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Conserved domains on  [gi|1774753247|ref|NP_001363150|]
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choline kinase alpha isoform e [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 ...
1-330 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: 535.28  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774753247   1 MLFQCSLPDTTATLGDEPRKVLLRLYGAILQmrscnkegseqaqkenefqGAEAMVLESVMFAILAERSLGPKLYGIFPQ 80
Cdd:cd05156    13 LLYLCSLPDGVVPVGGEPRKVLLRIYGQILQ-------------------AEESLVTESVIFALLSERGLGPKLYGIFPG 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774753247  81 GRLEQFIPSRRLDTEELSLPDISAEIAEKMATFHGMKMPFNKEPKWLFGTMEKYLKEVLRIKFTEESRI--KKLHKLLSY 158
Cdd:cd05156    74 GRLEEFIPSRPLTTDELSLPEISRKIARKMARFHSLEMPISKEPKWLFDTMERWLKEALSILFTDEPTKpsKQLELLLSY 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774753247 159 NLPLELENLRSLLESTPSPVVFCHNDCQEGNILLLEGRENSEKQKLMLIDFEYSSYNYRGFDIGNHFCEWMYDYSYEKYP 238
Cdd:cd05156   154 DLAKELGWLRSLLESTPSPVVFCHNDLQEGNILLLNGPENSEDDKLVLIDFEYCSYNYRGFDLANHFCEWAYDYTVPEPP 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774753247 239 FFRANIRKYPTKKQQLHFISSYLPAFQNDFENLSTEEKSIIKEEMLLEVNRFALASHFLWGLWSIVQAKISSIEFGYMDY 318
Cdd:cd05156   234 YFKINPENYPTREQQLHFIRAYLDEQYKDKTNDLTEERSKEEEKLLLEVNRFALASHFFWGLWSIVQAKISSIEFGYLEY 313
                         330
                  ....*....|..
gi 1774753247 319 AQARFDAYFHQK 330
Cdd:cd05156   314 AQARLDAYFKQK 325
 
Name Accession Description Interval E-value
ChoK_euk cd05156
Euykaryotic Choline Kinase; ChoK catalyzes the transfer of the gamma-phosphoryl group from ATP ...
1-330 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: 535.28  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774753247   1 MLFQCSLPDTTATLGDEPRKVLLRLYGAILQmrscnkegseqaqkenefqGAEAMVLESVMFAILAERSLGPKLYGIFPQ 80
Cdd:cd05156    13 LLYLCSLPDGVVPVGGEPRKVLLRIYGQILQ-------------------AEESLVTESVIFALLSERGLGPKLYGIFPG 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774753247  81 GRLEQFIPSRRLDTEELSLPDISAEIAEKMATFHGMKMPFNKEPKWLFGTMEKYLKEVLRIKFTEESRI--KKLHKLLSY 158
Cdd:cd05156    74 GRLEEFIPSRPLTTDELSLPEISRKIARKMARFHSLEMPISKEPKWLFDTMERWLKEALSILFTDEPTKpsKQLELLLSY 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774753247 159 NLPLELENLRSLLESTPSPVVFCHNDCQEGNILLLEGRENSEKQKLMLIDFEYSSYNYRGFDIGNHFCEWMYDYSYEKYP 238
Cdd:cd05156   154 DLAKELGWLRSLLESTPSPVVFCHNDLQEGNILLLNGPENSEDDKLVLIDFEYCSYNYRGFDLANHFCEWAYDYTVPEPP 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774753247 239 FFRANIRKYPTKKQQLHFISSYLPAFQNDFENLSTEEKSIIKEEMLLEVNRFALASHFLWGLWSIVQAKISSIEFGYMDY 318
Cdd:cd05156   234 YFKINPENYPTREQQLHFIRAYLDEQYKDKTNDLTEERSKEEEKLLLEVNRFALASHFFWGLWSIVQAKISSIEFGYLEY 313
                         330
                  ....*....|..
gi 1774753247 319 AQARFDAYFHQK 330
Cdd:cd05156   314 AQARLDAYFKQK 325
Choline_kinase pfam01633
Choline/ethanolamine kinase; Choline kinase catalyzes the committed step in the synthesis of ...
17-252 5.35e-84

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: 252.58  E-value: 5.35e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774753247  17 EPRKVLLRLYGAILQmrscnkegseqaqkenefqGAEAMVLESVMFAILAERSLGPKLYGIFPQGRLEQFIPSRRLDTEE 96
Cdd:pfam01633   1 SPRKVLLRIYGPGTE-------------------LLINREDEIVNFALLSERGLGPKLYGFFPNGRIEEFIPSRTLSTED 61
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774753247  97 LSLPDISAEIAEKMATFHGMKMPFNKEPkWLFGTMEKYLKEVLRIK-FTEESRIKKLHKLLSYNLPLELENLRSLLESTP 175
Cdd:pfam01633  62 LRDPEISKLIAKRLAELHSLEMPGKKSP-SLWKTMRKWLSLLKNLGaPESVNKSEQLKSINLEDLEKEINKLEKWLELLD 140
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1774753247 176 SPVVFCHNDCQEGNILLLEgrensEKQKLMLIDFEYSSYNYRGFDIGNHFCEWMYDYSYEKyPFFRANIRKYPTKKQ 252
Cdd:pfam01633 141 SPIVFCHNDLQSGNILLLN-----ETKRLVLIDFEYASYNYRGFDIANHFCEWAGDYHDPT-PFFKCDYSLYPTREE 211
PLN02236 PLN02236
choline kinase
3-333 4.41e-64

choline kinase


Pssm-ID: 177880 [Multi-domain]  Cd Length: 344  Bit Score: 206.43  E-value: 4.41e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774753247   3 FQCSLPDTTatlGDEPRKVLLRLYGailqmrscnkEGSEQA-QKENEFQGAEAMvlesvmfailAERSLGPKLYGIFPQG 81
Cdd:PLN02236   53 FQIKWPTKE---GNLGRKVLVRIYG----------EGVELFfDRDDEIRTFECM----------SRHGQGPRLLGRFPNG 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774753247  82 RLEQFIPSRRLDTEELSLPDISAEIAEKMATFHGMKMPFNKEPKwLFGTMEKYLKEVLRIKFTEESRIKKLHKLlsynlp 161
Cdd:PLN02236  110 RVEEFIHARTLSAADLRDPEISALIAAKLREFHSLDMPGPKNVL-LWDRLRNWLKEAKNLCSPEEAKEFRLDSL------ 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774753247 162 lelENLRSLLESTPSPVV----FCHNDCQEGNILLLEgrensEKQKLMLIDFEYSSYNYRGFDIGNHFCEWMYDYSYEKy 237
Cdd:PLN02236  183 ---EDEINLLEKELSGDDqeigFCHNDLQYGNIMIDE-----ETRAITIIDYEYASYNPVAYDIANHFCEMAADYHSET- 253
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774753247 238 PFfRANIRKYPTKKQQLHFISSYLPAfqndfenlSTEEKSIIKEEMLLE-VNRFALASHFLWGLWSIVQAKISSIEFGYM 316
Cdd:PLN02236  254 PH-ILDYSKYPGEEERRRFIRTYLSS--------SGEEPSDEEVEQLLDdVEKYTLASHLFWGLWGIISGHVNKIDFDYM 324
                         330
                  ....*....|....*..
gi 1774753247 317 DYAQARFDAYFHQKRKL 333
Cdd:PLN02236  325 EYARQRFEQYWLRKPEL 341
CotS COG0510
Thiamine kinase or a related kinase [Coenzyme transport and metabolism];
140-323 1.54e-13

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


Pssm-ID: 440276 [Multi-domain]  Cd Length: 156  Bit Score: 67.50  E-value: 1.54e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774753247 140 RIKFTEESRIKKLHKLLSynlplELENLRSLLESTPSPVVFCHNDCQEGNILLlegrenSEKQKLMLIDFEYSSYNYRGF 219
Cdd:COG0510    16 RLERYLALGPRDLPELLR-----RLEELERALAARPLPLVLCHGDLHPGNFLV------TDDGRLYLIDWEYAGLGDPAF 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774753247 220 DIGNHFCEWMYDysyekypffranirkyptKKQQLHFISSYlpafqnDFENLSteeksiikEEMLLEVNRFALASHFLWG 299
Cdd:COG0510    85 DLAALLVEYGLS------------------PEQAEELLEAY------GFGRPT--------EELLRRLRAYRALADLLWA 132
                         170       180
                  ....*....|....*....|....
gi 1774753247 300 LWSIVQAkISSIEFGYMDYAQARF 323
Cdd:COG0510   133 LWALVRA-AQEANGDLLKYLLRRL 155
spore_CotS TIGR02906
spore coat protein, CotS family; Members of this family include the spore coat proteins CotS ...
106-268 6.81e-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: 44.19  E-value: 6.81e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774753247 106 IAEKMATFH----GMKMPFNKEPKWLFGTM----EKYLKEVLRIK-----FTEESRIKKLH-KLLSYNLPLELENLRSLL 171
Cdd:TIGR02906  93 AAKGLALFHhaskGYVPPDGSKIRSKLGKWpkqfEKRLKELERFKkialeKKYKDEFDKLYlKEVDYFLERGKKALELLN 172
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774753247 172 ESTPSPVV--------FCHNDCQEGNILLLEGrensekqKLMLIDFEYSSYNYRGFDIGNHFCEWMYDYSYEKYPFFRAN 243
Cdd:TIGR02906 173 KSKYYDLCkeakkirgFCHQDYAYHNILLKDN-------EVYVIDFDYCTIDLPVRDLRKLIIKLMKKNGVWDLEKAKEI 245
                         170       180
                  ....*....|....*....|....*....
gi 1774753247 244 IRKY----PTKKQQLHFISSYLpAFQNDF 268
Cdd:TIGR02906 246 IEAYssinPLSKEEKEVLYIDL-AFPHKF 273
CHK smart00587
ZnF_C4 abd HLH domain containing kinases domain; subfamily of choline kinases
108-221 7.08e-03

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


Pssm-ID: 214734  Cd Length: 196  Bit Score: 37.31  E-value: 7.08e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774753247  108 EKMATFH--------------------GMKMPFNKE-PKWLFGTMEKYLKEVLRIK--FTEESRIKKLHKLLSYnlpLEL 164
Cdd:smart00587  30 KKLAKLHaasavlieeekgsyleefdeGLFERFKRMfSEEFIGGLENFLRELLSQPelLKVEEYIEKLDKLLDN---LED 106
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1774753247  165 ENLRSLLESTPSPVVFCHNDCQEGNILLLEGrENSEKQKLMLIDFEYSSYNYRGFDI 221
Cdd:smart00587 107 LKKEDKEPDEGEFNVLNHGDLWANNIMFKYD-DEGKPEDVALIDFQLSHYGSPAEDL 162
 
Name Accession Description Interval E-value
ChoK_euk cd05156
Euykaryotic Choline Kinase; ChoK catalyzes the transfer of the gamma-phosphoryl group from ATP ...
1-330 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: 535.28  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774753247   1 MLFQCSLPDTTATLGDEPRKVLLRLYGAILQmrscnkegseqaqkenefqGAEAMVLESVMFAILAERSLGPKLYGIFPQ 80
Cdd:cd05156    13 LLYLCSLPDGVVPVGGEPRKVLLRIYGQILQ-------------------AEESLVTESVIFALLSERGLGPKLYGIFPG 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774753247  81 GRLEQFIPSRRLDTEELSLPDISAEIAEKMATFHGMKMPFNKEPKWLFGTMEKYLKEVLRIKFTEESRI--KKLHKLLSY 158
Cdd:cd05156    74 GRLEEFIPSRPLTTDELSLPEISRKIARKMARFHSLEMPISKEPKWLFDTMERWLKEALSILFTDEPTKpsKQLELLLSY 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774753247 159 NLPLELENLRSLLESTPSPVVFCHNDCQEGNILLLEGRENSEKQKLMLIDFEYSSYNYRGFDIGNHFCEWMYDYSYEKYP 238
Cdd:cd05156   154 DLAKELGWLRSLLESTPSPVVFCHNDLQEGNILLLNGPENSEDDKLVLIDFEYCSYNYRGFDLANHFCEWAYDYTVPEPP 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774753247 239 FFRANIRKYPTKKQQLHFISSYLPAFQNDFENLSTEEKSIIKEEMLLEVNRFALASHFLWGLWSIVQAKISSIEFGYMDY 318
Cdd:cd05156   234 YFKINPENYPTREQQLHFIRAYLDEQYKDKTNDLTEERSKEEEKLLLEVNRFALASHFFWGLWSIVQAKISSIEFGYLEY 313
                         330
                  ....*....|..
gi 1774753247 319 AQARFDAYFHQK 330
Cdd:cd05156   314 AQARLDAYFKQK 325
ETNK_euk cd05157
Euykaryotic Ethanolamine kinase; ETNK catalyzes the transfer of the gamma-phosphoryl group ...
1-327 5.92e-97

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: 289.10  E-value: 5.92e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774753247   1 MLFQCSLPDttatlGDEPRKVLLRLYGAilqmrscnkegseqaqkenefqGAEAMV---LESVMFAILAERSLGPKLYGI 77
Cdd:cd05157    13 ALYKVTYPS-----GDTPKTVLVRIYGP----------------------GTELLIdrdRELRILQLLSRAGIGPKLYGR 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774753247  78 FPQGRLEQFIPSRRLDTEELSLPDISAEIAEKMATFHGMKMPFNKEPKW---LFGTMEKYLkEVLRIKFTEESRIKKLHK 154
Cdd:cd05157    66 FENGRVEEFLPGRTLTPEDLRDPKISRLIARRLAELHSIVPLGEIEGKKkpiLWTTIRKWL-DLAPEVFEDEKNKEKKLE 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774753247 155 LLSYN-LPLELENLRSLLES-TPSPVVFCHNDCQEGNILLLEgrensEKQKLMLIDFEYSSYNYRGFDIGNHFCEWMYDY 232
Cdd:cd05157   145 KVDLErLRKELEWLEKWLESlEKSPIVFCHNDLLYGNILYNE-----DDDSVTFIDFEYAGPNPRAFDIANHFCEWAGFY 219
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774753247 233 SYEKYpffraniRKYPTKKQQLHFISSYLPAFQNDFENLSTEEKSIikEEMLLEVNRFALASHFLWGLWSIVQAKISSIE 312
Cdd:cd05157   220 CVLDY-------SRYPTKEEQRNFLRAYLESLDGLPGGEEVSEEEV--EKLYNEVNLFRLASHLFWGLWALIQAAISSID 290
                         330
                  ....*....|....*
gi 1774753247 313 FGYMDYAQARFDAYF 327
Cdd:cd05157   291 FDYLGYAKERLDEYW 305
Choline_kinase pfam01633
Choline/ethanolamine kinase; Choline kinase catalyzes the committed step in the synthesis of ...
17-252 5.35e-84

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: 252.58  E-value: 5.35e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774753247  17 EPRKVLLRLYGAILQmrscnkegseqaqkenefqGAEAMVLESVMFAILAERSLGPKLYGIFPQGRLEQFIPSRRLDTEE 96
Cdd:pfam01633   1 SPRKVLLRIYGPGTE-------------------LLINREDEIVNFALLSERGLGPKLYGFFPNGRIEEFIPSRTLSTED 61
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774753247  97 LSLPDISAEIAEKMATFHGMKMPFNKEPkWLFGTMEKYLKEVLRIK-FTEESRIKKLHKLLSYNLPLELENLRSLLESTP 175
Cdd:pfam01633  62 LRDPEISKLIAKRLAELHSLEMPGKKSP-SLWKTMRKWLSLLKNLGaPESVNKSEQLKSINLEDLEKEINKLEKWLELLD 140
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1774753247 176 SPVVFCHNDCQEGNILLLEgrensEKQKLMLIDFEYSSYNYRGFDIGNHFCEWMYDYSYEKyPFFRANIRKYPTKKQ 252
Cdd:pfam01633 141 SPIVFCHNDLQSGNILLLN-----ETKRLVLIDFEYASYNYRGFDIANHFCEWAGDYHDPT-PFFKCDYSLYPTREE 211
ChoK-like_euk cd14021
Euykaryotic Choline Kinase and similar proteins; This group is composed of eukaryotic choline ...
1-303 1.53e-78

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: 239.48  E-value: 1.53e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774753247   1 MLFQCSLPDTTATLgdEPRKVLLRLYGAIlqmrscnkegseqaqkeneFQGAEAMVLESVMFAILAERSLGPKLYGIFPQ 80
Cdd:cd14021    13 QVYKVSLKDESDSL--EPKKVLFRIYGKY-------------------LSTLYDREKESEVFKILSEQGLGPKLIYKFDG 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774753247  81 GRLEQFIPSRRLDTEELSLPDISAEIAEKMATFHGMKMPfnkepkwlfgtmekylkevlrikfteesrikklhkllsynl 160
Cdd:cd14021    72 GRIEEYIDGRPLTTDELRNPSVLTSIAKLLAKFHKIKTP----------------------------------------- 110
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774753247 161 plelenlrsllestpsPVVFCHNDCQEGNILLLegrenSEKQKLMLIDFEYSSYNYRGFDIGNHFCEWMYDYSYEKYPFF 240
Cdd:cd14021   111 ----------------PVVFCHNDLQENNILLT-----NDQDGLRLIDFEYSGFNYRGYDIANFFNESMIDYDHPEPPYF 169
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1774753247 241 RANIRKYPTKKQQLHFISSYLPAFQNDFENLSTEEksiIKEEMLLEVNRFALASHFLWGLWSI 303
Cdd:cd14021   170 KIYKENYISEEEKRLFVSVYLSEYLEKNVLPSLDK---LVEQFLQEVEIFTLGSHLYWGLWSI 229
PLN02236 PLN02236
choline kinase
3-333 4.41e-64

choline kinase


Pssm-ID: 177880 [Multi-domain]  Cd Length: 344  Bit Score: 206.43  E-value: 4.41e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774753247   3 FQCSLPDTTatlGDEPRKVLLRLYGailqmrscnkEGSEQA-QKENEFQGAEAMvlesvmfailAERSLGPKLYGIFPQG 81
Cdd:PLN02236   53 FQIKWPTKE---GNLGRKVLVRIYG----------EGVELFfDRDDEIRTFECM----------SRHGQGPRLLGRFPNG 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774753247  82 RLEQFIPSRRLDTEELSLPDISAEIAEKMATFHGMKMPFNKEPKwLFGTMEKYLKEVLRIKFTEESRIKKLHKLlsynlp 161
Cdd:PLN02236  110 RVEEFIHARTLSAADLRDPEISALIAAKLREFHSLDMPGPKNVL-LWDRLRNWLKEAKNLCSPEEAKEFRLDSL------ 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774753247 162 lelENLRSLLESTPSPVV----FCHNDCQEGNILLLEgrensEKQKLMLIDFEYSSYNYRGFDIGNHFCEWMYDYSYEKy 237
Cdd:PLN02236  183 ---EDEINLLEKELSGDDqeigFCHNDLQYGNIMIDE-----ETRAITIIDYEYASYNPVAYDIANHFCEMAADYHSET- 253
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774753247 238 PFfRANIRKYPTKKQQLHFISSYLPAfqndfenlSTEEKSIIKEEMLLE-VNRFALASHFLWGLWSIVQAKISSIEFGYM 316
Cdd:PLN02236  254 PH-ILDYSKYPGEEERRRFIRTYLSS--------SGEEPSDEEVEQLLDdVEKYTLASHLFWGLWGIISGHVNKIDFDYM 324
                         330
                  ....*....|....*..
gi 1774753247 317 DYAQARFDAYFHQKRKL 333
Cdd:PLN02236  325 EYARQRFEQYWLRKPEL 341
PLN02421 PLN02421
phosphotransferase, alcohol group as acceptor/kinase
65-333 2.22e-60

phosphotransferase, alcohol group as acceptor/kinase


Pssm-ID: 215231 [Multi-domain]  Cd Length: 330  Bit Score: 196.50  E-value: 2.22e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774753247  65 LAERSLGPKLYGIFPQGRLEQFIPSRRLDTEELSLPDISAEIAEKMATFHGMKMPFNKEPKwLFGTMEKYLKEVLRIKFT 144
Cdd:PLN02421   70 LSAAGFGAKLLGVFGNGMIQSFINARTLTPSDMRKPKVAAEIAKELRRLHQVEIPGSKEPQ-LWNDIFKFYEKASTVKFE 148
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774753247 145 EESRIKKLHKLLSYNLPLELENLRSLLESTPSPVVFCHNDCQEGNILLlegreNSEKQKLMLIDFEYSSYNYRGFDIGNH 224
Cdd:PLN02421  149 DPEKQKKYETISFEELRDEIVELKEITDSLKAPVVFAHNDLLSGNLML-----NEDEGKLYFIDFEYGSYSYRGYDIGNH 223
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774753247 225 FCEwmydysyekYPFFRANIRKYPTKKQQLHFISSYLpafQNDFENLSTEEKSiikEEMLLEVNRFALASHFLWGLWSIV 304
Cdd:PLN02421  224 FNE---------YAGFDCDYSLYPSKEEQYHFFRHYL---RPDDPEEVSDAEL---EELFVETNFYALASHLYWAIWAIV 288
                         250       260
                  ....*....|....*....|....*....
gi 1774753247 305 QAKISSIEFGYMDYAQARFDAYFHQKRKL 333
Cdd:PLN02421  289 QAKMSPIDFDYLGYFFLRYKEYKRQKEKL 317
PTZ00296 PTZ00296
choline kinase; Provisional
2-333 5.38e-45

choline kinase; Provisional


Pssm-ID: 240350 [Multi-domain]  Cd Length: 442  Bit Score: 159.28  E-value: 5.38e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774753247   2 LFQCSLPDTTATlgDEP---RKVLLRLYGailqmrscnKEGSEQAQKENEFQgaeamvlesvMFAILAERSLGPKLYGIF 78
Cdd:PTZ00296  121 LFEVSLKEETAN--NYPsirRRVLFRIYG---------KDVDELYNPISEFE----------VYKTMSKYRIAPQLLNTF 179
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774753247  79 PQGRLEQFIPSRRLDTEELSLPDISAEIAEKMATFHGMK----MP--FNKEPKwLFGTMEKYLKEVLRIKFTEESR---- 148
Cdd:PTZ00296  180 SGGRIEEWLYGDPLRIDDLKNPSILIGIANVLGKFHTLSrkrhLPehWDRTPC-IFKMMEKWKNQLSKYKNIEKYQrdih 258
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774753247 149 --IKKLHKLLSYnlplelENLRSLLESTPSPVVFCHNDCQEGNILllegreNSEKqKLMLIDFEYSSYNYRGFDIGNHFC 226
Cdd:PTZ00296  259 kyIKESEKFIKF------MKVYSKSDNLANDIVFCHNDLQENNII------NTNK-CLRLIDFEYSGYNFLATDIANFFI 325
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774753247 227 EWMYDYSYEKYPFFRANIRKYPTKKQQLHFISSYLPAFQNDfeNLSTEEKSIIkEEMLLEVNRFALASHFLWGLWSIV-- 304
Cdd:PTZ00296  326 ETTIDYSVSHYPFFAIDKKKYISYENRKLFITAYLSNYLDK--SLVVPNPKII-DQILEAVEVQALGAHLLWGFWSIIrg 402
                         330       340       350
                  ....*....|....*....|....*....|
gi 1774753247 305 -QAKiSSIEFGYMDYAQARFDAYFHQKRKL 333
Cdd:PTZ00296  403 yQTK-SYNEFDFFLYAKERFKMYDEQKEYL 431
ChoK-like cd05151
Choline Kinase and similar proteins; This subfamily is composed of bacterial and eukaryotic ...
16-230 5.52e-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: 95.70  E-value: 5.52e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774753247  16 DEPRKVLLRLYGAILQMrscnkegseQAQKENEFQGAEAmvlesvmfaiLAERSLGPKLYGIFPQ--GRLEQFIPSRRLD 93
Cdd:cd05151    19 VAGKKYVLRIPGAGTEL---------LIDRENEKANSKA----------AAELGIAPEVIYFDPEtgVKITEFIEGATLL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774753247  94 TEELSLPDISAEIAEKMATFHGMKMPfnkepkwlfgtmekylkevlrikfteesrikklhkllsynlplelenlrslles 173
Cdd:cd05151    80 TNDFSDPENLERIAALLRKLHSSPLE------------------------------------------------------ 105
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1774753247 174 tpsPVVFCHNDCQEGNILLLEGRensekqkLMLIDFEYSSYNYRGFDIGNHFCEWMY 230
Cdd:cd05151   106 ---DLVLCHNDLVPGNFLLDDDR-------LYLIDWEYAGMNDPLFDLAALFSENNL 152
APH_ChoK_like cd05120
Aminoglycoside 3'-phosphotransferase and Choline Kinase family; This family is composed of APH, ...
17-230 3.44e-16

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: 74.65  E-value: 3.44e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774753247  17 EPRKVLLRLYGAILQmrscnkegseqaqkenefqgaEAMVLESVMFAILAERS--LGPKLYGIFP----QGRLEQFIPSR 90
Cdd:cd05120    19 DPREYVLKIGPPRLK---------------------KDLEKEAAMLQLLAGKLslPVPKVYGFGEsdgwEYLLMERIEGE 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774753247  91 RLDTE-----ELSLPDISAEIAEKMATFHGMKMPfnkepkwlfgtmekylkevlrikfteesrikklhkllsynlplele 165
Cdd:cd05120    78 TLSEVwprlsEEEKEKIADQLAEILAALHRIDSS---------------------------------------------- 111
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1774753247 166 nlrsllestpspvVFCHNDCQEGNILLLEgrensEKQKLMLIDFEYSSYNYRGFDIGNHFCEWMY 230
Cdd:cd05120   112 -------------VLTHGDLHPGNILVKP-----DGKLSGIIDWEFAGYGPPAFDYAAALRDWTE 158
CotS COG0510
Thiamine kinase or a related kinase [Coenzyme transport and metabolism];
140-323 1.54e-13

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


Pssm-ID: 440276 [Multi-domain]  Cd Length: 156  Bit Score: 67.50  E-value: 1.54e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774753247 140 RIKFTEESRIKKLHKLLSynlplELENLRSLLESTPSPVVFCHNDCQEGNILLlegrenSEKQKLMLIDFEYSSYNYRGF 219
Cdd:COG0510    16 RLERYLALGPRDLPELLR-----RLEELERALAARPLPLVLCHGDLHPGNFLV------TDDGRLYLIDWEYAGLGDPAF 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774753247 220 DIGNHFCEWMYDysyekypffranirkyptKKQQLHFISSYlpafqnDFENLSteeksiikEEMLLEVNRFALASHFLWG 299
Cdd:COG0510    85 DLAALLVEYGLS------------------PEQAEELLEAY------GFGRPT--------EELLRRLRAYRALADLLWA 132
                         170       180
                  ....*....|....*....|....
gi 1774753247 300 LWSIVQAkISSIEFGYMDYAQARF 323
Cdd:COG0510   133 LWALVRA-AQEANGDLLKYLLRRL 155
PTZ00384 PTZ00384
choline kinase; Provisional
64-304 2.96e-08

choline kinase; Provisional


Pssm-ID: 173576 [Multi-domain]  Cd Length: 383  Bit Score: 54.78  E-value: 2.96e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774753247  64 ILAERSLGPKLYGIFPQGRLEQFIPSRRLDTEELSLPDISAEIAEKMATFHgmKMPFNKEPK-W----LFGT-MEKYLKE 137
Cdd:PTZ00384  108 LLGDNNFGPKIIGRFGDFTIQEWVEGNTMGIDSLQNLSVLTGIASSLAKFH--KRVTELVPKeWdrtpMFLTkISTWSQH 185
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774753247 138 VLRIkfteesrIKKLHKLLSYN-LPLELENLRSLL-------ESTPSPVVFCHNDCQEGNILllegrenSEKQKLMLIDF 209
Cdd:PTZ00384  186 VERI-------IKKYNLDFDYNeLVQNYELFKKILnnhlntsNSITNSVLFCHNDLFFTNIL-------DFNQGIYFIDF 251
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774753247 210 EYSSYNYRGFDIGNHFCEWMYDYSYEKYPFFRANIRKYPTKKQQLHFISSYLPAFQNdfENLSTEEKSIikEEMLLEVNR 289
Cdd:PTZ00384  252 DFAGFNYVGWEIANFFVKLYIVYDPPTPPYFNSDDSLALSEEMKTIFVSVYLSQLLG--KNVLPSDDLV--KEFLQSLEI 327
                         250
                  ....*....|....*
gi 1774753247 290 FALASHFLWGLWSIV 304
Cdd:PTZ00384  328 HTLGVNLFWTYWGIV 342
APH pfam01636
Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance ...
14-228 1.80e-05

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: 45.18  E-value: 1.80e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774753247  14 LGDEPRKVLLRLYgailqmrscnKEGSEQAQKENEFQgaeamvlesvMFAILAERSLGPK---LYGIFPQGRLE------ 84
Cdd:pfam01636  16 VTTGDGRYVLRLP----------PPGRAAEELRRELA----------LLRHLAAAGVPPVprvLAGCTDAELLGlpfllm 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774753247  85 QFIP--SRRLDTEELSLPDISAEIAEKMATFHGMKMPFNKEPKWlfgtmEKYLKEVLRiKFTEESRIKKLHKLLSYNLPL 162
Cdd:pfam01636  76 EYLPgeVLARPLLPEERGALLEALGRALARLHAVDPAALPLAGR-----LARLLELLR-QLEAALARLLAAELLDRLEEL 149
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1774753247 163 ELENLRSLLESTP--SPVVFCHNDCQEGNILLLEGRENSEkqklmLIDFEYSSYNYRGFDIG---NHFCEW 228
Cdd:pfam01636 150 EERLLAALLALLPaeLPPVLVHGDLHPGNLLVDPGGRVSG-----VIDFEDAGLGDPAYDLAillNSWGRE 215
spore_CotS TIGR02906
spore coat protein, CotS family; Members of this family include the spore coat proteins CotS ...
106-268 6.81e-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: 44.19  E-value: 6.81e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774753247 106 IAEKMATFH----GMKMPFNKEPKWLFGTM----EKYLKEVLRIK-----FTEESRIKKLH-KLLSYNLPLELENLRSLL 171
Cdd:TIGR02906  93 AAKGLALFHhaskGYVPPDGSKIRSKLGKWpkqfEKRLKELERFKkialeKKYKDEFDKLYlKEVDYFLERGKKALELLN 172
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774753247 172 ESTPSPVV--------FCHNDCQEGNILLLEGrensekqKLMLIDFEYSSYNYRGFDIGNHFCEWMYDYSYEKYPFFRAN 243
Cdd:TIGR02906 173 KSKYYDLCkeakkirgFCHQDYAYHNILLKDN-------EVYVIDFDYCTIDLPVRDLRKLIIKLMKKNGVWDLEKAKEI 245
                         170       180
                  ....*....|....*....|....*....
gi 1774753247 244 IRKY----PTKKQQLHFISSYLpAFQNDF 268
Cdd:TIGR02906 246 IEAYssinPLSKEEKEVLYIDL-AFPHKF 273
HomoserineK_II cd05153
Type II Homoserine Kinase; This subfamily is composed of unusual homoserine kinases, from a ...
70-226 1.94e-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: 42.63  E-value: 1.94e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774753247  70 LGPKLYGIFPqgrleqFIPSRRLDTEElslPDISAEIAEKMATFHG------MKMPFNKEPKWlfgtMEKYLKevlRIKF 143
Cdd:cd05153    86 LNGKPAALFP------FLPGESLTTPT---PEQCRAIGAALARLHLalagfpPPRPNPRGLAW----WKPLAE---RLKA 149
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774753247 144 TEESRIKKLHKLLSynlpLELENLRSLLESTPsPVVFCHNDCQEGNILLLEGRENSekqklmLIDFEYSSYNYRGFDIG- 222
Cdd:cd05153   150 RLDLLAADDRALLE----DELARLQALAPSDL-PRGVIHADLFRDNVLFDGDRLSG------IIDFYDACYDPLLYDLAi 218

                  ....*.
gi 1774753247 223 --NHFC 226
Cdd:cd05153   219 alNDWC 224
EcKL pfam02958
Ecdysteroid kinase-like family; This family includes ecdysteroid 22-kinase, an enzyme ...
127-225 2.87e-03

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: 38.79  E-value: 2.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774753247 127 LFGTMEKYLKEVLRIKFTEESRI-KKLHKLLSyNLpleLENLRSLLESTPSP-VVFCHNDCQEGNILLLEGrENSEKQKL 204
Cdd:pfam02958 165 LMETGLDAAAEALREQLPEYEKYaEKLEKLKD-NY---FDRLLRLVEPTPGEfNVLNHGDLWVNNIMFKYD-DEGEPEDV 239
                          90       100
                  ....*....|....*....|.
gi 1774753247 205 MLIDFEYSSYNYRGFDIgNHF 225
Cdd:pfam02958 240 ILVDFQLSRYGSPAIDL-NYF 259
SrkA COG2334
Ser/Thr protein kinase RdoA involved in Cpx stress response, MazF antagonist [Signal ...
163-222 3.72e-03

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: 38.75  E-value: 3.72e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1774753247 163 ELENLRSLLESTPSPVVF--CHNDCQEGNILLLEGRensekqKLMLIDFEYSSYNYRGFDIG 222
Cdd:COG2334   162 LLDRLEARLAPLLGALPRgvIHGDLHPDNVLFDGDG------VSGLIDFDDAGYGPRLYDLA 217
CHK smart00587
ZnF_C4 abd HLH domain containing kinases domain; subfamily of choline kinases
108-221 7.08e-03

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


Pssm-ID: 214734  Cd Length: 196  Bit Score: 37.31  E-value: 7.08e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774753247  108 EKMATFH--------------------GMKMPFNKE-PKWLFGTMEKYLKEVLRIK--FTEESRIKKLHKLLSYnlpLEL 164
Cdd:smart00587  30 KKLAKLHaasavlieeekgsyleefdeGLFERFKRMfSEEFIGGLENFLRELLSQPelLKVEEYIEKLDKLLDN---LED 106
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1774753247  165 ENLRSLLESTPSPVVFCHNDCQEGNILLLEGrENSEKQKLMLIDFEYSSYNYRGFDI 221
Cdd:smart00587 107 LKKEDKEPDEGEFNVLNHGDLWANNIMFKYD-DEGKPEDVALIDFQLSHYGSPAEDL 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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