYLGGaWRRVQPEELRVYPVSGGLSNLLFRCSLPDhlpsVGEEPREVLLRLYGAILQGVDSLVLESVMFAILAERSLG 132
Cdd:PLN02421   2 CKALFKG-WSDLDDSDFSVERISGGITNLLLKVSVKE----ENGNEVSVTVRLFGPNTDYVIDRERELQAIKYLSAAGFG 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593981 133 PQLYGVFPEGRLEQYIPSRPLKTQELREPVLSAAIATKMAQFHGMEMPFTKEPHwLFGTMERYLKQIQDLPPTGLPEMNL 212
Cdd:PLN02421  77 AKLLGVFGNGMIQSFINARTLTPSDMRKPKVAAEIAKELRRLHQVEIPGSKEPQ-LWNDIFKFYEKASTVKFEDPEKQKK 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593981 213 LEMYS---LKDEMGNLRKLLESTPSPVVFCHNDIQEGNILLlsePENADSLMLVDFEYSSYNYRGFDIGNHFCEWV---Y 286
Cdd:PLN02421 156 YETISfeeLRDEIVELKEITDSLKAPVVFAHNDLLSGNLML---NEDEGKLYFIDFEYGSYSYRGYDIGNHFNEYAgfdC 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593981 287 DYTHeewpfykarptdYPTQEQQLHFIRHYLAEAKKGETLSQEeqrkLEEdLLVEVSRYALASHFFWGLWSILQASMSTI 366
Cdd:PLN02421 233 DYSL------------YPSKEEQYHFFRHYLRPDDPEEVSDAE----LEE-LFVETNFYALASHLYWAIWAIVQAKMSPI 295
                        330       340
                 ....*....|....*....|....*...
gi 119593981 367 EFGYLDYAQSRFQFYFQQKGQLTSVHSS 394
Cdd:PLN02421 296 DFDYLGYFFLRYKEYKRQKEKLLSLVRS 323
PTZ00296 PTZ00296
choline kinase; Provisional
61-390 4.96e-51

choline kinase; Provisional


Pssm-ID: 240350 [Multi-domain]  Cd Length: 442  Bit Score: 177.00  E-value: 4.96e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593981  61 WRRVQPEELRVYPVSGGLSNLLFRCSLP-DHLPSVGEEPREVLLRLYGAILQGVDSLVLESVMFAILAERSLGPQLYGVF 139
Cdd:PTZ00296 100 WRRFTEDDVRVNQILSGLTNQLFEVSLKeETANNYPSIRRRVLFRIYGKDVDELYNPISEFEVYKTMSKYRIAPQLLNTF 179
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593981 140 PEGRLEQYIPSRPLKTQELREPVLSAAIATKMAQFHGM----EMP--FTKEP-------HWL-----FGTMERYLKQIQD 201
Cdd:PTZ00296 180 SGGRIEEWLYGDPLRIDDLKNPSILIGIANVLGKFHTLsrkrHLPehWDRTPcifkmmeKWKnqlskYKNIEKYQRDIHK 259
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593981 202 LPPTGLPEMNLLEMYSLKDEMGNlrkllestpsPVVFCHNDIQEGNILllsepENADSLMLVDFEYSSYNYRGFDIGNHF 281
Cdd:PTZ00296 260 YIKESEKFIKFMKVYSKSDNLAN----------DIVFCHNDLQENNII-----NTNKCLRLIDFEYSGYNFLATDIANFF 324
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593981 282 CEWVYDYTHEEWPFYKARPTDYPTQEQQLHFIRHYLAEAKKGETLSQEEqrKLEEDLLVEVSRYALASHFFWGLWSILQA 361
Cdd:PTZ00296 325 IETTIDYSVSHYPFFAIDKKKYISYENRKLFITAYLSNYLDKSLVVPNP--KIIDQILEAVEVQALGAHLLWGFWSIIRG 402
                        330       340       350
                 ....*....|....*....|....*....|.
gi 119593981 362 --SMSTIEFGYLDYAQSRFQFYFQQKGQLTS 390
Cdd:PTZ00296 403 yqTKSYNEFDFFLYAKERFKMYDEQKEYLIS 433
ChoK-like cd05151
Choline Kinase and similar proteins; This subfamily is composed of bacterial and eukaryotic ...
69-286 4.75e-29

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: 110.34  E-value: 4.75e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593981  69 LRVYPVSGGLSNLLFRCSLPDhlpsvgeepREVLLRLYGAILQGVDSLVLESVMFAILAERSLGPQLYGVFPE--GRLEQ 146
Cdd:cd05151    1 ITIEPLKGGLTNKNYLVEVAG---------KKYVLRIPGAGTELLIDRENEKANSKAAAELGIAPEVIYFDPEtgVKITE 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593981 147 YIPSRPLKTQELREPVLSAAIATKMAQFHGMEMPftkephwlfgtmerylkqiqdlpptglpemnllemyslkdemgnlr 226
Cdd:cd05151   72 FIEGATLLTNDFSDPENLERIAALLRKLHSSPLE---------------------------------------------- 105
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593981 227 kllestpsPVVFCHNDIQEGNILLlsepeNADSLMLVDFEYSSYNYRGFDIGNHFCEWVY 286
Cdd:cd05151  106 --------DLVLCHNDLVPGNFLL-----DDDRLYLIDWEYAGMNDPLFDLAALFSENNL 152
APH_ChoK_like cd05120
Aminoglycoside 3'-phosphotransferase and Choline Kinase family; This family is composed of APH, ...
69-286 4.95e-20

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: 86.20  E-value: 4.95e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593981  69 LRVYPVSGGLSNLLFRCSlpdhlpsvgeEPREVLLRLYGAILQgvDSLVLESVMFAILAERS--LGPQLYGVFP----EG 142
Cdd:cd05120    1 ISVKLIKEGGDNKVYLLG----------DPREYVLKIGPPRLK--KDLEKEAAMLQLLAGKLslPVPKVYGFGEsdgwEY 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593981 143 RLEQYIPSRPLKTQ-----ELREPVLSAAIATKMAQFHGMEMPftkephwlfgtmerylkqiqdlpptglpemnllemys 217
Cdd:cd05120   69 LLMERIEGETLSEVwprlsEEEKEKIADQLAEILAALHRIDSS------------------------------------- 111
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119593981 218 lkdemgnlrkllestpspvVFCHNDIQEGNILLLSEPEnadSLMLVDFEYSSYNYRGFDIGNHFCEWVY 286
Cdd:cd05120  112 -------------------VLTHGDLHPGNILVKPDGK---LSGIIDWEFAGYGPPAFDYAAALRDWTE 158
CotS COG0510
Thiamine kinase or a related kinase [Coenzyme transport and metabolism];
173-379 4.70e-15

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


Pssm-ID: 440276 [Multi-domain]  Cd Length: 156  Bit Score: 72.12  E-value: 4.70e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593981 173 QFHGMEMPFTKEPhwlfgtmERYLKQIQDLPPTGLPEmnllemysLKDEMGNLRKLLESTPSPVVFCHNDIQEGNILLls 252
Cdd:COG0510    1 RLHASPALLRFDL-------FARLERYLALGPRDLPE--------LLRRLEELERALAARPLPLVLCHGDLHPGNFLV-- 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593981 253 epENADSLMLVDFEYSSYNYRGFDIGNHFCEWVYDytheewpfykarptdyptQEQQLHFIRHYLAEAkkgetlsqeeqr 332
Cdd:COG0510   64 --TDDGRLYLIDWEYAGLGDPAFDLAALLVEYGLS------------------PEQAEELLEAYGFGR------------ 111
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 119593981 333 kLEEDLLVEVSRYALASHFFWGLWSILQASmSTIEFGYLDYAQSRFQ 379
Cdd:COG0510  112 -PTEELLRRLRAYRALADLLWALWALVRAA-QEANGDLLKYLLRRLE 156
PTZ00384 PTZ00384
choline kinase; Provisional
61-381 7.12e-15

choline kinase; Provisional


Pssm-ID: 173576 [Multi-domain]  Cd Length: 383  Bit Score: 75.58  E-value: 7.12e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593981  61 WRRVQPEELRVYPVSGGLSNLLFRCSLPDhlpsvGEEPREVLLRLYGAILQGVDSLVLES-VMFAI---LAERSLGPQLY 136
Cdd:PTZ00384  45 WNNVNPEFIEIKKMNNGITNQVYQATLVD-----GDKDRYPIKSVCIKKSSTYNSLVIDNdLQYNIaklLGDNNFGPKII 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593981 137 GVFPEGRLEQYIPSRPLKTQELREPVLSAAIATKMAQFHG------------MEMPFTK----EPHwlfgtMERYLKQIQ 200
Cdd:PTZ00384 120 GRFGDFTIQEWVEGNTMGIDSLQNLSVLTGIASSLAKFHKrvtelvpkewdrTPMFLTKistwSQH-----VERIIKKYN 194
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593981 201 dlppTGLPEMNLLEMYSL-KDEMGNLRKLLESTPSPVVFCHNDIQEGNILllsepENADSLMLVDFEYSSYNYRGFDIGN 279
Cdd:PTZ00384 195 ----LDFDYNELVQNYELfKKILNNHLNTSNSITNSVLFCHNDLFFTNIL-----DFNQGIYFIDFDFAGFNYVGWEIAN 265
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593981 280 HFCEWVYDYTHEEWPFYKARPTDYPTQEQQLHFIRHYLAEAKKGETLSQEEqrkLEEDLLVEVSRYALASHFFWGLWSIL 359
Cdd:PTZ00384 266 FFVKLYIVYDPPTPPYFNSDDSLALSEEMKTIFVSVYLSQLLGKNVLPSDD---LVKEFLQSLEIHTLGVNLFWTYWGIV 342
                        330       340
                 ....*....|....*....|....
gi 119593981 360 QASMSTIE--FGYLDYAQSRFQFY 381
Cdd:PTZ00384 343 MNDKPKNElsKPVKFEAYAKFQYN 366
APH pfam01636
Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance ...
73-284 1.74e-04

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: 42.87  E-value: 1.74e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593981   73 PVSGGLSNLLFRcslpdhlpsVGEEPREVLLRLYgAILQGVDSLVLESVMFAILAERSLGP---QLYGVFPEGRLE---- 145
Cdd:pfam01636   4 PISSGASNRTYL---------VTTGDGRYVLRLP-PPGRAAEELRRELALLRHLAAAGVPPvprVLAGCTDAELLGlpfl 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593981  146 --QYIPSRPLKTQELREPVLS-----AAIATKMAQFHGMEMPFTKEPHWLfGTMERYLKQIQDLPPTGLPEMNLLEMysL 218
Cdd:pfam01636  74 lmEYLPGEVLARPLLPEERGAllealGRALARLHAVDPAALPLAGRLARL-LELLRQLEAALARLLAAELLDRLEEL--E 150
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119593981  219 KDEMGNLRKLLESTpSPVVFCHNDIQEGNILLLSEPEnadSLMLVDFEYSSYNYRGFDIG---NHFCEW 284
Cdd:pfam01636 151 ERLLAALLALLPAE-LPPVLVHGDLHPGNLLVDPGGR---VSGVIDFEDAGLGDPAYDLAillNSWGRE 215
YcbJ COG3173
Predicted kinase, aminoglycoside phosphotransferase (APT) family [General function prediction ...
51-285 2.84e-04

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


Pssm-ID: 442406 [Multi-domain]  Cd Length: 284  Bit Score: 42.41  E-value: 2.84e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593981  51 QWCREYLGGAWRRVqpeelRVYPVSGGLSNLLFRCSLPDhlpsvgeeprEVLLRLYGAILQGVDSLVLEsvmFAILA--E 128
Cdd:COG3173   10 ALLAAQLPGLAGLP-----EVEPLSGGWSNLTYRLDTGD----------RLVLRRPPRGLASAHDVRRE---ARVLRalA 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593981 129 RSLG---PQLYGVFPEGR-------LEQYIPSRPLKTQELRE-PVLSAAIATKMAQF----HGMEMP----FTKEPHWLF 189
Cdd:COG3173   72 PRLGvpvPRPLALGEDGEvigapfyVMEWVEGETLEDALPDLsPAERRALARALGEFlaalHAVDPAaaglADGRPEGLE 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593981 190 GTMERYLKQIQDLPPTGLPEMNLLEmyslkdemgNLRKLLEST---PSPVVFCHNDIQEGNILLlsEPENADSLMLVDFE 266
Cdd:COG3173  152 RQLARWRAQLRRALARTDDLPALRE---------RLAAWLAANlpeWGPPVLVHGDLRPGNLLV--DPDDGRLTAVIDWE 220
                        250
                 ....*....|....*....
gi 119593981 267 YSSYNYRGFDIGNHFCEWV 285
Cdd:COG3173  221 LATLGDPAADLAYLLLYWR 239
HomoserineK_II cd05153
Type II Homoserine Kinase; This subfamily is composed of unusual homoserine kinases, from a ...
147-282 9.81e-04

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: 40.70  E-value: 9.81e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593981 147 YIPSRPLKTqelREPVLSAAIATKMAQFH--GMEMPFTKEPHWLFGTMERYLKQIQDLPPTGLPEMNLLemysLKDEMGN 224
Cdd:cd05153   96 FLPGESLTT---PTPEQCRAIGAALARLHlaLAGFPPPRPNPRGLAWWKPLAERLKARLDLLAADDRAL----LEDELAR 168
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 119593981 225 LRKLLESTPsPVVFCHNDIQEGNILLlsepeNADSLM-LVDFEYSSYNYRGFDIG---NHFC 282
Cdd:cd05153  169 LQALAPSDL-PRGVIHADLFRDNVLF-----DGDRLSgIIDFYDACYDPLLYDLAialNDWC 224
spore_CotS TIGR02906
spore coat protein, CotS family; Members of this family include the spore coat proteins CotS ...
166-279 1.36e-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: 40.34  E-value: 1.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119593981  166 AIATKMAQFH----GMEMPFTKEPHWLFGTM-ERYLKQIQDLpptgLPEMNLLEMYSLKDEMGNL--------------- 225
Cdd:TIGR02906  92 KAAKGLALFHhaskGYVPPDGSKIRSKLGKWpKQFEKRLKEL----ERFKKIALEKKYKDEFDKLylkevdyflergkka 167
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119593981  226 -RKLLESTPSPVV--------FCHNDIQEGNILLlsepeNADSLMLVDFEYSSYNYRGFDIGN 279
Cdd:TIGR02906 168 lELLNKSKYYDLCkeakkirgFCHQDYAYHNILL-----KDNEVYVIDFDYCTIDLPVRDLRK 225
 
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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