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Conserved domains on  [gi|1919638952|ref|WP_193397120|]
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thiamine kinase [Pectobacterium quasiaquaticum]

Protein Classification

thiamine kinase( domain architecture ID 10021450)

thiamine kinase catalyzes the phosphorylation of thiamine to thiamine phosphate

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ycfN_thiK TIGR02721
thiamine kinase; Members of this family are the ycfN gene product of Escherichia coli, now ...
33-289 7.98e-122

thiamine kinase; Members of this family are the ycfN gene product of Escherichia coli, now identified as the salvage enzyme thiamine kinase (thiK), and additional proteobacterial homologs taken to be orthologs with equivalent function. [Biosynthesis of cofactors, prosthetic groups, and carriers, Thiamine]


:

Pssm-ID: 274268 [Multi-domain]  Cd Length: 256  Bit Score: 349.00  E-value: 7.98e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919638952  33 FELVGGLSSKSWRIRGPDIEWLARRQSPTERKMGVDRQREFALLRQMSAIGLAPQPRLWRDDWLIVEWVPGRIATQDEFL 112
Cdd:TIGR02721   2 QTLSGGLTNRSWRIEHPGISFVWRPQSPVCKALGVDRQREYQILQALSALGLAPKPILVNEHWLLVEWLEGEVITLDQFV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919638952 113 MMLANGEVARLLSQLHRQPRSGHPLDLKVLFAQHWQLMDPRRRSPALLRAHHYFQRAALPTPLALAPLHLDVHAENLLIT 192
Cdd:TIGR02721  82 ALDLLLELAALLHQLHSQPRFGYPLSLKARIAHYWLQIDPARRTPEWLRLYKQFRSAPEPAPLPLAPLHMDVHAYNLVVT 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919638952 193 PQETMLIDWEYASDGDIAFELAFIVRASQMEslAQTHFLQSYQRHRRGFSVSRLQQQMMQWFPWVDYLVLMWFEVRWQQT 272
Cdd:TIGR02721 162 PQGLKLIDWEYASDGDIALELAAIIRANDEE--QQQDFVQRYCQRRRIYSISVLWRQVKAWQPWVDYMAALWFELRWQQT 239
                         250
                  ....*....|....*..
gi 1919638952 273 KNPEFLADIPTLYHRLQ 289
Cdd:TIGR02721 240 GDPQFLELAQELRHRLC 256
 
Name Accession Description Interval E-value
ycfN_thiK TIGR02721
thiamine kinase; Members of this family are the ycfN gene product of Escherichia coli, now ...
33-289 7.98e-122

thiamine kinase; Members of this family are the ycfN gene product of Escherichia coli, now identified as the salvage enzyme thiamine kinase (thiK), and additional proteobacterial homologs taken to be orthologs with equivalent function. [Biosynthesis of cofactors, prosthetic groups, and carriers, Thiamine]


Pssm-ID: 274268 [Multi-domain]  Cd Length: 256  Bit Score: 349.00  E-value: 7.98e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919638952  33 FELVGGLSSKSWRIRGPDIEWLARRQSPTERKMGVDRQREFALLRQMSAIGLAPQPRLWRDDWLIVEWVPGRIATQDEFL 112
Cdd:TIGR02721   2 QTLSGGLTNRSWRIEHPGISFVWRPQSPVCKALGVDRQREYQILQALSALGLAPKPILVNEHWLLVEWLEGEVITLDQFV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919638952 113 MMLANGEVARLLSQLHRQPRSGHPLDLKVLFAQHWQLMDPRRRSPALLRAHHYFQRAALPTPLALAPLHLDVHAENLLIT 192
Cdd:TIGR02721  82 ALDLLLELAALLHQLHSQPRFGYPLSLKARIAHYWLQIDPARRTPEWLRLYKQFRSAPEPAPLPLAPLHMDVHAYNLVVT 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919638952 193 PQETMLIDWEYASDGDIAFELAFIVRASQMEslAQTHFLQSYQRHRRGFSVSRLQQQMMQWFPWVDYLVLMWFEVRWQQT 272
Cdd:TIGR02721 162 PQGLKLIDWEYASDGDIALELAAIIRANDEE--QQQDFVQRYCQRRRIYSISVLWRQVKAWQPWVDYMAALWFELRWQQT 239
                         250
                  ....*....|....*..
gi 1919638952 273 KNPEFLADIPTLYHRLQ 289
Cdd:TIGR02721 240 GDPQFLELAQELRHRLC 256
thiK PRK10271
thiamine kinase; Provisional
96-280 3.62e-39

thiamine kinase; Provisional


Pssm-ID: 182349  Cd Length: 188  Bit Score: 135.65  E-value: 3.62e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919638952  96 LIVEWVPGRIATQdeflmMLANGEVARLLSQLHRQPRSGHPLDLKVLFAQHWQLMDPRRRSPALLRAHHYFQRAALPTPL 175
Cdd:PRK10271    1 MAVDYLPGEVKSY-----LPDTNELAGLLYHLHQQPRFGWRITLLPLLEQYWQQSDPARRTPFWLRMLKRLRKAGEPRPL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919638952 176 ALAPLHLDVHAENLLITPQETMLIDWEYASDGDIAFELAfivrASQMESLAQTHFLQSYQRHRRGFSVSRLQQQMMQWFP 255
Cdd:PRK10271   76 RLAPLHMDVHAGNLVHSASGLRLIDWEYAGDGDIALELA----AVWVENTEQHRQLVNDYATRAKIDAAQLWRQVRRWFP 151
                         170       180
                  ....*....|....*....|....*..
gi 1919638952 256 WVDYLVLMWFEVRWQQTKNPEF--LAD 280
Cdd:PRK10271  152 WVLMLKAGWFEYRWRQTGDQQFirLAD 178
CotS COG0510
Thiamine kinase or a related kinase [Coenzyme transport and metabolism];
126-271 1.17e-27

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


Pssm-ID: 440276 [Multi-domain]  Cd Length: 156  Bit Score: 104.86  E-value: 1.17e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919638952 126 QLHRQPRSGhPLDLKVLFAQHWQlmDPRRRSPALLRAHHYFQRAALPTPLALAPLHLDVHAENLLITPQETM-LIDWEYA 204
Cdd:COG0510     1 RLHASPALL-RFDLFARLERYLA--LGPRDLPELLRRLEELERALAARPLPLVLCHGDLHPGNFLVTDDGRLyLIDWEYA 77
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1919638952 205 SDGDIAFELAFIVRASQMESLAQTHFLQSYQRHRRgfsVSRLQQQMMQWFPWVDYLVLMWFEVRWQQ 271
Cdd:COG0510    78 GLGDPAFDLAALLVEYGLSPEQAEELLEAYGFGRP---TEELLRRLRAYRALADLLWALWALVRAAQ 141
ChoK-like cd05151
Choline Kinase and similar proteins; This subfamily is composed of bacterial and eukaryotic ...
33-214 4.47e-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: 97.63  E-value: 4.47e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919638952  33 FELVGGLSSKSWRIRGPDIEWLARRQSPTErKMGVDRQREFALLRQMSAIGLAPQPRLWRDD--WLIVEWVPGRIATQDE 110
Cdd:cd05151     4 EPLKGGLTNKNYLVEVAGKKYVLRIPGAGT-ELLIDRENEKANSKAAAELGIAPEVIYFDPEtgVKITEFIEGATLLTND 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919638952 111 FL--MMLAngEVARLLSQLHRQPrsghpldlkvlfaqhwqlmdprrrspallrahhyfqraalptPLALAPLHLDVHAEN 188
Cdd:cd05151    83 FSdpENLE--RIAALLRKLHSSP------------------------------------------LEDLVLCHNDLVPGN 118
                         170       180
                  ....*....|....*....|....*.
gi 1919638952 189 LLITPQETMLIDWEYASDGDIAFELA 214
Cdd:cd05151   119 FLLDDDRLYLIDWEYAGMNDPLFDLA 144
APH pfam01636
Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance ...
37-236 3.67e-14

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: 70.22  E-value: 3.67e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919638952  37 GGLSSKSWRIRGPDIEWLARRQSPTERKmgVDRQREFALLRQMSAIGL--APQPRLWRDD-------WLIVEWVPGRIAT 107
Cdd:pfam01636   7 SGASNRTYLVTTGDGRYVLRLPPPGRAA--EELRRELALLRHLAAAGVppVPRVLAGCTDaellglpFLLMEYLPGEVLA 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919638952 108 QDEFLMMLAN--GEVARLLSQLHRQPRSGHPLD--LKVLFAQHWQLMDPRRRS---------PALLRAHHYFQRAALPTP 174
Cdd:pfam01636  85 RPLLPEERGAllEALGRALARLHAVDPAALPLAgrLARLLELLRQLEAALARLlaaelldrlEELEERLLAALLALLPAE 164
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1919638952 175 LALAPLHLDVHAENLLITPQE--TMLIDWEYASDGDIAFELAFIVRASQMEslAQTHFLQSYQR 236
Cdd:pfam01636 165 LPPVLVHGDLHPGNLLVDPGGrvSGVIDFEDAGLGDPAYDLAILLNSWGRE--LGAELLAAYLA 226
 
Name Accession Description Interval E-value
ycfN_thiK TIGR02721
thiamine kinase; Members of this family are the ycfN gene product of Escherichia coli, now ...
33-289 7.98e-122

thiamine kinase; Members of this family are the ycfN gene product of Escherichia coli, now identified as the salvage enzyme thiamine kinase (thiK), and additional proteobacterial homologs taken to be orthologs with equivalent function. [Biosynthesis of cofactors, prosthetic groups, and carriers, Thiamine]


Pssm-ID: 274268 [Multi-domain]  Cd Length: 256  Bit Score: 349.00  E-value: 7.98e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919638952  33 FELVGGLSSKSWRIRGPDIEWLARRQSPTERKMGVDRQREFALLRQMSAIGLAPQPRLWRDDWLIVEWVPGRIATQDEFL 112
Cdd:TIGR02721   2 QTLSGGLTNRSWRIEHPGISFVWRPQSPVCKALGVDRQREYQILQALSALGLAPKPILVNEHWLLVEWLEGEVITLDQFV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919638952 113 MMLANGEVARLLSQLHRQPRSGHPLDLKVLFAQHWQLMDPRRRSPALLRAHHYFQRAALPTPLALAPLHLDVHAENLLIT 192
Cdd:TIGR02721  82 ALDLLLELAALLHQLHSQPRFGYPLSLKARIAHYWLQIDPARRTPEWLRLYKQFRSAPEPAPLPLAPLHMDVHAYNLVVT 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919638952 193 PQETMLIDWEYASDGDIAFELAFIVRASQMEslAQTHFLQSYQRHRRGFSVSRLQQQMMQWFPWVDYLVLMWFEVRWQQT 272
Cdd:TIGR02721 162 PQGLKLIDWEYASDGDIALELAAIIRANDEE--QQQDFVQRYCQRRRIYSISVLWRQVKAWQPWVDYMAALWFELRWQQT 239
                         250
                  ....*....|....*..
gi 1919638952 273 KNPEFLADIPTLYHRLQ 289
Cdd:TIGR02721 240 GDPQFLELAQELRHRLC 256
thiK PRK10271
thiamine kinase; Provisional
96-280 3.62e-39

thiamine kinase; Provisional


Pssm-ID: 182349  Cd Length: 188  Bit Score: 135.65  E-value: 3.62e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919638952  96 LIVEWVPGRIATQdeflmMLANGEVARLLSQLHRQPRSGHPLDLKVLFAQHWQLMDPRRRSPALLRAHHYFQRAALPTPL 175
Cdd:PRK10271    1 MAVDYLPGEVKSY-----LPDTNELAGLLYHLHQQPRFGWRITLLPLLEQYWQQSDPARRTPFWLRMLKRLRKAGEPRPL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919638952 176 ALAPLHLDVHAENLLITPQETMLIDWEYASDGDIAFELAfivrASQMESLAQTHFLQSYQRHRRGFSVSRLQQQMMQWFP 255
Cdd:PRK10271   76 RLAPLHMDVHAGNLVHSASGLRLIDWEYAGDGDIALELA----AVWVENTEQHRQLVNDYATRAKIDAAQLWRQVRRWFP 151
                         170       180
                  ....*....|....*....|....*..
gi 1919638952 256 WVDYLVLMWFEVRWQQTKNPEF--LAD 280
Cdd:PRK10271  152 WVLMLKAGWFEYRWRQTGDQQFirLAD 178
CotS COG0510
Thiamine kinase or a related kinase [Coenzyme transport and metabolism];
126-271 1.17e-27

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


Pssm-ID: 440276 [Multi-domain]  Cd Length: 156  Bit Score: 104.86  E-value: 1.17e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919638952 126 QLHRQPRSGhPLDLKVLFAQHWQlmDPRRRSPALLRAHHYFQRAALPTPLALAPLHLDVHAENLLITPQETM-LIDWEYA 204
Cdd:COG0510     1 RLHASPALL-RFDLFARLERYLA--LGPRDLPELLRRLEELERALAARPLPLVLCHGDLHPGNFLVTDDGRLyLIDWEYA 77
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1919638952 205 SDGDIAFELAFIVRASQMESLAQTHFLQSYQRHRRgfsVSRLQQQMMQWFPWVDYLVLMWFEVRWQQ 271
Cdd:COG0510    78 GLGDPAFDLAALLVEYGLSPEQAEELLEAYGFGRP---TEELLRRLRAYRALADLLWALWALVRAAQ 141
ChoK-like cd05151
Choline Kinase and similar proteins; This subfamily is composed of bacterial and eukaryotic ...
33-214 4.47e-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: 97.63  E-value: 4.47e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919638952  33 FELVGGLSSKSWRIRGPDIEWLARRQSPTErKMGVDRQREFALLRQMSAIGLAPQPRLWRDD--WLIVEWVPGRIATQDE 110
Cdd:cd05151     4 EPLKGGLTNKNYLVEVAGKKYVLRIPGAGT-ELLIDRENEKANSKAAAELGIAPEVIYFDPEtgVKITEFIEGATLLTND 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919638952 111 FL--MMLAngEVARLLSQLHRQPrsghpldlkvlfaqhwqlmdprrrspallrahhyfqraalptPLALAPLHLDVHAEN 188
Cdd:cd05151    83 FSdpENLE--RIAALLRKLHSSP------------------------------------------LEDLVLCHNDLVPGN 118
                         170       180
                  ....*....|....*....|....*.
gi 1919638952 189 LLITPQETMLIDWEYASDGDIAFELA 214
Cdd:cd05151   119 FLLDDDRLYLIDWEYAGMNDPLFDLA 144
APH pfam01636
Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance ...
37-236 3.67e-14

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: 70.22  E-value: 3.67e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919638952  37 GGLSSKSWRIRGPDIEWLARRQSPTERKmgVDRQREFALLRQMSAIGL--APQPRLWRDD-------WLIVEWVPGRIAT 107
Cdd:pfam01636   7 SGASNRTYLVTTGDGRYVLRLPPPGRAA--EELRRELALLRHLAAAGVppVPRVLAGCTDaellglpFLLMEYLPGEVLA 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919638952 108 QDEFLMMLAN--GEVARLLSQLHRQPRSGHPLD--LKVLFAQHWQLMDPRRRS---------PALLRAHHYFQRAALPTP 174
Cdd:pfam01636  85 RPLLPEERGAllEALGRALARLHAVDPAALPLAgrLARLLELLRQLEAALARLlaaelldrlEELEERLLAALLALLPAE 164
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1919638952 175 LALAPLHLDVHAENLLITPQE--TMLIDWEYASDGDIAFELAFIVRASQMEslAQTHFLQSYQR 236
Cdd:pfam01636 165 LPPVLVHGDLHPGNLLVDPGGrvSGVIDFEDAGLGDPAYDLAILLNSWGRE--LGAELLAAYLA 226
YcbJ COG3173
Predicted kinase, aminoglycoside phosphotransferase (APT) family [General function prediction ...
12-242 1.04e-13

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


Pssm-ID: 442406 [Multi-domain]  Cd Length: 284  Bit Score: 69.76  E-value: 1.04e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919638952  12 QQQLTATIQKHFP-TVEMADIRfELVGGLSSKSWRIRGPDiEWLARRQsPTERKMGVDRQREFALLRQMSAIG--LAPQP 88
Cdd:COG3173     5 EAALRALLAAQLPgLAGLPEVE-PLSGGWSNLTYRLDTGD-RLVLRRP-PRGLASAHDVRREARVLRALAPRLgvPVPRP 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919638952  89 RLWRDD-------WLIVEWVPGRIATQDEFLMMLANG-----EVARLLSQLHRQPRSGHPLDLKVLFAQHWQL------- 149
Cdd:COG3173    82 LALGEDgevigapFYVMEWVEGETLEDALPDLSPAERralarALGEFLAALHAVDPAAAGLADGRPEGLERQLarwraql 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919638952 150 ---MDPRRRSPALLRAHHYFQRAALPTPLALAPLHLDVHAENLLITPQE---TMLIDWEYASDGDIAFELAFIVRASQME 223
Cdd:COG3173   162 rraLARTDDLPALRERLAAWLAANLPEWGPPVLVHGDLRPGNLLVDPDDgrlTAVIDWELATLGDPAADLAYLLLYWRLP 241
                         250       260
                  ....*....|....*....|..
gi 1919638952 224 SL---AQTHFLQSYQRHRRGFS 242
Cdd:COG3173   242 DDllgPRAAFLAAYEEATGDLD 263
SrkA COG2334
Ser/Thr protein kinase RdoA involved in Cpx stress response, MazF antagonist [Signal ...
72-238 6.37e-08

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: 53.01  E-value: 6.37e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919638952  72 EFALLRQMSAIGLA-PQPRLWRDD----------WLIVEWVPGRIATQDEFLMMlanGEVARLLSQLHR--------QPR 132
Cdd:COG2334    57 ELALLAHLAAAGLPvPAPVPTRDGetllelegrpAALFPFLPGRSPEEPSPEQL---EELGRLLARLHRaladfprpNAR 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919638952 133 SGHPLDLKVLFAQHWQLMDPRRRspALLRAHHYFQRAAL---PTPLALAPLHLDVHAENLLITPQE-TMLIDWEYASDGD 208
Cdd:COG2334   134 DLAWWDELLERLLGPLLPDPEDR--ALLEELLDRLEARLaplLGALPRGVIHGDLHPDNVLFDGDGvSGLIDFDDAGYGP 211
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1919638952 209 IAFELAFIVRASQMESLAQT---HFLQSYQRHR 238
Cdd:COG2334   212 RLYDLAIALNGWADGPLDPArlaALLEGYRAVR 244
APH_ChoK_like cd05120
Aminoglycoside 3'-phosphotransferase and Choline Kinase family; This family is composed of APH, ...
30-218 9.19e-08

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: 50.76  E-value: 9.19e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919638952  30 DIRFELVGGLSSKSWRIRGPDiEWLARRQSPTERKmgvDRQREFALLRQMSAIGLAPQPRL---WRDD---WLIVEWVPG 103
Cdd:cd05120     1 ISVKLIKEGGDNKVYLLGDPR-EYVLKIGPPRLKK---DLEKEAAMLQLLAGKLSLPVPKVygfGESDgweYLLMERIEG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919638952 104 RIATQDEFLMMLAN-----GEVARLLSQLHRqprsghpLDLKVLFaqhwqlmdprrrspallrahhyfqraalptplala 178
Cdd:cd05120    77 ETLSEVWPRLSEEEkekiaDQLAEILAALHR-------IDSSVLT----------------------------------- 114
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1919638952 179 plHLDVHAENLLITPQE--TMLIDWEYASDGDIAFELAFIVR 218
Cdd:cd05120   115 --HGDLHPGNILVKPDGklSGIIDWEFAGYGPPAFDYAAALR 154
HomoserineK_II cd05153
Type II Homoserine Kinase; This subfamily is composed of unusual homoserine kinases, from a ...
97-239 3.46e-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: 50.72  E-value: 3.46e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919638952  97 IVEWVPGRIATQDEFLMMlanGEVARLLSQLHR-----QPRSGHPLDL---KVLFAQHWQLMDPRRRSP-ALLRAHHYFQ 167
Cdd:cd05153    93 LFPFLPGESLTTPTPEQC---RAIGAALARLHLalagfPPPRPNPRGLawwKPLAERLKARLDLLAADDrALLEDELARL 169
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919638952 168 RAALPTPLALAPLHLDVHAENLLITPQE-TMLIDWEYASDGDIAFELA-------FIVRASQMESLAQThFLQSYQRHRR 239
Cdd:cd05153   170 QALAPSDLPRGVIHADLFRDNVLFDGDRlSGIIDFYDACYDPLLYDLAialndwcFDDDGKLDPERAKA-LLAGYQSVRP 248
ACAD10_11_N-like cd05154
N-terminal domain of Acyl-CoA dehydrogenase (ACAD) 10 and 11, and similar proteins; This ...
35-208 6.15e-07

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: 49.54  E-value: 6.15e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919638952  35 LVGGLSSKSWRIR----GPDIEWLARRQSPTERKMGV-DRQREFALLRQMSAIGL-APQPRLWRDD-------WLIVEWV 101
Cdd:cd05154     6 LSGGASNETYLVDaggdGGGRRLVLRRPPPGGLLPSAhDLEREYRVLRALAGTGVpVPRVLALCEDpsvlgapFYVMERV 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919638952 102 PGRIATQDEFLMMLANGEVARL-------LSQLHR----------QPRSGHPLDLKV-LFAQHWQLMDPRRRsPALLRAH 163
Cdd:cd05154    86 DGRVLPDPLPRPDLSPEERRALarslvdaLAALHSvdpaalgladLGRPEGYLERQVdRWRRQLEAAATDPP-PALEEAL 164
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1919638952 164 HYFqRAALPTPLALAPLHLDVHAENLLITPQE--TMLIDWEYASDGD 208
Cdd:cd05154   165 RWL-RANLPADGRPVLVHGDFRLGNLLFDPDGrvTAVLDWELATLGD 210
ChoK-like_euk cd14021
Euykaryotic Choline Kinase and similar proteins; This group is composed of eukaryotic choline ...
56-214 8.10e-07

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: 48.80  E-value: 8.10e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919638952  56 RRQSPTERKMgVDRQREFALLRQMSAIGLAPQPRLWRDDWLIVEWVPGRIATQDEFLMMLANGEVARLLSQLHRQPRsgh 135
Cdd:cd14021    34 RIYGKYLSTL-YDREKESEVFKILSEQGLGPKLIYKFDGGRIEEYIDGRPLTTDELRNPSVLTSIAKLLAKFHKIKT--- 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919638952 136 pldLKVLFAqhwqlmdprrrspallrahhyfqraalptplalaplHLDVHAENLLITPQET--MLIDWEYASDGDIAFEL 213
Cdd:cd14021   110 ---PPVVFC------------------------------------HNDLQENNILLTNDQDglRLIDFEYSGFNYRGYDI 150

                  .
gi 1919638952 214 A 214
Cdd:cd14021   151 A 151
APH_ChoK_like_1 cd05155
Uncharacterized bacterial proteins with similarity to Aminoglycoside 3'-phosphotransferase and ...
95-214 8.34e-04

Uncharacterized bacterial proteins with similarity to Aminoglycoside 3'-phosphotransferase and Choline kinase; This subfamily is composed of uncharacterized bacterial proteins with similarity to APH and ChoK. Other APH/ChoK-like proteins include 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). These proteins 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-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: 270704 [Multi-domain]  Cd Length: 234  Bit Score: 39.91  E-value: 8.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919638952  95 WLIVEWVPGRIAT--QDEFLMMLAnGEVARLLSQLHR-------QPRSGHPLDLKVLfaqhwqlmDPRRRSPALLRAHHY 165
Cdd:cd05155    70 WSVYRWLEGETAAdaPLADPAAAA-EDLARFLAALHAidpagppNPGRGNPLRGRDL--------AVRDAEEALAALAGL 140
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1919638952 166 FQRA--------ALPTPLALAP---LHLDVHAENLLITPQE-TMLIDWEYASDGDIAFELA 214
Cdd:cd05155   141 LDVAaaralwerALAAPAWAGPpvwLHGDLHPGNLLVRDGRlSAVIDFGDLGVGDPACDLA 201
Choline_kinase pfam01633
Choline/ethanolamine kinase; Choline kinase catalyzes the committed step in the synthesis of ...
45-214 1.01e-03

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: 39.56  E-value: 1.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919638952  45 RIRGPDIEWLarrqspterkmgVDRQREFALLRQMSAIGLAPQPRLWRDDWLIVEWVPGRIATQDEFLMMLANGEVARLL 124
Cdd:pfam01633   8 RIYGPGTELL------------INREDEIVNFALLSERGLGPKLYGFFPNGRIEEFIPSRTLSTEDLRDPEISKLIAKRL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919638952 125 SQLHrqprSGHPLDLKVLFAqhWQLMdprRRSPALLRAHhyFQRAALPTPLAL-----------------------APL- 180
Cdd:pfam01633  76 AELH----SLEMPGKKSPSL--WKTM---RKWLSLLKNL--GAPESVNKSEQLksinledlekeinklekwlelldSPIv 144
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1919638952 181 --HLDVHAENLLITPQ--ETMLIDWEYASDGDIAFELA 214
Cdd:pfam01633 145 fcHNDLQSGNILLLNEtkRLVLIDFEYASYNYRGFDIA 182
 
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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