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Conserved domains on  [gi|490870618|ref|WP_004732633|]
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MULTISPECIES: hypothetical protein [Vibrio]

Protein Classification

nucleoside/nucleotide kinase family protein( domain architecture ID 106737)

nucleoside/nucleotide kinase family protein may catalyze the reversible phosphate group transfer from nucleoside triphosphates to nucleosides/nucleotides, nucleoside monophosphates, or sugars

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
NK super family cl17190
Nucleoside/nucleotide kinase (NK) is a protein superfamily consisting of multiple families of ...
20-216 2.60e-56

Nucleoside/nucleotide kinase (NK) is a protein superfamily consisting of multiple families of enzymes that share structural similarity and are functionally related to the catalysis of the reversible phosphate group transfer from nucleoside triphosphates to nucleosides/nucleotides, nucleoside monophosphates, or sugars. Members of this family play a wide variety of essential roles in nucleotide metabolism, the biosynthesis of coenzymes and aromatic compounds, as well as the metabolism of sugar and sulfate.


The actual alignment was detected with superfamily member PRK09270:

Pssm-ID: 450170  Cd Length: 229  Bit Score: 178.59  E-value: 2.60e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490870618  20 ANTYQESGKQVLViGISGAPATGKSTLSESLLSGLSQLGFKAQLC-PMDGFHYPNSVLKEKGLTSVKGSIETFDVTSLAH 98
Cdd:PRK09270  24 AALQAEPQRRTIV-GIAGPPGAGKSTLAEFLEALLQQDGELPAIQvPMDGFHLDNAVLDAHGLRPRKGAPETFDVAGLAA 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490870618  99 LLsEAVTPNTDAFFWPKYCRELHDPIVEGFLIEPDTQIILLEGNYIYSTDEDWRPVSDLIDLKIFLTASEEVLRERLISR 178
Cdd:PRK09270 103 LL-RRLRAGDDEVYWPVFDRSLEDPVADAIVVPPTARLVIVEGNYLLLDEEPWRRLAGLFDFTIFLDAPAEVLRERLVAR 181
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 490870618 179 HLAGGKSKQEALDKTERVDLVNALKIKQYESNADYVIQ 216
Cdd:PRK09270 182 KLAGGLSPEAAEAFVLRNDGPNARLVLETSRPADLVLE 219
 
Name Accession Description Interval E-value
PRK09270 PRK09270
nucleoside triphosphate hydrolase domain-containing protein; Reviewed
20-216 2.60e-56

nucleoside triphosphate hydrolase domain-containing protein; Reviewed


Pssm-ID: 236442  Cd Length: 229  Bit Score: 178.59  E-value: 2.60e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490870618  20 ANTYQESGKQVLViGISGAPATGKSTLSESLLSGLSQLGFKAQLC-PMDGFHYPNSVLKEKGLTSVKGSIETFDVTSLAH 98
Cdd:PRK09270  24 AALQAEPQRRTIV-GIAGPPGAGKSTLAEFLEALLQQDGELPAIQvPMDGFHLDNAVLDAHGLRPRKGAPETFDVAGLAA 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490870618  99 LLsEAVTPNTDAFFWPKYCRELHDPIVEGFLIEPDTQIILLEGNYIYSTDEDWRPVSDLIDLKIFLTASEEVLRERLISR 178
Cdd:PRK09270 103 LL-RRLRAGDDEVYWPVFDRSLEDPVADAIVVPPTARLVIVEGNYLLLDEEPWRRLAGLFDFTIFLDAPAEVLRERLVAR 181
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 490870618 179 HLAGGKSKQEALDKTERVDLVNALKIKQYESNADYVIQ 216
Cdd:PRK09270 182 KLAGGLSPEAAEAFVLRNDGPNARLVLETSRPADLVLE 219
CoaA COG1072
Panthothenate kinase [Coenzyme transport and metabolism]; Panthothenate kinase is part of the ...
24-216 3.03e-40

Panthothenate kinase [Coenzyme transport and metabolism]; Panthothenate kinase is part of the Pathway/BioSystem: Pantothenate/CoA biosynthesis


Pssm-ID: 440690  Cd Length: 309  Bit Score: 139.66  E-value: 3.03e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490870618  24 QESGKQVLVIGISGAPATGK-----------STLSESLlsglsqlgfKAQLCPMDGFHYPNSVLKEKGLTSVKGSIETFD 92
Cdd:COG1072   80 QADKKTPFIIGIAGSVAVGKsttarllqallSRWPEHP---------KVELVTTDGFLYPNAVLERRGLMDRKGFPESYD 150
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490870618  93 VTSLAHLLSEaVTPNTDAFFWPKYCRELHDPIVEGFLIEPDTQIILLEGNYI-YSTDEDWRPVSDLIDLKIFLTASEEVL 171
Cdd:COG1072  151 RRGLLRFLAR-VKSGDPEVRAPVYSHLLYDIVPGAIVVVDQPDILIVEGNNVlQDEPNPWLFVSDFFDFSIYVDADEEDL 229
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490870618 172 RERLISRHLAG----------------GKSKQEALDKTE----RVDLVN-ALKIKQYESNADYVIQ 216
Cdd:COG1072  230 REWYVERFLKLretafrdpdsyfhryaGLSEEEARAWAEeiwrEINLPNlAENILPTRSRADLILR 295
panK_bact TIGR00554
pantothenate kinase, bacterial type; Shown to be a homodimer in E. coli. This enzyme catalyzes ...
32-206 1.86e-16

pantothenate kinase, bacterial type; Shown to be a homodimer in E. coli. This enzyme catalyzes the rate-limiting step in the biosynthesis of coenzyme A. It is very well conserved from E. coli to B. subtilis, but differs considerably from known eukaryotic forms, described in a separate model. [Biosynthesis of cofactors, prosthetic groups, and carriers, Pantothenate and coenzyme A]


Pssm-ID: 273134  Cd Length: 290  Bit Score: 76.19  E-value: 1.86e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490870618   32 VIGISGAPATGKSTLSESLLSGLSQ--LGFKAQLCPMDGFHYPNSVLKEKGLTSVKGSIETFDVTSLAHLLSEAVT--PN 107
Cdd:TIGR00554  64 IISIAGSVAVGKSTSARILQALLSHwpEERKVDLITTDGFLHPLNKLKEDGLLKKKGFPESYDMHKLIKFLADLKSgkPN 143
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490870618  108 TDAffwPKYCRELHDPIVEGF--LIEPDtqIILLEG--------NYIYSTDEDWrpVSDLIDLKIFLTASEEVLRERLIS 177
Cdd:TIGR00554 144 VTA---PIYSHLIYDIIPDGDdtVDKPD--ILILEGlnvlqsgmDKPHDPDHTF--VSDFVDFSIYVDAEEDLLKEWYIK 216
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 490870618  178 RHLA----------------GGKSKQEALDKTERV-DLVNALKIKQ 206
Cdd:TIGR00554 217 RFLKfregafndpdsyfhhyAKLSKEEAIATAMKIwDEINGLNLKQ 262
PanK cd02025
Pantothenate kinase (PanK) catalyzes the phosphorylation of pantothenic acid to form 4 ...
32-180 3.52e-14

Pantothenate kinase (PanK) catalyzes the phosphorylation of pantothenic acid to form 4'-phosphopantothenic, which is the first of five steps in coenzyme A (CoA) biosynthetic pathway. The reaction carried out by this enzyme is a key regulatory point in CoA biosynthesis.


Pssm-ID: 238983  Cd Length: 220  Bit Score: 68.49  E-value: 3.52e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490870618  32 VIGISGAPATGKSTLSESLLS--GLSQLGFKAQLCPMDGFHYPNSVLKEKGLTSVKGSIETFDVTSLAHLLS--EAVTPN 107
Cdd:cd02025    1 IIGIAGSVAVGKSTTARVLQAllSRWPDHPNVELITTDGFLYPNKELIERGLMDRKGFPESYDMEALLKFLKdiKSGKKN 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490870618 108 TDAffwPKYCRELHDPIVEGFLI--EPDtqIILLEGNYIYSTDEDWRP-VSDLIDLKIFLTASEEVLRERLISRHL 180
Cdd:cd02025   81 VKI---PVYSHLTYDVIPGEKQTvdQPD--ILIIEGLNVLQTGQNPRLfVSDFFDFSIYVDADEDDIEKWYIKRFL 151
 
Name Accession Description Interval E-value
PRK09270 PRK09270
nucleoside triphosphate hydrolase domain-containing protein; Reviewed
20-216 2.60e-56

nucleoside triphosphate hydrolase domain-containing protein; Reviewed


Pssm-ID: 236442  Cd Length: 229  Bit Score: 178.59  E-value: 2.60e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490870618  20 ANTYQESGKQVLViGISGAPATGKSTLSESLLSGLSQLGFKAQLC-PMDGFHYPNSVLKEKGLTSVKGSIETFDVTSLAH 98
Cdd:PRK09270  24 AALQAEPQRRTIV-GIAGPPGAGKSTLAEFLEALLQQDGELPAIQvPMDGFHLDNAVLDAHGLRPRKGAPETFDVAGLAA 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490870618  99 LLsEAVTPNTDAFFWPKYCRELHDPIVEGFLIEPDTQIILLEGNYIYSTDEDWRPVSDLIDLKIFLTASEEVLRERLISR 178
Cdd:PRK09270 103 LL-RRLRAGDDEVYWPVFDRSLEDPVADAIVVPPTARLVIVEGNYLLLDEEPWRRLAGLFDFTIFLDAPAEVLRERLVAR 181
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 490870618 179 HLAGGKSKQEALDKTERVDLVNALKIKQYESNADYVIQ 216
Cdd:PRK09270 182 KLAGGLSPEAAEAFVLRNDGPNARLVLETSRPADLVLE 219
CoaA COG1072
Panthothenate kinase [Coenzyme transport and metabolism]; Panthothenate kinase is part of the ...
24-216 3.03e-40

Panthothenate kinase [Coenzyme transport and metabolism]; Panthothenate kinase is part of the Pathway/BioSystem: Pantothenate/CoA biosynthesis


Pssm-ID: 440690  Cd Length: 309  Bit Score: 139.66  E-value: 3.03e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490870618  24 QESGKQVLVIGISGAPATGK-----------STLSESLlsglsqlgfKAQLCPMDGFHYPNSVLKEKGLTSVKGSIETFD 92
Cdd:COG1072   80 QADKKTPFIIGIAGSVAVGKsttarllqallSRWPEHP---------KVELVTTDGFLYPNAVLERRGLMDRKGFPESYD 150
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490870618  93 VTSLAHLLSEaVTPNTDAFFWPKYCRELHDPIVEGFLIEPDTQIILLEGNYI-YSTDEDWRPVSDLIDLKIFLTASEEVL 171
Cdd:COG1072  151 RRGLLRFLAR-VKSGDPEVRAPVYSHLLYDIVPGAIVVVDQPDILIVEGNNVlQDEPNPWLFVSDFFDFSIYVDADEEDL 229
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490870618 172 RERLISRHLAG----------------GKSKQEALDKTE----RVDLVN-ALKIKQYESNADYVIQ 216
Cdd:COG1072  230 REWYVERFLKLretafrdpdsyfhryaGLSEEEARAWAEeiwrEINLPNlAENILPTRSRADLILR 295
panK_bact TIGR00554
pantothenate kinase, bacterial type; Shown to be a homodimer in E. coli. This enzyme catalyzes ...
32-206 1.86e-16

pantothenate kinase, bacterial type; Shown to be a homodimer in E. coli. This enzyme catalyzes the rate-limiting step in the biosynthesis of coenzyme A. It is very well conserved from E. coli to B. subtilis, but differs considerably from known eukaryotic forms, described in a separate model. [Biosynthesis of cofactors, prosthetic groups, and carriers, Pantothenate and coenzyme A]


Pssm-ID: 273134  Cd Length: 290  Bit Score: 76.19  E-value: 1.86e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490870618   32 VIGISGAPATGKSTLSESLLSGLSQ--LGFKAQLCPMDGFHYPNSVLKEKGLTSVKGSIETFDVTSLAHLLSEAVT--PN 107
Cdd:TIGR00554  64 IISIAGSVAVGKSTSARILQALLSHwpEERKVDLITTDGFLHPLNKLKEDGLLKKKGFPESYDMHKLIKFLADLKSgkPN 143
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490870618  108 TDAffwPKYCRELHDPIVEGF--LIEPDtqIILLEG--------NYIYSTDEDWrpVSDLIDLKIFLTASEEVLRERLIS 177
Cdd:TIGR00554 144 VTA---PIYSHLIYDIIPDGDdtVDKPD--ILILEGlnvlqsgmDKPHDPDHTF--VSDFVDFSIYVDAEEDLLKEWYIK 216
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 490870618  178 RHLA----------------GGKSKQEALDKTERV-DLVNALKIKQ 206
Cdd:TIGR00554 217 RFLKfregafndpdsyfhhyAKLSKEEAIATAMKIwDEINGLNLKQ 262
PanK cd02025
Pantothenate kinase (PanK) catalyzes the phosphorylation of pantothenic acid to form 4 ...
32-180 3.52e-14

Pantothenate kinase (PanK) catalyzes the phosphorylation of pantothenic acid to form 4'-phosphopantothenic, which is the first of five steps in coenzyme A (CoA) biosynthetic pathway. The reaction carried out by this enzyme is a key regulatory point in CoA biosynthesis.


Pssm-ID: 238983  Cd Length: 220  Bit Score: 68.49  E-value: 3.52e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490870618  32 VIGISGAPATGKSTLSESLLS--GLSQLGFKAQLCPMDGFHYPNSVLKEKGLTSVKGSIETFDVTSLAHLLS--EAVTPN 107
Cdd:cd02025    1 IIGIAGSVAVGKSTTARVLQAllSRWPDHPNVELITTDGFLYPNKELIERGLMDRKGFPESYDMEALLKFLKdiKSGKKN 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490870618 108 TDAffwPKYCRELHDPIVEGFLI--EPDtqIILLEGNYIYSTDEDWRP-VSDLIDLKIFLTASEEVLRERLISRHL 180
Cdd:cd02025   81 VKI---PVYSHLTYDVIPGEKQTvdQPD--ILIIEGLNVLQTGQNPRLfVSDFFDFSIYVDADEDDIEKWYIKRFL 151
PRK06696 PRK06696
uridine kinase; Validated
30-216 7.27e-09

uridine kinase; Validated


Pssm-ID: 180660  Cd Length: 223  Bit Score: 53.83  E-value: 7.27e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490870618  30 VLVIGISGAPATGKSTLSESLLSGLSQLGFKAQLCPMDGFHYPNSVLKEKGLTSVKGSIE-TFDVTSLAHLLSEAVTPNT 108
Cdd:PRK06696  22 PLRVAIDGITASGKTTFADELAEEIKKRGRPVIRASIDDFHNPRVIRYRRGRESAEGYYEdAYDYTALRRLLLDPLGPNG 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490870618 109 D-----AFFWPKYCRELHDPIVEGfliePDTQIILLEGNYIYstdedwRP-VSDLIDLKIFLTASEEVLRERLISRHLAG 182
Cdd:PRK06696 102 DrqyrtASHDLKTDIPVHNPPLLA----APNAVLIVDGTFLL------RPeLRDLWDYKIFLDTDFEVSRRRGAKRDTEA 171
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 490870618 183 GKSKQEAlDKTERVDLVNALKIKQYESN----ADYVIQ 216
Cdd:PRK06696 172 FGSYEEA-EKMYLARYHPAQKLYIAEANpkerADVVID 208
Udk COG0572
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway ...
28-217 1.22e-07

Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway/BioSystem: Pyrimidine salvage


Pssm-ID: 440337 [Multi-domain]  Cd Length: 206  Bit Score: 50.22  E-value: 1.22e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490870618  28 KQVLVIGISGAPATGKSTlsesllsglsqlgFKAQLC-----------PMDGFHYPNSVLK--EKGLTsvkG--SIETFD 92
Cdd:COG0572    5 GKPRIIGIAGPSGSGKTT-------------FARRLAeqlgadkvvviSLDDYYKDREHLPldERGKP---NfdHPEAFD 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490870618  93 VTSLAHLLS-----EAVTpntdaffWPKYCRELHDPIVEGFLIEPDtQIILLEGNYIYSTDEdwrpVSDLIDLKIFLTAS 167
Cdd:COG0572   69 LDLLNEHLEplkagESVE-------LPVYDFATGTRSGETVKVEPA-DVIIVEGIHALNDEL----LRDLLDLKIYVDAD 136
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 490870618 168 EEVLRERLISR-HLAGGKSKQEALDKT-ERVDLVNALKIKQYESNADYVIQT 217
Cdd:COG0572  137 TDVRLIRRIVRdGEERGRTAESVIEQYwATVRPGHEQYIEPTKEYADIVIPN 188
UMPK cd02023
Uridine monophosphate kinase (UMPK, EC 2.7.1.48), also known as uridine kinase or ...
114-210 3.06e-04

Uridine monophosphate kinase (UMPK, EC 2.7.1.48), also known as uridine kinase or uridine-cytidine kinase (UCK), catalyzes the reversible phosphoryl transfer from ATP to uridine or cytidine to yield UMP or CMP. In the primidine nucleotide-salvage pathway, this enzyme combined with nucleoside diphosphate kinases further phosphorylates UMP and CMP to form UTP and CTP. This kinase also catalyzes the phosphorylation of several cytotoxic ribonucleoside analogs such as 5-flurrouridine and cyclopentenyl-cytidine.


Pssm-ID: 238981 [Multi-domain]  Cd Length: 198  Bit Score: 40.23  E-value: 3.06e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490870618 114 PKYCRELHDPIVEGFLIEPdTQIILLEGNYIYSTDEdwrpVSDLIDLKIFLTASEEVLRERLISRhlaggkskqealDKT 193
Cdd:cd02023   80 PVYDFKTHSRLKETVTVYP-ADVIILEGILALYDKE----LRDLMDLKIFVDTDADVRLIRRIER------------DIV 142
                         90
                 ....*....|....*..
gi 490870618 194 ERVDLVNAlKIKQYESN 210
Cdd:cd02023  143 ERGRDLES-VINQYLKF 158
NRK1 cd02024
Nicotinamide riboside kinase (NRK) is an enzyme involved in the metabolism of nicotinamide ...
119-178 8.21e-03

Nicotinamide riboside kinase (NRK) is an enzyme involved in the metabolism of nicotinamide adenine dinucleotide (NAD+). This enzyme catalyzes the phosphorylation of nicotinamide riboside (NR) to form nicotinamide mononucleotide (NMN). It defines the NR salvage pathway of NAD+ biosynthesis in addition to the pathways through nicotinic acid mononucleotide (NaMN). This enzyme can also phosphorylate the anticancer drug tiazofurin, which is an analog of nicotinamide riboside.


Pssm-ID: 238982 [Multi-domain]  Cd Length: 187  Bit Score: 36.15  E-value: 8.21e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 490870618 119 ELHDPIVEGFLIepdtqiillegnYIYstdedwRPVSDLIDLKIFLTASEEVLRERLISR 178
Cdd:cd02024  110 DLHILIVDGFLL------------YNY------KPLVDLFDIRYFLRVPYETCKRRREAR 151
 
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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