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Conserved domains on  [gi|489938539|ref|WP_003841846|]
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MULTISPECIES: thiamine kinase [Citrobacter]

Protein Classification

thiamine kinase( domain architecture ID 10013473)

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
thiK PRK10271
thiamine kinase; Provisional
87-274 8.23e-118

thiamine kinase; Provisional


:

Pssm-ID: 182349  Cd Length: 188  Bit Score: 335.18  E-value: 8.23e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489938539  87 MAVEFFHGKVESRLPDADELAGLLYHLHQQPRLGWRISLLPLLEQYWQCGDPARRTPCWLRALKRLRKRGEPRPLRLGPL 166
Cdd:PRK10271   1 MAVDYLPGEVKSYLPDTNELAGLLYHLHQQPRFGWRITLLPLLEQYWQQSDPARRTPFWLRMLKRLRKAGEPRPLRLAPL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489938539 167 HMDVHGDNIVRTASGLRLIDWEYAGDGDIALELAAVWVSDESQHQQLVSTYAQRAHIEPDVLWRQVRQWQPWIMMLKAGW 246
Cdd:PRK10271  81 HMDVHAGNLVHSASGLRLIDWEYAGDGDIALELAAVWVENTEQHRQLVNDYATRAKIDAAQLWRQVRRWFPWVLMLKAGW 160
                        170       180
                 ....*....|....*....|....*...
gi 489938539 247 FEYRWRQTGDRQFIRLADETWRQLTMKG 274
Cdd:PRK10271 161 FEYRWRQTGDQQFIRLADDTWRQLLIKQ 188
 
Name Accession Description Interval E-value
thiK PRK10271
thiamine kinase; Provisional
87-274 8.23e-118

thiamine kinase; Provisional


Pssm-ID: 182349  Cd Length: 188  Bit Score: 335.18  E-value: 8.23e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489938539  87 MAVEFFHGKVESRLPDADELAGLLYHLHQQPRLGWRISLLPLLEQYWQCGDPARRTPCWLRALKRLRKRGEPRPLRLGPL 166
Cdd:PRK10271   1 MAVDYLPGEVKSYLPDTNELAGLLYHLHQQPRFGWRITLLPLLEQYWQQSDPARRTPFWLRMLKRLRKAGEPRPLRLAPL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489938539 167 HMDVHGDNIVRTASGLRLIDWEYAGDGDIALELAAVWVSDESQHQQLVSTYAQRAHIEPDVLWRQVRQWQPWIMMLKAGW 246
Cdd:PRK10271  81 HMDVHAGNLVHSASGLRLIDWEYAGDGDIALELAAVWVENTEQHRQLVNDYATRAKIDAAQLWRQVRRWFPWVLMLKAGW 160
                        170       180
                 ....*....|....*....|....*...
gi 489938539 247 FEYRWRQTGDRQFIRLADETWRQLTMKG 274
Cdd:PRK10271 161 FEYRWRQTGDQQFIRLADDTWRQLLIKQ 188
ycfN_thiK TIGR02721
thiamine kinase; Members of this family are the ycfN gene product of Escherichia coli, now ...
31-270 3.06e-110

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: 318.57  E-value: 3.06e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489938539   31 GLSGGSCIIEHHSHRLVLRCHHDPDAPES-HFLRQYHALKHLP-ENLAPRPHFYTRGWMAVEFFHGKVESR-----LPDA 103
Cdd:TIGR02721   7 GLTNRSWRIEHPGISFVWRPQSPVCKALGvDRQREYQILQALSaLGLAPKPILVNEHWLLVEWLEGEVITLdqfvaLDLL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489938539  104 DELAGLLYHLHQQPRLGWRISLLPLLEQYWQCGDPARRTPCWLRALKRLRKRGEPRPLRLGPLHMDVHGDNIVRTASGLR 183
Cdd:TIGR02721  87 LELAALLHQLHSQPRFGYPLSLKARIAHYWLQIDPARRTPEWLRLYKQFRSAPEPAPLPLAPLHMDVHAYNLVVTPQGLK 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489938539  184 LIDWEYAGDGDIALELAAVWV-SDESQHQQLVSTYAQRAHIEP-DVLWRQVRQWQPWIMMLKAGWFEYRWRQTGDRQFIR 261
Cdd:TIGR02721 167 LIDWEYASDGDIALELAAIIRaNDEEQQQDFVQRYCQRRRIYSiSVLWRQVKAWQPWVDYMAALWFELRWQQTGDPQFLE 246

                  ....*....
gi 489938539  262 LADETWRQL 270
Cdd:TIGR02721 247 LAQELRHRL 255
CotS COG0510
Thiamine kinase or a related kinase [Coenzyme transport and metabolism];
112-253 2.82e-31

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


Pssm-ID: 440276 [Multi-domain]  Cd Length: 156  Bit Score: 113.72  E-value: 2.82e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489938539 112 HLHQQPRLGwRISLLPLLEQYWQcgDPARRTPCWLRALKRLRKRGEPRPLRLGPLHMDVHGDNIVRTASG-LRLIDWEYA 190
Cdd:COG0510    1 RLHASPALL-RFDLFARLERYLA--LGPRDLPELLRRLEELERALAARPLPLVLCHGDLHPGNFLVTDDGrLYLIDWEYA 77
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489938539 191 GDGDIALELAAVWVS---DESQHQQLVSTYAQRAHiePDVLWRQVRQWQPWIMMLKAGWFEYRWRQ 253
Cdd:COG0510   78 GLGDPAFDLAALLVEyglSPEQAEELLEAYGFGRP--TEELLRRLRAYRALADLLWALWALVRAAQ 141
ChoK-like cd05151
Choline Kinase and similar proteins; This subfamily is composed of bacterial and eukaryotic ...
32-202 8.97e-12

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: 61.42  E-value: 8.97e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489938539  32 LSGG----SCIIEHHSHRLVLRChhdPDAPESHFL-RQ--YHALKHL-PENLAPRPHFY--TRGWMAVEFFHGK-----V 96
Cdd:cd05151    6 LKGGltnkNYLVEVAGKKYVLRI---PGAGTELLIdREneKANSKAAaELGIAPEVIYFdpETGVKITEFIEGAtlltnD 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489938539  97 ESRLPDADELAGLLYHLHQQPrlgwrisLLPLleqywqcgdparrTPCwlralkrlrkrgeprplrlgplHMDVHGDNIV 176
Cdd:cd05151   83 FSDPENLERIAALLRKLHSSP-------LEDL-------------VLC----------------------HNDLVPGNFL 120
                        170       180
                 ....*....|....*....|....*.
gi 489938539 177 RTASGLRLIDWEYAGDGDIALELAAV 202
Cdd:cd05151  121 LDDDRLYLIDWEYAGMNDPLFDLAAL 146
APH pfam01636
Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance ...
45-205 2.50e-07

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: 50.58  E-value: 2.50e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489938539   45 RLVLRCHHDPDAPES--HFLRQYHALKHLPENLAPRPHFYT-------RGWMAVEFFHGKVESRLPD-------ADELAG 108
Cdd:pfam01636  22 RYVLRLPPPGRAAEElrRELALLRHLAAAGVPPVPRVLAGCtdaellgLPFLLMEYLPGEVLARPLLpeergalLEALGR 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489938539  109 LLYHLHQQP--------RLGWRISLLPLLEQYWQCGDPA----RRTPCWLRALKRLRKRGePRPLRLGPLHMDVHGDNIV 176
Cdd:pfam01636 102 ALARLHAVDpaalplagRLARLLELLRQLEAALARLLAAelldRLEELEERLLAALLALL-PAELPPVLVHGDLHPGNLL 180
                         170       180       190
                  ....*....|....*....|....*....|.
gi 489938539  177 RTASG--LRLIDWEYAGDGDIALELAAVWVS 205
Cdd:pfam01636 181 VDPGGrvSGVIDFEDAGLGDPAYDLAILLNS 211
 
Name Accession Description Interval E-value
thiK PRK10271
thiamine kinase; Provisional
87-274 8.23e-118

thiamine kinase; Provisional


Pssm-ID: 182349  Cd Length: 188  Bit Score: 335.18  E-value: 8.23e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489938539  87 MAVEFFHGKVESRLPDADELAGLLYHLHQQPRLGWRISLLPLLEQYWQCGDPARRTPCWLRALKRLRKRGEPRPLRLGPL 166
Cdd:PRK10271   1 MAVDYLPGEVKSYLPDTNELAGLLYHLHQQPRFGWRITLLPLLEQYWQQSDPARRTPFWLRMLKRLRKAGEPRPLRLAPL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489938539 167 HMDVHGDNIVRTASGLRLIDWEYAGDGDIALELAAVWVSDESQHQQLVSTYAQRAHIEPDVLWRQVRQWQPWIMMLKAGW 246
Cdd:PRK10271  81 HMDVHAGNLVHSASGLRLIDWEYAGDGDIALELAAVWVENTEQHRQLVNDYATRAKIDAAQLWRQVRRWFPWVLMLKAGW 160
                        170       180
                 ....*....|....*....|....*...
gi 489938539 247 FEYRWRQTGDRQFIRLADETWRQLTMKG 274
Cdd:PRK10271 161 FEYRWRQTGDQQFIRLADDTWRQLLIKQ 188
ycfN_thiK TIGR02721
thiamine kinase; Members of this family are the ycfN gene product of Escherichia coli, now ...
31-270 3.06e-110

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: 318.57  E-value: 3.06e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489938539   31 GLSGGSCIIEHHSHRLVLRCHHDPDAPES-HFLRQYHALKHLP-ENLAPRPHFYTRGWMAVEFFHGKVESR-----LPDA 103
Cdd:TIGR02721   7 GLTNRSWRIEHPGISFVWRPQSPVCKALGvDRQREYQILQALSaLGLAPKPILVNEHWLLVEWLEGEVITLdqfvaLDLL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489938539  104 DELAGLLYHLHQQPRLGWRISLLPLLEQYWQCGDPARRTPCWLRALKRLRKRGEPRPLRLGPLHMDVHGDNIVRTASGLR 183
Cdd:TIGR02721  87 LELAALLHQLHSQPRFGYPLSLKARIAHYWLQIDPARRTPEWLRLYKQFRSAPEPAPLPLAPLHMDVHAYNLVVTPQGLK 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489938539  184 LIDWEYAGDGDIALELAAVWV-SDESQHQQLVSTYAQRAHIEP-DVLWRQVRQWQPWIMMLKAGWFEYRWRQTGDRQFIR 261
Cdd:TIGR02721 167 LIDWEYASDGDIALELAAIIRaNDEEQQQDFVQRYCQRRRIYSiSVLWRQVKAWQPWVDYMAALWFELRWQQTGDPQFLE 246

                  ....*....
gi 489938539  262 LADETWRQL 270
Cdd:TIGR02721 247 LAQELRHRL 255
CotS COG0510
Thiamine kinase or a related kinase [Coenzyme transport and metabolism];
112-253 2.82e-31

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


Pssm-ID: 440276 [Multi-domain]  Cd Length: 156  Bit Score: 113.72  E-value: 2.82e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489938539 112 HLHQQPRLGwRISLLPLLEQYWQcgDPARRTPCWLRALKRLRKRGEPRPLRLGPLHMDVHGDNIVRTASG-LRLIDWEYA 190
Cdd:COG0510    1 RLHASPALL-RFDLFARLERYLA--LGPRDLPELLRRLEELERALAARPLPLVLCHGDLHPGNFLVTDDGrLYLIDWEYA 77
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489938539 191 GDGDIALELAAVWVS---DESQHQQLVSTYAQRAHiePDVLWRQVRQWQPWIMMLKAGWFEYRWRQ 253
Cdd:COG0510   78 GLGDPAFDLAALLVEyglSPEQAEELLEAYGFGRP--TEELLRRLRAYRALADLLWALWALVRAAQ 141
ChoK-like cd05151
Choline Kinase and similar proteins; This subfamily is composed of bacterial and eukaryotic ...
32-202 8.97e-12

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: 61.42  E-value: 8.97e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489938539  32 LSGG----SCIIEHHSHRLVLRChhdPDAPESHFL-RQ--YHALKHL-PENLAPRPHFY--TRGWMAVEFFHGK-----V 96
Cdd:cd05151    6 LKGGltnkNYLVEVAGKKYVLRI---PGAGTELLIdREneKANSKAAaELGIAPEVIYFdpETGVKITEFIEGAtlltnD 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489938539  97 ESRLPDADELAGLLYHLHQQPrlgwrisLLPLleqywqcgdparrTPCwlralkrlrkrgeprplrlgplHMDVHGDNIV 176
Cdd:cd05151   83 FSDPENLERIAALLRKLHSSP-------LEDL-------------VLC----------------------HNDLVPGNFL 120
                        170       180
                 ....*....|....*....|....*.
gi 489938539 177 RTASGLRLIDWEYAGDGDIALELAAV 202
Cdd:cd05151  121 LDDDRLYLIDWEYAGMNDPLFDLAAL 146
YcbJ COG3173
Predicted kinase, aminoglycoside phosphotransferase (APT) family [General function prediction ...
45-229 1.87e-08

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


Pssm-ID: 442406 [Multi-domain]  Cd Length: 284  Bit Score: 53.97  E-value: 1.87e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489938539  45 RLVLRCHHDPDAPESHFLRQYHALKHLPENL---APRPHFYT-------RGWMAVEFFHGKV-ESRLPD---------AD 104
Cdd:COG3173   44 RLVLRRPPRGLASAHDVRREARVLRALAPRLgvpVPRPLALGedgevigAPFYVMEWVEGETlEDALPDlspaerralAR 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489938539 105 ELAGLLYHLHQQP----------RLGWRISLLPLLEQYWQCGDPARRTPCWLRALKRLRKRGEPRPLRLGPLHMDVHGDN 174
Cdd:COG3173  124 ALGEFLAALHAVDpaaagladgrPEGLERQLARWRAQLRRALARTDDLPALRERLAAWLAANLPEWGPPVLVHGDLRPGN 203
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489938539 175 IVRTASGLRL---IDWEYAGDGDIALELA---AVWVSDE---SQHQQLVSTYAQRAHIEPDVLW 229
Cdd:COG3173  204 LLVDPDDGRLtavIDWELATLGDPAADLAyllLYWRLPDdllGPRAAFLAAYEEATGDLDDLTW 267
APH pfam01636
Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance ...
45-205 2.50e-07

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: 50.58  E-value: 2.50e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489938539   45 RLVLRCHHDPDAPES--HFLRQYHALKHLPENLAPRPHFYT-------RGWMAVEFFHGKVESRLPD-------ADELAG 108
Cdd:pfam01636  22 RYVLRLPPPGRAAEElrRELALLRHLAAAGVPPVPRVLAGCtdaellgLPFLLMEYLPGEVLARPLLpeergalLEALGR 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489938539  109 LLYHLHQQP--------RLGWRISLLPLLEQYWQCGDPA----RRTPCWLRALKRLRKRGePRPLRLGPLHMDVHGDNIV 176
Cdd:pfam01636 102 ALARLHAVDpaalplagRLARLLELLRQLEAALARLLAAelldRLEELEERLLAALLALL-PAELPPVLVHGDLHPGNLL 180
                         170       180       190
                  ....*....|....*....|....*....|.
gi 489938539  177 RTASG--LRLIDWEYAGDGDIALELAAVWVS 205
Cdd:pfam01636 181 VDPGGrvSGVIDFEDAGLGDPAYDLAILLNS 211
SrkA COG2334
Ser/Thr protein kinase RdoA involved in Cpx stress response, MazF antagonist [Signal ...
45-235 3.04e-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: 41.45  E-value: 3.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489938539  45 RLVLRCHHDPDAPESHFLRQYHALKHL--PENLAPRP----------HFYTRGWMAVEFFHGKVESRLPDAD--ELAGLL 110
Cdd:COG2334   38 RYVLKLYRPGRWSPEEIPFELALLAHLaaAGLPVPAPvptrdgetllELEGRPAALFPFLPGRSPEEPSPEQleELGRLL 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489938539 111 YHLHQQ----PRLGWRiSLLPLLEQYWQCGDPARRTPCWLRALKRLRKR------GEPRPLRLGPLHMDVHGDNI-VRTA 179
Cdd:COG2334  118 ARLHRAladfPRPNAR-DLAWWDELLERLLGPLLPDPEDRALLEELLDRlearlaPLLGALPRGVIHGDLHPDNVlFDGD 196
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489938539 180 SGLRLIDWEYAGDGDIALELAAV--WVSDESQHQQLVS------------TYAQRAHIEPDVLWRQVRQW 235
Cdd:COG2334  197 GVSGLIDFDDAGYGPRLYDLAIAlnGWADGPLDPARLAallegyravrplTEAELAALPPLLRLRALRFL 266
HomoserineK_II cd05153
Type II Homoserine Kinase; This subfamily is composed of unusual homoserine kinases, from a ...
119-246 2.03e-03

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: 38.78  E-value: 2.03e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489938539 119 LGWRISLLPLLEQYWQCGDPARRTpcWLRA-LKRLRKRgEPRPLRLGPLHMDVHGDNIVRTASGLR-LIDWEYAGDGDIA 196
Cdd:cd05153  137 LAWWKPLAERLKARLDLLAADDRA--LLEDeLARLQAL-APSDLPRGVIHADLFRDNVLFDGDRLSgIIDFYDACYDPLL 213
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 489938539 197 LELAAV---WVSDESQH------QQLVSTYAQRAHIEPDVLWRqvrqwqpWIMMLKAGW 246
Cdd:cd05153  214 YDLAIAlndWCFDDDGKldperaKALLAGYQSVRPLTEEEKAA-------LPLLLRAAA 265
PTZ00296 PTZ00296
choline kinase; Provisional
167-200 7.90e-03

choline kinase; Provisional


Pssm-ID: 240350 [Multi-domain]  Cd Length: 442  Bit Score: 37.56  E-value: 7.90e-03
                         10        20        30
                 ....*....|....*....|....*....|....
gi 489938539 167 HMDVHGDNIVRTASGLRLIDWEYAGDGDIALELA 200
Cdd:PTZ00296 288 HNDLQENNIINTNKCLRLIDFEYSGYNFLATDIA 321
 
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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