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Conserved domains on  [gi|2462522672|ref|XP_054223520|]
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choline kinase alpha isoform X4 [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 ...
1-298 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: 514.87  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462522672   1 MLFQCSLPDTTATLGDEPRKVLLRLYGAILQmGAEAMVLESVMFAILAERSLGPKLYGIFPQGRLEQFIPSRRLDTEELS 80
Cdd:cd05156    13 LLYLCSLPDGVVPVGGEPRKVLLRIYGQILQ-AEESLVTESVIFALLSERGLGPKLYGIFPGGRLEEFIPSRPLTTDELS 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462522672  81 LPDISAEIAEKMATFHGMKMPFNKEPKWLFGTMEKYLKEVLRIKFTEESRI--KKLHKLLSYNLPLELENLRSLLESTPS 158
Cdd:cd05156    92 LPEISRKIARKMARFHSLEMPISKEPKWLFDTMERWLKEALSILFTDEPTKpsKQLELLLSYDLAKELGWLRSLLESTPS 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462522672 159 PVVFCHNDCQEGNILLLEGRENSEKQKLMLIDFEYSSYNYRGFDIGNHFCEWMYDYSYEKYPFFRANIRKYPTKKQQLHF 238
Cdd:cd05156   172 PVVFCHNDLQEGNILLLNGPENSEDDKLVLIDFEYCSYNYRGFDLANHFCEWAYDYTVPEPPYFKINPENYPTREQQLHF 251
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462522672 239 ISSYLPAFQNDFENLSTEEKSIIKEEMLLEVNRFALASHFLWGLWSIVQAKISSIEFGYM 298
Cdd:cd05156   252 IRAYLDEQYKDKTNDLTEERSKEEEKLLLEVNRFALASHFFWGLWSIVQAKISSIEFGYL 311
 
Name Accession Description Interval E-value
ChoK_euk cd05156
Euykaryotic Choline Kinase; ChoK catalyzes the transfer of the gamma-phosphoryl group from ATP ...
1-298 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: 514.87  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462522672   1 MLFQCSLPDTTATLGDEPRKVLLRLYGAILQmGAEAMVLESVMFAILAERSLGPKLYGIFPQGRLEQFIPSRRLDTEELS 80
Cdd:cd05156    13 LLYLCSLPDGVVPVGGEPRKVLLRIYGQILQ-AEESLVTESVIFALLSERGLGPKLYGIFPGGRLEEFIPSRPLTTDELS 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462522672  81 LPDISAEIAEKMATFHGMKMPFNKEPKWLFGTMEKYLKEVLRIKFTEESRI--KKLHKLLSYNLPLELENLRSLLESTPS 158
Cdd:cd05156    92 LPEISRKIARKMARFHSLEMPISKEPKWLFDTMERWLKEALSILFTDEPTKpsKQLELLLSYDLAKELGWLRSLLESTPS 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462522672 159 PVVFCHNDCQEGNILLLEGRENSEKQKLMLIDFEYSSYNYRGFDIGNHFCEWMYDYSYEKYPFFRANIRKYPTKKQQLHF 238
Cdd:cd05156   172 PVVFCHNDLQEGNILLLNGPENSEDDKLVLIDFEYCSYNYRGFDLANHFCEWAYDYTVPEPPYFKINPENYPTREQQLHF 251
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462522672 239 ISSYLPAFQNDFENLSTEEKSIIKEEMLLEVNRFALASHFLWGLWSIVQAKISSIEFGYM 298
Cdd:cd05156   252 IRAYLDEQYKDKTNDLTEERSKEEEKLLLEVNRFALASHFFWGLWSIVQAKISSIEFGYL 311
Choline_kinase pfam01633
Choline/ethanolamine kinase; Choline kinase catalyzes the committed step in the synthesis of ...
17-234 2.33e-88

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: 264.52  E-value: 2.33e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462522672  17 EPRKVLLRLYGAILQmGAEAMVLESVMFAILAERSLGPKLYGIFPQGRLEQFIPSRRLDTEELSLPDISAEIAEKMATFH 96
Cdd:pfam01633   1 SPRKVLLRIYGPGTE-LLINREDEIVNFALLSERGLGPKLYGFFPNGRIEEFIPSRTLSTEDLRDPEISKLIAKRLAELH 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462522672  97 GMKMPFNKEPkWLFGTMEKYLKEVLRIK-FTEESRIKKLHKLLSYNLPLELENLRSLLESTPSPVVFCHNDCQEGNILLL 175
Cdd:pfam01633  80 SLEMPGKKSP-SLWKTMRKWLSLLKNLGaPESVNKSEQLKSINLEDLEKEINKLEKWLELLDSPIVFCHNDLQSGNILLL 158
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462522672 176 EgrensEKQKLMLIDFEYSSYNYRGFDIGNHFCEWMYDYSYEKyPFFRANIRKYPTKKQ 234
Cdd:pfam01633 159 N-----ETKRLVLIDFEYASYNYRGFDIANHFCEWAGDYHDPT-PFFKCDYSLYPTREE 211
PLN02236 PLN02236
choline kinase
3-298 1.21e-57

choline kinase


Pssm-ID: 177880 [Multi-domain]  Cd Length: 344  Bit Score: 190.26  E-value: 1.21e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462522672   3 FQCSLPDTTatlGDEPRKVLLRLYGAilqmGAEAMVL---ESVMFAILAERSLGPKLYGIFPQGRLEQFIPSRRLDTEEL 79
Cdd:PLN02236   53 FQIKWPTKE---GNLGRKVLVRIYGE----GVELFFDrddEIRTFECMSRHGQGPRLLGRFPNGRVEEFIHARTLSAADL 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462522672  80 SLPDISAEIAEKMATFHGMKMPFNKEPKwLFGTMEKYLKEVLRIKFTEESRIKKLHKllsynlpleLENLRSLLESTPSP 159
Cdd:PLN02236  126 RDPEISALIAAKLREFHSLDMPGPKNVL-LWDRLRNWLKEAKNLCSPEEAKEFRLDS---------LEDEINLLEKELSG 195
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462522672 160 VV----FCHNDCQEGNILLLEgrensEKQKLMLIDFEYSSYNYRGFDIGNHFCEWMYDYSYEKyPfFRANIRKYPTKKQQ 235
Cdd:PLN02236  196 DDqeigFCHNDLQYGNIMIDE-----ETRAITIIDYEYASYNPVAYDIANHFCEMAADYHSET-P-HILDYSKYPGEEER 268
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462522672 236 LHFISSYLPAfqndfenlSTEEKSIIKEEMLL-EVNRFALASHFLWGLWSIVQAKISSIEFGYM 298
Cdd:PLN02236  269 RRFIRTYLSS--------SGEEPSDEEVEQLLdDVEKYTLASHLFWGLWGIISGHVNKIDFDYM 324
CotS COG0510
Thiamine kinase or a related kinase [Coenzyme transport and metabolism];
122-288 6.22e-13

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


Pssm-ID: 440276 [Multi-domain]  Cd Length: 156  Bit Score: 65.96  E-value: 6.22e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462522672 122 RIKFTEESRIKKLHKLLSynlplELENLRSLLESTPSPVVFCHNDCQEGNILLlegrenSEKQKLMLIDFEYSSYNYRGF 201
Cdd:COG0510    16 RLERYLALGPRDLPELLR-----RLEELERALAARPLPLVLCHGDLHPGNFLV------TDDGRLYLIDWEYAGLGDPAF 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462522672 202 DIGNHFCEWMYDysyekypffranirkyptKKQQLHFISSYlpafqnDFENLSteeksiikEEMLLEVNRFALASHFLWG 281
Cdd:COG0510    85 DLAALLVEYGLS------------------PEQAEELLEAY------GFGRPT--------EELLRRLRAYRALADLLWA 132

                  ....*..
gi 2462522672 282 LWSIVQA 288
Cdd:COG0510   133 LWALVRA 139
spore_CotS TIGR02906
spore coat protein, CotS family; Members of this family include the spore coat proteins CotS ...
88-250 1.53e-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: 46.12  E-value: 1.53e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462522672  88 IAEKMATFH----GMKMPFNKEPKWLFGTM----EKYLKEVLRIK-----FTEESRIKKLH-KLLSYNLPLELENLRSLL 153
Cdd:TIGR02906  93 AAKGLALFHhaskGYVPPDGSKIRSKLGKWpkqfEKRLKELERFKkialeKKYKDEFDKLYlKEVDYFLERGKKALELLN 172
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462522672 154 ESTPSPVV--------FCHNDCQEGNILLLEGrensekqKLMLIDFEYSSYNYRGFDIGNHFCEWMYDYSYEKYPFFRAN 225
Cdd:TIGR02906 173 KSKYYDLCkeakkirgFCHQDYAYHNILLKDN-------EVYVIDFDYCTIDLPVRDLRKLIIKLMKKNGVWDLEKAKEI 245
                         170       180
                  ....*....|....*....|....*....
gi 2462522672 226 IRKY----PTKKQQLHFISSYLpAFQNDF 250
Cdd:TIGR02906 246 IEAYssinPLSKEEKEVLYIDL-AFPHKF 273
CHK smart00587
ZnF_C4 abd HLH domain containing kinases domain; subfamily of choline kinases
90-203 2.26e-03

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


Pssm-ID: 214734  Cd Length: 196  Bit Score: 38.85  E-value: 2.26e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462522672   90 EKMATFH--------------------GMKMPFNKE-PKWLFGTMEKYLKEVLRIK--FTEESRIKKLHKLLSYnlpLEL 146
Cdd:smart00587  30 KKLAKLHaasavlieeekgsyleefdeGLFERFKRMfSEEFIGGLENFLRELLSQPelLKVEEYIEKLDKLLDN---LED 106
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462522672  147 ENLRSLLESTPSPVVFCHNDCQEGNILLLEGrENSEKQKLMLIDFEYSSYNYRGFDI 203
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 ...
1-298 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: 514.87  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462522672   1 MLFQCSLPDTTATLGDEPRKVLLRLYGAILQmGAEAMVLESVMFAILAERSLGPKLYGIFPQGRLEQFIPSRRLDTEELS 80
Cdd:cd05156    13 LLYLCSLPDGVVPVGGEPRKVLLRIYGQILQ-AEESLVTESVIFALLSERGLGPKLYGIFPGGRLEEFIPSRPLTTDELS 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462522672  81 LPDISAEIAEKMATFHGMKMPFNKEPKWLFGTMEKYLKEVLRIKFTEESRI--KKLHKLLSYNLPLELENLRSLLESTPS 158
Cdd:cd05156    92 LPEISRKIARKMARFHSLEMPISKEPKWLFDTMERWLKEALSILFTDEPTKpsKQLELLLSYDLAKELGWLRSLLESTPS 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462522672 159 PVVFCHNDCQEGNILLLEGRENSEKQKLMLIDFEYSSYNYRGFDIGNHFCEWMYDYSYEKYPFFRANIRKYPTKKQQLHF 238
Cdd:cd05156   172 PVVFCHNDLQEGNILLLNGPENSEDDKLVLIDFEYCSYNYRGFDLANHFCEWAYDYTVPEPPYFKINPENYPTREQQLHF 251
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462522672 239 ISSYLPAFQNDFENLSTEEKSIIKEEMLLEVNRFALASHFLWGLWSIVQAKISSIEFGYM 298
Cdd:cd05156   252 IRAYLDEQYKDKTNDLTEERSKEEEKLLLEVNRFALASHFFWGLWSIVQAKISSIEFGYL 311
ETNK_euk cd05157
Euykaryotic Ethanolamine kinase; ETNK catalyzes the transfer of the gamma-phosphoryl group ...
1-298 5.19e-94

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: 282.55  E-value: 5.19e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462522672   1 MLFQCSLPDttatlGDEPRKVLLRLYGAilqmGAEAMV---LESVMFAILAERSLGPKLYGIFPQGRLEQFIPSRRLDTE 77
Cdd:cd05157    13 ALYKVTYPS-----GDTPKTVLVRIYGP----GTELLIdrdRELRILQLLSRAGIGPKLYGRFENGRVEEFLPGRTLTPE 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462522672  78 ELSLPDISAEIAEKMATFHGMKMPFNKEPKW---LFGTMEKYLkEVLRIKFTEESRIKKLHKLLSYN-LPLELENLRSLL 153
Cdd:cd05157    84 DLRDPKISRLIARRLAELHSIVPLGEIEGKKkpiLWTTIRKWL-DLAPEVFEDEKNKEKKLEKVDLErLRKELEWLEKWL 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462522672 154 ES-TPSPVVFCHNDCQEGNILLLEgrensEKQKLMLIDFEYSSYNYRGFDIGNHFCEWMYDYSYEKYpffraniRKYPTK 232
Cdd:cd05157   163 ESlEKSPIVFCHNDLLYGNILYNE-----DDDSVTFIDFEYAGPNPRAFDIANHFCEWAGFYCVLDY-------SRYPTK 230
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462522672 233 KQQLHFISSYLPAFQNDFENLSTEEKSIikEEMLLEVNRFALASHFLWGLWSIVQAKISSIEFGYM 298
Cdd:cd05157   231 EEQRNFLRAYLESLDGLPGGEEVSEEEV--EKLYNEVNLFRLASHLFWGLWALIQAAISSIDFDYL 294
Choline_kinase pfam01633
Choline/ethanolamine kinase; Choline kinase catalyzes the committed step in the synthesis of ...
17-234 2.33e-88

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: 264.52  E-value: 2.33e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462522672  17 EPRKVLLRLYGAILQmGAEAMVLESVMFAILAERSLGPKLYGIFPQGRLEQFIPSRRLDTEELSLPDISAEIAEKMATFH 96
Cdd:pfam01633   1 SPRKVLLRIYGPGTE-LLINREDEIVNFALLSERGLGPKLYGFFPNGRIEEFIPSRTLSTEDLRDPEISKLIAKRLAELH 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462522672  97 GMKMPFNKEPkWLFGTMEKYLKEVLRIK-FTEESRIKKLHKLLSYNLPLELENLRSLLESTPSPVVFCHNDCQEGNILLL 175
Cdd:pfam01633  80 SLEMPGKKSP-SLWKTMRKWLSLLKNLGaPESVNKSEQLKSINLEDLEKEINKLEKWLELLDSPIVFCHNDLQSGNILLL 158
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462522672 176 EgrensEKQKLMLIDFEYSSYNYRGFDIGNHFCEWMYDYSYEKyPFFRANIRKYPTKKQ 234
Cdd:pfam01633 159 N-----ETKRLVLIDFEYASYNYRGFDIANHFCEWAGDYHDPT-PFFKCDYSLYPTREE 211
ChoK-like_euk cd14021
Euykaryotic Choline Kinase and similar proteins; This group is composed of eukaryotic choline ...
1-285 2.69e-83

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: 252.19  E-value: 2.69e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462522672   1 MLFQCSLPDTTATLgdEPRKVLLRLYGAILQmGAEAMVLESVMFAILAERSLGPKLYGIFPQGRLEQFIPSRRLDTEELS 80
Cdd:cd14021    13 QVYKVSLKDESDSL--EPKKVLFRIYGKYLS-TLYDREKESEVFKILSEQGLGPKLIYKFDGGRIEEYIDGRPLTTDELR 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462522672  81 LPDISAEIAEKMATFHGMKMPfnkepkwlfgtmekylkevlrikfteesrikklhkllsynlplelenlrsllestpsPV 160
Cdd:cd14021    90 NPSVLTSIAKLLAKFHKIKTP---------------------------------------------------------PV 112
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462522672 161 VFCHNDCQEGNILLLegrenSEKQKLMLIDFEYSSYNYRGFDIGNHFCEWMYDYSYEKYPFFRANIRKYPTKKQQLHFIS 240
Cdd:cd14021   113 VFCHNDLQENNILLT-----NDQDGLRLIDFEYSGFNYRGYDIANFFNESMIDYDHPEPPYFKIYKENYISEEEKRLFVS 187
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 2462522672 241 SYLPAFQNDFENLSTEEksiIKEEMLLEVNRFALASHFLWGLWSI 285
Cdd:cd14021   188 VYLSEYLEKNVLPSLDK---LVEQFLQEVEIFTLGSHLYWGLWSI 229
PLN02236 PLN02236
choline kinase
3-298 1.21e-57

choline kinase


Pssm-ID: 177880 [Multi-domain]  Cd Length: 344  Bit Score: 190.26  E-value: 1.21e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462522672   3 FQCSLPDTTatlGDEPRKVLLRLYGAilqmGAEAMVL---ESVMFAILAERSLGPKLYGIFPQGRLEQFIPSRRLDTEEL 79
Cdd:PLN02236   53 FQIKWPTKE---GNLGRKVLVRIYGE----GVELFFDrddEIRTFECMSRHGQGPRLLGRFPNGRVEEFIHARTLSAADL 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462522672  80 SLPDISAEIAEKMATFHGMKMPFNKEPKwLFGTMEKYLKEVLRIKFTEESRIKKLHKllsynlpleLENLRSLLESTPSP 159
Cdd:PLN02236  126 RDPEISALIAAKLREFHSLDMPGPKNVL-LWDRLRNWLKEAKNLCSPEEAKEFRLDS---------LEDEINLLEKELSG 195
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462522672 160 VV----FCHNDCQEGNILLLEgrensEKQKLMLIDFEYSSYNYRGFDIGNHFCEWMYDYSYEKyPfFRANIRKYPTKKQQ 235
Cdd:PLN02236  196 DDqeigFCHNDLQYGNIMIDE-----ETRAITIIDYEYASYNPVAYDIANHFCEMAADYHSET-P-HILDYSKYPGEEER 268
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462522672 236 LHFISSYLPAfqndfenlSTEEKSIIKEEMLL-EVNRFALASHFLWGLWSIVQAKISSIEFGYM 298
Cdd:PLN02236  269 RRFIRTYLSS--------SGEEPSDEEVEQLLdDVEKYTLASHLFWGLWGIISGHVNKIDFDYM 324
PLN02421 PLN02421
phosphotransferase, alcohol group as acceptor/kinase
21-298 2.82e-57

phosphotransferase, alcohol group as acceptor/kinase


Pssm-ID: 215231 [Multi-domain]  Cd Length: 330  Bit Score: 188.79  E-value: 2.82e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462522672  21 VLLRLYG----AILQMGAEAMVLesvmfAILAERSLGPKLYGIFPQGRLEQFIPSRRLDTEELSLPDISAEIAEKMATFH 96
Cdd:PLN02421   45 VTVRLFGpntdYVIDRERELQAI-----KYLSAAGFGAKLLGVFGNGMIQSFINARTLTPSDMRKPKVAAEIAKELRRLH 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462522672  97 GMKMPFNKEPKwLFGTMEKYLKEVLRIKFTEESRIKKLHKLLSYNLPLELENLRSLLESTPSPVVFCHNDCQEGNILLle 176
Cdd:PLN02421  120 QVEIPGSKEPQ-LWNDIFKFYEKASTVKFEDPEKQKKYETISFEELRDEIVELKEITDSLKAPVVFAHNDLLSGNLML-- 196
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462522672 177 greNSEKQKLMLIDFEYSSYNYRGFDIGNHFCEwmydysyekYPFFRANIRKYPTKKQQLHFISSYLpafQNDFENLSTE 256
Cdd:PLN02421  197 ---NEDEGKLYFIDFEYGSYSYRGYDIGNHFNE---------YAGFDCDYSLYPSKEEQYHFFRHYL---RPDDPEEVSD 261
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 2462522672 257 EKSiikEEMLLEVNRFALASHFLWGLWSIVQAKISSIEFGYM 298
Cdd:PLN02421  262 AEL---EELFVETNFYALASHLYWAIWAIVQAKMSPIDFDYL 300
PTZ00296 PTZ00296
choline kinase; Provisional
2-288 1.11e-42

choline kinase; Provisional


Pssm-ID: 240350 [Multi-domain]  Cd Length: 442  Bit Score: 153.51  E-value: 1.11e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462522672   2 LFQCSLPDTTATlgDEP---RKVLLRLYGAILQMGAEAmVLESVMFAILAERSLGPKLYGIFPQGRLEQFIPSRRLDTEE 78
Cdd:PTZ00296  121 LFEVSLKEETAN--NYPsirRRVLFRIYGKDVDELYNP-ISEFEVYKTMSKYRIAPQLLNTFSGGRIEEWLYGDPLRIDD 197
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462522672  79 LSLPDISAEIAEKMATFHGMK----MP--FNKEPKwLFGTMEKYLKEVLRIKFTEESR------IKKLHKLLSYnlplel 146
Cdd:PTZ00296  198 LKNPSILIGIANVLGKFHTLSrkrhLPehWDRTPC-IFKMMEKWKNQLSKYKNIEKYQrdihkyIKESEKFIKF------ 270
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462522672 147 ENLRSLLESTPSPVVFCHNDCQEGNILllegreNSEKqKLMLIDFEYSSYNYRGFDIGNHFCEWMYDYSYEKYPFFRANI 226
Cdd:PTZ00296  271 MKVYSKSDNLANDIVFCHNDLQENNII------NTNK-CLRLIDFEYSGYNFLATDIANFFIETTIDYSVSHYPFFAIDK 343
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462522672 227 RKYPTKKQQLHFISSYLPAFQNDfeNLSTEEKSIIkEEMLLEVNRFALASHFLWGLWSIVQA 288
Cdd:PTZ00296  344 KKYISYENRKLFITAYLSNYLDK--SLVVPNPKII-DQILEAVEVQALGAHLLWGFWSIIRG 402
ChoK-like cd05151
Choline Kinase and similar proteins; This subfamily is composed of bacterial and eukaryotic ...
16-212 3.26e-27

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: 104.56  E-value: 3.26e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462522672  16 DEPRKVLLRLYGAILQMGaEAMVLESVMFAILAERSLGPKLYGIFPQ--GRLEQFIPSRRLDTEELSLPDISAEIAEKMA 93
Cdd:cd05151    19 VAGKKYVLRIPGAGTELL-IDRENEKANSKAAAELGIAPEVIYFDPEtgVKITEFIEGATLLTNDFSDPENLERIAALLR 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462522672  94 TFHGMKMPfnkepkwlfgtmekylkevlrikfteesrikklhkllsynlplelenlrsllestpsPVVFCHNDCQEGNIL 173
Cdd:cd05151    98 KLHSSPLE---------------------------------------------------------DLVLCHNDLVPGNFL 120
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2462522672 174 LLEGRensekqkLMLIDFEYSSYNYRGFDIGNHFCEWMY 212
Cdd:cd05151   121 LDDDR-------LYLIDWEYAGMNDPLFDLAALFSENNL 152
APH_ChoK_like cd05120
Aminoglycoside 3'-phosphotransferase and Choline Kinase family; This family is composed of APH, ...
17-212 1.29e-18

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: 81.58  E-value: 1.29e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462522672  17 EPRKVLLRLYGAILQmgaEAMVLESVMFAILAERS--LGPKLYGIFP----QGRLEQFIPSRRLDTE-----ELSLPDIS 85
Cdd:cd05120    19 DPREYVLKIGPPRLK---KDLEKEAAMLQLLAGKLslPVPKVYGFGEsdgwEYLLMERIEGETLSEVwprlsEEEKEKIA 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462522672  86 AEIAEKMATFHGMKMPfnkepkwlfgtmekylkevlrikfteesrikklhkllsynlplelenlrsllestpspvVFCHN 165
Cdd:cd05120    96 DQLAEILAALHRIDSS-----------------------------------------------------------VLTHG 116
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2462522672 166 DCQEGNILLLEgrensEKQKLMLIDFEYSSYNYRGFDIGNHFCEWMY 212
Cdd:cd05120   117 DLHPGNILVKP-----DGKLSGIIDWEFAGYGPPAFDYAAALRDWTE 158
CotS COG0510
Thiamine kinase or a related kinase [Coenzyme transport and metabolism];
122-288 6.22e-13

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


Pssm-ID: 440276 [Multi-domain]  Cd Length: 156  Bit Score: 65.96  E-value: 6.22e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462522672 122 RIKFTEESRIKKLHKLLSynlplELENLRSLLESTPSPVVFCHNDCQEGNILLlegrenSEKQKLMLIDFEYSSYNYRGF 201
Cdd:COG0510    16 RLERYLALGPRDLPELLR-----RLEELERALAARPLPLVLCHGDLHPGNFLV------TDDGRLYLIDWEYAGLGDPAF 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462522672 202 DIGNHFCEWMYDysyekypffranirkyptKKQQLHFISSYlpafqnDFENLSteeksiikEEMLLEVNRFALASHFLWG 281
Cdd:COG0510    85 DLAALLVEYGLS------------------PEQAEELLEAY------GFGRPT--------EELLRRLRAYRALADLLWA 132

                  ....*..
gi 2462522672 282 LWSIVQA 288
Cdd:COG0510   133 LWALVRA 139
PTZ00384 PTZ00384
choline kinase; Provisional
46-286 1.94e-08

choline kinase; Provisional


Pssm-ID: 173576 [Multi-domain]  Cd Length: 383  Bit Score: 55.55  E-value: 1.94e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462522672  46 ILAERSLGPKLYGIFPQGRLEQFIPSRRLDTEELSLPDISAEIAEKMATFHgmKMPFNKEPK-W----LFGT-MEKYLKE 119
Cdd:PTZ00384  108 LLGDNNFGPKIIGRFGDFTIQEWVEGNTMGIDSLQNLSVLTGIASSLAKFH--KRVTELVPKeWdrtpMFLTkISTWSQH 185
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462522672 120 VLRIkfteesrIKKLHKLLSYN-LPLELENLRSLL-------ESTPSPVVFCHNDCQEGNILllegrenSEKQKLMLIDF 191
Cdd:PTZ00384  186 VERI-------IKKYNLDFDYNeLVQNYELFKKILnnhlntsNSITNSVLFCHNDLFFTNIL-------DFNQGIYFIDF 251
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462522672 192 EYSSYNYRGFDIGNHFCEWMYDYSYEKYPFFRANIRKYPTKKQQLHFISSYLPAFQNdfENLSTEEKSIikEEMLLEVNR 271
Cdd:PTZ00384  252 DFAGFNYVGWEIANFFVKLYIVYDPPTPPYFNSDDSLALSEEMKTIFVSVYLSQLLG--KNVLPSDDLV--KEFLQSLEI 327
                         250
                  ....*....|....*
gi 2462522672 272 FALASHFLWGLWSIV 286
Cdd:PTZ00384  328 HTLGVNLFWTYWGIV 342
APH pfam01636
Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance ...
14-210 3.74e-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: 47.50  E-value: 3.74e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462522672  14 LGDEPRKVLLRLY------GAILQMGAEAMVLES-------VMFAILAERSLGPKLYGIFPqgrleqFIP--SRRLDTEE 78
Cdd:pfam01636  16 VTTGDGRYVLRLPppgraaEELRRELALLRHLAAagvppvpRVLAGCTDAELLGLPFLLME------YLPgeVLARPLLP 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462522672  79 LSLPDISAEIAEKMATFHGMKMPFNKEPKWlfgtmEKYLKEVLRiKFTEESRIKKLHKLLSYNLPLELENLRSLLESTP- 157
Cdd:pfam01636  90 EERGALLEALGRALARLHAVDPAALPLAGR-----LARLLELLR-QLEAALARLLAAELLDRLEELEERLLAALLALLPa 163
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462522672 158 -SPVVFCHNDCQEGNILLLEGRENSEkqklmLIDFEYSSYNYRGFDIG---NHFCEW 210
Cdd:pfam01636 164 eLPPVLVHGDLHPGNLLVDPGGRVSG-----VIDFEDAGLGDPAYDLAillNSWGRE 215
spore_CotS TIGR02906
spore coat protein, CotS family; Members of this family include the spore coat proteins CotS ...
88-250 1.53e-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: 46.12  E-value: 1.53e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462522672  88 IAEKMATFH----GMKMPFNKEPKWLFGTM----EKYLKEVLRIK-----FTEESRIKKLH-KLLSYNLPLELENLRSLL 153
Cdd:TIGR02906  93 AAKGLALFHhaskGYVPPDGSKIRSKLGKWpkqfEKRLKELERFKkialeKKYKDEFDKLYlKEVDYFLERGKKALELLN 172
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462522672 154 ESTPSPVV--------FCHNDCQEGNILLLEGrensekqKLMLIDFEYSSYNYRGFDIGNHFCEWMYDYSYEKYPFFRAN 225
Cdd:TIGR02906 173 KSKYYDLCkeakkirgFCHQDYAYHNILLKDN-------EVYVIDFDYCTIDLPVRDLRKLIIKLMKKNGVWDLEKAKEI 245
                         170       180
                  ....*....|....*....|....*....
gi 2462522672 226 IRKY----PTKKQQLHFISSYLpAFQNDF 250
Cdd:TIGR02906 246 IEAYssinPLSKEEKEVLYIDL-AFPHKF 273
HomoserineK_II cd05153
Type II Homoserine Kinase; This subfamily is composed of unusual homoserine kinases, from a ...
52-208 1.87e-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: 1.87e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462522672  52 LGPKLYGIFPqgrleqFIPSRRLDTEElslPDISAEIAEKMATFHG------MKMPFNKEPKWlfgtMEKYLKevlRIKF 125
Cdd:cd05153    86 LNGKPAALFP------FLPGESLTTPT---PEQCRAIGAALARLHLalagfpPPRPNPRGLAW----WKPLAE---RLKA 149
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462522672 126 TEESRIKKLHKLLSynlpLELENLRSLLESTPsPVVFCHNDCQEGNILLLEGRENSekqklmLIDFEYSSYNYRGFDIG- 204
Cdd:cd05153   150 RLDLLAADDRALLE----DELARLQALAPSDL-PRGVIHADLFRDNVLFDGDRLSG------IIDFYDACYDPLLYDLAi 218

                  ....*.
gi 2462522672 205 --NHFC 208
Cdd:cd05153   219 alNDWC 224
EcKL pfam02958
Ecdysteroid kinase-like family; This family includes ecdysteroid 22-kinase, an enzyme ...
109-207 1.17e-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: 40.33  E-value: 1.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462522672 109 LFGTMEKYLKEVLRIKFTEESRI-KKLHKLLSyNLpleLENLRSLLESTPSP-VVFCHNDCQEGNILLLEGrENSEKQKL 186
Cdd:pfam02958 165 LMETGLDAAAEALREQLPEYEKYaEKLEKLKD-NY---FDRLLRLVEPTPGEfNVLNHGDLWVNNIMFKYD-DEGEPEDV 239
                          90       100
                  ....*....|....*....|.
gi 2462522672 187 MLIDFEYSSYNYRGFDIgNHF 207
Cdd:pfam02958 240 ILVDFQLSRYGSPAIDL-NYF 259
CHK smart00587
ZnF_C4 abd HLH domain containing kinases domain; subfamily of choline kinases
90-203 2.26e-03

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


Pssm-ID: 214734  Cd Length: 196  Bit Score: 38.85  E-value: 2.26e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462522672   90 EKMATFH--------------------GMKMPFNKE-PKWLFGTMEKYLKEVLRIK--FTEESRIKKLHKLLSYnlpLEL 146
Cdd:smart00587  30 KKLAKLHaasavlieeekgsyleefdeGLFERFKRMfSEEFIGGLENFLRELLSQPelLKVEEYIEKLDKLLDN---LED 106
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462522672  147 ENLRSLLESTPSPVVFCHNDCQEGNILLLEGrENSEKQKLMLIDFEYSSYNYRGFDI 203
Cdd:smart00587 107 LKKEDKEPDEGEFNVLNHGDLWANNIMFKYD-DEGKPEDVALIDFQLSHYGSPAEDL 162
SrkA COG2334
Ser/Thr protein kinase RdoA involved in Cpx stress response, MazF antagonist [Signal ...
145-204 4.81e-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: 4.81e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462522672 145 ELENLRSLLESTPSPVVF--CHNDCQEGNILLLEGRensekqKLMLIDFEYSSYNYRGFDIG 204
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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