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Conserved domains on  [gi|158303302|ref|NP_780652|]
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ethanolamine kinase 2 [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 ...
82-374 1.46e-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: 409.66  E-value: 1.46e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303302  82 VRTKRFKDGITNKLLACYV-EEDMRDCVLVRVYGERTELLVDRENEVRNFQLLRAHGCAPKLYCTFQNGLCYEYVQGVAL 160
Cdd:cd05157    1 IKVKRITGGITNALYKVTYpSGDTPKTVLVRIYGPGTELLIDRDRELRILQLLSRAGIGPKLYGRFENGRVEEFLPGRTL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303302 161 GPEHIREPQLFRLIALEMAKIHTIHANGSL---PKPTLWHKMHRYFTLVKDEISP----SLSADVPKVEVLEQELAWLKE 233
Cdd:cd05157   81 TPEDLRDPKISRLIARRLAELHSIVPLGEIegkKKPILWTTIRKWLDLAPEVFEDeknkEKKLEKVDLERLRKELEWLEK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303302 234 HLSQLD-SPVVFCHNDLLCKNIIYDSDKGRVCFIDYEYAGYNYQAFDIGNHFNEFAGVN-VVDYSRYPARETQVQWLRYY 311
Cdd:cd05157  161 WLESLEkSPIVFCHNDLLYGNILYNEDDDSVTFIDFEYAGPNPRAFDIANHFCEWAGFYcVLDYSRYPTKEEQRNFLRAY 240
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 158303302 312 LEA----QKGTAASPREVERLYAQVNKFALASHFFWALWALIQNQYSTISFDFLRYAVIRFNQYFKV 374
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 ...
82-374 1.46e-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: 409.66  E-value: 1.46e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303302  82 VRTKRFKDGITNKLLACYV-EEDMRDCVLVRVYGERTELLVDRENEVRNFQLLRAHGCAPKLYCTFQNGLCYEYVQGVAL 160
Cdd:cd05157    1 IKVKRITGGITNALYKVTYpSGDTPKTVLVRIYGPGTELLIDRDRELRILQLLSRAGIGPKLYGRFENGRVEEFLPGRTL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303302 161 GPEHIREPQLFRLIALEMAKIHTIHANGSL---PKPTLWHKMHRYFTLVKDEISP----SLSADVPKVEVLEQELAWLKE 233
Cdd:cd05157   81 TPEDLRDPKISRLIARRLAELHSIVPLGEIegkKKPILWTTIRKWLDLAPEVFEDeknkEKKLEKVDLERLRKELEWLEK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303302 234 HLSQLD-SPVVFCHNDLLCKNIIYDSDKGRVCFIDYEYAGYNYQAFDIGNHFNEFAGVN-VVDYSRYPARETQVQWLRYY 311
Cdd:cd05157  161 WLESLEkSPIVFCHNDLLYGNILYNEDDDSVTFIDFEYAGPNPRAFDIANHFCEWAGFYcVLDYSRYPTKEEQRNFLRAY 240
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 158303302 312 LEA----QKGTAASPREVERLYAQVNKFALASHFFWALWALIQNQYSTISFDFLRYAVIRFNQYFKV 374
Cdd:cd05157  241 LESldglPGGEEVSEEEVEKLYNEVNLFRLASHLFWGLWALIQAAISSIDFDYLGYAKERLDEYWGD 307
PLN02421 PLN02421
phosphotransferase, alcohol group as acceptor/kinase
90-381 1.36e-83

phosphotransferase, alcohol group as acceptor/kinase


Pssm-ID: 215231 [Multi-domain]  Cd Length: 330  Bit Score: 257.74  E-value: 1.36e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303302  90 GITNKLLACYVEEDMRD--CVLVRVYGERTELLVDRENEVRNFQLLRAHGCAPKLYCTFQNGLCYEYVQGVALGPEHIRE 167
Cdd:PLN02421  25 GITNLLLKVSVKEENGNevSVTVRLFGPNTDYVIDRERELQAIKYLSAAGFGAKLLGVFGNGMIQSFINARTLTPSDMRK 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303302 168 PQLFRLIALEMAKIHTIHANGSlPKPTLWHKMHRYF----TLVKDEISPSLSADVPKVEVLEQELAWLKEHLSQLDSPVV 243
Cdd:PLN02421 105 PKVAAEIAKELRRLHQVEIPGS-KEPQLWNDIFKFYekasTVKFEDPEKQKKYETISFEELRDEIVELKEITDSLKAPVV 183
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303302 244 FCHNDLLCKNIIYDSDKGRVCFIDYEYAGYNYQAFDIGNHFNEFAGVNvVDYSRYPARETQVQWLRYYLEAQKGTAASPR 323
Cdd:PLN02421 184 FAHNDLLSGNLMLNEDEGKLYFIDFEYGSYSYRGYDIGNHFNEYAGFD-CDYSLYPSKEEQYHFFRHYLRPDDPEEVSDA 262
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 158303302 324 EVERLYAQVNKFALASHFFWALWALIQNQYSTISFDFLRYAVIRFNQYFKVKPQVSAL 381
Cdd:PLN02421 263 ELEELFVETNFYALASHLYWAIWAIVQAKMSPIDFDYLGYFFLRYKEYKRQKEKLLSL 320
Choline_kinase pfam01633
Choline/ethanolamine kinase; Choline kinase catalyzes the committed step in the synthesis of ...
105-302 8.53e-80

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: 243.72  E-value: 8.53e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303302  105 RDCVLVRVYGERTELLVDRENEVRNFQLLRAHGCAPKLYCTFQNGLCYEYVQGVALGPEHIREPQLFRLIALEMAKIHTI 184
Cdd:pfam01633   2 PRKVLLRIYGPGTELLINREDEIVNFALLSERGLGPKLYGFFPNGRIEEFIPSRTLSTEDLRDPEISKLIAKRLAELHSL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303302  185 HANGSlPKPTLWHKMHRYFTLVKDEISP-----SLSADVPKVEVLEQELAWLKEHLSQLDSPVVFCHNDLLCKNIIYDSD 259
Cdd:pfam01633  82 EMPGK-KSPSLWKTMRKWLSLLKNLGAPesvnkSEQLKSINLEDLEKEINKLEKWLELLDSPIVFCHNDLQSGNILLLNE 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 158303302  260 KGRVCFIDYEYAGYNYQAFDIGNHFNEFAGVN-------VVDYSRYPARE 302
Cdd:pfam01633 161 TKRLVLIDFEYASYNYRGFDIANHFCEWAGDYhdptpffKCDYSLYPTRE 210
CotS COG0510
Thiamine kinase or a related kinase [Coenzyme transport and metabolism];
183-369 5.88e-21

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


Pssm-ID: 440276 [Multi-domain]  Cd Length: 156  Bit Score: 88.30  E-value: 5.88e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303302 183 TIHANGSLPKPTLWHKMHRYftlvkdeispsLSADVPKVEVLEQELAWLKEHLSQLDSPVVFCHNDLLCKNIIYDSDkGR 262
Cdd:COG0510    1 RLHASPALLRFDLFARLERY-----------LALGPRDLPELLRRLEELERALAARPLPLVLCHGDLHPGNFLVTDD-GR 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303302 263 VCFIDYEYAGYNYQAFDIGNHFNEFagvnvvdysRYPARETQvQWLRYYLeaqkGTAASPREVERLYAqvnkFALASHFF 342
Cdd:COG0510   69 LYLIDWEYAGLGDPAFDLAALLVEY---------GLSPEQAE-ELLEAYG----FGRPTEELLRRLRA----YRALADLL 130
                        170       180
                 ....*....|....*....|....*..
gi 158303302 343 WALWALIQNQYSTIsFDFLRYAVIRFN 369
Cdd:COG0510  131 WALWALVRAAQEAN-GDLLKYLLRRLE 156
spore_CotS TIGR02906
spore coat protein, CotS family; Members of this family include the spore coat proteins CotS ...
141-282 2.80e-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: 2.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303302  141 KLYCTFqNGLCY---EYVQGvalgpehiRE-----PQLFRLIALEMAKIHT-----IHANGSLPKpTLWHKMHRYFTLVK 207
Cdd:TIGR02906  61 ELYVKY-NGDLYvltEWIEG--------REcdfnnPIDLKKAAKGLALFHHaskgyVPPDGSKIR-SKLGKWPKQFEKRL 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303302  208 DEIS----------PSLSADVPKVEVLEQELAWLKEHL------------SQLDSPVVFCHNDLLCKNIIYDSDKgrVCF 265
Cdd:TIGR02906 131 KELErfkkialekkYKDEFDKLYLKEVDYFLERGKKALellnkskyydlcKEAKKIRGFCHQDYAYHNILLKDNE--VYV 208
                         170
                  ....*....|....*..
gi 158303302  266 IDYEYAGYNYQAFDIGN 282
Cdd:TIGR02906 209 IDFDYCTIDLPVRDLRK 225
 
Name Accession Description Interval E-value
ETNK_euk cd05157
Euykaryotic Ethanolamine kinase; ETNK catalyzes the transfer of the gamma-phosphoryl group ...
82-374 1.46e-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: 409.66  E-value: 1.46e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303302  82 VRTKRFKDGITNKLLACYV-EEDMRDCVLVRVYGERTELLVDRENEVRNFQLLRAHGCAPKLYCTFQNGLCYEYVQGVAL 160
Cdd:cd05157    1 IKVKRITGGITNALYKVTYpSGDTPKTVLVRIYGPGTELLIDRDRELRILQLLSRAGIGPKLYGRFENGRVEEFLPGRTL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303302 161 GPEHIREPQLFRLIALEMAKIHTIHANGSL---PKPTLWHKMHRYFTLVKDEISP----SLSADVPKVEVLEQELAWLKE 233
Cdd:cd05157   81 TPEDLRDPKISRLIARRLAELHSIVPLGEIegkKKPILWTTIRKWLDLAPEVFEDeknkEKKLEKVDLERLRKELEWLEK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303302 234 HLSQLD-SPVVFCHNDLLCKNIIYDSDKGRVCFIDYEYAGYNYQAFDIGNHFNEFAGVN-VVDYSRYPARETQVQWLRYY 311
Cdd:cd05157  161 WLESLEkSPIVFCHNDLLYGNILYNEDDDSVTFIDFEYAGPNPRAFDIANHFCEWAGFYcVLDYSRYPTKEEQRNFLRAY 240
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 158303302 312 LEA----QKGTAASPREVERLYAQVNKFALASHFFWALWALIQNQYSTISFDFLRYAVIRFNQYFKV 374
Cdd:cd05157  241 LESldglPGGEEVSEEEVEKLYNEVNLFRLASHLFWGLWALIQAAISSIDFDYLGYAKERLDEYWGD 307
PLN02421 PLN02421
phosphotransferase, alcohol group as acceptor/kinase
90-381 1.36e-83

phosphotransferase, alcohol group as acceptor/kinase


Pssm-ID: 215231 [Multi-domain]  Cd Length: 330  Bit Score: 257.74  E-value: 1.36e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303302  90 GITNKLLACYVEEDMRD--CVLVRVYGERTELLVDRENEVRNFQLLRAHGCAPKLYCTFQNGLCYEYVQGVALGPEHIRE 167
Cdd:PLN02421  25 GITNLLLKVSVKEENGNevSVTVRLFGPNTDYVIDRERELQAIKYLSAAGFGAKLLGVFGNGMIQSFINARTLTPSDMRK 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303302 168 PQLFRLIALEMAKIHTIHANGSlPKPTLWHKMHRYF----TLVKDEISPSLSADVPKVEVLEQELAWLKEHLSQLDSPVV 243
Cdd:PLN02421 105 PKVAAEIAKELRRLHQVEIPGS-KEPQLWNDIFKFYekasTVKFEDPEKQKKYETISFEELRDEIVELKEITDSLKAPVV 183
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303302 244 FCHNDLLCKNIIYDSDKGRVCFIDYEYAGYNYQAFDIGNHFNEFAGVNvVDYSRYPARETQVQWLRYYLEAQKGTAASPR 323
Cdd:PLN02421 184 FAHNDLLSGNLMLNEDEGKLYFIDFEYGSYSYRGYDIGNHFNEYAGFD-CDYSLYPSKEEQYHFFRHYLRPDDPEEVSDA 262
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 158303302 324 EVERLYAQVNKFALASHFFWALWALIQNQYSTISFDFLRYAVIRFNQYFKVKPQVSAL 381
Cdd:PLN02421 263 ELEELFVETNFYALASHLYWAIWAIVQAKMSPIDFDYLGYFFLRYKEYKRQKEKLLSL 320
Choline_kinase pfam01633
Choline/ethanolamine kinase; Choline kinase catalyzes the committed step in the synthesis of ...
105-302 8.53e-80

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: 243.72  E-value: 8.53e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303302  105 RDCVLVRVYGERTELLVDRENEVRNFQLLRAHGCAPKLYCTFQNGLCYEYVQGVALGPEHIREPQLFRLIALEMAKIHTI 184
Cdd:pfam01633   2 PRKVLLRIYGPGTELLINREDEIVNFALLSERGLGPKLYGFFPNGRIEEFIPSRTLSTEDLRDPEISKLIAKRLAELHSL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303302  185 HANGSlPKPTLWHKMHRYFTLVKDEISP-----SLSADVPKVEVLEQELAWLKEHLSQLDSPVVFCHNDLLCKNIIYDSD 259
Cdd:pfam01633  82 EMPGK-KSPSLWKTMRKWLSLLKNLGAPesvnkSEQLKSINLEDLEKEINKLEKWLELLDSPIVFCHNDLQSGNILLLNE 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 158303302  260 KGRVCFIDYEYAGYNYQAFDIGNHFNEFAGVN-------VVDYSRYPARE 302
Cdd:pfam01633 161 TKRLVLIDFEYASYNYRGFDIANHFCEWAGDYhdptpffKCDYSLYPTRE 210
ChoK_euk cd05156
Euykaryotic Choline Kinase; ChoK catalyzes the transfer of the gamma-phosphoryl group from ATP ...
82-376 8.57e-71

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: 224.81  E-value: 8.57e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303302  82 VRTKRFKDGITNKLLACYVEEDMRD------CVLVRVYGERTELLVDRENEVRNFQLLRAHGCAPKLYCTFQNGLCYEYV 155
Cdd:cd05156    1 FGIKTITGGLSNLLYLCSLPDGVVPvggeprKVLLRIYGQILQAEESLVTESVIFALLSERGLGPKLYGIFPGGRLEEFI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303302 156 QGVALGPEHIREPQLFRLIALEMAKIHTIHANGSLPKPTLWHKMHRYFTLVKDEISPSLSADV------PKVEVLEQELA 229
Cdd:cd05156   81 PSRPLTTDELSLPEISRKIARKMARFHSLEMPISKEPKWLFDTMERWLKEALSILFTDEPTKPskqlelLLSYDLAKELG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303302 230 WLKEHLSQLDSPVVFCHNDLLCKNIIYDSDKG-----RVCFIDYEYAGYNYQAFDIGNHFNEfagvNVVDY--------- 295
Cdd:cd05156  161 WLRSLLESTPSPVVFCHNDLQEGNILLLNGPEnseddKLVLIDFEYCSYNYRGFDLANHFCE----WAYDYtvpeppyfk 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303302 296 ---SRYPARETQVQWLRYYLEAQK------GTAASPREVERLYAQVNKFALASHFFWALWALIQNQYSTISFDFLRYAVI 366
Cdd:cd05156  237 inpENYPTREQQLHFIRAYLDEQYkdktndLTEERSKEEEKLLLEVNRFALASHFFWGLWSIVQAKISSIEFGYLEYAQA 316
                        330
                 ....*....|
gi 158303302 367 RFNQYFKVKP 376
Cdd:cd05156  317 RLDAYFKQKE 326
PLN02236 PLN02236
choline kinase
60-378 1.06e-69

choline kinase


Pssm-ID: 177880 [Multi-domain]  Cd Length: 344  Bit Score: 222.61  E-value: 1.06e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303302  60 DDILPGALR-LIRELRPHW----KPEQVRTKRFKDGITNKLLACY---VEEDMRDCVLVRVYGERTELLVDRENEVRNFQ 131
Cdd:PLN02236  12 SGRIPDELKrILHSLASKWgdvvDDEALQVIPLKGAMTNEVFQIKwptKEGNLGRKVLVRIYGEGVELFFDRDDEIRTFE 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303302 132 LLRAHGCAPKLYCTFQNGLCYEYVQGVALGPEHIREPQLFRLIALEMAKIHTIHANGSlPKPTLWHKMHRYFTLVKdEIS 211
Cdd:PLN02236  92 CMSRHGQGPRLLGRFPNGRVEEFIHARTLSAADLRDPEISALIAAKLREFHSLDMPGP-KNVLLWDRLRNWLKEAK-NLC 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303302 212 PSLSADVPKVEVLEQELAWLKEHLSQLDSPVVFCHNDLLCKNIIYDSDKGRVCFIDYEYAGYNYQAFDIGNHFNEFAG-- 289
Cdd:PLN02236 170 SPEEAKEFRLDSLEDEINLLEKELSGDDQEIGFCHNDLQYGNIMIDEETRAITIIDYEYASYNPVAYDIANHFCEMAAdy 249
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303302 290 ----VNVVDYSRYPARETQVQWLRYYLEAQkGTAASPREVERLYAQVNKFALASHFFWALWALIQNQYSTISFDFLRYAV 365
Cdd:PLN02236 250 hsetPHILDYSKYPGEEERRRFIRTYLSSS-GEEPSDEEVEQLLDDVEKYTLASHLFWGLWGIISGHVNKIDFDYMEYAR 328
                        330
                 ....*....|...
gi 158303302 366 IRFNQYFKVKPQV 378
Cdd:PLN02236 329 QRFEQYWLRKPEL 341
ChoK-like_euk cd14021
Euykaryotic Choline Kinase and similar proteins; This group is composed of eukaryotic choline ...
85-348 8.81e-52

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: 172.45  E-value: 8.81e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303302  85 KRFKDGITNKL----LACYVEEDMRDCVLVRVYGERTELLVDRENEVRNFQLLRAHGCAPKLYCTFQNGLCYEYVQGVAL 160
Cdd:cd14021    4 IRILSGLTNQVykvsLKDESDSLEPKKVLFRIYGKYLSTLYDREKESEVFKILSEQGLGPKLIYKFDGGRIEEYIDGRPL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303302 161 GPEHIREPQLFRLIALEMAKIHTIHangslpkptlwhkmhryftlvkdeispslsadvpkvevleqelawlkehlsqlDS 240
Cdd:cd14021   84 TTDELRNPSVLTSIAKLLAKFHKIK-----------------------------------------------------TP 110
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303302 241 PVVFCHNDLLCKNIIYDSDKGRVCFIDYEYAGYNYQAFDIGNHFNEFAGVNVV--------DYSRYPARETQVQWLRYYL 312
Cdd:cd14021  111 PVVFCHNDLQENNILLTNDQDGLRLIDFEYSGFNYRGYDIANFFNESMIDYDHpeppyfkiYKENYISEEEKRLFVSVYL 190
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 158303302 313 EAQKGT---AASPREVERLYAQVNKFALASHFFWALWAL 348
Cdd:cd14021  191 SEYLEKnvlPSLDKLVEQFLQEVEIFTLGSHLYWGLWSI 229
PTZ00296 PTZ00296
choline kinase; Provisional
76-371 9.48e-36

choline kinase; Provisional


Pssm-ID: 240350 [Multi-domain]  Cd Length: 442  Bit Score: 135.79  E-value: 9.48e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303302  76 HWKPEQVRTKRFKDGITNKLLACYVEED-------MRDCVLVRVYGERTELLVDRENEVRNFQLLRAHGCAPKLYCTFQN 148
Cdd:PTZ00296 102 RFTEDDVRVNQILSGLTNQLFEVSLKEEtannypsIRRRVLFRIYGKDVDELYNPISEFEVYKTMSKYRIAPQLLNTFSG 181
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303302 149 GLCYEYVQGVALGPEHIREPQLFRLIALEMAKIHTIHANGSLPK-----PTLWHKMHRYftlvKDEISPSLSADVPKVEV 223
Cdd:PTZ00296 182 GRIEEWLYGDPLRIDDLKNPSILIGIANVLGKFHTLSRKRHLPEhwdrtPCIFKMMEKW----KNQLSKYKNIEKYQRDI 257
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303302 224 --LEQELAWLKEHLSQ------LDSPVVFCHNDLLCKNIIyDSDKGrVCFIDYEYAGYNYQAFDIGNHFNEFA---GVN- 291
Cdd:PTZ00296 258 hkYIKESEKFIKFMKVysksdnLANDIVFCHNDLQENNII-NTNKC-LRLIDFEYSGYNFLATDIANFFIETTidySVSh 335
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303302 292 ----VVDYSRYPARETQVQWLRYYLEA--QKGTAA-SPREVERLYAQVNKFALASHFFWALWALIQNqYSTIS---FDFL 361
Cdd:PTZ00296 336 ypffAIDKKKYISYENRKLFITAYLSNylDKSLVVpNPKIIDQILEAVEVQALGAHLLWGFWSIIRG-YQTKSyneFDFF 414
                        330
                 ....*....|
gi 158303302 362 RYAVIRFNQY 371
Cdd:PTZ00296 415 LYAKERFKMY 424
ChoK-like cd05151
Choline Kinase and similar proteins; This subfamily is composed of bacterial and eukaryotic ...
82-287 1.46e-27

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


Pssm-ID: 270700 [Multi-domain]  Cd Length: 152  Bit Score: 106.10  E-value: 1.46e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303302  82 VRTKRFKDGITNKLLACYVEEdmRDCVLvRVYGERTELLVDRENEVRNFQLLRAHGCAPK-LYCTFQNG-LCYEYVQGVA 159
Cdd:cd05151    1 ITIEPLKGGLTNKNYLVEVAG--KKYVL-RIPGAGTELLIDRENEKANSKAAAELGIAPEvIYFDPETGvKITEFIEGAT 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303302 160 LGPEHIREPQLFRLIALEMAKIHtihangSLPKPTLwhkmhryftlvkdeispslsadvpkvevleqelawlkehlsqld 239
Cdd:cd05151   78 LLTNDFSDPENLERIAALLRKLH------SSPLEDL-------------------------------------------- 107
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 158303302 240 spvVFCHNDLLCKNIIYDSDkgRVCFIDYEYAGYNYQAFDIGNHFNEF 287
Cdd:cd05151  108 ---VLCHNDLVPGNFLLDDD--RLYLIDWEYAGMNDPLFDLAALFSEN 150
CotS COG0510
Thiamine kinase or a related kinase [Coenzyme transport and metabolism];
183-369 5.88e-21

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


Pssm-ID: 440276 [Multi-domain]  Cd Length: 156  Bit Score: 88.30  E-value: 5.88e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303302 183 TIHANGSLPKPTLWHKMHRYftlvkdeispsLSADVPKVEVLEQELAWLKEHLSQLDSPVVFCHNDLLCKNIIYDSDkGR 262
Cdd:COG0510    1 RLHASPALLRFDLFARLERY-----------LALGPRDLPELLRRLEELERALAARPLPLVLCHGDLHPGNFLVTDD-GR 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303302 263 VCFIDYEYAGYNYQAFDIGNHFNEFagvnvvdysRYPARETQvQWLRYYLeaqkGTAASPREVERLYAqvnkFALASHFF 342
Cdd:COG0510   69 LYLIDWEYAGLGDPAFDLAALLVEY---------GLSPEQAE-ELLEAYG----FGRPTEELLRRLRA----YRALADLL 130
                        170       180
                 ....*....|....*....|....*..
gi 158303302 343 WALWALIQNQYSTIsFDFLRYAVIRFN 369
Cdd:COG0510  131 WALWALVRAAQEAN-GDLLKYLLRRLE 156
APH_ChoK_like cd05120
Aminoglycoside 3'-phosphotransferase and Choline Kinase family; This family is composed of APH, ...
85-287 1.29e-11

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: 62.32  E-value: 1.29e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303302  85 KRFKDGITNKLLACYVEEDmrdcVLVRVYgeRTELLVDRENEVRNFQLLRAHGC--APKLYCTF----QNGLCYEYVQGV 158
Cdd:cd05120    4 KLIKEGGDNKVYLLGDPRE----YVLKIG--PPRLKKDLEKEAAMLQLLAGKLSlpVPKVYGFGesdgWEYLLMERIEGE 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303302 159 ALGPEhirepqlfrlialemakihtihangslpkptlWHKMhryftlvkdeiSPSlsadvpKVEVLEQELAwlkEHLSQL 238
Cdd:cd05120   78 TLSEV--------------------------------WPRL-----------SEE------EKEKIADQLA---EILAAL 105
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 158303302 239 DS--PVVFCHNDLLCKNIIYDSDKGRVCFIDYEYAGYNYQAFDIGNHFNEF 287
Cdd:cd05120  106 HRidSSVLTHGDLHPGNILVKPDGKLSGIIDWEFAGYGPPAFDYAAALRDW 156
PTZ00384 PTZ00384
choline kinase; Provisional
75-351 1.86e-11

choline kinase; Provisional


Pssm-ID: 173576 [Multi-domain]  Cd Length: 383  Bit Score: 64.80  E-value: 1.86e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303302  75 PHW---KPEQVRTKRFKDGITNKL-LACYVEEDMR----DCVLVRVYGERTELLVDRENEVRNFQLLRAHGCAPKLYCTF 146
Cdd:PTZ00384  43 PFWnnvNPEFIEIKKMNNGITNQVyQATLVDGDKDrypiKSVCIKKSSTYNSLVIDNDLQYNIAKLLGDNNFGPKIIGRF 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303302 147 QNGLCYEYVQGVALGPEHIREPQLFRLIALEMAKIHTiHANGSLPKPtlWHKMHRYFTLVK------DEISPSLSADVPK 220
Cdd:PTZ00384 123 GDFTIQEWVEGNTMGIDSLQNLSVLTGIASSLAKFHK-RVTELVPKE--WDRTPMFLTKIStwsqhvERIIKKYNLDFDY 199
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303302 221 VEVLEQ-EL--AWLKEHLSQLDS---PVVFCHNDLLCKNIIyDSDKGrVCFIDYEYAGYNYQAFDIGNHFNEFAGVNVVD 294
Cdd:PTZ00384 200 NELVQNyELfkKILNNHLNTSNSitnSVLFCHNDLFFTNIL-DFNQG-IYFIDFDFAGFNYVGWEIANFFVKLYIVYDPP 277
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 158303302 295 YSRY--------PARETQVQWLRYYLEAQKGTAASPRE--VERLYAQVNKFALASHFFWALWALIQN 351
Cdd:PTZ00384 278 TPPYfnsddslaLSEEMKTIFVSVYLSQLLGKNVLPSDdlVKEFLQSLEIHTLGVNLFWTYWGIVMN 344
APH pfam01636
Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance ...
85-285 6.66e-11

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: 61.75  E-value: 6.66e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303302   85 KRFKDGITNklLACYVEEDMRDcVLVRVYgERTELLVDRENEVRNFQLLRAHG----CAPKLYCTFQNGLC-----YEYV 155
Cdd:pfam01636   3 RPISSGASN--RTYLVTTGDGR-YVLRLP-PPGRAAEELRRELALLRHLAAAGvppvPRVLAGCTDAELLGlpfllMEYL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303302  156 QGVALGPEHIREPQ--LFRLIALEMAKIHTIHANGSlpKPTLWHKMHRYF-TLVKDEISPSLSADVPKV--EVLEQELAW 230
Cdd:pfam01636  79 PGEVLARPLLPEERgaLLEALGRALARLHAVDPAAL--PLAGRLARLLELlRQLEAALARLLAAELLDRleELEERLLAA 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 158303302  231 LKEHLsQLDSPVVFCHNDLLCKNIIYDSDKGRVCFIDYEYAGYNYQAFDIGNHFN 285
Cdd:pfam01636 157 LLALL-PAELPPVLVHGDLHPGNLLVDPGGRVSGVIDFEDAGLGDPAYDLAILLN 210
YcbJ COG3173
Predicted kinase, aminoglycoside phosphotransferase (APT) family [General function prediction ...
68-320 1.26e-08

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


Pssm-ID: 442406 [Multi-domain]  Cd Length: 284  Bit Score: 55.51  E-value: 1.26e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303302  68 RLIRELRPHWKPEqVRTKRFKDGITNKLLACYVEEDMrdcvLVRVYGERTELLVDRENEVRNFQLLRAHG----CAPKLY 143
Cdd:COG3173   10 ALLAAQLPGLAGL-PEVEPLSGGWSNLTYRLDTGDRL----VLRRPPRGLASAHDVRREARVLRALAPRLgvpvPRPLAL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303302 144 CTFQNGL-----CYEYVQGVALGPEHIRE-PQLFRLIALEM----AKIHTIHANGSLPKPTLWHKMHRYFTLVKDEISPS 213
Cdd:COG3173   85 GEDGEVIgapfyVMEWVEGETLEDALPDLsPAERRALARALgeflAALHAVDPAAAGLADGRPEGLERQLARWRAQLRRA 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303302 214 LSADVPKVEVLEQELAWLKEHLSqLDSPVVFCHNDLLCKNIIYDSDKGRVC-FIDYEYAGYNYQAFDIGNH------FNE 286
Cdd:COG3173  165 LARTDDLPALRERLAAWLAANLP-EWGPPVLVHGDLRPGNLLVDPDDGRLTaVIDWELATLGDPAADLAYLllywrlPDD 243
                        250       260       270
                 ....*....|....*....|....*....|....
gi 158303302 287 FAGVNVVDYSRYPARETQVQWLRYYLEAQKGTAA 320
Cdd:COG3173  244 LLGPRAAFLAAYEEATGDLDDLTWWALADPELAA 277
HomoserineK_II cd05153
Type II Homoserine Kinase; This subfamily is composed of unusual homoserine kinases, from a ...
162-348 2.60e-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: 2.60e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303302 162 PEHIREPQLFRLIALeMAKIHTIHANGSLPKPT--LWHKMHRYFTLVKDEISPSLSADVpkvEVLEQELAWLKEHLSQlD 239
Cdd:cd05153  102 LTTPTPEQCRAIGAA-LARLHLALAGFPPPRPNprGLAWWKPLAERLKARLDLLAADDR---ALLEDELARLQALAPS-D 176
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303302 240 SPVVFCHNDLLCKNIIYDSDKgRVCFIDYEYAGYNYQAFDIGNHFNEFAGVNvvDYSRYPARETqvQWLRYYleaQKGTA 319
Cdd:cd05153  177 LPRGVIHADLFRDNVLFDGDR-LSGIIDFYDACYDPLLYDLAIALNDWCFDD--DGKLDPERAK--ALLAGY---QSVRP 248
                        170       180
                 ....*....|....*....|....*....
gi 158303302 320 ASPREVERLYAQvnkFALASHFFWALWAL 348
Cdd:cd05153  249 LTEEEKAALPLL---LRAAALRFWLSRLY 274
SrkA COG2334
Ser/Thr protein kinase RdoA involved in Cpx stress response, MazF antagonist [Signal ...
102-281 1.27e-06

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: 49.54  E-value: 1.27e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303302 102 EDMRDCVLvRVY--GERTELLVDRENEVRNFqlLRAHGCA-PKLYCTFQNGL----------CYEYVQGVALGPEHireP 168
Cdd:COG2334   34 EDGRRYVL-KLYrpGRWSPEEIPFELALLAH--LAAAGLPvPAPVPTRDGETllelegrpaaLFPFLPGRSPEEPS---P 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303302 169 QLFRLIALEMAKIHTIHANGSLPKPT---LWHKMHRYFtLVKDEISPSLSAdvpkveVLEQELAWLKEHLSQLDSPVVF- 244
Cdd:COG2334  108 EQLEELGRLLARLHRALADFPRPNARdlaWWDELLERL-LGPLLPDPEDRA------LLEELLDRLEARLAPLLGALPRg 180
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 158303302 245 -CHNDLLCKNIIYDSDKGrVCFIDYEYAGYNYQAFDIG 281
Cdd:COG2334  181 vIHGDLHPDNVLFDGDGV-SGLIDFDDAGYGPRLYDLA 217
ACAD10_11_N-like cd05154
N-terminal domain of Acyl-CoA dehydrogenase (ACAD) 10 and 11, and similar proteins; This ...
105-314 4.22e-05

N-terminal domain of Acyl-CoA dehydrogenase (ACAD) 10 and 11, and similar proteins; This subfamily is composed of the N-terminal domains of vertebrate ACAD10 and ACAD11, and similar uncharacterized bacterial and eukaryotic proteins. ACADs are a family of flavoproteins that are involved in the beta-oxidation of fatty acyl-CoA derivatives. ACAD deficiency can cause metabolic disorders including muscle fatigue, hypoglycemia, and hepatic lipidosis. There are at least 11 distinct ACADs, some of which show distinct substrate specificities to either straight-chain or branched-chain fatty acids. ACAD10 is widely expressed in human tissues and highly expressed in liver, kidney, pancreas, and spleen. ACAD10 and ACAD11 are both significantly expressed in human brain tissues. They contain a long N-terminal domain with similarity to phosphotransferases with a Protein Kinase fold, which is absent in other ACADs. They may exhibit multiple functions in acyl-CoA oxidation pathways. ACAD11 utilizes substrates with carbon chain lengths of 20 to 26, with optimal activity towards C22CoA. ACAD10 may be associated with an increased risk in type II diabetes. The ACAD10/11-like 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: 270703 [Multi-domain]  Cd Length: 254  Bit Score: 44.53  E-value: 4.22e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303302 105 RDCVLvRVYGERTELLV--DRENEVRNFQLLRAHGC-APKLYCtfqngLC------------YEYVQGVALG---PEHIR 166
Cdd:cd05154   26 RRLVL-RRPPPGGLLPSahDLEREYRVLRALAGTGVpVPRVLA-----LCedpsvlgapfyvMERVDGRVLPdplPRPDL 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303302 167 EPQLFRLIALEM----AKIHTI--HANG--SLPKPT--------LWHKMHRyftlvkdeispslSADVPKVEVLEQELAW 230
Cdd:cd05154  100 SPEERRALARSLvdalAALHSVdpAALGlaDLGRPEgylerqvdRWRRQLE-------------AAATDPPPALEEALRW 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303302 231 LKEHLSQlDSPVVFCHNDLLCKNIIYDSDKGRVCFIDYEYA---------GYNYQAFDIGNHFNEFAGVNVVDysRYPAR 301
Cdd:cd05154  167 LRANLPA-DGRPVLVHGDFRLGNLLFDPDGRVTAVLDWELAtlgdpledlAWLLARWWRPGDPPGLAAPTRLP--GFPSR 243
                        250
                 ....*....|...
gi 158303302 302 EtqvQWLRYYLEA 314
Cdd:cd05154  244 E---ELLARYEEA 253
CotI COG5881
Spore coat protein CotI/CotS, protein kinase superfamily [Cell cycle control, cell division, ...
244-282 2.42e-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: 42.57  E-value: 2.42e-04
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 158303302 244 FCHNDLLCKNIIYDsDKGRVCFIDYEYAGYNYQAFDIGN 282
Cdd:COG5881  203 FCHHDYAYHNILID-EDGKIYIIDFDYCIYDLPVHDLAK 240
spore_CotS TIGR02906
spore coat protein, CotS family; Members of this family include the spore coat proteins CotS ...
141-282 2.80e-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: 2.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303302  141 KLYCTFqNGLCY---EYVQGvalgpehiRE-----PQLFRLIALEMAKIHT-----IHANGSLPKpTLWHKMHRYFTLVK 207
Cdd:TIGR02906  61 ELYVKY-NGDLYvltEWIEG--------REcdfnnPIDLKKAAKGLALFHHaskgyVPPDGSKIR-SKLGKWPKQFEKRL 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303302  208 DEIS----------PSLSADVPKVEVLEQELAWLKEHL------------SQLDSPVVFCHNDLLCKNIIYDSDKgrVCF 265
Cdd:TIGR02906 131 KELErfkkialekkYKDEFDKLYLKEVDYFLERGKKALellnkskyydlcKEAKKIRGFCHQDYAYHNILLKDNE--VYV 208
                         170
                  ....*....|....*..
gi 158303302  266 IDYEYAGYNYQAFDIGN 282
Cdd:TIGR02906 209 IDFDYCTIDLPVRDLRK 225
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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