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Conserved domains on  [gi|226694197|sp|P35790|]
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RecName: Full=Choline kinase alpha; Short=CK; AltName: Full=CHETK-alpha; AltName: Full=Ethanolamine kinase; Short=EK

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 ...
111-452 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: 566.87  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226694197 111 FHISVIRGGLSNMLFQCSLPDTTATLGDEPRKVLLRLYGAILQmrscnkegseqaqkenefqGAEAMVLESVMFAILAER 190
Cdd:cd05156    1 FGIKTITGGLSNLLYLCSLPDGVVPVGGEPRKVLLRIYGQILQ-------------------AEESLVTESVIFALLSER 61
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226694197 191 SLGPKLYGIFPQGRLEQFIPSRRLDTEELSLPDISAEIAEKMATFHGMKMPFNKEPKWLFGTMEKYLKEVLRIKFTEESR 270
Cdd:cd05156   62 GLGPKLYGIFPGGRLEEFIPSRPLTTDELSLPEISRKIARKMARFHSLEMPISKEPKWLFDTMERWLKEALSILFTDEPT 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226694197 271 I--KKLHKLLSYNLPLELENLRSLLESTPSPVVFCHNDCQEGNILLLEGRENSEKQKLMLIDFEYSSYNYRGFDIGNHFC 348
Cdd:cd05156  142 KpsKQLELLLSYDLAKELGWLRSLLESTPSPVVFCHNDLQEGNILLLNGPENSEDDKLVLIDFEYCSYNYRGFDLANHFC 221
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226694197 349 EWMYDYSYEKYPFFRANIRKYPTKKQQLHFISSYLPAFQNDFENLSTEEKSIIKEEMLLEVNRFALASHFLWGLWSIVQA 428
Cdd:cd05156  222 EWAYDYTVPEPPYFKINPENYPTREQQLHFIRAYLDEQYKDKTNDLTEERSKEEEKLLLEVNRFALASHFFWGLWSIVQA 301
                        330       340
                 ....*....|....*....|....
gi 226694197 429 KISSIEFGYMDYAQARFDAYFHQK 452
Cdd:cd05156  302 KISSIEFGYLEYAQARLDAYFKQK 325
 
Name Accession Description Interval E-value
ChoK_euk cd05156
Euykaryotic Choline Kinase; ChoK catalyzes the transfer of the gamma-phosphoryl group from ATP ...
111-452 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: 566.87  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226694197 111 FHISVIRGGLSNMLFQCSLPDTTATLGDEPRKVLLRLYGAILQmrscnkegseqaqkenefqGAEAMVLESVMFAILAER 190
Cdd:cd05156    1 FGIKTITGGLSNLLYLCSLPDGVVPVGGEPRKVLLRIYGQILQ-------------------AEESLVTESVIFALLSER 61
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226694197 191 SLGPKLYGIFPQGRLEQFIPSRRLDTEELSLPDISAEIAEKMATFHGMKMPFNKEPKWLFGTMEKYLKEVLRIKFTEESR 270
Cdd:cd05156   62 GLGPKLYGIFPGGRLEEFIPSRPLTTDELSLPEISRKIARKMARFHSLEMPISKEPKWLFDTMERWLKEALSILFTDEPT 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226694197 271 I--KKLHKLLSYNLPLELENLRSLLESTPSPVVFCHNDCQEGNILLLEGRENSEKQKLMLIDFEYSSYNYRGFDIGNHFC 348
Cdd:cd05156  142 KpsKQLELLLSYDLAKELGWLRSLLESTPSPVVFCHNDLQEGNILLLNGPENSEDDKLVLIDFEYCSYNYRGFDLANHFC 221
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226694197 349 EWMYDYSYEKYPFFRANIRKYPTKKQQLHFISSYLPAFQNDFENLSTEEKSIIKEEMLLEVNRFALASHFLWGLWSIVQA 428
Cdd:cd05156  222 EWAYDYTVPEPPYFKINPENYPTREQQLHFIRAYLDEQYKDKTNDLTEERSKEEEKLLLEVNRFALASHFFWGLWSIVQA 301
                        330       340
                 ....*....|....*....|....
gi 226694197 429 KISSIEFGYMDYAQARFDAYFHQK 452
Cdd:cd05156  302 KISSIEFGYLEYAQARLDAYFKQK 325
Choline_kinase pfam01633
Choline/ethanolamine kinase; Choline kinase catalyzes the committed step in the synthesis of ...
139-374 1.91e-85

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


Pssm-ID: 396278 [Multi-domain]  Cd Length: 211  Bit Score: 260.67  E-value: 1.91e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226694197  139 EPRKVLLRLYGAILQmrscnkegseqaqkenefqGAEAMVLESVMFAILAERSLGPKLYGIFPQGRLEQFIPSRRLDTEE 218
Cdd:pfam01633   1 SPRKVLLRIYGPGTE-------------------LLINREDEIVNFALLSERGLGPKLYGFFPNGRIEEFIPSRTLSTED 61
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226694197  219 LSLPDISAEIAEKMATFHGMKMPFNKEPkWLFGTMEKYLKEVLRIK-FTEESRIKKLHKLLSYNLPLELENLRSLLESTP 297
Cdd:pfam01633  62 LRDPEISKLIAKRLAELHSLEMPGKKSP-SLWKTMRKWLSLLKNLGaPESVNKSEQLKSINLEDLEKEINKLEKWLELLD 140
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 226694197  298 SPVVFCHNDCQEGNILLLEgrensEKQKLMLIDFEYSSYNYRGFDIGNHFCEWMYDYSYEKyPFFRANIRKYPTKKQ 374
Cdd:pfam01633 141 SPIVFCHNDLQSGNILLLN-----ETKRLVLIDFEYASYNYRGFDIANHFCEWAGDYHDPT-PFFKCDYSLYPTREE 211
PLN02236 PLN02236
choline kinase
99-455 4.59e-66

choline kinase


Pssm-ID: 177880 [Multi-domain]  Cd Length: 344  Bit Score: 215.29  E-value: 4.59e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226694197  99 LPGAWRGLREDE-FHISVIRGGLSNMLFQCSLPDTTatlGDEPRKVLLRLYGailqmrscnkEGSEQA-QKENEFQGAEA 176
Cdd:PLN02236  26 LASKWGDVVDDEaLQVIPLKGAMTNEVFQIKWPTKE---GNLGRKVLVRIYG----------EGVELFfDRDDEIRTFEC 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226694197 177 MvlesvmfailAERSLGPKLYGIFPQGRLEQFIPSRRLDTEELSLPDISAEIAEKMATFHGMKMPFNKEPKwLFGTMEKY 256
Cdd:PLN02236  93 M----------SRHGQGPRLLGRFPNGRVEEFIHARTLSAADLRDPEISALIAAKLREFHSLDMPGPKNVL-LWDRLRNW 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226694197 257 LKEVLRIKFTEESRIKKLHKLlsynlplelENLRSLLESTPSPVV----FCHNDCQEGNILLLEgrensEKQKLMLIDFE 332
Cdd:PLN02236 162 LKEAKNLCSPEEAKEFRLDSL---------EDEINLLEKELSGDDqeigFCHNDLQYGNIMIDE-----ETRAITIIDYE 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226694197 333 YSSYNYRGFDIGNHFCEWMYDYSYEKyPFfRANIRKYPTKKQQLHFISSYLPAfqndfenlSTEEKSIIKEEMLLE-VNR 411
Cdd:PLN02236 228 YASYNPVAYDIANHFCEMAADYHSET-PH-ILDYSKYPGEEERRRFIRTYLSS--------SGEEPSDEEVEQLLDdVEK 297
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 226694197 412 FALASHFLWGLWSIVQAKISSIEFGYMDYAQARFDAYFHQKRKL 455
Cdd:PLN02236 298 YTLASHLFWGLWGIISGHVNKIDFDYMEYARQRFEQYWLRKPEL 341
CotS COG0510
Thiamine kinase or a related kinase [Coenzyme transport and metabolism];
262-445 1.13e-13

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


Pssm-ID: 440276 [Multi-domain]  Cd Length: 156  Bit Score: 68.27  E-value: 1.13e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226694197 262 RIKFTEESRIKKLHKLLSynlplELENLRSLLESTPSPVVFCHNDCQEGNILLlegrenSEKQKLMLIDFEYSSYNYRGF 341
Cdd:COG0510   16 RLERYLALGPRDLPELLR-----RLEELERALAARPLPLVLCHGDLHPGNFLV------TDDGRLYLIDWEYAGLGDPAF 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226694197 342 DIGNHFCEWMYDysyekypffranirkyptKKQQLHFISSYlpafqnDFENLSteeksiikEEMLLEVNRFALASHFLWG 421
Cdd:COG0510   85 DLAALLVEYGLS------------------PEQAEELLEAY------GFGRPT--------EELLRRLRAYRALADLLWA 132
                        170       180
                 ....*....|....*....|....
gi 226694197 422 LWSIVQAkISSIEFGYMDYAQARF 445
Cdd:COG0510  133 LWALVRA-AQEANGDLLKYLLRRL 155
spore_CotS TIGR02906
spore coat protein, CotS family; Members of this family include the spore coat proteins CotS ...
228-390 6.97e-06

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: 47.66  E-value: 6.97e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226694197  228 IAEKMATFH----GMKMPFNKEPKWLFGTM----EKYLKEVLRIK-----FTEESRIKKLH-KLLSYNLPLELENLRSLL 293
Cdd:TIGR02906  93 AAKGLALFHhaskGYVPPDGSKIRSKLGKWpkqfEKRLKELERFKkialeKKYKDEFDKLYlKEVDYFLERGKKALELLN 172
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226694197  294 ESTPSPVV--------FCHNDCQEGNILLLEGrensekqKLMLIDFEYSSYNYRGFDIGNHFCEWMYDYSYEKYPFFRAN 365
Cdd:TIGR02906 173 KSKYYDLCkeakkirgFCHQDYAYHNILLKDN-------EVYVIDFDYCTIDLPVRDLRKLIIKLMKKNGVWDLEKAKEI 245
                         170       180
                  ....*....|....*....|....*....
gi 226694197  366 IRKY----PTKKQQLHFISSYLpAFQNDF 390
Cdd:TIGR02906 246 IEAYssinPLSKEEKEVLYIDL-AFPHKF 273
CHK smart00587
ZnF_C4 abd HLH domain containing kinases domain; subfamily of choline kinases
230-343 1.36e-03

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


Pssm-ID: 214734  Cd Length: 196  Bit Score: 40.01  E-value: 1.36e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226694197   230 EKMATFH--------------------GMKMPFNKE-PKWLFGTMEKYLKEVLRIK--FTEESRIKKLHKLLSYnlpLEL 286
Cdd:smart00587  30 KKLAKLHaasavlieeekgsyleefdeGLFERFKRMfSEEFIGGLENFLRELLSQPelLKVEEYIEKLDKLLDN---LED 106
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 226694197   287 ENLRSLLESTPSPVVFCHNDCQEGNILLLEGrENSEKQKLMLIDFEYSSYNYRGFDI 343
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 ...
111-452 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: 566.87  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226694197 111 FHISVIRGGLSNMLFQCSLPDTTATLGDEPRKVLLRLYGAILQmrscnkegseqaqkenefqGAEAMVLESVMFAILAER 190
Cdd:cd05156    1 FGIKTITGGLSNLLYLCSLPDGVVPVGGEPRKVLLRIYGQILQ-------------------AEESLVTESVIFALLSER 61
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226694197 191 SLGPKLYGIFPQGRLEQFIPSRRLDTEELSLPDISAEIAEKMATFHGMKMPFNKEPKWLFGTMEKYLKEVLRIKFTEESR 270
Cdd:cd05156   62 GLGPKLYGIFPGGRLEEFIPSRPLTTDELSLPEISRKIARKMARFHSLEMPISKEPKWLFDTMERWLKEALSILFTDEPT 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226694197 271 I--KKLHKLLSYNLPLELENLRSLLESTPSPVVFCHNDCQEGNILLLEGRENSEKQKLMLIDFEYSSYNYRGFDIGNHFC 348
Cdd:cd05156  142 KpsKQLELLLSYDLAKELGWLRSLLESTPSPVVFCHNDLQEGNILLLNGPENSEDDKLVLIDFEYCSYNYRGFDLANHFC 221
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226694197 349 EWMYDYSYEKYPFFRANIRKYPTKKQQLHFISSYLPAFQNDFENLSTEEKSIIKEEMLLEVNRFALASHFLWGLWSIVQA 428
Cdd:cd05156  222 EWAYDYTVPEPPYFKINPENYPTREQQLHFIRAYLDEQYKDKTNDLTEERSKEEEKLLLEVNRFALASHFFWGLWSIVQA 301
                        330       340
                 ....*....|....*....|....
gi 226694197 429 KISSIEFGYMDYAQARFDAYFHQK 452
Cdd:cd05156  302 KISSIEFGYLEYAQARLDAYFKQK 325
ETNK_euk cd05157
Euykaryotic Ethanolamine kinase; ETNK catalyzes the transfer of the gamma-phosphoryl group ...
111-449 1.26e-103

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: 310.67  E-value: 1.26e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226694197 111 FHISVIRGGLSNMLFQCSLPDttatlGDEPRKVLLRLYGailqmrscnkEGSEQA---QKENEfqgaeamvlesvMFAIL 187
Cdd:cd05157    1 IKVKRITGGITNALYKVTYPS-----GDTPKTVLVRIYG----------PGTELLidrDRELR------------ILQLL 53
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226694197 188 AERSLGPKLYGIFPQGRLEQFIPSRRLDTEELSLPDISAEIAEKMATFHGMKMPFNKEPKW---LFGTMEKYLkEVLRIK 264
Cdd:cd05157   54 SRAGIGPKLYGRFENGRVEEFLPGRTLTPEDLRDPKISRLIARRLAELHSIVPLGEIEGKKkpiLWTTIRKWL-DLAPEV 132
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226694197 265 FTEESRIKKLHKLLSYN-LPLELENLRSLLES-TPSPVVFCHNDCQEGNILLLEgrensEKQKLMLIDFEYSSYNYRGFD 342
Cdd:cd05157  133 FEDEKNKEKKLEKVDLErLRKELEWLEKWLESlEKSPIVFCHNDLLYGNILYNE-----DDDSVTFIDFEYAGPNPRAFD 207
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226694197 343 IGNHFCEWMYDYSYEKYpffraniRKYPTKKQQLHFISSYLPAFQNDFENLSTEEKSIikEEMLLEVNRFALASHFLWGL 422
Cdd:cd05157  208 IANHFCEWAGFYCVLDY-------SRYPTKEEQRNFLRAYLESLDGLPGGEEVSEEEV--EKLYNEVNLFRLASHLFWGL 278
                        330       340
                 ....*....|....*....|....*..
gi 226694197 423 WSIVQAKISSIEFGYMDYAQARFDAYF 449
Cdd:cd05157  279 WALIQAAISSIDFDYLGYAKERLDEYW 305
ChoK-like_euk cd14021
Euykaryotic Choline Kinase and similar proteins; This group is composed of eukaryotic choline ...
112-425 9.86e-87

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: 264.90  E-value: 9.86e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226694197 112 HISVIRGGLSNMLFQCSLPDTTATLgdEPRKVLLRLYGAIlqmrscnkegseqaqkeneFQGAEAMVLESVMFAILAERS 191
Cdd:cd14021    2 LVIRILSGLTNQVYKVSLKDESDSL--EPKKVLFRIYGKY-------------------LSTLYDREKESEVFKILSEQG 60
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226694197 192 LGPKLYGIFPQGRLEQFIPSRRLDTEELSLPDISAEIAEKMATFHGMKMPfnkepkwlfgtmekylkevlrikfteesri 271
Cdd:cd14021   61 LGPKLIYKFDGGRIEEYIDGRPLTTDELRNPSVLTSIAKLLAKFHKIKTP------------------------------ 110
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226694197 272 kklhkllsynlplelenlrsllestpsPVVFCHNDCQEGNILLLegrenSEKQKLMLIDFEYSSYNYRGFDIGNHFCEWM 351
Cdd:cd14021  111 ---------------------------PVVFCHNDLQENNILLT-----NDQDGLRLIDFEYSGFNYRGYDIANFFNESM 158
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 226694197 352 YDYSYEKYPFFRANIRKYPTKKQQLHFISSYLPAFQNDFENLSTEEksiIKEEMLLEVNRFALASHFLWGLWSI 425
Cdd:cd14021  159 IDYDHPEPPYFKIYKENYISEEEKRLFVSVYLSEYLEKNVLPSLDK---LVEQFLQEVEIFTLGSHLYWGLWSI 229
Choline_kinase pfam01633
Choline/ethanolamine kinase; Choline kinase catalyzes the committed step in the synthesis of ...
139-374 1.91e-85

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


Pssm-ID: 396278 [Multi-domain]  Cd Length: 211  Bit Score: 260.67  E-value: 1.91e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226694197  139 EPRKVLLRLYGAILQmrscnkegseqaqkenefqGAEAMVLESVMFAILAERSLGPKLYGIFPQGRLEQFIPSRRLDTEE 218
Cdd:pfam01633   1 SPRKVLLRIYGPGTE-------------------LLINREDEIVNFALLSERGLGPKLYGFFPNGRIEEFIPSRTLSTED 61
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226694197  219 LSLPDISAEIAEKMATFHGMKMPFNKEPkWLFGTMEKYLKEVLRIK-FTEESRIKKLHKLLSYNLPLELENLRSLLESTP 297
Cdd:pfam01633  62 LRDPEISKLIAKRLAELHSLEMPGKKSP-SLWKTMRKWLSLLKNLGaPESVNKSEQLKSINLEDLEKEINKLEKWLELLD 140
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 226694197  298 SPVVFCHNDCQEGNILLLEgrensEKQKLMLIDFEYSSYNYRGFDIGNHFCEWMYDYSYEKyPFFRANIRKYPTKKQ 374
Cdd:pfam01633 141 SPIVFCHNDLQSGNILLLN-----ETKRLVLIDFEYASYNYRGFDIANHFCEWAGDYHDPT-PFFKCDYSLYPTREE 211
PLN02236 PLN02236
choline kinase
99-455 4.59e-66

choline kinase


Pssm-ID: 177880 [Multi-domain]  Cd Length: 344  Bit Score: 215.29  E-value: 4.59e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226694197  99 LPGAWRGLREDE-FHISVIRGGLSNMLFQCSLPDTTatlGDEPRKVLLRLYGailqmrscnkEGSEQA-QKENEFQGAEA 176
Cdd:PLN02236  26 LASKWGDVVDDEaLQVIPLKGAMTNEVFQIKWPTKE---GNLGRKVLVRIYG----------EGVELFfDRDDEIRTFEC 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226694197 177 MvlesvmfailAERSLGPKLYGIFPQGRLEQFIPSRRLDTEELSLPDISAEIAEKMATFHGMKMPFNKEPKwLFGTMEKY 256
Cdd:PLN02236  93 M----------SRHGQGPRLLGRFPNGRVEEFIHARTLSAADLRDPEISALIAAKLREFHSLDMPGPKNVL-LWDRLRNW 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226694197 257 LKEVLRIKFTEESRIKKLHKLlsynlplelENLRSLLESTPSPVV----FCHNDCQEGNILLLEgrensEKQKLMLIDFE 332
Cdd:PLN02236 162 LKEAKNLCSPEEAKEFRLDSL---------EDEINLLEKELSGDDqeigFCHNDLQYGNIMIDE-----ETRAITIIDYE 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226694197 333 YSSYNYRGFDIGNHFCEWMYDYSYEKyPFfRANIRKYPTKKQQLHFISSYLPAfqndfenlSTEEKSIIKEEMLLE-VNR 411
Cdd:PLN02236 228 YASYNPVAYDIANHFCEMAADYHSET-PH-ILDYSKYPGEEERRRFIRTYLSS--------SGEEPSDEEVEQLLDdVEK 297
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 226694197 412 FALASHFLWGLWSIVQAKISSIEFGYMDYAQARFDAYFHQKRKL 455
Cdd:PLN02236 298 YTLASHLFWGLWGIISGHVNKIDFDYMEYARQRFEQYWLRKPEL 341
PLN02421 PLN02421
phosphotransferase, alcohol group as acceptor/kinase
95-455 5.76e-66

phosphotransferase, alcohol group as acceptor/kinase


Pssm-ID: 215231 [Multi-domain]  Cd Length: 330  Bit Score: 214.60  E-value: 5.76e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226694197  95 CKEFLPGaWRGLREDEFHISVIRGGLSNMLFQCSLPDTTatlgDEPRKVLLRLYGAilqmrscNKEGSeqAQKENEFQGa 174
Cdd:PLN02421   2 CKALFKG-WSDLDDSDFSVERISGGITNLLLKVSVKEEN----GNEVSVTVRLFGP-------NTDYV--IDRERELQA- 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226694197 175 eamvlesvmFAILAERSLGPKLYGIFPQGRLEQFIPSRRLDTEELSLPDISAEIAEKMATFHGMKMPFNKEPKwLFGTME 254
Cdd:PLN02421  67 ---------IKYLSAAGFGAKLLGVFGNGMIQSFINARTLTPSDMRKPKVAAEIAKELRRLHQVEIPGSKEPQ-LWNDIF 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226694197 255 KYLKEVLRIKFTEESRIKKLHKLLSYNLPLELENLRSLLESTPSPVVFCHNDCQEGNILLlegreNSEKQKLMLIDFEYS 334
Cdd:PLN02421 137 KFYEKASTVKFEDPEKQKKYETISFEELRDEIVELKEITDSLKAPVVFAHNDLLSGNLML-----NEDEGKLYFIDFEYG 211
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226694197 335 SYNYRGFDIGNHFCEwmydysyekYPFFRANIRKYPTKKQQLHFISSYLpafQNDFENLSTEEKSiikEEMLLEVNRFAL 414
Cdd:PLN02421 212 SYSYRGYDIGNHFNE---------YAGFDCDYSLYPSKEEQYHFFRHYL---RPDDPEEVSDAEL---EELFVETNFYAL 276
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 226694197 415 ASHFLWGLWSIVQAKISSIEFGYMDYAQARFDAYFHQKRKL 455
Cdd:PLN02421 277 ASHLYWAIWAIVQAKMSPIDFDYLGYFFLRYKEYKRQKEKL 317
PTZ00296 PTZ00296
choline kinase; Provisional
95-455 2.67e-53

choline kinase; Provisional


Pssm-ID: 240350 [Multi-domain]  Cd Length: 442  Bit Score: 184.71  E-value: 2.67e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226694197  95 CKEFLPGaWRGLREDEFHISVIRGGLSNMLFQCSLPDTTATlgDEP---RKVLLRLYGailqmrscnKEGSEQAQKENEF 171
Cdd:PTZ00296  93 CLEKVPE-WRRFTEDDVRVNQILSGLTNQLFEVSLKEETAN--NYPsirRRVLFRIYG---------KDVDELYNPISEF 160
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226694197 172 QgaeamvlesvMFAILAERSLGPKLYGIFPQGRLEQFIPSRRLDTEELSLPDISAEIAEKMATFHGMK----MP--FNKE 245
Cdd:PTZ00296 161 E----------VYKTMSKYRIAPQLLNTFSGGRIEEWLYGDPLRIDDLKNPSILIGIANVLGKFHTLSrkrhLPehWDRT 230
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226694197 246 PKwLFGTMEKYLKEVLRIKFTEESR------IKKLHKLLSYnlplelENLRSLLESTPSPVVFCHNDCQEGNILllegre 319
Cdd:PTZ00296 231 PC-IFKMMEKWKNQLSKYKNIEKYQrdihkyIKESEKFIKF------MKVYSKSDNLANDIVFCHNDLQENNII------ 297
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226694197 320 NSEKqKLMLIDFEYSSYNYRGFDIGNHFCEWMYDYSYEKYPFFRANIRKYPTKKQQLHFISSYLPAFQNDfeNLSTEEKS 399
Cdd:PTZ00296 298 NTNK-CLRLIDFEYSGYNFLATDIANFFIETTIDYSVSHYPFFAIDKKKYISYENRKLFITAYLSNYLDK--SLVVPNPK 374
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 226694197 400 IIkEEMLLEVNRFALASHFLWGLWSIV---QAKiSSIEFGYMDYAQARFDAYFHQKRKL 455
Cdd:PTZ00296 375 II-DQILEAVEVQALGAHLLWGFWSIIrgyQTK-SYNEFDFFLYAKERFKMYDEQKEYL 431
ChoK-like cd05151
Choline Kinase and similar proteins; This subfamily is composed of bacterial and eukaryotic ...
112-352 1.16e-28

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: 1.16e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226694197 112 HISVIRGGLSNMLFQCSlpdttatlgDEPRKVLLRLYGAILQMrscnkegseQAQKENEFQGAEAmvlesvmfaiLAERS 191
Cdd:cd05151    2 TIEPLKGGLTNKNYLVE---------VAGKKYVLRIPGAGTEL---------LIDRENEKANSKA----------AAELG 53
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226694197 192 LGPKLYGIFPQ--GRLEQFIPSRRLDTEELSLPDISAEIAEKMATFHGMKMPfnkepkwlfgtmekylkevlrikftees 269
Cdd:cd05151   54 IAPEVIYFDPEtgVKITEFIEGATLLTNDFSDPENLERIAALLRKLHSSPLE---------------------------- 105
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226694197 270 rikklhkllsynlplelenlrsllestpsPVVFCHNDCQEGNILLLEGRensekqkLMLIDFEYSSYNYRGFDIGNHFCE 349
Cdd:cd05151  106 -----------------------------DLVLCHNDLVPGNFLLDDDR-------LYLIDWEYAGMNDPLFDLAALFSE 149

                 ...
gi 226694197 350 WMY 352
Cdd:cd05151  150 NNL 152
APH_ChoK_like cd05120
Aminoglycoside 3'-phosphotransferase and Choline Kinase family; This family is composed of APH, ...
112-352 1.50e-19

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: 85.05  E-value: 1.50e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226694197 112 HISVIRGGLSNMLFQCSlpdttatlgdEPRKVLLRLYGAILQmrscnkegseqaqkenefqgaEAMVLESVMFAILAERS 191
Cdd:cd05120    2 SVKLIKEGGDNKVYLLG----------DPREYVLKIGPPRLK---------------------KDLEKEAAMLQLLAGKL 50
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226694197 192 --LGPKLYGIFP----QGRLEQFIPSRRLDTE-----ELSLPDISAEIAEKMATFHGMKMPfnkepkwlfgtmekylkev 260
Cdd:cd05120   51 slPVPKVYGFGEsdgwEYLLMERIEGETLSEVwprlsEEEKEKIADQLAEILAALHRIDSS------------------- 111
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226694197 261 lrikfteesrikklhkllsynlplelenlrsllestpspvVFCHNDCQEGNILLLEgrensEKQKLMLIDFEYSSYNYRG 340
Cdd:cd05120  112 ----------------------------------------VLTHGDLHPGNILVKP-----DGKLSGIIDWEFAGYGPPA 146
                        250
                 ....*....|..
gi 226694197 341 FDIGNHFCEWMY 352
Cdd:cd05120  147 FDYAAALRDWTE 158
CotS COG0510
Thiamine kinase or a related kinase [Coenzyme transport and metabolism];
262-445 1.13e-13

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


Pssm-ID: 440276 [Multi-domain]  Cd Length: 156  Bit Score: 68.27  E-value: 1.13e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226694197 262 RIKFTEESRIKKLHKLLSynlplELENLRSLLESTPSPVVFCHNDCQEGNILLlegrenSEKQKLMLIDFEYSSYNYRGF 341
Cdd:COG0510   16 RLERYLALGPRDLPELLR-----RLEELERALAARPLPLVLCHGDLHPGNFLV------TDDGRLYLIDWEYAGLGDPAF 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226694197 342 DIGNHFCEWMYDysyekypffranirkyptKKQQLHFISSYlpafqnDFENLSteeksiikEEMLLEVNRFALASHFLWG 421
Cdd:COG0510   85 DLAALLVEYGLS------------------PEQAEELLEAY------GFGRPT--------EELLRRLRAYRALADLLWA 132
                        170       180
                 ....*....|....*....|....
gi 226694197 422 LWSIVQAkISSIEFGYMDYAQARF 445
Cdd:COG0510  133 LWALVRA-AQEANGDLLKYLLRRL 155
PTZ00384 PTZ00384
choline kinase; Provisional
186-426 5.25e-09

choline kinase; Provisional


Pssm-ID: 173576 [Multi-domain]  Cd Length: 383  Bit Score: 57.87  E-value: 5.25e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226694197 186 ILAERSLGPKLYGIFPQGRLEQFIPSRRLDTEELSLPDISAEIAEKMATFHgmKMPFNKEPK-W----LFGT-MEKYLKE 259
Cdd:PTZ00384 108 LLGDNNFGPKIIGRFGDFTIQEWVEGNTMGIDSLQNLSVLTGIASSLAKFH--KRVTELVPKeWdrtpMFLTkISTWSQH 185
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226694197 260 VLRIkfteesrIKKLHKLLSYN-LPLELENLRSLL-------ESTPSPVVFCHNDCQEGNILllegrenSEKQKLMLIDF 331
Cdd:PTZ00384 186 VERI-------IKKYNLDFDYNeLVQNYELFKKILnnhlntsNSITNSVLFCHNDLFFTNIL-------DFNQGIYFIDF 251
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226694197 332 EYSSYNYRGFDIGNHFCEWMYDYSYEKYPFFRANIRKYPTKKQQLHFISSYLPAFQNdfENLSTEEKSIikEEMLLEVNR 411
Cdd:PTZ00384 252 DFAGFNYVGWEIANFFVKLYIVYDPPTPPYFNSDDSLALSEEMKTIFVSVYLSQLLG--KNVLPSDDLV--KEFLQSLEI 327
                        250
                 ....*....|....*
gi 226694197 412 FALASHFLWGLWSIV 426
Cdd:PTZ00384 328 HTLGVNLFWTYWGIV 342
APH pfam01636
Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance ...
112-350 1.52e-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: 49.04  E-value: 1.52e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226694197  112 HISVIRGGLSNMLFQcslpdttatLGDEPRKVLLRLYgailqmrscnKEGSEQAQKENEFQgaeamvlesvMFAILAERS 191
Cdd:pfam01636   1 TLRPISSGASNRTYL---------VTTGDGRYVLRLP----------PPGRAAEELRRELA----------LLRHLAAAG 51
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226694197  192 LGPK---LYGIFPQGRLE------QFIP--SRRLDTEELSLPDISAEIAEKMATFHGMKMPFNKEPKWlfgtmEKYLKEV 260
Cdd:pfam01636  52 VPPVprvLAGCTDAELLGlpfllmEYLPgeVLARPLLPEERGALLEALGRALARLHAVDPAALPLAGR-----LARLLEL 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226694197  261 LRiKFTEESRIKKLHKLLSYNLPLELENLRSLLESTP--SPVVFCHNDCQEGNILLLEGRENSEkqklmLIDFEYSSYNY 338
Cdd:pfam01636 127 LR-QLEAALARLLAAELLDRLEELEERLLAALLALLPaeLPPVLVHGDLHPGNLLVDPGGRVSG-----VIDFEDAGLGD 200
                         250
                  ....*....|....*
gi 226694197  339 RGFDIG---NHFCEW 350
Cdd:pfam01636 201 PAYDLAillNSWGRE 215
spore_CotS TIGR02906
spore coat protein, CotS family; Members of this family include the spore coat proteins CotS ...
228-390 6.97e-06

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: 47.66  E-value: 6.97e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226694197  228 IAEKMATFH----GMKMPFNKEPKWLFGTM----EKYLKEVLRIK-----FTEESRIKKLH-KLLSYNLPLELENLRSLL 293
Cdd:TIGR02906  93 AAKGLALFHhaskGYVPPDGSKIRSKLGKWpkqfEKRLKELERFKkialeKKYKDEFDKLYlKEVDYFLERGKKALELLN 172
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226694197  294 ESTPSPVV--------FCHNDCQEGNILLLEGrensekqKLMLIDFEYSSYNYRGFDIGNHFCEWMYDYSYEKYPFFRAN 365
Cdd:TIGR02906 173 KSKYYDLCkeakkirgFCHQDYAYHNILLKDN-------EVYVIDFDYCTIDLPVRDLRKLIIKLMKKNGVWDLEKAKEI 245
                         170       180
                  ....*....|....*....|....*....
gi 226694197  366 IRKY----PTKKQQLHFISSYLpAFQNDF 390
Cdd:TIGR02906 246 IEAYssinPLSKEEKEVLYIDL-AFPHKF 273
HomoserineK_II cd05153
Type II Homoserine Kinase; This subfamily is composed of unusual homoserine kinases, from a ...
192-348 2.52e-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: 43.02  E-value: 2.52e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226694197 192 LGPKLYGIFPqgrleqFIPSRRLDTEElslPDISAEIAEKMATFHG------MKMPFNKEPKWlfgtMEKYLKevlRIKF 265
Cdd:cd05153   86 LNGKPAALFP------FLPGESLTTPT---PEQCRAIGAALARLHLalagfpPPRPNPRGLAW----WKPLAE---RLKA 149
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226694197 266 TEESRIKKLHKLLSynlpLELENLRSLLESTPsPVVFCHNDCQEGNILLLEGRensekqKLMLIDFEYSSYNYRGFDIG- 344
Cdd:cd05153  150 RLDLLAADDRALLE----DELARLQALAPSDL-PRGVIHADLFRDNVLFDGDR------LSGIIDFYDACYDPLLYDLAi 218

                 ....*.
gi 226694197 345 --NHFC 348
Cdd:cd05153  219 alNDWC 224
EcKL pfam02958
Ecdysteroid kinase-like family; This family includes ecdysteroid 22-kinase, an enzyme ...
249-347 1.02e-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: 41.10  E-value: 1.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226694197  249 LFGTMEKYLKEVLRIKFTEESRI-KKLHKLLSyNLpleLENLRSLLESTPSP-VVFCHNDCQEGNILLLEGrENSEKQKL 326
Cdd:pfam02958 165 LMETGLDAAAEALREQLPEYEKYaEKLEKLKD-NY---FDRLLRLVEPTPGEfNVLNHGDLWVNNIMFKYD-DEGEPEDV 239
                          90       100
                  ....*....|....*....|.
gi 226694197  327 MLIDFEYSSYNYRGFDIgNHF 347
Cdd:pfam02958 240 ILVDFQLSRYGSPAIDL-NYF 259
CHK smart00587
ZnF_C4 abd HLH domain containing kinases domain; subfamily of choline kinases
230-343 1.36e-03

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


Pssm-ID: 214734  Cd Length: 196  Bit Score: 40.01  E-value: 1.36e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226694197   230 EKMATFH--------------------GMKMPFNKE-PKWLFGTMEKYLKEVLRIK--FTEESRIKKLHKLLSYnlpLEL 286
Cdd:smart00587  30 KKLAKLHaasavlieeekgsyleefdeGLFERFKRMfSEEFIGGLENFLRELLSQPelLKVEEYIEKLDKLLDN---LED 106
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 226694197   287 ENLRSLLESTPSPVVFCHNDCQEGNILLLEGrENSEKQKLMLIDFEYSSYNYRGFDI 343
Cdd:smart00587 107 LKKEDKEPDEGEFNVLNHGDLWANNIMFKYD-DEGKPEDVALIDFQLSHYGSPAEDL 162
SrkA COG2334
Ser/Thr protein kinase RdoA involved in Cpx stress response, MazF antagonist [Signal ...
285-344 7.48e-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: 38.37  E-value: 7.48e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 226694197 285 ELENLRSLLESTPSPVVF--CHNDCQEGNILLLEGRensekqKLMLIDFEYSSYNYRGFDIG 344
Cdd:COG2334  162 LLDRLEARLAPLLGALPRgvIHGDLHPDNVLFDGDG------VSGLIDFDDAGYGPRLYDLA 217
 
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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