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Conserved domains on  [gi|186659525|ref|NP_060678|]
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ethanolamine kinase 2 isoform 1 [Homo sapiens]

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 ...
83-375 2.12e-140

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: 401.57  E-value: 2.12e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186659525  83 VRTKRFTDGITNKLVACYVEEDMQ-DCVLVRVYGERTELLVDRENEVRNFQLLRAHSCAPKLYCTFQNGLCYEYMQGVAL 161
Cdd:cd05157    1 IKVKRITGGITNALYKVTYPSGDTpKTVLVRIYGPGTELLIDRDRELRILQLLSRAGIGPKLYGRFENGRVEEFLPGRTL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186659525 162 EPEHIREPRLFRLIALEMAKIHTIHANGSL---PKPILWHKMHNYFTLVKNEI----NPSLSADVPKVEVLERELAWLKE 234
Cdd:cd05157   81 TPEDLRDPKISRLIARRLAELHSIVPLGEIegkKKPILWTTIRKWLDLAPEVFedekNKEKKLEKVDLERLRKELEWLEK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186659525 235 HLSQLE-SPVVFCHNDLLCKNIIYDSIKGHVRFIDYEYAGYNYQAFDIGNHFNEFAGVNEV-DYCLYPARETQLQWLHYY 312
Cdd:cd05157  161 WLESLEkSPIVFCHNDLLYGNILYNEDDDSVTFIDFEYAGPNPRAFDIANHFCEWAGFYCVlDYSRYPTKEEQRNFLRAY 240
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 186659525 313 LQA----QKGMAVTPREVQRLYVQVNKFALASHFFWALWALIQNQYSTIDFDFLRYAVIRFNQYFKV 375
Cdd:cd05157  241 LESldglPGGEEVSEEEVEKLYNEVNLFRLASHLFWGLWALIQAAISSIDFDYLGYAKERLDEYWGD 307
 
Name Accession Description Interval E-value
ETNK_euk cd05157
Euykaryotic Ethanolamine kinase; ETNK catalyzes the transfer of the gamma-phosphoryl group ...
83-375 2.12e-140

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: 401.57  E-value: 2.12e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186659525  83 VRTKRFTDGITNKLVACYVEEDMQ-DCVLVRVYGERTELLVDRENEVRNFQLLRAHSCAPKLYCTFQNGLCYEYMQGVAL 161
Cdd:cd05157    1 IKVKRITGGITNALYKVTYPSGDTpKTVLVRIYGPGTELLIDRDRELRILQLLSRAGIGPKLYGRFENGRVEEFLPGRTL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186659525 162 EPEHIREPRLFRLIALEMAKIHTIHANGSL---PKPILWHKMHNYFTLVKNEI----NPSLSADVPKVEVLERELAWLKE 234
Cdd:cd05157   81 TPEDLRDPKISRLIARRLAELHSIVPLGEIegkKKPILWTTIRKWLDLAPEVFedekNKEKKLEKVDLERLRKELEWLEK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186659525 235 HLSQLE-SPVVFCHNDLLCKNIIYDSIKGHVRFIDYEYAGYNYQAFDIGNHFNEFAGVNEV-DYCLYPARETQLQWLHYY 312
Cdd:cd05157  161 WLESLEkSPIVFCHNDLLYGNILYNEDDDSVTFIDFEYAGPNPRAFDIANHFCEWAGFYCVlDYSRYPTKEEQRNFLRAY 240
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 186659525 313 LQA----QKGMAVTPREVQRLYVQVNKFALASHFFWALWALIQNQYSTIDFDFLRYAVIRFNQYFKV 375
Cdd:cd05157  241 LESldglPGGEEVSEEEVEKLYNEVNLFRLASHLFWGLWALIQAAISSIDFDYLGYAKERLDEYWGD 307
PLN02421 PLN02421
phosphotransferase, alcohol group as acceptor/kinase
87-382 1.43e-80

phosphotransferase, alcohol group as acceptor/kinase


Pssm-ID: 215231 [Multi-domain]  Cd Length: 330  Bit Score: 250.04  E-value: 1.43e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186659525  87 RFTDGITNKLVACYVEEDMQD--CVLVRVYGERTELLVDRENEVRNFQLLRAHSCAPKLYCTFQNGLCYEYMQGVALEPE 164
Cdd:PLN02421  21 RISGGITNLLLKVSVKEENGNevSVTVRLFGPNTDYVIDRERELQAIKYLSAAGFGAKLLGVFGNGMIQSFINARTLTPS 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186659525 165 HIREPRLFRLIALEMAKIHTIHANGSlPKPILWHKMHNYF----TLVKNEINPSLSADVPKVEVLERELAWLKEHLSQLE 240
Cdd:PLN02421 101 DMRKPKVAAEIAKELRRLHQVEIPGS-KEPQLWNDIFKFYekasTVKFEDPEKQKKYETISFEELRDEIVELKEITDSLK 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186659525 241 SPVVFCHNDLLCKNIIYDSIKGHVRFIDYEYAGYNYQAFDIGNHFNEFAGVnEVDYCLYPARETQLQWLHYYLQAQKGMA 320
Cdd:PLN02421 180 APVVFAHNDLLSGNLMLNEDEGKLYFIDFEYGSYSYRGYDIGNHFNEYAGF-DCDYSLYPSKEEQYHFFRHYLRPDDPEE 258
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 186659525 321 VTPREVQRLYVQVNKFALASHFFWALWALIQNQYSTIDFDFLRYAVIRFNQYFKVKPQASAL 382
Cdd:PLN02421 259 VSDAELEELFVETNFYALASHLYWAIWAIVQAKMSPIDFDYLGYFFLRYKEYKRQKEKLLSL 320
Choline_kinase pfam01633
Choline/ethanolamine kinase; Choline kinase catalyzes the committed step in the synthesis of ...
106-303 3.98e-75

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: 231.78  E-value: 3.98e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186659525  106 QDCVLVRVYGERTELLVDRENEVRNFQLLRAHSCAPKLYCTFQNGLCYEYMQGVALEPEHIREPRLFRLIALEMAKIHTI 185
Cdd:pfam01633   2 PRKVLLRIYGPGTELLINREDEIVNFALLSERGLGPKLYGFFPNGRIEEFIPSRTLSTEDLRDPEISKLIAKRLAELHSL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186659525  186 HANGSlPKPILWHKMHNYFTLVKNEINP-----SLSADVPKVEVLERELAWLKEHLSQLESPVVFCHNDLLCKNIIYDSI 260
Cdd:pfam01633  82 EMPGK-KSPSLWKTMRKWLSLLKNLGAPesvnkSEQLKSINLEDLEKEINKLEKWLELLDSPIVFCHNDLQSGNILLLNE 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 186659525  261 KGHVRFIDYEYAGYNYQAFDIGNHFNEFAGVNE-------VDYCLYPARE 303
Cdd:pfam01633 161 TKRLVLIDFEYASYNYRGFDIANHFCEWAGDYHdptpffkCDYSLYPTRE 210
CotS COG0510
Thiamine kinase or a related kinase [Coenzyme transport and metabolism];
215-370 9.21e-19

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


Pssm-ID: 440276 [Multi-domain]  Cd Length: 156  Bit Score: 82.52  E-value: 9.21e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186659525 215 LSADVPKVEVLERELAWLKEHLSQLESPVVFCHNDLLCKNIIYDSiKGHVRFIDYEYAGYNYQAFDIGNHFNEFaGVNEv 294
Cdd:COG0510   21 LALGPRDLPELLRRLEELERALAARPLPLVLCHGDLHPGNFLVTD-DGRLYLIDWEYAGLGDPAFDLAALLVEY-GLSP- 97
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 186659525 295 dyclyparETQLQWLHYYLqaqkGMAVTPREVQRLYVqvnkFALASHFFWALWALIQNQYSTiDFDFLRYAVIRFN 370
Cdd:COG0510   98 --------EQAEELLEAYG----FGRPTEELLRRLRA----YRALADLLWALWALVRAAQEA-NGDLLKYLLRRLE 156
spore_CotS TIGR02906
spore coat protein, CotS family; Members of this family include the spore coat proteins CotS ...
172-283 2.78e-04

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


Pssm-ID: 131952 [Multi-domain]  Cd Length: 313  Bit Score: 42.27  E-value: 2.78e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186659525  172 FRLIALEMAKIHT-----IHANGSLPKpILWHKMHNYFTLVKNEIN----------PSLSADVPKVEVLERELAWLKEHL 236
Cdd:TIGR02906  90 LKKAAKGLALFHHaskgyVPPDGSKIR-SKLGKWPKQFEKRLKELErfkkialekkYKDEFDKLYLKEVDYFLERGKKAL 168
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 186659525  237 ------------SQLESPVVFCHNDLLCKNIIYDsiKGHVRFIDYEYAGYNYQAFDIGN 283
Cdd:TIGR02906 169 ellnkskyydlcKEAKKIRGFCHQDYAYHNILLK--DNEVYVIDFDYCTIDLPVRDLRK 225
 
Name Accession Description Interval E-value
ETNK_euk cd05157
Euykaryotic Ethanolamine kinase; ETNK catalyzes the transfer of the gamma-phosphoryl group ...
83-375 2.12e-140

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: 401.57  E-value: 2.12e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186659525  83 VRTKRFTDGITNKLVACYVEEDMQ-DCVLVRVYGERTELLVDRENEVRNFQLLRAHSCAPKLYCTFQNGLCYEYMQGVAL 161
Cdd:cd05157    1 IKVKRITGGITNALYKVTYPSGDTpKTVLVRIYGPGTELLIDRDRELRILQLLSRAGIGPKLYGRFENGRVEEFLPGRTL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186659525 162 EPEHIREPRLFRLIALEMAKIHTIHANGSL---PKPILWHKMHNYFTLVKNEI----NPSLSADVPKVEVLERELAWLKE 234
Cdd:cd05157   81 TPEDLRDPKISRLIARRLAELHSIVPLGEIegkKKPILWTTIRKWLDLAPEVFedekNKEKKLEKVDLERLRKELEWLEK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186659525 235 HLSQLE-SPVVFCHNDLLCKNIIYDSIKGHVRFIDYEYAGYNYQAFDIGNHFNEFAGVNEV-DYCLYPARETQLQWLHYY 312
Cdd:cd05157  161 WLESLEkSPIVFCHNDLLYGNILYNEDDDSVTFIDFEYAGPNPRAFDIANHFCEWAGFYCVlDYSRYPTKEEQRNFLRAY 240
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 186659525 313 LQA----QKGMAVTPREVQRLYVQVNKFALASHFFWALWALIQNQYSTIDFDFLRYAVIRFNQYFKV 375
Cdd:cd05157  241 LESldglPGGEEVSEEEVEKLYNEVNLFRLASHLFWGLWALIQAAISSIDFDYLGYAKERLDEYWGD 307
PLN02421 PLN02421
phosphotransferase, alcohol group as acceptor/kinase
87-382 1.43e-80

phosphotransferase, alcohol group as acceptor/kinase


Pssm-ID: 215231 [Multi-domain]  Cd Length: 330  Bit Score: 250.04  E-value: 1.43e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186659525  87 RFTDGITNKLVACYVEEDMQD--CVLVRVYGERTELLVDRENEVRNFQLLRAHSCAPKLYCTFQNGLCYEYMQGVALEPE 164
Cdd:PLN02421  21 RISGGITNLLLKVSVKEENGNevSVTVRLFGPNTDYVIDRERELQAIKYLSAAGFGAKLLGVFGNGMIQSFINARTLTPS 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186659525 165 HIREPRLFRLIALEMAKIHTIHANGSlPKPILWHKMHNYF----TLVKNEINPSLSADVPKVEVLERELAWLKEHLSQLE 240
Cdd:PLN02421 101 DMRKPKVAAEIAKELRRLHQVEIPGS-KEPQLWNDIFKFYekasTVKFEDPEKQKKYETISFEELRDEIVELKEITDSLK 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186659525 241 SPVVFCHNDLLCKNIIYDSIKGHVRFIDYEYAGYNYQAFDIGNHFNEFAGVnEVDYCLYPARETQLQWLHYYLQAQKGMA 320
Cdd:PLN02421 180 APVVFAHNDLLSGNLMLNEDEGKLYFIDFEYGSYSYRGYDIGNHFNEYAGF-DCDYSLYPSKEEQYHFFRHYLRPDDPEE 258
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 186659525 321 VTPREVQRLYVQVNKFALASHFFWALWALIQNQYSTIDFDFLRYAVIRFNQYFKVKPQASAL 382
Cdd:PLN02421 259 VSDAELEELFVETNFYALASHLYWAIWAIVQAKMSPIDFDYLGYFFLRYKEYKRQKEKLLSL 320
Choline_kinase pfam01633
Choline/ethanolamine kinase; Choline kinase catalyzes the committed step in the synthesis of ...
106-303 3.98e-75

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: 231.78  E-value: 3.98e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186659525  106 QDCVLVRVYGERTELLVDRENEVRNFQLLRAHSCAPKLYCTFQNGLCYEYMQGVALEPEHIREPRLFRLIALEMAKIHTI 185
Cdd:pfam01633   2 PRKVLLRIYGPGTELLINREDEIVNFALLSERGLGPKLYGFFPNGRIEEFIPSRTLSTEDLRDPEISKLIAKRLAELHSL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186659525  186 HANGSlPKPILWHKMHNYFTLVKNEINP-----SLSADVPKVEVLERELAWLKEHLSQLESPVVFCHNDLLCKNIIYDSI 260
Cdd:pfam01633  82 EMPGK-KSPSLWKTMRKWLSLLKNLGAPesvnkSEQLKSINLEDLEKEINKLEKWLELLDSPIVFCHNDLQSGNILLLNE 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 186659525  261 KGHVRFIDYEYAGYNYQAFDIGNHFNEFAGVNE-------VDYCLYPARE 303
Cdd:pfam01633 161 TKRLVLIDFEYASYNYRGFDIANHFCEWAGDYHdptpffkCDYSLYPTRE 210
ChoK_euk cd05156
Euykaryotic Choline Kinase; ChoK catalyzes the transfer of the gamma-phosphoryl group from ATP ...
83-377 4.62e-69

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: 220.19  E-value: 4.62e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186659525  83 VRTKRFTDGITNKLVAC------YVEEDMQDCVLVRVYGERTELLVDRENEVRNFQLLRAHSCAPKLYCTFQNGLCYEYM 156
Cdd:cd05156    1 FGIKTITGGLSNLLYLCslpdgvVPVGGEPRKVLLRIYGQILQAEESLVTESVIFALLSERGLGPKLYGIFPGGRLEEFI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186659525 157 QGVALEPEHIREPRLFRLIALEMAKIHTIHANGSLPKPILWHKMHNYFTLVKNEINPSLSADV------PKVEVLERELA 230
Cdd:cd05156   81 PSRPLTTDELSLPEISRKIARKMARFHSLEMPISKEPKWLFDTMERWLKEALSILFTDEPTKPskqlelLLSYDLAKELG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186659525 231 WLKEHLSQLESPVVFCHNDLLCKNIIYDSIKGH-----VRFIDYEYAGYNYQAFDIGNHFNEFAGVNEVD------YCL- 298
Cdd:cd05156  161 WLRSLLESTPSPVVFCHNDLQEGNILLLNGPENseddkLVLIDFEYCSYNYRGFDLANHFCEWAYDYTVPeppyfkINPe 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186659525 299 -YPARETQLQWLHYYLQAQKGM------AVTPREVQRLYVQVNKFALASHFFWALWALIQNQYSTIDFDFLRYAVIRFNQ 371
Cdd:cd05156  241 nYPTREQQLHFIRAYLDEQYKDktndltEERSKEEEKLLLEVNRFALASHFFWGLWSIVQAKISSIEFGYLEYAQARLDA 320

                 ....*.
gi 186659525 372 YFKVKP 377
Cdd:cd05156  321 YFKQKE 326
PLN02236 PLN02236
choline kinase
60-378 8.73e-63

choline kinase


Pssm-ID: 177880 [Multi-domain]  Cd Length: 344  Bit Score: 204.89  E-value: 8.73e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186659525  60 PDDILPGALR-LIQELRPHW----KPEQVRTKRFTDGITNKLVACY---VEEDMQDCVLVRVYGERTELLVDRENEVRNF 131
Cdd:PLN02236  11 SSGRIPDELKrILHSLASKWgdvvDDEALQVIPLKGAMTNEVFQIKwptKEGNLGRKVLVRIYGEGVELFFDRDDEIRTF 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186659525 132 QLLRAHSCAPKLYCTFQNGLCYEYMQGVALEPEHIREPRLFRLIALEMAKIHTIHANGSlPKPILWHKMHNYFTLVKNEI 211
Cdd:PLN02236  91 ECMSRHGQGPRLLGRFPNGRVEEFIHARTLSAADLRDPEISALIAAKLREFHSLDMPGP-KNVLLWDRLRNWLKEAKNLC 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186659525 212 NPSLSADVpKVEVLERELAWLKEHLSQLESPVVFCHNDLLCKNIIYDSIKGHVRFIDYEYAGYNYQAFDIGNHFNEFAG- 290
Cdd:PLN02236 170 SPEEAKEF-RLDSLEDEINLLEKELSGDDQEIGFCHNDLQYGNIMIDEETRAITIIDYEYASYNPVAYDIANHFCEMAAd 248
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186659525 291 -----VNEVDYCLYPARETQLQWLHYYLQAQkGMAVTPREVQRLYVQVNKFALASHFFWALWALIQNQYSTIDFDFLRYA 365
Cdd:PLN02236 249 yhsetPHILDYSKYPGEEERRRFIRTYLSSS-GEEPSDEEVEQLLDDVEKYTLASHLFWGLWGIISGHVNKIDFDYMEYA 327
                        330
                 ....*....|...
gi 186659525 366 VIRFNQYFKVKPQ 378
Cdd:PLN02236 328 RQRFEQYWLRKPE 340
ChoK-like_euk cd14021
Euykaryotic Choline Kinase and similar proteins; This group is composed of eukaryotic choline ...
86-349 2.54e-47

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: 160.90  E-value: 2.54e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186659525  86 KRFTDGITNKL----VACYVEEDMQDCVLVRVYGERTELLVDRENEVRNFQLLRAHSCAPKLYCTFQNGLCYEYMQGVAL 161
Cdd:cd14021    4 IRILSGLTNQVykvsLKDESDSLEPKKVLFRIYGKYLSTLYDREKESEVFKILSEQGLGPKLIYKFDGGRIEEYIDGRPL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186659525 162 EPEHIREPRLFRLIALEMAKIHTIHangslpkpilwhkmhnyftlvkneinpslsadvpkvevlerelawlkehlsqlES 241
Cdd:cd14021   84 TTDELRNPSVLTSIAKLLAKFHKIK-----------------------------------------------------TP 110
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186659525 242 PVVFCHNDLLCKNIIYDSIKGHVRFIDYEYAGYNYQAFDIGNHFNEFAGVNEV--------DYCLYPARETQLQWLHYYL 313
Cdd:cd14021  111 PVVFCHNDLQENNILLTNDQDGLRLIDFEYSGFNYRGYDIANFFNESMIDYDHpeppyfkiYKENYISEEEKRLFVSVYL 190
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 186659525 314 QAQKGMAVTP---REVQRLYVQVNKFALASHFFWALWAL 349
Cdd:cd14021  191 SEYLEKNVLPsldKLVEQFLQEVEIFTLGSHLYWGLWSI 229
PTZ00296 PTZ00296
choline kinase; Provisional
77-372 3.45e-34

choline kinase; Provisional


Pssm-ID: 240350 [Multi-domain]  Cd Length: 442  Bit Score: 131.55  E-value: 3.45e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186659525  77 HWKPEQVRTKRFTDGITNKLVACYVEEDMQDC-------VLVRVYGERTELLVDRENEVRNFQLLRAHSCAPKLYCTFQN 149
Cdd:PTZ00296 102 RFTEDDVRVNQILSGLTNQLFEVSLKEETANNypsirrrVLFRIYGKDVDELYNPISEFEVYKTMSKYRIAPQLLNTFSG 181
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186659525 150 GLCYEYMQGVALEPEHIREPRLFRLIALEMAKIHTIHANGSLPK-----PILWHKMHNYFTLVKNEINpsLSADVPKVEV 224
Cdd:PTZ00296 182 GRIEEWLYGDPLRIDDLKNPSILIGIANVLGKFHTLSRKRHLPEhwdrtPCIFKMMEKWKNQLSKYKN--IEKYQRDIHK 259
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186659525 225 LERELAWLKEHLSQ------LESPVVFCHNDLLCKNIIyDSIKGhVRFIDYEYAGYNYQAFDIGNHFNEFAgvneVDYCL 298
Cdd:PTZ00296 260 YIKESEKFIKFMKVysksdnLANDIVFCHNDLQENNII-NTNKC-LRLIDFEYSGYNFLATDIANFFIETT----IDYSV 333
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186659525 299 ------------YPARETQLQWLHYYLQA--QKGMAV-TPREVQRLYVQVNKFALASHFFWALWALIQ--NQYSTIDFDF 361
Cdd:PTZ00296 334 shypffaidkkkYISYENRKLFITAYLSNylDKSLVVpNPKIIDQILEAVEVQALGAHLLWGFWSIIRgyQTKSYNEFDF 413
                        330
                 ....*....|.
gi 186659525 362 LRYAVIRFNQY 372
Cdd:PTZ00296 414 FLYAKERFKMY 424
ChoK-like cd05151
Choline Kinase and similar proteins; This subfamily is composed of bacterial and eukaryotic ...
83-288 1.60e-25

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: 100.71  E-value: 1.60e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186659525  83 VRTKRFTDGITNKlvaCYVEEDMQDCVLVRVYGERTELLVDRENEVRNFQLLRAHSCAPK-LYCTFQNG-LCYEYMQGVA 160
Cdd:cd05151    1 ITIEPLKGGLTNK---NYLVEVAGKKYVLRIPGAGTELLIDRENEKANSKAAAELGIAPEvIYFDPETGvKITEFIEGAT 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186659525 161 LEPEHIREPRLFRLIALEMAKIHTIHANgslpkpilwhkmhnyftlvkneinpslsadvpkvevlerelawlkehlsqle 240
Cdd:cd05151   78 LLTNDFSDPENLERIAALLRKLHSSPLE---------------------------------------------------- 105
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 186659525 241 sPVVFCHNDLLCKNIIYDsiKGHVRFIDYEYAGYNYQAFDIGNHFNEF 288
Cdd:cd05151  106 -DLVLCHNDLVPGNFLLD--DDRLYLIDWEYAGMNDPLFDLAALFSEN 150
CotS COG0510
Thiamine kinase or a related kinase [Coenzyme transport and metabolism];
215-370 9.21e-19

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


Pssm-ID: 440276 [Multi-domain]  Cd Length: 156  Bit Score: 82.52  E-value: 9.21e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186659525 215 LSADVPKVEVLERELAWLKEHLSQLESPVVFCHNDLLCKNIIYDSiKGHVRFIDYEYAGYNYQAFDIGNHFNEFaGVNEv 294
Cdd:COG0510   21 LALGPRDLPELLRRLEELERALAARPLPLVLCHGDLHPGNFLVTD-DGRLYLIDWEYAGLGDPAFDLAALLVEY-GLSP- 97
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 186659525 295 dyclyparETQLQWLHYYLqaqkGMAVTPREVQRLYVqvnkFALASHFFWALWALIQNQYSTiDFDFLRYAVIRFN 370
Cdd:COG0510   98 --------EQAEELLEAYG----FGRPTEELLRRLRA----YRALADLLWALWALVRAAQEA-NGDLLKYLLRRLE 156
APH_ChoK_like cd05120
Aminoglycoside 3'-phosphotransferase and Choline Kinase family; This family is composed of APH, ...
86-288 2.02e-10

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: 58.85  E-value: 2.02e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186659525  86 KRFTDGITNKLVACYVEEDmqdcVLVRVYgeRTELLVDRENEVRNFQLLRAHSC--APKLYCTF----QNGLCYEYMQGV 159
Cdd:cd05120    4 KLIKEGGDNKVYLLGDPRE----YVLKIG--PPRLKKDLEKEAAMLQLLAGKLSlpVPKVYGFGesdgWEYLLMERIEGE 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186659525 160 ALEPEhireprlfrlialemakihtihangslpkpilWHKMhnyftlvkneinpslsaDVPKVEVLERELAwlkEHLSQL 239
Cdd:cd05120   78 TLSEV--------------------------------WPRL-----------------SEEEKEKIADQLA---EILAAL 105
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 186659525 240 ES--PVVFCHNDLLCKNIIYDSIKGHVRFIDYEYAGYNYQAFDIGNHFNEF 288
Cdd:cd05120  106 HRidSSVLTHGDLHPGNILVKPDGKLSGIIDWEFAGYGPPAFDYAAALRDW 156
PTZ00384 PTZ00384
choline kinase; Provisional
76-370 2.72e-10

choline kinase; Provisional


Pssm-ID: 173576 [Multi-domain]  Cd Length: 383  Bit Score: 61.33  E-value: 2.72e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186659525  76 PHW---KPEQVRTKRFTDGITNKL-VACYVEEDMQ----DCVLVRVYGERTELLVDRENEVRNFQLLRAHSCAPKLYCTF 147
Cdd:PTZ00384  43 PFWnnvNPEFIEIKKMNNGITNQVyQATLVDGDKDrypiKSVCIKKSSTYNSLVIDNDLQYNIAKLLGDNNFGPKIIGRF 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186659525 148 QNGLCYEYMQGVALEPEHIREPRLFRLIALEMAKIHTiHANGSLPK-----PILWHKMHNYFTLVKNEINP-SLSAD--- 218
Cdd:PTZ00384 123 GDFTIQEWVEGNTMGIDSLQNLSVLTGIASSLAKFHK-RVTELVPKewdrtPMFLTKISTWSQHVERIIKKyNLDFDyne 201
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186659525 219 -VPKVEVLERelaWLKEHLSQLES---PVVFCHNDLLCKNIIyDSIKGhVRFIDYEYAGYNYQAFDIGNHFNEFAGVNEV 294
Cdd:PTZ00384 202 lVQNYELFKK---ILNNHLNTSNSitnSVLFCHNDLFFTNIL-DFNQG-IYFIDFDFAGFNYVGWEIANFFVKLYIVYDP 276
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186659525 295 DYCLY--------PARETQLQWLHYYLQAQKGMAVTPRE--VQRLYVQVNKFALASHFFWALWALI-----QNQYStIDF 359
Cdd:PTZ00384 277 PTPPYfnsddslaLSEEMKTIFVSVYLSQLLGKNVLPSDdlVKEFLQSLEIHTLGVNLFWTYWGIVmndkpKNELS-KPV 355
                        330
                 ....*....|.
gi 186659525 360 DFLRYAVIRFN 370
Cdd:PTZ00384 356 KFEAYAKFQYN 366
APH pfam01636
Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance ...
86-286 1.71e-08

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: 54.81  E-value: 1.71e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186659525   86 KRFTDGITNKLVacYVEEDMQDcVLVRVYgERTELLVDRENEVRNFQLLRAHS----CAPKLYCTFQNGLC-----YEYM 156
Cdd:pfam01636   3 RPISSGASNRTY--LVTTGDGR-YVLRLP-PPGRAAEELRRELALLRHLAAAGvppvPRVLAGCTDAELLGlpfllMEYL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186659525  157 QGVALEPEHIRE--PRLFRLIALEMAKIHTIHANGslpKPILWHKMHN--YFTLVKNEINPSLSADVPKV--EVLERELA 230
Cdd:pfam01636  79 PGEVLARPLLPEerGALLEALGRALARLHAVDPAA---LPLAGRLARLleLLRQLEAALARLLAAELLDRleELEERLLA 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 186659525  231 WLKEHLsQLESPVVFCHNDLLCKNIIYDSiKGHVR-FIDYEYAGYNYQAFDIGNHFN 286
Cdd:pfam01636 156 ALLALL-PAELPPVLVHGDLHPGNLLVDP-GGRVSgVIDFEDAGLGDPAYDLAILLN 210
HomoserineK_II cd05153
Type II Homoserine Kinase; This subfamily is composed of unusual homoserine kinases, from a ...
161-349 2.40e-07

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: 51.88  E-value: 2.40e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186659525 161 LEPEHIREPRL--FRLIALEMAKIHTIHANGSLPKPI--LWHKMHNYFTLVKNEINPSLSADVpkvEVLERELAWLKEH- 235
Cdd:cd05153   97 LPGESLTTPTPeqCRAIGAALARLHLALAGFPPPRPNprGLAWWKPLAERLKARLDLLAADDR---ALLEDELARLQALa 173
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186659525 236 LSQLesPVVFCHNDLLCKNIIY--DSIKGhvrFIDYEYAGYNYQAFDIGNHFNEFAGvnEVDYCLYPARETQLqwLHYYl 313
Cdd:cd05153  174 PSDL--PRGVIHADLFRDNVLFdgDRLSG---IIDFYDACYDPLLYDLAIALNDWCF--DDDGKLDPERAKAL--LAGY- 243
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 186659525 314 QAQKGMavTPREVQRLYVQvnkFALASHFFWALWAL 349
Cdd:cd05153  244 QSVRPL--TEEEKAALPLL---LRAAALRFWLSRLY 274
YcbJ COG3173
Predicted kinase, aminoglycoside phosphotransferase (APT) family [General function prediction ...
69-284 1.82e-05

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


Pssm-ID: 442406 [Multi-domain]  Cd Length: 284  Bit Score: 45.88  E-value: 1.82e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186659525  69 RLIQELRPHWKPEqVRTKRFTDGITNKLVACYVEEDMqdcvLVRVYGERTELLVDRENEVRNFQLLRAHS----CAPKLY 144
Cdd:COG3173   10 ALLAAQLPGLAGL-PEVEPLSGGWSNLTYRLDTGDRL----VLRRPPRGLASAHDVRREARVLRALAPRLgvpvPRPLAL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186659525 145 CTFQNGL-----CYEYMQGVALEPEHIREP-----RLFRLIALEMAKIHTI---HANGSLPKPI-------LWHKMHnyf 204
Cdd:COG3173   85 GEDGEVIgapfyVMEWVEGETLEDALPDLSpaerrALARALGEFLAALHAVdpaAAGLADGRPEglerqlaRWRAQL--- 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186659525 205 tlvknEINPSLSADVPkvEVLERELAWLKEHLSqLESPVVFCHNDLLCKNIIYDSIKGHVR-FIDYEYAGYNYQAFDIGN 283
Cdd:COG3173  162 -----RRALARTDDLP--ALRERLAAWLAANLP-EWGPPVLVHGDLRPGNLLVDPDDGRLTaVIDWELATLGDPAADLAY 233

                 .
gi 186659525 284 H 284
Cdd:COG3173  234 L 234
spore_CotS TIGR02906
spore coat protein, CotS family; Members of this family include the spore coat proteins CotS ...
172-283 2.78e-04

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


Pssm-ID: 131952 [Multi-domain]  Cd Length: 313  Bit Score: 42.27  E-value: 2.78e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186659525  172 FRLIALEMAKIHT-----IHANGSLPKpILWHKMHNYFTLVKNEIN----------PSLSADVPKVEVLERELAWLKEHL 236
Cdd:TIGR02906  90 LKKAAKGLALFHHaskgyVPPDGSKIR-SKLGKWPKQFEKRLKELErfkkialekkYKDEFDKLYLKEVDYFLERGKKAL 168
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 186659525  237 ------------SQLESPVVFCHNDLLCKNIIYDsiKGHVRFIDYEYAGYNYQAFDIGN 283
Cdd:TIGR02906 169 ellnkskyydlcKEAKKIRGFCHQDYAYHNILLK--DNEVYVIDFDYCTIDLPVRDLRK 225
SrkA COG2334
Ser/Thr protein kinase RdoA involved in Cpx stress response, MazF antagonist [Signal ...
152-282 8.99e-04

Ser/Thr protein kinase RdoA involved in Cpx stress response, MazF antagonist [Signal transduction mechanisms]; Ser/Thr protein kinase RdoA involved in Cpx stress response, MazF antagonist is part of the Pathway/BioSystem: Threonine biosynthesis


Pssm-ID: 441905 [Multi-domain]  Cd Length: 297  Bit Score: 40.68  E-value: 8.99e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186659525 152 CYEYMQGVALEPEHirePRLFRLIALEMAKIHTIHANGSLPKPilwHKMHNYFTLVKNEINPSLsADVPKVEVLERELAW 231
Cdd:COG2334   93 LFPFLPGRSPEEPS---PEQLEELGRLLARLHRALADFPRPNA---RDLAWWDELLERLLGPLL-PDPEDRALLEELLDR 165
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 186659525 232 LKEHLSQLESPVVF--CHNDLLCKNIIYDSiKGHVRFIDYEYAGYNYQAFDIG 282
Cdd:COG2334  166 LEARLAPLLGALPRgvIHGDLHPDNVLFDG-DGVSGLIDFDDAGYGPRLYDLA 217
CotI COG5881
Spore coat protein CotI/CotS, protein kinase superfamily [Cell cycle control, cell division, ...
245-283 6.01e-03

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: 38.34  E-value: 6.01e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 186659525 245 FCHNDLLCKNIIYDSiKGHVRFIDYEYAGYNYQAFDIGN 283
Cdd:COG5881  203 FCHHDYAYHNILIDE-DGKIYIIDFDYCIYDLPVHDLAK 240
 
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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