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Conserved domains on  [gi|1958643008|ref|XP_038959042|]
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choline kinase alpha isoform X4 [Rattus norvegicus]

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 ...
1-276 2.66e-172

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: 478.66  E-value: 2.66e-172
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643008   1 MVLESVMFAILAERSLGPKLYGIFPQGRLEQFIPSRRLDTEELCLPDISAEIAEKMATFHGMKMPFNKEPKWLFGTMEKY 80
Cdd:cd05156    48 LVTESVIFALLSERGLGPKLYGIFPGGRLEEFIPSRPLTTDELSLPEISRKIARKMARFHSLEMPISKEPKWLFDTMERW 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643008  81 LNQVLRLKFSREARVQ--QLHKFLSYNLPLELENLRSLLQYTRSPVVFCHNDCQEGNILLLEGQENSEKQKLMLIDFEYS 158
Cdd:cd05156   128 LKEALSILFTDEPTKPskQLELLLSYDLAKELGWLRSLLESTPSPVVFCHNDLQEGNILLLNGPENSEDDKLVLIDFEYC 207
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643008 159 SYNYRGFDIGNHFCEWMYDYTYEKYPFFRANIQKYPTRKQQLHFISSYLTTFQNDFESLSSEEQSATKEDMLLEVNRFAL 238
Cdd:cd05156   208 SYNYRGFDLANHFCEWAYDYTVPEPPYFKINPENYPTREQQLHFIRAYLDEQYKDKTNDLTEERSKEEEKLLLEVNRFAL 287
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1958643008 239 ASHFLWGLWSIVQAKISSIEFGYMEYAQARFDAYFDQK 276
Cdd:cd05156   288 ASHFFWGLWSIVQAKISSIEFGYLEYAQARLDAYFKQK 325
 
Name Accession Description Interval E-value
ChoK_euk cd05156
Euykaryotic Choline Kinase; ChoK catalyzes the transfer of the gamma-phosphoryl group from ATP ...
1-276 2.66e-172

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: 478.66  E-value: 2.66e-172
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643008   1 MVLESVMFAILAERSLGPKLYGIFPQGRLEQFIPSRRLDTEELCLPDISAEIAEKMATFHGMKMPFNKEPKWLFGTMEKY 80
Cdd:cd05156    48 LVTESVIFALLSERGLGPKLYGIFPGGRLEEFIPSRPLTTDELSLPEISRKIARKMARFHSLEMPISKEPKWLFDTMERW 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643008  81 LNQVLRLKFSREARVQ--QLHKFLSYNLPLELENLRSLLQYTRSPVVFCHNDCQEGNILLLEGQENSEKQKLMLIDFEYS 158
Cdd:cd05156   128 LKEALSILFTDEPTKPskQLELLLSYDLAKELGWLRSLLESTPSPVVFCHNDLQEGNILLLNGPENSEDDKLVLIDFEYC 207
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643008 159 SYNYRGFDIGNHFCEWMYDYTYEKYPFFRANIQKYPTRKQQLHFISSYLTTFQNDFESLSSEEQSATKEDMLLEVNRFAL 238
Cdd:cd05156   208 SYNYRGFDLANHFCEWAYDYTVPEPPYFKINPENYPTREQQLHFIRAYLDEQYKDKTNDLTEERSKEEEKLLLEVNRFAL 287
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1958643008 239 ASHFLWGLWSIVQAKISSIEFGYMEYAQARFDAYFDQK 276
Cdd:cd05156   288 ASHFFWGLWSIVQAKISSIEFGYLEYAQARLDAYFKQK 325
Choline_kinase pfam01633
Choline/ethanolamine kinase; Choline kinase catalyzes the committed step in the synthesis of ...
1-198 4.88e-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: 250.65  E-value: 4.88e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643008   1 MVLESVMFAILAERSLGPKLYGIFPQGRLEQFIPSRRLDTEELCLPDISAEIAEKMATFHGMKMPFNKEPkWLFGTMEKY 80
Cdd:pfam01633  20 REDEIVNFALLSERGLGPKLYGFFPNGRIEEFIPSRTLSTEDLRDPEISKLIAKRLAELHSLEMPGKKSP-SLWKTMRKW 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643008  81 LNQVLRLK-FSREARVQQLHKFLSYNLPLELENLRSLLQYTRSPVVFCHNDCQEGNILLLEgqensEKQKLMLIDFEYSS 159
Cdd:pfam01633  99 LSLLKNLGaPESVNKSEQLKSINLEDLEKEINKLEKWLELLDSPIVFCHNDLQSGNILLLN-----ETKRLVLIDFEYAS 173
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1958643008 160 YNYRGFDIGNHFCEWMYDYTYEKyPFFRANIQKYPTRKQ 198
Cdd:pfam01633 174 YNYRGFDIANHFCEWAGDYHDPT-PFFKCDYSLYPTREE 211
PLN02236 PLN02236
choline kinase
8-279 4.25e-61

choline kinase


Pssm-ID: 177880 [Multi-domain]  Cd Length: 344  Bit Score: 196.80  E-value: 4.25e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643008   8 FAILAERSLGPKLYGIFPQGRLEQFIPSRRLDTEELCLPDISAEIAEKMATFHGMKMPFNKEPKwLFGTMEKYLNQVLRL 87
Cdd:PLN02236   90 FECMSRHGQGPRLLGRFPNGRVEEFIHARTLSAADLRDPEISALIAAKLREFHSLDMPGPKNVL-LWDRLRNWLKEAKNL 168
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643008  88 KFSREARVQQLHKflsynlpleLENLRSLLQYTRSPVV----FCHNDCQEGNILLLEgqensEKQKLMLIDFEYSSYNYR 163
Cdd:PLN02236  169 CSPEEAKEFRLDS---------LEDEINLLEKELSGDDqeigFCHNDLQYGNIMIDE-----ETRAITIIDYEYASYNPV 234
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643008 164 GFDIGNHFCEWMYDYTYEKyPFfRANIQKYPTRKQQLHFISSYLttfqndfeSLSSEEQSATK-EDMLLEVNRFALASHF 242
Cdd:PLN02236  235 AYDIANHFCEMAADYHSET-PH-ILDYSKYPGEEERRRFIRTYL--------SSSGEEPSDEEvEQLLDDVEKYTLASHL 304
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1958643008 243 LWGLWSIVQAKISSIEFGYMEYAQARFDAYFDQKRKL 279
Cdd:PLN02236  305 FWGLWGIISGHVNKIDFDYMEYARQRFEQYWLRKPEL 341
CotS COG0510
Thiamine kinase or a related kinase [Coenzyme transport and metabolism];
86-269 2.53e-11

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


Pssm-ID: 440276 [Multi-domain]  Cd Length: 156  Bit Score: 60.57  E-value: 2.53e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643008  86 RLKFSREARVQQLHKFLSynlplELENLRSLLQYTRSPVVFCHNDCQEGNILLlegqenSEKQKLMLIDFEYSSYNYRGF 165
Cdd:COG0510    16 RLERYLALGPRDLPELLR-----RLEELERALAARPLPLVLCHGDLHPGNFLV------TDDGRLYLIDWEYAGLGDPAF 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643008 166 DIGNHFCEWMYDytyekypffraniqkyptRKQQLHFISSYlttfqnDFESLSSEEqsatkedmLLEVNRFALASHFLWG 245
Cdd:COG0510    85 DLAALLVEYGLS------------------PEQAEELLEAY------GFGRPTEEL--------LRRLRAYRALADLLWA 132
                         170       180
                  ....*....|....*....|....
gi 1958643008 246 LWSIVQAkISSIEFGYMEYAQARF 269
Cdd:COG0510   133 LWALVRA-AQEANGDLLKYLLRRL 155
spore_CotS TIGR02906
spore coat protein, CotS family; Members of this family include the spore coat proteins CotS ...
45-169 5.43e-04

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: 40.73  E-value: 5.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643008  45 LPDISAEIAEKMATFhgMKMPFNKEPKWLFG-----TMEKYLNQVLRLKfsrearvQQLHKFLSYNLPLELENLRSllqy 119
Cdd:TIGR02906 122 WPKQFEKRLKELERF--KKIALEKKYKDEFDklylkEVDYFLERGKKAL-------ELLNKSKYYDLCKEAKKIRG---- 188
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1958643008 120 trspvvFCHNDCQEGNILLLEGqensekqKLMLIDFEYSSYNYRGFDIGN 169
Cdd:TIGR02906 189 ------FCHQDYAYHNILLKDN-------EVYVIDFDYCTIDLPVRDLRK 225
 
Name Accession Description Interval E-value
ChoK_euk cd05156
Euykaryotic Choline Kinase; ChoK catalyzes the transfer of the gamma-phosphoryl group from ATP ...
1-276 2.66e-172

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: 478.66  E-value: 2.66e-172
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643008   1 MVLESVMFAILAERSLGPKLYGIFPQGRLEQFIPSRRLDTEELCLPDISAEIAEKMATFHGMKMPFNKEPKWLFGTMEKY 80
Cdd:cd05156    48 LVTESVIFALLSERGLGPKLYGIFPGGRLEEFIPSRPLTTDELSLPEISRKIARKMARFHSLEMPISKEPKWLFDTMERW 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643008  81 LNQVLRLKFSREARVQ--QLHKFLSYNLPLELENLRSLLQYTRSPVVFCHNDCQEGNILLLEGQENSEKQKLMLIDFEYS 158
Cdd:cd05156   128 LKEALSILFTDEPTKPskQLELLLSYDLAKELGWLRSLLESTPSPVVFCHNDLQEGNILLLNGPENSEDDKLVLIDFEYC 207
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643008 159 SYNYRGFDIGNHFCEWMYDYTYEKYPFFRANIQKYPTRKQQLHFISSYLTTFQNDFESLSSEEQSATKEDMLLEVNRFAL 238
Cdd:cd05156   208 SYNYRGFDLANHFCEWAYDYTVPEPPYFKINPENYPTREQQLHFIRAYLDEQYKDKTNDLTEERSKEEEKLLLEVNRFAL 287
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1958643008 239 ASHFLWGLWSIVQAKISSIEFGYMEYAQARFDAYFDQK 276
Cdd:cd05156   288 ASHFFWGLWSIVQAKISSIEFGYLEYAQARLDAYFKQK 325
ETNK_euk cd05157
Euykaryotic Ethanolamine kinase; ETNK catalyzes the transfer of the gamma-phosphoryl group ...
4-275 5.36e-93

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: 277.15  E-value: 5.36e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643008   4 ESVMFAILAERSLGPKLYGIFPQGRLEQFIPSRRLDTEELCLPDISAEIAEKMATFHGMKMPFNKEPKW---LFGTMEKY 80
Cdd:cd05157    46 ELRILQLLSRAGIGPKLYGRFENGRVEEFLPGRTLTPEDLRDPKISRLIARRLAELHSIVPLGEIEGKKkpiLWTTIRKW 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643008  81 LNQVLRLKFSREARVQQLHKFLSYNLPLELENLRSLL-QYTRSPVVFCHNDCQEGNILLLEgqensEKQKLMLIDFEYSS 159
Cdd:cd05157   126 LDLAPEVFEDEKNKEKKLEKVDLERLRKELEWLEKWLeSLEKSPIVFCHNDLLYGNILYNE-----DDDSVTFIDFEYAG 200
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643008 160 YNYRGFDIGNHFCEWMYDYTYEKYpffraniQKYPTRKQQLHFISSYLTTFQNDFESLSSEEQSAtkEDMLLEVNRFALA 239
Cdd:cd05157   201 PNPRAFDIANHFCEWAGFYCVLDY-------SRYPTKEEQRNFLRAYLESLDGLPGGEEVSEEEV--EKLYNEVNLFRLA 271
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1958643008 240 SHFLWGLWSIVQAKISSIEFGYMEYAQARFDAYFDQ 275
Cdd:cd05157   272 SHLFWGLWALIQAAISSIDFDYLGYAKERLDEYWGD 307
Choline_kinase pfam01633
Choline/ethanolamine kinase; Choline kinase catalyzes the committed step in the synthesis of ...
1-198 4.88e-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: 250.65  E-value: 4.88e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643008   1 MVLESVMFAILAERSLGPKLYGIFPQGRLEQFIPSRRLDTEELCLPDISAEIAEKMATFHGMKMPFNKEPkWLFGTMEKY 80
Cdd:pfam01633  20 REDEIVNFALLSERGLGPKLYGFFPNGRIEEFIPSRTLSTEDLRDPEISKLIAKRLAELHSLEMPGKKSP-SLWKTMRKW 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643008  81 LNQVLRLK-FSREARVQQLHKFLSYNLPLELENLRSLLQYTRSPVVFCHNDCQEGNILLLEgqensEKQKLMLIDFEYSS 159
Cdd:pfam01633  99 LSLLKNLGaPESVNKSEQLKSINLEDLEKEINKLEKWLELLDSPIVFCHNDLQSGNILLLN-----ETKRLVLIDFEYAS 173
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1958643008 160 YNYRGFDIGNHFCEWMYDYTYEKyPFFRANIQKYPTRKQ 198
Cdd:pfam01633 174 YNYRGFDIANHFCEWAGDYHDPT-PFFKCDYSLYPTREE 211
ChoK-like_euk cd14021
Euykaryotic Choline Kinase and similar proteins; This group is composed of eukaryotic choline ...
1-249 6.58e-71

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: 217.91  E-value: 6.58e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643008   1 MVLESVMFAILAERSLGPKLYGIFPQGRLEQFIPSRRLDTEELCLPDISAEIAEKMATFHGMKMPfnkepkwlfgtmeky 80
Cdd:cd14021    46 REKESEVFKILSEQGLGPKLIYKFDGGRIEEYIDGRPLTTDELRNPSVLTSIAKLLAKFHKIKTP--------------- 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643008  81 lnqvlrlkfsrearvqqlhkflsynlplelenlrsllqytrsPVVFCHNDCQEGNILLLegqenSEKQKLMLIDFEYSSY 160
Cdd:cd14021   111 ------------------------------------------PVVFCHNDLQENNILLT-----NDQDGLRLIDFEYSGF 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643008 161 NYRGFDIGNHFCEWMYDYTYEKYPFFRANIQKYPTRKQQLHFISSYLTTFQNDFESLSSEEqsaTKEDMLLEVNRFALAS 240
Cdd:cd14021   144 NYRGYDIANFFNESMIDYDHPEPPYFKIYKENYISEEEKRLFVSVYLSEYLEKNVLPSLDK---LVEQFLQEVEIFTLGS 220

                  ....*....
gi 1958643008 241 HFLWGLWSI 249
Cdd:cd14021   221 HLYWGLWSI 229
PLN02236 PLN02236
choline kinase
8-279 4.25e-61

choline kinase


Pssm-ID: 177880 [Multi-domain]  Cd Length: 344  Bit Score: 196.80  E-value: 4.25e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643008   8 FAILAERSLGPKLYGIFPQGRLEQFIPSRRLDTEELCLPDISAEIAEKMATFHGMKMPFNKEPKwLFGTMEKYLNQVLRL 87
Cdd:PLN02236   90 FECMSRHGQGPRLLGRFPNGRVEEFIHARTLSAADLRDPEISALIAAKLREFHSLDMPGPKNVL-LWDRLRNWLKEAKNL 168
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643008  88 KFSREARVQQLHKflsynlpleLENLRSLLQYTRSPVV----FCHNDCQEGNILLLEgqensEKQKLMLIDFEYSSYNYR 163
Cdd:PLN02236  169 CSPEEAKEFRLDS---------LEDEINLLEKELSGDDqeigFCHNDLQYGNIMIDE-----ETRAITIIDYEYASYNPV 234
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643008 164 GFDIGNHFCEWMYDYTYEKyPFfRANIQKYPTRKQQLHFISSYLttfqndfeSLSSEEQSATK-EDMLLEVNRFALASHF 242
Cdd:PLN02236  235 AYDIANHFCEMAADYHSET-PH-ILDYSKYPGEEERRRFIRTYL--------SSSGEEPSDEEvEQLLDDVEKYTLASHL 304
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1958643008 243 LWGLWSIVQAKISSIEFGYMEYAQARFDAYFDQKRKL 279
Cdd:PLN02236  305 FWGLWGIISGHVNKIDFDYMEYARQRFEQYWLRKPEL 341
PLN02421 PLN02421
phosphotransferase, alcohol group as acceptor/kinase
11-279 1.03e-56

phosphotransferase, alcohol group as acceptor/kinase


Pssm-ID: 215231 [Multi-domain]  Cd Length: 330  Bit Score: 184.94  E-value: 1.03e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643008  11 LAERSLGPKLYGIFPQGRLEQFIPSRRLDTEELCLPDISAEIAEKMATFHGMKMPFNKEPKwLFGTMEKYLNQVLRLKFS 90
Cdd:PLN02421   70 LSAAGFGAKLLGVFGNGMIQSFINARTLTPSDMRKPKVAAEIAKELRRLHQVEIPGSKEPQ-LWNDIFKFYEKASTVKFE 148
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643008  91 REARVQQLHKFLSYNLPLELENLRSLLQYTRSPVVFCHNDCQEGNILLlegqeNSEKQKLMLIDFEYSSYNYRGFDIGNH 170
Cdd:PLN02421  149 DPEKQKKYETISFEELRDEIVELKEITDSLKAPVVFAHNDLLSGNLML-----NEDEGKLYFIDFEYGSYSYRGYDIGNH 223
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643008 171 FCEwmydytyekYPFFRANIQKYPTRKQQLHFISSYLttfQNDFESLSSEEQSatkEDMLLEVNRFALASHFLWGLWSIV 250
Cdd:PLN02421  224 FNE---------YAGFDCDYSLYPSKEEQYHFFRHYL---RPDDPEEVSDAEL---EELFVETNFYALASHLYWAIWAIV 288
                         250       260
                  ....*....|....*....|....*....
gi 1958643008 251 QAKISSIEFGYMEYAQARFDAYFDQKRKL 279
Cdd:PLN02421  289 QAKMSPIDFDYLGYFFLRYKEYKRQKEKL 317
PTZ00296 PTZ00296
choline kinase; Provisional
2-279 3.57e-43

choline kinase; Provisional


Pssm-ID: 240350 [Multi-domain]  Cd Length: 442  Bit Score: 152.74  E-value: 3.57e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643008   2 VLESVMFAILAERSLGPKLYGIFPQGRLEQFIPSRRLDTEELCLPDISAEIAEKMATFHGMK----MP--FNKEPKwLFG 75
Cdd:PTZ00296  157 ISEFEVYKTMSKYRIAPQLLNTFSGGRIEEWLYGDPLRIDDLKNPSILIGIANVLGKFHTLSrkrhLPehWDRTPC-IFK 235
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643008  76 TMEKYLNQVLRLKF-SREAR-----VQQLHKFLSY-NLPLELENLRSllqytrsPVVFCHNDCQEGNILllegqeNSEKq 148
Cdd:PTZ00296  236 MMEKWKNQLSKYKNiEKYQRdihkyIKESEKFIKFmKVYSKSDNLAN-------DIVFCHNDLQENNII------NTNK- 301
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643008 149 KLMLIDFEYSSYNYRGFDIGNHFCEWMYDYTYEKYPFFRANIQKYPTRKQQLHFISSYLTTFQNDfeSLSSEEQSATkeD 228
Cdd:PTZ00296  302 CLRLIDFEYSGYNFLATDIANFFIETTIDYSVSHYPFFAIDKKKYISYENRKLFITAYLSNYLDK--SLVVPNPKII--D 377
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1958643008 229 MLLE-VNRFALASHFLWGLWSIV---QAKiSSIEFGYMEYAQARFDAYFDQKRKL 279
Cdd:PTZ00296  378 QILEaVEVQALGAHLLWGFWSIIrgyQTK-SYNEFDFFLYAKERFKMYDEQKEYL 431
ChoK-like cd05151
Choline Kinase and similar proteins; This subfamily is composed of bacterial and eukaryotic ...
2-176 1.93e-22

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: 90.69  E-value: 1.93e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643008   2 VLESVMFAILAERSLGPKLYGIFPQ--GRLEQFIPSRRLDTEELCLPDISAEIAEKMATFHGMKMPfnkepkwlfgtmek 79
Cdd:cd05151    40 ENEKANSKAAAELGIAPEVIYFDPEtgVKITEFIEGATLLTNDFSDPENLERIAALLRKLHSSPLE-------------- 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643008  80 ylnqvlrlkfsrearvqqlhkflsynlplelenlrsllqytrsPVVFCHNDCQEGNILLLEGqensekqKLMLIDFEYSS 159
Cdd:cd05151   106 -------------------------------------------DLVLCHNDLVPGNFLLDDD-------RLYLIDWEYAG 135
                         170
                  ....*....|....*..
gi 1958643008 160 YNYRGFDIGNHFCEWMY 176
Cdd:cd05151   136 MNDPLFDLAALFSENNL 152
APH_ChoK_like cd05120
Aminoglycoside 3'-phosphotransferase and Choline Kinase family; This family is composed of APH, ...
1-176 4.24e-15

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: 71.18  E-value: 4.24e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643008   1 MVLESVMFAILAERS--LGPKLYGIFP----QGRLEQFIPSRRLDTEELCL-----PDISAEIAEKMATFHGMKMPfnke 69
Cdd:cd05120    36 LEKEAAMLQLLAGKLslPVPKVYGFGEsdgwEYLLMERIEGETLSEVWPRLseeekEKIADQLAEILAALHRIDSS---- 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643008  70 pkwlfgtmekylnqvlrlkfsrearvqqlhkflsynlplelenlrsllqytrspvVFCHNDCQEGNILLLEgqensEKQK 149
Cdd:cd05120   112 -------------------------------------------------------VLTHGDLHPGNILVKP-----DGKL 131
                         170       180
                  ....*....|....*....|....*..
gi 1958643008 150 LMLIDFEYSSYNYRGFDIGNHFCEWMY 176
Cdd:cd05120   132 SGIIDWEFAGYGPPAFDYAAALRDWTE 158
CotS COG0510
Thiamine kinase or a related kinase [Coenzyme transport and metabolism];
86-269 2.53e-11

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


Pssm-ID: 440276 [Multi-domain]  Cd Length: 156  Bit Score: 60.57  E-value: 2.53e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643008  86 RLKFSREARVQQLHKFLSynlplELENLRSLLQYTRSPVVFCHNDCQEGNILLlegqenSEKQKLMLIDFEYSSYNYRGF 165
Cdd:COG0510    16 RLERYLALGPRDLPELLR-----RLEELERALAARPLPLVLCHGDLHPGNFLV------TDDGRLYLIDWEYAGLGDPAF 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643008 166 DIGNHFCEWMYDytyekypffraniqkyptRKQQLHFISSYlttfqnDFESLSSEEqsatkedmLLEVNRFALASHFLWG 245
Cdd:COG0510    85 DLAALLVEYGLS------------------PEQAEELLEAY------GFGRPTEEL--------LRRLRAYRALADLLWA 132
                         170       180
                  ....*....|....*....|....
gi 1958643008 246 LWSIVQAkISSIEFGYMEYAQARF 269
Cdd:COG0510   133 LWALVRA-AQEANGDLLKYLLRRL 155
PTZ00384 PTZ00384
choline kinase; Provisional
124-250 2.87e-07

choline kinase; Provisional


Pssm-ID: 173576 [Multi-domain]  Cd Length: 383  Bit Score: 50.93  E-value: 2.87e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643008 124 VVFCHNDCQEGNILllegqenSEKQKLMLIDFEYSSYNYRGFDIGNHFCEWMYDYTYEKYPFFRANIQKYPTRKQQLHFI 203
Cdd:PTZ00384  227 VLFCHNDLFFTNIL-------DFNQGIYFIDFDFAGFNYVGWEIANFFVKLYIVYDPPTPPYFNSDDSLALSEEMKTIFV 299
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1958643008 204 SSYLTTF--QNdfeSLSSEEqsaTKEDMLLEVNRFALASHFLWGLWSIV 250
Cdd:PTZ00384  300 SVYLSQLlgKN---VLPSDD---LVKEFLQSLEIHTLGVNLFWTYWGIV 342
APH pfam01636
Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance ...
8-174 1.22e-06

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: 48.27  E-value: 1.22e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643008   8 FAILAERSLGPKLYGIFPqgrleqFIP--SRRLDTEELCLPDISAEIAEKMATFHG---MKMPFNKEPKWLFGTMEKYLN 82
Cdd:pfam01636  59 LAGCTDAELLGLPFLLME------YLPgeVLARPLLPEERGALLEALGRALARLHAvdpAALPLAGRLARLLELLRQLEA 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643008  83 QVLRLKFS-----REARVQQLHKFLSYNLPLELenlrsllqytrsPVVFCHNDCQEGNILLLEGQENSEkqklmLIDFEY 157
Cdd:pfam01636 133 ALARLLAAelldrLEELEERLLAALLALLPAEL------------PPVLVHGDLHPGNLLVDPGGRVSG-----VIDFED 195
                         170       180
                  ....*....|....*....|
gi 1958643008 158 SSYNYRGFDIG---NHFCEW 174
Cdd:pfam01636 196 AGLGDPAYDLAillNSWGRE 215
HomoserineK_II cd05153
Type II Homoserine Kinase; This subfamily is composed of unusual homoserine kinases, from a ...
16-172 1.30e-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: 1.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643008  16 LGPKLYGIFPqgrleqFIP--SRRLDTEELClpdisAEIAEKMATFHG------MKMPFNKEPKWlfgtMEKYLNQVLrl 87
Cdd:cd05153    86 LNGKPAALFP------FLPgeSLTTPTPEQC-----RAIGAALARLHLalagfpPPRPNPRGLAW----WKPLAERLK-- 148
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643008  88 kfsreARVQQLHKFLSYNLPLELENLRsLLQYTRSPVVFCHNDCQEGNILLLEGQensekqKLMLIDFEYSSYNYRGFDI 167
Cdd:cd05153   149 -----ARLDLLAADDRALLEDELARLQ-ALAPSDLPRGVIHADLFRDNVLFDGDR------LSGIIDFYDACYDPLLYDL 216

                  ....*...
gi 1958643008 168 G---NHFC 172
Cdd:cd05153   217 AialNDWC 224
SrkA COG2334
Ser/Thr protein kinase RdoA involved in Cpx stress response, MazF antagonist [Signal ...
14-168 1.98e-04

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: 42.22  E-value: 1.98e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643008  14 RSLGPKLYGIFPqgrleqFIP--SRRLDTEELClpdisAEIAEKMATFH----GMKMPFNKEPKWLFGTMEKYLNQVLRL 87
Cdd:COG2334    84 LELEGRPAALFP------FLPgrSPEEPSPEQL-----EELGRLLARLHralaDFPRPNARDLAWWDELLERLLGPLLPD 152
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643008  88 KfSREARVQQLHKFLSYNLPLELENLRSLLqytrspvvfCHNDCQEGNILLLEGqensekQKLMLIDFEYSSYNYRGFDI 167
Cdd:COG2334   153 P-EDRALLEELLDRLEARLAPLLGALPRGV---------IHGDLHPDNVLFDGD------GVSGLIDFDDAGYGPRLYDL 216

                  .
gi 1958643008 168 G 168
Cdd:COG2334   217 A 217
spore_CotS TIGR02906
spore coat protein, CotS family; Members of this family include the spore coat proteins CotS ...
45-169 5.43e-04

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: 40.73  E-value: 5.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643008  45 LPDISAEIAEKMATFhgMKMPFNKEPKWLFG-----TMEKYLNQVLRLKfsrearvQQLHKFLSYNLPLELENLRSllqy 119
Cdd:TIGR02906 122 WPKQFEKRLKELERF--KKIALEKKYKDEFDklylkEVDYFLERGKKAL-------ELLNKSKYYDLCKEAKKIRG---- 188
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1958643008 120 trspvvFCHNDCQEGNILLLEGqensekqKLMLIDFEYSSYNYRGFDIGN 169
Cdd:TIGR02906 189 ------FCHQDYAYHNILLKDN-------EVYVIDFDYCTIDLPVRDLRK 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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