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Conserved domains on  [gi|226371696|ref|NP_083526|]
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ethanolamine kinase 1 [Mus musculus]

Protein Classification

ethanolamine kinase( domain architecture ID 10142388)

ethanolamine kinase catalyzes the transfer of the gamma-phosphoryl group from ATP to ethanolamine (Etn), the first step in the CDP-Etn pathway for the formation of the major phospholipid, phosphatidylethanolamine (PtdEtn)

CATH:  1.10.510.10
EC:  2.7.1.82
Gene Ontology:  GO:0004305|GO:0006646|GO:0005524
PubMed:  16244704

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ETNK_euk cd05157
Euykaryotic Ethanolamine kinase; ETNK catalyzes the transfer of the gamma-phosphoryl group ...
49-351 1.73e-143

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: 408.51  E-value: 1.73e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371696  49 VTLQLFTDGITNKLIACYV-GDTMEDVVLVRIYGNKTELLVDRDEEVKSFRVLQAHGCAPQLYCTFNNGLCYEFIQGEAL 127
Cdd:cd05157    1 IKVKRITGGITNALYKVTYpSGDTPKTVLVRIYGPGTELLIDRDRELRILQLLSRAGIGPKLYGRFENGRVEEFLPGRTL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371696 128 DPQHVCNPAIFRLIARQLAKIHAIHAHNGW--IPKSNLWLKMGKYFSLIPTGFaDENINKRFLSEIPSPQLLQEEMTWMK 205
Cdd:cd05157   81 TPEDLRDPKISRLIARRLAELHSIVPLGEIegKKKPILWTTIRKWLDLAPEVF-EDEKNKEKKLEKVDLERLRKELEWLE 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371696 206 ELLSSL-GSPVVLCHNDLLCKNIIYNEKQGDVQFIDYEYSGYNYLAYDIGNHFNEFAGVSDV-DYSLYPDRELQGQWLRS 283
Cdd:cd05157  160 KWLESLeKSPIVFCHNDLLYGNILYNEDDDSVTFIDFEYAGPNPRAFDIANHFCEWAGFYCVlDYSRYPTKEEQRNFLRA 239
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 226371696 284 YLEAYKEYKGfGSDVTEKEVETLFIQVNQFALASHFFWGLWALIQAKYSTIEFDFLGYAVVRFNQYFK 351
Cdd:cd05157  240 YLESLDGLPG-GEEVSEEEVEKLYNEVNLFRLASHLFWGLWALIQAAISSIDFDYLGYAKERLDEYWG 306
 
Name Accession Description Interval E-value
ETNK_euk cd05157
Euykaryotic Ethanolamine kinase; ETNK catalyzes the transfer of the gamma-phosphoryl group ...
49-351 1.73e-143

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: 408.51  E-value: 1.73e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371696  49 VTLQLFTDGITNKLIACYV-GDTMEDVVLVRIYGNKTELLVDRDEEVKSFRVLQAHGCAPQLYCTFNNGLCYEFIQGEAL 127
Cdd:cd05157    1 IKVKRITGGITNALYKVTYpSGDTPKTVLVRIYGPGTELLIDRDRELRILQLLSRAGIGPKLYGRFENGRVEEFLPGRTL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371696 128 DPQHVCNPAIFRLIARQLAKIHAIHAHNGW--IPKSNLWLKMGKYFSLIPTGFaDENINKRFLSEIPSPQLLQEEMTWMK 205
Cdd:cd05157   81 TPEDLRDPKISRLIARRLAELHSIVPLGEIegKKKPILWTTIRKWLDLAPEVF-EDEKNKEKKLEKVDLERLRKELEWLE 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371696 206 ELLSSL-GSPVVLCHNDLLCKNIIYNEKQGDVQFIDYEYSGYNYLAYDIGNHFNEFAGVSDV-DYSLYPDRELQGQWLRS 283
Cdd:cd05157  160 KWLESLeKSPIVFCHNDLLYGNILYNEDDDSVTFIDFEYAGPNPRAFDIANHFCEWAGFYCVlDYSRYPTKEEQRNFLRA 239
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 226371696 284 YLEAYKEYKGfGSDVTEKEVETLFIQVNQFALASHFFWGLWALIQAKYSTIEFDFLGYAVVRFNQYFK 351
Cdd:cd05157  240 YLESLDGLPG-GEEVSEEEVEKLYNEVNLFRLASHLFWGLWALIQAAISSIDFDYLGYAKERLDEYWG 306
Choline_kinase pfam01633
Choline/ethanolamine kinase; Choline kinase catalyzes the committed step in the synthesis of ...
75-275 5.35e-86

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: 258.74  E-value: 5.35e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371696   75 VLVRIYGNKTELLVDRDEEVKSFRVLQAHGCAPQLYCTFNNGLCYEFIQGEALDPQHVCNPAIFRLIARQLAKIHAIHAH 154
Cdd:pfam01633   5 VLLRIYGPGTELLINREDEIVNFALLSERGLGPKLYGFFPNGRIEEFIPSRTLSTEDLRDPEISKLIAKRLAELHSLEMP 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371696  155 ngWIPKSNLWLKMGKYFSLIPTGFADENINKRFLSEIPSPQLLQEEMTWMKELLSSLGSPVVLCHNDLLCKNIIYNEKQG 234
Cdd:pfam01633  85 --GKKSPSLWKTMRKWLSLLKNLGAPESVNKSEQLKSINLEDLEKEINKLEKWLELLDSPIVFCHNDLQSGNILLLNETK 162
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 226371696  235 DVQFIDYEYSGYNYLAYDIGNHFNEFAGV-------SDVDYSLYPDRE 275
Cdd:pfam01633 163 RLVLIDFEYASYNYRGFDIANHFCEWAGDyhdptpfFKCDYSLYPTRE 210
PLN02421 PLN02421
phosphotransferase, alcohol group as acceptor/kinase
36-359 3.26e-84

phosphotransferase, alcohol group as acceptor/kinase


Pssm-ID: 215231 [Multi-domain]  Cd Length: 330  Bit Score: 258.51  E-value: 3.26e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371696  36 LLRHLRPHW---DPREVTLQLFTDGITNKLIACYVGDTMED--VVLVRIYGNKTELLVDRDEEVKSFRVLQAHGCAPQLY 110
Cdd:PLN02421   1 VCKALFKGWsdlDDSDFSVERISGGITNLLLKVSVKEENGNevSVTVRLFGPNTDYVIDRERELQAIKYLSAAGFGAKLL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371696 111 CTFNNGLCYEFIQGEALDPQHVCNPAIFRLIARQLAKIHAIHahngwIPKSN---LWLKMGKYFSLIPTGFADENINKRF 187
Cdd:PLN02421  81 GVFGNGMIQSFINARTLTPSDMRKPKVAAEIAKELRRLHQVE-----IPGSKepqLWNDIFKFYEKASTVKFEDPEKQKK 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371696 188 LSEIpSPQLLQEEMTWMKELLSSLGSPVVLCHNDLLCKNIIYNEKQGDVQFIDYEYSGYNYLAYDIGNHFNEFAGVsDVD 267
Cdd:PLN02421 156 YETI-SFEELRDEIVELKEITDSLKAPVVFAHNDLLSGNLMLNEDEGKLYFIDFEYGSYSYRGYDIGNHFNEYAGF-DCD 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371696 268 YSLYPDRELQGQWLRSYLEAYKEYKgfgsdVTEKEVETLFIQVNQFALASHFFWGLWALIQAKYSTIEFDFLGYAVVRFN 347
Cdd:PLN02421 234 YSLYPSKEEQYHFFRHYLRPDDPEE-----VSDAELEELFVETNFYALASHLYWAIWAIVQAKMSPIDFDYLGYFFLRYK 308
                        330
                 ....*....|..
gi 226371696 348 QYFKMKPEVTAL 359
Cdd:PLN02421 309 EYKRQKEKLLSL 320
CotS COG0510
Thiamine kinase or a related kinase [Coenzyme transport and metabolism];
195-347 9.39e-15

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


Pssm-ID: 440276 [Multi-domain]  Cd Length: 156  Bit Score: 70.97  E-value: 9.39e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371696 195 QLLQEEMTWMKELLSSLGSPVVLCHNDLLCKNIIYNEkQGDVQFIDYEYSGYNYLAYDIGNHFNEFAgvsdvdyslyPDR 274
Cdd:COG0510   29 PELLRRLEELERALAARPLPLVLCHGDLHPGNFLVTD-DGRLYLIDWEYAGLGDPAFDLAALLVEYG----------LSP 97
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 226371696 275 ELQGQWLRSYleaykeykgFGSDVTEKEVEtlfiQVNQFALASHFFWGLWALIQAKYSTiEFDFLGYAVVRFN 347
Cdd:COG0510   98 EQAEELLEAY---------GFGRPTEELLR----RLRAYRALADLLWALWALVRAAQEA-NGDLLKYLLRRLE 156
spore_CotS TIGR02906
spore coat protein, CotS family; Members of this family include the spore coat proteins CotS ...
109-323 6.04e-05

spore coat protein, CotS family; Members of this family include the spore coat proteins CotS and YtaA from Bacillus subtilis and, from other endospore-forming bacteria, homologs that are more closely related to these two than to the spore coat proteins YutH and YsxE. The CotS family is more broadly distributed than YutH or YsxE, but still is not universal among spore-formers. [Cellular processes, Sporulation and germination]


Pssm-ID: 131952 [Multi-domain]  Cd Length: 313  Bit Score: 44.19  E-value: 6.04e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371696  109 LYCTFNNGL--CYEFIQGEALDpqhVCNPAIFRLIARQLAKIHaiHAHNGWIPKSNL-----WLKMGKYF---------- 171
Cdd:TIGR02906  62 LYVKYNGDLyvLTEWIEGRECD---FNNPIDLKKAAKGLALFH--HASKGYVPPDGSkirskLGKWPKQFekrlkelerf 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371696  172 -SLIPTGFADENINKRFLSEIP--------SPQLLQ--EEMTWMKELLSSLGspvvLCHNDLLCKNIIYneKQGDVQFID 240
Cdd:TIGR02906 137 kKIALEKKYKDEFDKLYLKEVDyflergkkALELLNksKYYDLCKEAKKIRG----FCHQDYAYHNILL--KDNEVYVID 210
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371696  241 YEYSGYNYLAYDIGNHFNEFA---GVSDVDyslypdrelqgqWLRSYLEAYKEYkgfgSDVTEKEVETLFIqvnqFALAS 317
Cdd:TIGR02906 211 FDYCTIDLPVRDLRKLIIKLMkknGVWDLE------------KAKEIIEAYSSI----NPLSKEEKEVLYI----DLAFP 270

                  ....*.
gi 226371696  318 HFFWGL 323
Cdd:TIGR02906 271 HKFWKI 276
CHK smart00587
ZnF_C4 abd HLH domain containing kinases domain; subfamily of choline kinases
139-253 3.14e-03

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


Pssm-ID: 214734  Cd Length: 196  Bit Score: 38.47  E-value: 3.14e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371696   139 RLIARQLAKIHAIHAH-----NGWIPKS-NLWLKMGKYFSLIPTGFADENINKRFLSEIPSP-----------QLLQEEM 201
Cdd:smart00587  26 SLVLKKLAKLHAASAVlieeeKGSYLEEfDEGLFERFKRMFSEEFIGGLENFLRELLSQPELlkveeyiekldKLLDNLE 105
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 226371696   202 TWMKELL-SSLGSPVVLCHNDLLCKNIIY----NEKQGDVQFIDYEYSGYNYLAYDI 253
Cdd:smart00587 106 DLKKEDKePDEGEFNVLNHGDLWANNIMFkyddEGKPEDVALIDFQLSHYGSPAEDL 162
 
Name Accession Description Interval E-value
ETNK_euk cd05157
Euykaryotic Ethanolamine kinase; ETNK catalyzes the transfer of the gamma-phosphoryl group ...
49-351 1.73e-143

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: 408.51  E-value: 1.73e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371696  49 VTLQLFTDGITNKLIACYV-GDTMEDVVLVRIYGNKTELLVDRDEEVKSFRVLQAHGCAPQLYCTFNNGLCYEFIQGEAL 127
Cdd:cd05157    1 IKVKRITGGITNALYKVTYpSGDTPKTVLVRIYGPGTELLIDRDRELRILQLLSRAGIGPKLYGRFENGRVEEFLPGRTL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371696 128 DPQHVCNPAIFRLIARQLAKIHAIHAHNGW--IPKSNLWLKMGKYFSLIPTGFaDENINKRFLSEIPSPQLLQEEMTWMK 205
Cdd:cd05157   81 TPEDLRDPKISRLIARRLAELHSIVPLGEIegKKKPILWTTIRKWLDLAPEVF-EDEKNKEKKLEKVDLERLRKELEWLE 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371696 206 ELLSSL-GSPVVLCHNDLLCKNIIYNEKQGDVQFIDYEYSGYNYLAYDIGNHFNEFAGVSDV-DYSLYPDRELQGQWLRS 283
Cdd:cd05157  160 KWLESLeKSPIVFCHNDLLYGNILYNEDDDSVTFIDFEYAGPNPRAFDIANHFCEWAGFYCVlDYSRYPTKEEQRNFLRA 239
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 226371696 284 YLEAYKEYKGfGSDVTEKEVETLFIQVNQFALASHFFWGLWALIQAKYSTIEFDFLGYAVVRFNQYFK 351
Cdd:cd05157  240 YLESLDGLPG-GEEVSEEEVEKLYNEVNLFRLASHLFWGLWALIQAAISSIDFDYLGYAKERLDEYWG 306
Choline_kinase pfam01633
Choline/ethanolamine kinase; Choline kinase catalyzes the committed step in the synthesis of ...
75-275 5.35e-86

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: 258.74  E-value: 5.35e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371696   75 VLVRIYGNKTELLVDRDEEVKSFRVLQAHGCAPQLYCTFNNGLCYEFIQGEALDPQHVCNPAIFRLIARQLAKIHAIHAH 154
Cdd:pfam01633   5 VLLRIYGPGTELLINREDEIVNFALLSERGLGPKLYGFFPNGRIEEFIPSRTLSTEDLRDPEISKLIAKRLAELHSLEMP 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371696  155 ngWIPKSNLWLKMGKYFSLIPTGFADENINKRFLSEIPSPQLLQEEMTWMKELLSSLGSPVVLCHNDLLCKNIIYNEKQG 234
Cdd:pfam01633  85 --GKKSPSLWKTMRKWLSLLKNLGAPESVNKSEQLKSINLEDLEKEINKLEKWLELLDSPIVFCHNDLQSGNILLLNETK 162
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 226371696  235 DVQFIDYEYSGYNYLAYDIGNHFNEFAGV-------SDVDYSLYPDRE 275
Cdd:pfam01633 163 RLVLIDFEYASYNYRGFDIANHFCEWAGDyhdptpfFKCDYSLYPTRE 210
PLN02421 PLN02421
phosphotransferase, alcohol group as acceptor/kinase
36-359 3.26e-84

phosphotransferase, alcohol group as acceptor/kinase


Pssm-ID: 215231 [Multi-domain]  Cd Length: 330  Bit Score: 258.51  E-value: 3.26e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371696  36 LLRHLRPHW---DPREVTLQLFTDGITNKLIACYVGDTMED--VVLVRIYGNKTELLVDRDEEVKSFRVLQAHGCAPQLY 110
Cdd:PLN02421   1 VCKALFKGWsdlDDSDFSVERISGGITNLLLKVSVKEENGNevSVTVRLFGPNTDYVIDRERELQAIKYLSAAGFGAKLL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371696 111 CTFNNGLCYEFIQGEALDPQHVCNPAIFRLIARQLAKIHAIHahngwIPKSN---LWLKMGKYFSLIPTGFADENINKRF 187
Cdd:PLN02421  81 GVFGNGMIQSFINARTLTPSDMRKPKVAAEIAKELRRLHQVE-----IPGSKepqLWNDIFKFYEKASTVKFEDPEKQKK 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371696 188 LSEIpSPQLLQEEMTWMKELLSSLGSPVVLCHNDLLCKNIIYNEKQGDVQFIDYEYSGYNYLAYDIGNHFNEFAGVsDVD 267
Cdd:PLN02421 156 YETI-SFEELRDEIVELKEITDSLKAPVVFAHNDLLSGNLMLNEDEGKLYFIDFEYGSYSYRGYDIGNHFNEYAGF-DCD 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371696 268 YSLYPDRELQGQWLRSYLEAYKEYKgfgsdVTEKEVETLFIQVNQFALASHFFWGLWALIQAKYSTIEFDFLGYAVVRFN 347
Cdd:PLN02421 234 YSLYPSKEEQYHFFRHYLRPDDPEE-----VSDAELEELFVETNFYALASHLYWAIWAIVQAKMSPIDFDYLGYFFLRYK 308
                        330
                 ....*....|..
gi 226371696 348 QYFKMKPEVTAL 359
Cdd:PLN02421 309 EYKRQKEKLLSL 320
ChoK_euk cd05156
Euykaryotic Choline Kinase; ChoK catalyzes the transfer of the gamma-phosphoryl group from ATP ...
57-354 2.17e-73

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: 230.59  E-value: 2.17e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371696  57 GITNKLIACYVGDTMEDV------VLVRIYGN---KTELLVDrdEEVkSFRVLQAHGCAPQLYCTFNNGLCYEFIQGEAL 127
Cdd:cd05156    9 GLSNLLYLCSLPDGVVPVggeprkVLLRIYGQilqAEESLVT--ESV-IFALLSERGLGPKLYGIFPGGRLEEFIPSRPL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371696 128 DPQHVCNPAIFRLIARQLAKIHAIHahngwIPKSN----LWLKMGKYFS-LIPTGFADENINKRFLSEIPSPQLLQEEMT 202
Cdd:cd05156   86 TTDELSLPEISRKIARKMARFHSLE-----MPISKepkwLFDTMERWLKeALSILFTDEPTKPSKQLELLLSYDLAKELG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371696 203 WMKELLSSLGSPVVLCHND------LLCKNIIYNEKQgDVQFIDYEYSGYNYLAYDIGNHFNEFA---------GVSdVD 267
Cdd:cd05156  161 WLRSLLESTPSPVVFCHNDlqegniLLLNGPENSEDD-KLVLIDFEYCSYNYRGFDLANHFCEWAydytvpeppYFK-IN 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371696 268 YSLYPDRELQGQWLRSYLEAYKEYKG-FGSDVTEKEVETLFIQVNQFALASHFFWGLWALIQAKYSTIEFDFLGYAVVRF 346
Cdd:cd05156  239 PENYPTREQQLHFIRAYLDEQYKDKTnDLTEERSKEEEKLLLEVNRFALASHFFWGLWSIVQAKISSIEFGYLEYAQARL 318

                 ....*...
gi 226371696 347 NQYFKMKP 354
Cdd:cd05156  319 DAYFKQKE 326
PLN02236 PLN02236
choline kinase
26-356 2.52e-58

choline kinase


Pssm-ID: 177880 [Multi-domain]  Cd Length: 344  Bit Score: 192.57  E-value: 2.52e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371696  26 EQRCRDGALSLLRHLRPHW----DPREVTLQLFTDGITNKLIAC-YVGDTMEDV--VLVRIYGNKTELLVDRDEEVKSFR 98
Cdd:PLN02236  12 SGRIPDELKRILHSLASKWgdvvDDEALQVIPLKGAMTNEVFQIkWPTKEGNLGrkVLVRIYGEGVELFFDRDDEIRTFE 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371696  99 VLQAHGCAPQLYCTFNNGLCYEFIQGEALDPQHVCNPAIFRLIARQLAKIHAIHahngwIPKSN---LWLKM----GKYF 171
Cdd:PLN02236  92 CMSRHGQGPRLLGRFPNGRVEEFIHARTLSAADLRDPEISALIAAKLREFHSLD-----MPGPKnvlLWDRLrnwlKEAK 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371696 172 SLIPTGFADENINKRFLSEIpspQLLQEEmtwmkelLSSLGSPVVLCHNDLLCKNIIYNEKQGDVQFIDYEYSGYNYLAY 251
Cdd:PLN02236 167 NLCSPEEAKEFRLDSLEDEI---NLLEKE-------LSGDDQEIGFCHNDLQYGNIMIDEETRAITIIDYEYASYNPVAY 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371696 252 DIGNHFNEFAGV--SD----VDYSLYPDRELQGQWLRSYLEAYkeykgfGSDVTEKEVETLFIQVNQFALASHFFWGLWA 325
Cdd:PLN02236 237 DIANHFCEMAADyhSEtphiLDYSKYPGEEERRRFIRTYLSSS------GEEPSDEEVEQLLDDVEKYTLASHLFWGLWG 310
                        330       340       350
                 ....*....|....*....|....*....|.
gi 226371696 326 LIQAKYSTIEFDFLGYAVVRFNQYFKMKPEV 356
Cdd:PLN02236 311 IISGHVNKIDFDYMEYARQRFEQYWLRKPEL 341
ChoK-like_euk cd14021
Euykaryotic Choline Kinase and similar proteins; This group is composed of eukaryotic choline ...
57-326 6.15e-46

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: 156.66  E-value: 6.15e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371696  57 GITNKLIACYVGDTMEDV----VLVRIYGNKTELLVDRDEEVKSFRVLQAHGCAPQLYCTFNNGLCYEFIQGEALDPQHV 132
Cdd:cd14021    9 GLTNQVYKVSLKDESDSLepkkVLFRIYGKYLSTLYDREKESEVFKILSEQGLGPKLIYKFDGGRIEEYIDGRPLTTDEL 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371696 133 CNPAIFRLIARQLAKIHAIHAhngwipksnlwlkmgkyfsliptgfadeninkrflseipspqllqeemtwmkellsslg 212
Cdd:cd14021   89 RNPSVLTSIAKLLAKFHKIKT----------------------------------------------------------- 109
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371696 213 SPVVLCHNDLLCKNIIYNEKQGDVQFIDYEYSGYNYLAYDIGNHFNEFAGVSDV--------DYSLYPDRELQGQWLRSY 284
Cdd:cd14021  110 PPVVFCHNDLQENNILLTNDQDGLRLIDFEYSGFNYRGYDIANFFNESMIDYDHpeppyfkiYKENYISEEEKRLFVSVY 189
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 226371696 285 LEAYKEYKGFGSDvtEKEVETLFIQVNQFALASHFFWGLWAL 326
Cdd:cd14021  190 LSEYLEKNVLPSL--DKLVEQFLQEVEIFTLGSHLYWGLWSI 229
PTZ00296 PTZ00296
choline kinase; Provisional
43-361 1.06e-35

choline kinase; Provisional


Pssm-ID: 240350 [Multi-domain]  Cd Length: 442  Bit Score: 135.02  E-value: 1.06e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371696  43 HWDPREVTLQLFTDGITNKLIACYVG-DTMEDV------VLVRIYGNKTELLVDRDEEVKSFRVLQAHGCAPQLYCTFNN 115
Cdd:PTZ00296 102 RFTEDDVRVNQILSGLTNQLFEVSLKeETANNYpsirrrVLFRIYGKDVDELYNPISEFEVYKTMSKYRIAPQLLNTFSG 181
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371696 116 GLCYEFIQGEALDPQHVCNPAIFRLIARQLAKIHAIHAHNGwIPKSnlWLKMGKYFSLIPTgFADENINKRFLSEIPSP- 194
Cdd:PTZ00296 182 GRIEEWLYGDPLRIDDLKNPSILIGIANVLGKFHTLSRKRH-LPEH--WDRTPCIFKMMEK-WKNQLSKYKNIEKYQRDi 257
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371696 195 -QLLQEEMTWMKEL-----LSSLGSPVVLCHNDLLCKNIIYNEKQgdVQFIDYEYSGYNYLAYDIGNHFNEFAgvsdVDY 268
Cdd:PTZ00296 258 hKYIKESEKFIKFMkvyskSDNLANDIVFCHNDLQENNIINTNKC--LRLIDFEYSGYNFLATDIANFFIETT----IDY 331
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371696 269 SL------------YPDRELQGQWLRSYLEAYKEYKGFGSDvtEKEVETLFIQVNQFALASHFFWGLWALI---QAKyST 333
Cdd:PTZ00296 332 SVshypffaidkkkYISYENRKLFITAYLSNYLDKSLVVPN--PKIIDQILEAVEVQALGAHLLWGFWSIIrgyQTK-SY 408
                        330       340
                 ....*....|....*....|....*...
gi 226371696 334 IEFDFLGYAVVRFNQYFKMKPEVTALKM 361
Cdd:PTZ00296 409 NEFDFFLYAKERFKMYDEQKEYLISNNI 436
ChoK-like cd05151
Choline Kinase and similar proteins; This subfamily is composed of bacterial and eukaryotic ...
49-260 8.64e-24

Choline Kinase and similar proteins; This subfamily is composed of bacterial and eukaryotic choline kinases, as well as eukaryotic ethanolamine kinase. ChoK catalyzes the transfer of the gamma-phosphoryl group from ATP (or CTP) to its substrate, choline, producing phosphorylcholine (PCho), a precursor to the biosynthesis of two major membrane phospholipids, phosphatidylcholine (PC), and sphingomyelin (SM). Although choline is the preferred substrate, ChoK also shows substantial activity towards ethanolamine and its N-methylated derivatives. Bacterial ChoK is also referred to as licA protein. ETNK catalyzes the transfer of the gamma-phosphoryl group from CTP to ethanolamine (Etn), the first step in the CDP-Etn pathway for the formation of the major phospholipid, phosphatidylethanolamine (PtdEtn). Unlike ChoK, ETNK shows specific activity for its substrate and displays negligible activity towards N-methylated derivatives of Etn. ChoK plays an important role in cell signaling pathways and the regulation of cell growth. The ChoK subfamily is part of a larger superfamily that includes the catalytic domains of other kinases, such as the typical serine/threonine/tyrosine protein kinases (PKs), RIO kinases, actin-fragmin kinase (AFK), and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270700 [Multi-domain]  Cd Length: 152  Bit Score: 95.70  E-value: 8.64e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371696  49 VTLQLFTDGITNKliaCYVGDTMEDVVLVRIYGNKTELLVDRDEEVKSFRVLQAHGCAPQ-LYCTFNNG-LCYEFIQGEA 126
Cdd:cd05151    1 ITIEPLKGGLTNK---NYLVEVAGKKYVLRIPGAGTELLIDRENEKANSKAAAELGIAPEvIYFDPETGvKITEFIEGAT 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371696 127 LDPQHVCNPAIFRLIARQLAKIHAihahngwipksnlwlkmgkyfsliptgfadeninkrflSEIPspqllqeemtwmke 206
Cdd:cd05151   78 LLTNDFSDPENLERIAALLRKLHS--------------------------------------SPLE-------------- 105
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 226371696 207 llsslgsPVVLCHNDLLCKNIIYNEKQgdVQFIDYEYSGYNYLAYDIGNHFNEF 260
Cdd:cd05151  106 -------DLVLCHNDLVPGNFLLDDDR--LYLIDWEYAGMNDPLFDLAALFSEN 150
CotS COG0510
Thiamine kinase or a related kinase [Coenzyme transport and metabolism];
195-347 9.39e-15

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


Pssm-ID: 440276 [Multi-domain]  Cd Length: 156  Bit Score: 70.97  E-value: 9.39e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371696 195 QLLQEEMTWMKELLSSLGSPVVLCHNDLLCKNIIYNEkQGDVQFIDYEYSGYNYLAYDIGNHFNEFAgvsdvdyslyPDR 274
Cdd:COG0510   29 PELLRRLEELERALAARPLPLVLCHGDLHPGNFLVTD-DGRLYLIDWEYAGLGDPAFDLAALLVEYG----------LSP 97
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 226371696 275 ELQGQWLRSYleaykeykgFGSDVTEKEVEtlfiQVNQFALASHFFWGLWALIQAKYSTiEFDFLGYAVVRFN 347
Cdd:COG0510   98 EQAEELLEAY---------GFGRPTEELLR----RLRAYRALADLLWALWALVRAAQEA-NGDLLKYLLRRLE 156
APH pfam01636
Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance ...
50-290 4.58e-13

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: 67.91  E-value: 4.58e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371696   50 TLQLFTDGITNKliACYVGDTMEDVVLvRIYgNKTELLVDRDEEVKSFRVLQAHG----CAPQLYCTFNNGLC-----YE 120
Cdd:pfam01636   1 TLRPISSGASNR--TYLVTTGDGRYVL-RLP-PPGRAAEELRRELALLRHLAAAGvppvPRVLAGCTDAELLGlpfllME 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371696  121 FIQGEAL--DPQHVCNPAIFRLIARQLAKIHAIHAHNG---WIPKSNLWLKmgkyfslipTGFADENINKRFLSEIPS-P 194
Cdd:pfam01636  77 YLPGEVLarPLLPEERGALLEALGRALARLHAVDPAALplaGRLARLLELL---------RQLEAALARLLAAELLDRlE 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371696  195 QLLQEEMTWMKELLSSlGSPVVLCHNDLLCKNIIYNEKQGDVQFIDYEYSGYNYLAYDIGNHFNEFagvsdvdyslypDR 274
Cdd:pfam01636 148 ELEERLLAALLALLPA-ELPPVLVHGDLHPGNLLVDPGGRVSGVIDFEDAGLGDPAYDLAILLNSW------------GR 214
                         250
                  ....*....|....*.
gi 226371696  275 ELQGQWLRSYLEAYKE 290
Cdd:pfam01636 215 ELGAELLAAYLAAYGA 230
PTZ00384 PTZ00384
choline kinase; Provisional
37-347 9.58e-09

choline kinase; Provisional


Pssm-ID: 173576 [Multi-domain]  Cd Length: 383  Bit Score: 56.32  E-value: 9.58e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371696  37 LRHLrPHWD---PREVTLQLFTDGITNKLIACYVGDTMEDV-----VLVRIYGNKTELLVDRDEEVKSFRVLQAHGCAPQ 108
Cdd:PTZ00384  39 IRHV-PFWNnvnPEFIEIKKMNNGITNQVYQATLVDGDKDRypiksVCIKKSSTYNSLVIDNDLQYNIAKLLGDNNFGPK 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371696 109 LYCTFNNGLCYEFIQGEALDPQHVCNPAIFRLIARQLAKIHAIHAHngWIPKSnlWLKMGKYFSLIPTGFAD-ENINKRF 187
Cdd:PTZ00384 118 IIGRFGDFTIQEWVEGNTMGIDSLQNLSVLTGIASSLAKFHKRVTE--LVPKE--WDRTPMFLTKISTWSQHvERIIKKY 193
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371696 188 LSEIPSPQLLQE-EMtwMKELLS-------SLGSPVVLCHNDLLCKNIIyNEKQGdVQFIDYEYSGYNYLAYDIGNHFNE 259
Cdd:PTZ00384 194 NLDFDYNELVQNyEL--FKKILNnhlntsnSITNSVLFCHNDLFFTNIL-DFNQG-IYFIDFDFAGFNYVGWEIANFFVK 269
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371696 260 FAGVSDVD---YSLYPD-----RELQGQWLRSYLEAYKEYKGFGSDVTEKEvetlFIQ-VNQFALASHFFWGLWALIQAK 330
Cdd:PTZ00384 270 LYIVYDPPtppYFNSDDslalsEEMKTIFVSVYLSQLLGKNVLPSDDLVKE----FLQsLEIHTLGVNLFWTYWGIVMND 345
                        330       340
                 ....*....|....*....|.
gi 226371696 331 YSTIEF----DFLGYAVVRFN 347
Cdd:PTZ00384 346 KPKNELskpvKFEAYAKFQYN 366
HomoserineK_II cd05153
Type II Homoserine Kinase; This subfamily is composed of unusual homoserine kinases, from a ...
119-331 5.22e-08

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: 53.80  E-value: 5.22e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371696 119 YEFIQGEALDPQhvcNPAIFRLIARQLAKIHAI-----------HAHNGWIPksnLWLKMGKYFSLIPTGFADeninkrf 187
Cdd:cd05153   94 FPFLPGESLTTP---TPEQCRAIGAALARLHLAlagfppprpnpRGLAWWKP---LAERLKARLDLLAADDRA------- 160
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371696 188 lseipspqLLQEEMTW-MKELLSSLgsPVVLCHNDLLCKNIIYNekqGD--VQFIDYEYSGYNYLAYDIGNHFNEFAgvS 264
Cdd:cd05153  161 --------LLEDELARlQALAPSDL--PRGVIHADLFRDNVLFD---GDrlSGIIDFYDACYDPLLYDLAIALNDWC--F 225
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 226371696 265 DVDYSLYPDRelqgqwLRSYLEAYKEYKGFgsdvTEKEVETLFIqvnQFALASHFFWgLWALIQAKY 331
Cdd:cd05153  226 DDDGKLDPER------AKALLAGYQSVRPL----TEEEKAALPL---LLRAAALRFW-LSRLYDFHL 278
SrkA COG2334
Ser/Thr protein kinase RdoA involved in Cpx stress response, MazF antagonist [Signal ...
118-288 4.26e-07

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: 51.08  E-value: 4.26e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371696 118 CYEFIQGEALDPQhvcNPAIFRLIARQLAKIHAIHAhnGWIPKSnlwlkmgkyfsliPTGFA--DENINKRFLSEIPSP- 194
Cdd:COG2334   93 LFPFLPGRSPEEP---SPEQLEELGRLLARLHRALA--DFPRPN-------------ARDLAwwDELLERLLGPLLPDPe 154
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371696 195 --QLLQEEMTWMKELLSSLGS--PVVLCHNDLLCKNIIYNEKQGDVqFIDYEYSGYNYLAYDIGnhfnefAGVSDVdysl 270
Cdd:COG2334  155 drALLEELLDRLEARLAPLLGalPRGVIHGDLHPDNVLFDGDGVSG-LIDFDDAGYGPRLYDLA------IALNGW---- 223
                        170
                 ....*....|....*...
gi 226371696 271 yPDRELQGQWLRSYLEAY 288
Cdd:COG2334  224 -ADGPLDPARLAALLEGY 240
YcbJ COG3173
Predicted kinase, aminoglycoside phosphotransferase (APT) family [General function prediction ...
36-299 2.41e-06

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


Pssm-ID: 442406 [Multi-domain]  Cd Length: 284  Bit Score: 48.57  E-value: 2.41e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371696  36 LLRHLRPHWDpREVTLQLFTDGITNKLiacYVGDTMEDVVLvRIY--GNKTELLVDRdeEvksFRVLQA-HGCA------ 106
Cdd:COG3173   11 LLAAQLPGLA-GLPEVEPLSGGWSNLT---YRLDTGDRLVL-RRPprGLASAHDVRR--E---ARVLRAlAPRLgvpvpr 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371696 107 PQLYCTFNNGL-----CYEFIQGEALDPQ-HVCNPAIFRLIARQLAK-IHAIHAhngwIPKSNLWLKMGKyfsliPTGFA 179
Cdd:COG3173   81 PLALGEDGEVIgapfyVMEWVEGETLEDAlPDLSPAERRALARALGEfLAALHA----VDPAAAGLADGR-----PEGLE 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371696 180 ------DENINKRFLSEIPSPQLLQEEMTWMKELLSSLGsPVVLCHNDLLCKNIIYNEKQGDVQ-FIDYEYSGYNYLAYD 252
Cdd:COG3173  152 rqlarwRAQLRRALARTDDLPALRERLAAWLAANLPEWG-PPVLVHGDLRPGNLLVDPDDGRLTaVIDWELATLGDPAAD 230
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 226371696 253 IGNHFNEFAGVSDvdysLYPDRELqgqwlrsYLEAYKEYKGFGSDVT 299
Cdd:COG3173  231 LAYLLLYWRLPDD----LLGPRAA-------FLAAYEEATGDLDDLT 266
APH_ChoK_like cd05120
Aminoglycoside 3'-phosphotransferase and Choline Kinase family; This family is composed of APH, ...
214-260 3.82e-06

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: 46.53  E-value: 3.82e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 226371696 214 PVVLCHNDLLCKNIIYNEKQGDVQFIDYEYSGYNYLAYDIGNHFNEF 260
Cdd:cd05120  110 SSVLTHGDLHPGNILVKPDGKLSGIIDWEFAGYGPPAFDYAAALRDW 156
spore_CotS TIGR02906
spore coat protein, CotS family; Members of this family include the spore coat proteins CotS ...
109-323 6.04e-05

spore coat protein, CotS family; Members of this family include the spore coat proteins CotS and YtaA from Bacillus subtilis and, from other endospore-forming bacteria, homologs that are more closely related to these two than to the spore coat proteins YutH and YsxE. The CotS family is more broadly distributed than YutH or YsxE, but still is not universal among spore-formers. [Cellular processes, Sporulation and germination]


Pssm-ID: 131952 [Multi-domain]  Cd Length: 313  Bit Score: 44.19  E-value: 6.04e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371696  109 LYCTFNNGL--CYEFIQGEALDpqhVCNPAIFRLIARQLAKIHaiHAHNGWIPKSNL-----WLKMGKYF---------- 171
Cdd:TIGR02906  62 LYVKYNGDLyvLTEWIEGRECD---FNNPIDLKKAAKGLALFH--HASKGYVPPDGSkirskLGKWPKQFekrlkelerf 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371696  172 -SLIPTGFADENINKRFLSEIP--------SPQLLQ--EEMTWMKELLSSLGspvvLCHNDLLCKNIIYneKQGDVQFID 240
Cdd:TIGR02906 137 kKIALEKKYKDEFDKLYLKEVDyflergkkALELLNksKYYDLCKEAKKIRG----FCHQDYAYHNILL--KDNEVYVID 210
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371696  241 YEYSGYNYLAYDIGNHFNEFA---GVSDVDyslypdrelqgqWLRSYLEAYKEYkgfgSDVTEKEVETLFIqvnqFALAS 317
Cdd:TIGR02906 211 FDYCTIDLPVRDLRKLIIKLMkknGVWDLE------------KAKEIIEAYSSI----NPLSKEEKEVLYI----DLAFP 270

                  ....*.
gi 226371696  318 HFFWGL 323
Cdd:TIGR02906 271 HKFWKI 276
CotI COG5881
Spore coat protein CotI/CotS, protein kinase superfamily [Cell cycle control, cell division, ...
108-323 7.63e-04

Spore coat protein CotI/CotS, protein kinase superfamily [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 444583 [Multi-domain]  Cd Length: 331  Bit Score: 41.03  E-value: 7.63e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371696 108 QLYCTFNNGLCY--EFIQGEALDpqhVCNPAIFRLIARQLAKIHA----IHAHNGWIPKSNL--WLK--------MGKYF 171
Cdd:COG5881   75 KPYVKYGGKLYYltEWIEGRECD---YKNPEDLKKAAETLAEFHKaskgFEPPPGSKGRSHLgkWPErfekrleeLEKFK 151
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371696 172 SLIPTGFADENINKRFLSEIPspQLLQEEMTWMKELLSSLGSPVV--------LCHNDLLCKNIIYNEKqGDVQFIDYEY 243
Cdd:COG5881  152 KIAEKKKNKNEFDRLFLKNID--YFLEQAEKALELLEKSAYYKLVkeakkeggFCHHDYAYHNILIDED-GKIYIIDFDY 228
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371696 244 SGYNYLAYDIGNHFNEF--AGVSDVDyslypdrelqgqWLRSYLEAY-KEYKgfgsdVTEKEVETLFIqvnqFALASHFF 320
Cdd:COG5881  229 CIYDLPVHDLAKLLRRVmkRGNWDIE------------KAKEILEAYnKINP-----LSKEEIEVLLA----FLLFPQKF 287

                 ...
gi 226371696 321 WGL 323
Cdd:COG5881  288 WRL 290
EcKL pfam02958
Ecdysteroid kinase-like family; This family includes ecdysteroid 22-kinase, an enzyme ...
127-257 1.86e-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: 39.56  E-value: 1.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371696  127 LDPQHVcnpaifRLIARQLAKIHAI-------------HAHNGWIPKSNLWLKMGKYFSLIPTGFADENInKRFLSEIPS 193
Cdd:pfam02958 111 LDLEHT------KLVLEKLAKFHAAsaalkelqpevfkQLKKGLFEEDYVNGAIKEFFEPLMETGLDAAA-EALREQLPE 183
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 226371696  194 PQLLQEEMTWMK----ELLSSLGSP-----VVLCHNDLLCKNII--YNEKQG--DVQFIDYEYSGYNYLAYDIgNHF 257
Cdd:pfam02958 184 YEKYAEKLEKLKdnyfDRLLRLVEPtpgefNVLNHGDLWVNNIMfkYDDEGEpeDVILVDFQLSRYGSPAIDL-NYF 259
CHK smart00587
ZnF_C4 abd HLH domain containing kinases domain; subfamily of choline kinases
139-253 3.14e-03

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


Pssm-ID: 214734  Cd Length: 196  Bit Score: 38.47  E-value: 3.14e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371696   139 RLIARQLAKIHAIHAH-----NGWIPKS-NLWLKMGKYFSLIPTGFADENINKRFLSEIPSP-----------QLLQEEM 201
Cdd:smart00587  26 SLVLKKLAKLHAASAVlieeeKGSYLEEfDEGLFERFKRMFSEEFIGGLENFLRELLSQPELlkveeyiekldKLLDNLE 105
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 226371696   202 TWMKELL-SSLGSPVVLCHNDLLCKNIIY----NEKQGDVQFIDYEYSGYNYLAYDI 253
Cdd:smart00587 106 DLKKEDKePDEGEFNVLNHGDLWANNIMFkyddEGKPEDVALIDFQLSHYGSPAEDL 162
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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