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Conserved domains on  [gi|520907919|ref|WP_020327915|]
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MULTISPECIES: uridine kinase [Vibrio]

Protein Classification

uridine-cytidine kinase( domain architecture ID 10792545)

uridine kinase, or uridine cytidine kinase, catalyzes the ATP-dependent phosphorylation of uridine or cytidine to yield UMP or CMP

EC:  2.7.1.48
Gene Ontology:  GO:0005737|GO:0044206|GO:0005829|GO:0016310|GO:0043771|GO:0005524|GO:0004849|GO:0044211
PubMed:  27239701

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
PRK05480 PRK05480
uridine/cytidine kinase; Provisional
 2-212 2.40e-135

uridine/cytidine kinase; Provisional


:

Pssm-ID: 235492 [Multi-domain]  Cd Length: 209  Bit Score: 377.58  E-value: 2.40e-135
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520907919   2 SDNNQCVIVGIAGASASGKSLIASTIYNELrakvGDHQIGVITEDCYYKDQSHLSMEDRVKTNYDHPNALDHDLLCEHLQ 81
Cdd:PRK05480   1 MMMKKPIIIGIAGGSGSGKTTVASTIYEEL----GDESIAVIPQDSYYKDQSHLSFEERVKTNYDHPDAFDHDLLIEHLK 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520907919  82 KLTRGEAVEVPEYSYTEHTRTSNTTTMTPKKVIILEGILLLTDPRLRDLMHATIFMDTPLDICLLRRVKRDVEERGRTME 161
Cdd:PRK05480  77 ALKAGKAIEIPVYDYTEHTRSKETIRVEPKDVIILEGILLLEDERLRDLMDIKIFVDTPLDIRLIRRLKRDVNERGRSLE 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 520907919 162 SVLSQYQKTVRPMFMQFIEPSKQYADIIVPRGGKNRIAIDVLKAHIAKLLK 212
Cdd:PRK05480 157 SVINQYLSTVRPMHLQFIEPSKRYADIIIPEGGKNRVAIDILKAKIRQLLE 207
 
Name Accession Description Interval E-value
PRK05480 PRK05480
uridine/cytidine kinase; Provisional
 2-212 2.40e-135

uridine/cytidine kinase; Provisional


Pssm-ID: 235492 [Multi-domain]  Cd Length: 209  Bit Score: 377.58  E-value: 2.40e-135
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520907919   2 SDNNQCVIVGIAGASASGKSLIASTIYNELrakvGDHQIGVITEDCYYKDQSHLSMEDRVKTNYDHPNALDHDLLCEHLQ 81
Cdd:PRK05480   1 MMMKKPIIIGIAGGSGSGKTTVASTIYEEL----GDESIAVIPQDSYYKDQSHLSFEERVKTNYDHPDAFDHDLLIEHLK 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520907919  82 KLTRGEAVEVPEYSYTEHTRTSNTTTMTPKKVIILEGILLLTDPRLRDLMHATIFMDTPLDICLLRRVKRDVEERGRTME 161
Cdd:PRK05480  77 ALKAGKAIEIPVYDYTEHTRSKETIRVEPKDVIILEGILLLEDERLRDLMDIKIFVDTPLDIRLIRRLKRDVNERGRSLE 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 520907919 162 SVLSQYQKTVRPMFMQFIEPSKQYADIIVPRGGKNRIAIDVLKAHIAKLLK 212
Cdd:PRK05480 157 SVINQYLSTVRPMHLQFIEPSKRYADIIIPEGGKNRVAIDILKAKIRQLLE 207
udk TIGR00235
uridine kinase; Model contains a number of longer eukaryotic proteins and starts bringing in ...
 2-212 3.97e-103

uridine kinase; Model contains a number of longer eukaryotic proteins and starts bringing in phosphoribulokinase hits at scores of 160 and below [Purines, pyrimidines, nucleosides, and nucleotides, Salvage of nucleosides and nucleotides]


Pssm-ID: 272977  Cd Length: 207  Bit Score: 296.22  E-value: 3.97e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520907919    2 SDNNQCVIVGIAGASASGKSLIASTIYNELrakvGDHQIGVITEDCYYKDQSHLSMEDRVKTNYDHPNALDHDLLCEHLQ 81
Cdd:TIGR00235   1 MDKPKGIIIGIGGGSGSGKTTVARKIYEQL----GKLEIVIISQDNYYKDQSHLEMAERKKTNFDHPDAFDNDLLYEHLK 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520907919   82 KLTRGEAVEVPEYSYTEHTRTSNTTTMTPKKVIILEGILLLTDPRLRDLMHATIFMDTPLDICLLRRVKRDVEERGRTME 161
Cdd:TIGR00235  77 NLKNGSPIDVPVYDYVNHTRPKETVHIEPKDVVILEGIMPLFDERLRDLMDLKIFVDTPLDIRLIRRIERDINERGRSLD 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 520907919  162 SVLSQYQKTVRPMFMQFIEPSKQYADIIVPRGGKNRIAIDVLKAHIAKLLK 212
Cdd:TIGR00235 157 SVIDQYRKTVRPMYEQFVEPTKQYADLIIPEGGRNEVAINVLDTKIKHLLE 207
UMPK cd02023
Uridine monophosphate kinase (UMPK, EC 2.7.1.48), also known as uridine kinase or ...
 9-210 4.08e-92

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: 267.88  E-value: 4.08e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520907919   9 IVGIAGASASGKSLIASTIYNELrakvGDHQIGVITEDCYYKDQSHLSMEDRVKTNYDHPNALDHDLLCEHLQKLTRGEA 88
Cdd:cd02023    1 IIGIAGGSGSGKTTVAEEIIEQL----GNPKVVIISQDSYYKDLSHEELEERKNNNYDHPDAFDFDLLISHLQDLKNGKS 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520907919  89 VEVPEYSYTEHTRTSNTTTMTPKKVIILEGILLLTDPRLRDLMHATIFMDTPLDICLLRRVKRDVEERGRTMESVLSQYQ 168
Cdd:cd02023   77 VEIPVYDFKTHSRLKETVTVYPADVIILEGILALYDKELRDLMDLKIFVDTDADVRLIRRIERDIVERGRDLESVINQYL 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 520907919 169 KTVRPMFMQFIEPSKQYADIIVPRGGKNRIAIDVLKAHIAKL 210
Cdd:cd02023  157 KFVKPMHEQFIEPTKRYADVIIPRGGDNHVAIDLIVQHIKSK 198
Udk COG0572
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway ...
 1-209 2.99e-91

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: 265.94  E-value: 2.99e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520907919   1 MSDNNQCVIVGIAGASASGKSLIASTIYNELRAkvgdHQIGVITEDCYYKDQSHLSMEDRVKTNYDHPNALDHDLLCEHL 80
Cdd:COG0572    1 AARSGKPRIIGIAGPSGSGKTTFARRLAEQLGA----DKVVVISLDDYYKDREHLPLDERGKPNFDHPEAFDLDLLNEHL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520907919  81 QKLTRGEAVEVPEYSYTEHTRTSNTTTMTPKKVIILEGILLLTDPRLRDLMHATIFMDTPLDICLLRRVKRDVEERGRTM 160
Cdd:COG0572   77 EPLKAGESVELPVYDFATGTRSGETVKVEPADVIIVEGIHALNDELLRDLLDLKIYVDADTDVRLIRRIVRDGEERGRTA 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 520907919 161 ESVLSQYQKTVRPMFMQFIEPSKQYADIIVPRGG-KNRIAIDVLKAHIAK 209
Cdd:COG0572  157 ESVIEQYWATVRPGHEQYIEPTKEYADIVIPNGGpLNPVALDLLVARLLS 206
PRK pfam00485
Phosphoribulokinase / Uridine kinase family; This family matches three types of P-loop ...
 9-199 9.56e-41

Phosphoribulokinase / Uridine kinase family; This family matches three types of P-loop containing kinases: phosphoribulokinases, uridine kinases and bacterial pantothenate kinases(CoaA). Arabidopsis and other organizms have a dual uridine kinase/uracil phosphoribosyltransferase protein where the N-terminal region consists of a UK domain and the C-terminal region of a UPRT domain.


Pssm-ID: 425711 [Multi-domain]  Cd Length: 196  Bit Score: 137.53  E-value: 9.56e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520907919    9 IVGIAGASASGKSLIASTIYNELRA----KVGDHQIGVITEDCYYKDQSHLSMEDRVKTNYDH--PNALDHDLLCEHLQK 82
Cdd:pfam00485   1 VIGVAGSSGSGKTTVARRIVSIFGRegvpAVGIEGDSFHSTDRFYMDLHPEDRKRAGNNGYSFdgPEANDFDLLYEQFKE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520907919   83 LTRGEAVEVPEYSYTEHTRTSNTTTMTPKKVIILEGILLLTDPRLRDLMHATIFMDTPLDICLLRRVKRDVEERGRTMES 162
Cdd:pfam00485  81 LKEGGSVDKPIYNHVTHERDPTPELIEGADVLVIEGLHALYDERVAQLLDLKIYVDPDIDLELARKIQRDMAERGHSLEG 160

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 520907919  163 VLSQYQKtVRPMFMQFIEPSKQYADIIVPRGGKNRIA 199
Cdd:pfam00485 161 VTDSILF-RKPDYVNYIDPQFSYADLIIQRVPTNDTA 196
 
Name Accession Description Interval E-value
PRK05480 PRK05480
uridine/cytidine kinase; Provisional
 2-212 2.40e-135

uridine/cytidine kinase; Provisional


Pssm-ID: 235492 [Multi-domain]  Cd Length: 209  Bit Score: 377.58  E-value: 2.40e-135
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520907919   2 SDNNQCVIVGIAGASASGKSLIASTIYNELrakvGDHQIGVITEDCYYKDQSHLSMEDRVKTNYDHPNALDHDLLCEHLQ 81
Cdd:PRK05480   1 MMMKKPIIIGIAGGSGSGKTTVASTIYEEL----GDESIAVIPQDSYYKDQSHLSFEERVKTNYDHPDAFDHDLLIEHLK 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520907919  82 KLTRGEAVEVPEYSYTEHTRTSNTTTMTPKKVIILEGILLLTDPRLRDLMHATIFMDTPLDICLLRRVKRDVEERGRTME 161
Cdd:PRK05480  77 ALKAGKAIEIPVYDYTEHTRSKETIRVEPKDVIILEGILLLEDERLRDLMDIKIFVDTPLDIRLIRRLKRDVNERGRSLE 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 520907919 162 SVLSQYQKTVRPMFMQFIEPSKQYADIIVPRGGKNRIAIDVLKAHIAKLLK 212
Cdd:PRK05480 157 SVINQYLSTVRPMHLQFIEPSKRYADIIIPEGGKNRVAIDILKAKIRQLLE 207
udk TIGR00235
uridine kinase; Model contains a number of longer eukaryotic proteins and starts bringing in ...
 2-212 3.97e-103

uridine kinase; Model contains a number of longer eukaryotic proteins and starts bringing in phosphoribulokinase hits at scores of 160 and below [Purines, pyrimidines, nucleosides, and nucleotides, Salvage of nucleosides and nucleotides]


Pssm-ID: 272977  Cd Length: 207  Bit Score: 296.22  E-value: 3.97e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520907919    2 SDNNQCVIVGIAGASASGKSLIASTIYNELrakvGDHQIGVITEDCYYKDQSHLSMEDRVKTNYDHPNALDHDLLCEHLQ 81
Cdd:TIGR00235   1 MDKPKGIIIGIGGGSGSGKTTVARKIYEQL----GKLEIVIISQDNYYKDQSHLEMAERKKTNFDHPDAFDNDLLYEHLK 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520907919   82 KLTRGEAVEVPEYSYTEHTRTSNTTTMTPKKVIILEGILLLTDPRLRDLMHATIFMDTPLDICLLRRVKRDVEERGRTME 161
Cdd:TIGR00235  77 NLKNGSPIDVPVYDYVNHTRPKETVHIEPKDVVILEGIMPLFDERLRDLMDLKIFVDTPLDIRLIRRIERDINERGRSLD 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 520907919  162 SVLSQYQKTVRPMFMQFIEPSKQYADIIVPRGGKNRIAIDVLKAHIAKLLK 212
Cdd:TIGR00235 157 SVIDQYRKTVRPMYEQFVEPTKQYADLIIPEGGRNEVAINVLDTKIKHLLE 207
UMPK cd02023
Uridine monophosphate kinase (UMPK, EC 2.7.1.48), also known as uridine kinase or ...
 9-210 4.08e-92

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: 267.88  E-value: 4.08e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520907919   9 IVGIAGASASGKSLIASTIYNELrakvGDHQIGVITEDCYYKDQSHLSMEDRVKTNYDHPNALDHDLLCEHLQKLTRGEA 88
Cdd:cd02023    1 IIGIAGGSGSGKTTVAEEIIEQL----GNPKVVIISQDSYYKDLSHEELEERKNNNYDHPDAFDFDLLISHLQDLKNGKS 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520907919  89 VEVPEYSYTEHTRTSNTTTMTPKKVIILEGILLLTDPRLRDLMHATIFMDTPLDICLLRRVKRDVEERGRTMESVLSQYQ 168
Cdd:cd02023   77 VEIPVYDFKTHSRLKETVTVYPADVIILEGILALYDKELRDLMDLKIFVDTDADVRLIRRIERDIVERGRDLESVINQYL 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 520907919 169 KTVRPMFMQFIEPSKQYADIIVPRGGKNRIAIDVLKAHIAKL 210
Cdd:cd02023  157 KFVKPMHEQFIEPTKRYADVIIPRGGDNHVAIDLIVQHIKSK 198
Udk COG0572
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway ...
 1-209 2.99e-91

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: 265.94  E-value: 2.99e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520907919   1 MSDNNQCVIVGIAGASASGKSLIASTIYNELRAkvgdHQIGVITEDCYYKDQSHLSMEDRVKTNYDHPNALDHDLLCEHL 80
Cdd:COG0572    1 AARSGKPRIIGIAGPSGSGKTTFARRLAEQLGA----DKVVVISLDDYYKDREHLPLDERGKPNFDHPEAFDLDLLNEHL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520907919  81 QKLTRGEAVEVPEYSYTEHTRTSNTTTMTPKKVIILEGILLLTDPRLRDLMHATIFMDTPLDICLLRRVKRDVEERGRTM 160
Cdd:COG0572   77 EPLKAGESVELPVYDFATGTRSGETVKVEPADVIIVEGIHALNDELLRDLLDLKIYVDADTDVRLIRRIVRDGEERGRTA 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 520907919 161 ESVLSQYQKTVRPMFMQFIEPSKQYADIIVPRGG-KNRIAIDVLKAHIAK 209
Cdd:COG0572  157 ESVIEQYWATVRPGHEQYIEPTKEYADIVIPNGGpLNPVALDLLVARLLS 206
PTZ00301 PTZ00301
uridine kinase; Provisional
 7-211 2.91e-72

uridine kinase; Provisional


Pssm-ID: 140322 [Multi-domain]  Cd Length: 210  Bit Score: 218.33  E-value: 2.91e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520907919   7 CVIVGIAGASASGKSLIASTIYNELRAKVGDHQIGVITEDCYYKDQSHLSMEDRVKTNYDHPNALDHDLLCEHLQKLTRG 86
Cdd:PTZ00301   3 CTVIGISGASGSGKSSLSTNIVSELMAHCGPVSIGVICEDFYYRDQSNIPESERAYTNYDHPKSLEHDLLTTHLRELKSG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520907919  87 EAVEVPEYSYTEHTRTSNTTTMTPKKVIILEGILLLTDPRLRDLMHATIFMDTPLDICLLRRVKRDVEERGRTMESVLSQ 166
Cdd:PTZ00301  83 KTVQIPQYDYVHHTRSDTAVTMTPKSVLIVEGILLFTNAELRNEMDCLIFVDTPLDICLIRRAKRDMRERGRTFESVIEQ 162

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 520907919 167 YQKTVRPMFMQFIEPSKQYADIIVPRGGKNRIAIDVLKAHIAKLL 211
Cdd:PTZ00301 163 YEATVRPMYYAYVEPSKVYADIIVPSWKDNSVAVGVLRAKLNHDL 207
PRK pfam00485
Phosphoribulokinase / Uridine kinase family; This family matches three types of P-loop ...
 9-199 9.56e-41

Phosphoribulokinase / Uridine kinase family; This family matches three types of P-loop containing kinases: phosphoribulokinases, uridine kinases and bacterial pantothenate kinases(CoaA). Arabidopsis and other organizms have a dual uridine kinase/uracil phosphoribosyltransferase protein where the N-terminal region consists of a UK domain and the C-terminal region of a UPRT domain.


Pssm-ID: 425711 [Multi-domain]  Cd Length: 196  Bit Score: 137.53  E-value: 9.56e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520907919    9 IVGIAGASASGKSLIASTIYNELRA----KVGDHQIGVITEDCYYKDQSHLSMEDRVKTNYDH--PNALDHDLLCEHLQK 82
Cdd:pfam00485   1 VIGVAGSSGSGKTTVARRIVSIFGRegvpAVGIEGDSFHSTDRFYMDLHPEDRKRAGNNGYSFdgPEANDFDLLYEQFKE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520907919   83 LTRGEAVEVPEYSYTEHTRTSNTTTMTPKKVIILEGILLLTDPRLRDLMHATIFMDTPLDICLLRRVKRDVEERGRTMES 162
Cdd:pfam00485  81 LKEGGSVDKPIYNHVTHERDPTPELIEGADVLVIEGLHALYDERVAQLLDLKIYVDPDIDLELARKIQRDMAERGHSLEG 160

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 520907919  163 VLSQYQKtVRPMFMQFIEPSKQYADIIVPRGGKNRIA 199
Cdd:pfam00485 161 VTDSILF-RKPDYVNYIDPQFSYADLIIQRVPTNDTA 196
PRK cd02026
Phosphoribulokinase (PRK) is an enzyme involved in the Benson-Calvin cycle in chloroplasts or ...
 9-190 9.27e-29

Phosphoribulokinase (PRK) is an enzyme involved in the Benson-Calvin cycle in chloroplasts or photosynthetic prokaryotes. This enzyme catalyzes the phosphorylation of D-ribulose 5-phosphate to form D-ribulose 1, 5-biphosphate, using ATP and NADPH produced by the primary reactions of photosynthesis.


Pssm-ID: 238984 [Multi-domain]  Cd Length: 273  Bit Score: 108.58  E-value: 9.27e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520907919   9 IVGIAGASASGKSliasTIYNELRAKVGDHQIGVITEDCYYKdqshLSMEDRVKTNYD--HPNALDHDLLCEHLQKLTRG 86
Cdd:cd02026    1 IIGVAGDSGCGKS----TFLRRLTSLFGSDLVTVICLDDYHS----LDRKGRKETGITalDPRANNFDLMYEQLKALKEG 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520907919  87 EAVEVPEYSYtEHTRTSNTTTMTPKKVIILEGILLLTDPRLRDLMHATIFMDTPLDICLLRRVKRDVEERGRTMESVLSQ 166
Cdd:cd02026   73 QAIEKPIYNH-VTGLIDPPELIKPTKIVVIEGLHPLYDERVRELLDFSVYLDISDEVKFAWKIQRDMAERGHSLEDVLAS 151

                        170       180
                 ....*....|....*....|....
gi 520907919 167 YQKTvRPMFMQFIEPSKQYADIIV 190
Cdd:cd02026  152 IEAR-KPDFEAYIDPQKQYADVVI 174
PRK07429 PRK07429
phosphoribulokinase; Provisional
 8-190 2.36e-28

phosphoribulokinase; Provisional


Pssm-ID: 180975  Cd Length: 327  Bit Score: 108.56  E-value: 2.36e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520907919   8 VIVGIAGASASGKSliasTIYNELRAKVGDHQIGVITEDCYYKdqshLSMEDRVKTNYD--HPNALDHDLLCEHLQKLTR 85
Cdd:PRK07429   9 VLLGVAGDSGCGKT----TFLRGLADLLGEELVTVICTDDYHS----YDRKQRKELGITalDPRANNLDIMYEHLKALKT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520907919  86 GEAVEVPEYSYtEHTRTSNTTTMTPKKVIILEGILLLTDPRLRDLMHATIFMDTPLDICLLRRVKRDVEERGRTMESVLS 165
Cdd:PRK07429  81 GQPILKPIYNH-ETGTFDPPEYIEPNKIVVVEGLHPLYDERVRELYDFKVYLDPPEEVKIAWKIKRDMAKRGHTYEQVLA 159

                        170       180
                 ....*....|....*....|....*
gi 520907919 166 QYQKTvRPMFMQFIEPSKQYADIIV 190
Cdd:PRK07429 160 EIEAR-EPDFEAYIRPQRQWADVVI 183
UMPK_like cd02028
Uridine monophosphate kinase_like (UMPK_like) is a family of proteins highly similar to the ...
 9-190 4.01e-23

Uridine monophosphate kinase_like (UMPK_like) is a family of proteins highly similar to the uridine monophosphate kinase (UMPK, EC 2.7.1.48), also known as uridine kinase or uridine-cytidine kinase (UCK).


Pssm-ID: 238986 [Multi-domain]  Cd Length: 179  Bit Score: 91.21  E-value: 4.01e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520907919   9 IVGIAGASASGKSLIASTIYNELRAKVgdHQIGVITEDCYYKDQSHLSMEDrvkTNYDHPNALDHDLLCEHLQKLTRGEA 88
Cdd:cd02028    1 VVGIAGPSGSGKTTFAKKLSNQLRVNG--IGPVVISLDDYYVPRKTPRDED---GNYDFESILDLDLLNKNLHDLLNGKE 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520907919  89 VEVPEYSYTEHTRTSNTTTMTPK-KVIILEGILLLtDPRLRDLMHATIFMDTPLDIC-LLRRVKRDVEERGRTMESVLSQ 166
Cdd:cd02028   76 VELPIYDFRTGKRRGYRKLKLPPsGVVILEGIYAL-NERLRSLLDIRVAVSGGVHLNrLLRRVVRDIQFRGYSAELTILM 154

                        170       180
                 ....*....|....*....|....
gi 520907919 167 YQktVRPMFMQFIEPSKQYADIIV 190
Cdd:cd02028  155 WP--SVPSGEEFIIPPLQEAAIVM 176
PLN02318 PLN02318
phosphoribulokinase/uridine kinase
 4-188 6.73e-21

phosphoribulokinase/uridine kinase


Pssm-ID: 177952 [Multi-domain]  Cd Length: 656  Bit Score: 89.92  E-value: 6.73e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520907919   4 NNQCVIVGIAGASASGKSLIASTIYNELRAkvgdhqIGVITEDcYYKDQSHLsmedrVKTNYDHPNALDHDLLCEHLQKL 83
Cdd:PLN02318  62 NDGIILVGVAGPSGAGKTVFTEKVLNFMPS------IAVISMD-NYNDSSRI-----IDGNFDDPRLTDYDTLLDNIHDL 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520907919  84 TRGEAVEVPEYSYTEHTRTSNTTTMTPK-KVIILEGILLLTDpRLRDLMHATIFMDTPLDICLLRRVKRDVEERGRTMES 162
Cdd:PLN02318 130 KAGKSVQVPIYDFKSSSRVGYRTLEVPSsRIVIIEGIYALSE-KLRPLLDLRVSVTGGVHFDLVKRVLRDIQRAGQEPEE 208

                        170       180
                 ....*....|....*....|....*.
gi 520907919 163 VLSQYQKTVRPMFMQFIEPSKQYADI 188
Cdd:PLN02318 209 IIHQISETVYPMYKAFIEPDLQTAHI 234
PLN02348 PLN02348
phosphoribulokinase
 67-190 8.17e-20

phosphoribulokinase


Pssm-ID: 215198  Cd Length: 395  Bit Score: 86.44  E-value: 8.17e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520907919  67 HPNALDHDLLCEHLQKLTRGEAVEVPEYSYTEhTRTSNTTTMTPKKVIILEGILLLTDPRLRDLMHATIFMDTPLDICLL 146
Cdd:PLN02348 120 DPRANNFDLMYEQVKALKEGKAVEKPIYNHVT-GLLDPPELIEPPKILVIEGLHPMYDERVRDLLDFSIYLDISDDVKFA 198

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 520907919 147 RRVKRDVEERGRTMESVLSQYQKTvRPMFMQFIEPSKQYADIIV 190
Cdd:PLN02348 199 WKIQRDMAERGHSLESIKASIEAR-KPDFDAYIDPQKQYADVVI 241
NRK1 cd02024
Nicotinamide riboside kinase (NRK) is an enzyme involved in the metabolism of nicotinamide ...
 9-152 1.30e-13

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: 66.19  E-value: 1.30e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520907919   9 IVGIAGASASGKSLIAstiyNELRAKVGDhqIGVITEDCYYKDQSHLSMEDRVKTNYDHPNALDHDLLCE---------H 79
Cdd:cd02024    1 IVGISGVTNSGKTTLA----KLLQRILPN--CCVIHQDDFFKPEDEIPVDENGFKQWDVLEALDMEAMMStldywretgH 74

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 520907919  80 LQKLTRGEAVEV-----PEYSYTEHTRTSNTTTMTPKKVIILEGILLLTDPRLRDLMHATIFMDTPLDICLLRRVKRD 152
Cdd:cd02024   75 FPKFLRSHGNENdpekeFIEDAQIEETKADLLGAEDLHILIVDGFLLYNYKPLVDLFDIRYFLRVPYETCKRRREART 152
PRK08233 PRK08233
hypothetical protein; Provisional
 9-212 2.66e-09

hypothetical protein; Provisional


Pssm-ID: 181310 [Multi-domain]  Cd Length: 182  Bit Score: 54.36  E-value: 2.66e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520907919   9 IVGIAGASASGKSLIASTIYNELRAKVgdhqigvitedCYYKDQSHLSM--EDRVK-----TNYdhpNALDHDLLCEHLQ 81
Cdd:PRK08233   5 IITIAAVSGGGKTTLTERLTHKLKNSK-----------ALYFDRYDFDNcpEDICKwidkgANY---SEWVLTPLIKDIQ 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520907919  82 kltrgEAVEVPEYSYtehtrtsntttmtpkkvIILEGILLLTDPRLRDLMHATIFMDTPLDICLLRRVKRDVEErgRTME 161
Cdd:PRK08233  71 -----ELIAKSNVDY-----------------IIVDYPFAYLNSEMRQFIDVTIFIDTPLDIAMARRILRDFKE--DTGN 126

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 520907919 162 SV---LSQYQKTVRPMFMQFIEPSKQYADIIVprggKNRIAIDVLKAHIAKLLK 212
Cdd:PRK08233 127 EIhndLKHYLNYARPLYLEALHTVKPNADIVL----DGALSVEEIINQIEEELY 176
PanK cd02025
Pantothenate kinase (PanK) catalyzes the phosphorylation of pantothenic acid to form 4 ...
 9-193 1.49e-04

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: 41.14  E-value: 1.49e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520907919   9 IVGIAGASASGKSLIAStIYNELRAKVGDH-QIGVITEDCYYKDQSHLSMEDRVKTNyDHPNALDHDLLCEHLQKLTRG- 86
Cdd:cd02025    1 IIGIAGSVAVGKSTTAR-VLQALLSRWPDHpNVELITTDGFLYPNKELIERGLMDRK-GFPESYDMEALLKFLKDIKSGk 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520907919  87 EAVEVPEYSYTEHTRTSNTTTMTPKKVI-ILEGILLLTDPRLR-----DLMHATIFMDTPLDiCL----LRRVKRDVEER 156
Cdd:cd02025   79 KNVKIPVYSHLTYDVIPGEKQTVDQPDIlIIEGLNVLQTGQNPrlfvsDFFDFSIYVDADED-DIekwyIKRFLKLRETA 157

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 520907919 157 GRTMESVLSQYQK---------------TV-RPMFMQFIEPSKQYADIIVPRG 193
Cdd:cd02025  158 FSDPDSYFHRYAKmseeeaiafarevwkNInLKNLRENILPTRNRADLILEKG 210
PRK06696 PRK06696
uridine kinase; Validated
 10-157 2.90e-03

uridine kinase; Validated


Pssm-ID: 180660  Cd Length: 223  Bit Score: 37.65  E-value: 2.90e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520907919  10 VGIAGASASGKSliasTIYNELRAKVGDHQIGVItedCYYKDQSHLSMEDRVKTNYDHP-----NALDHDLLCEHLQK-- 82
Cdd:PRK06696  25 VAIDGITASGKT----TFADELAEEIKKRGRPVI---RASIDDFHNPRVIRYRRGRESAegyyeDAYDYTALRRLLLDpl 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520907919  83 --------------LTRGEAVEVPEysytehtrtsntTTMTPKKVIILEGILLLTdPRLRDLMHATIFMDTPLDICLLRR 148
Cdd:PRK06696  98 gpngdrqyrtashdLKTDIPVHNPP------------LLAAPNAVLIVDGTFLLR-PELRDLWDYKIFLDTDFEVSRRRG 164


                 ....*....
gi 520907919 149 VKRDVEERG 157
Cdd:PRK06696 165 AKRDTEAFG 173
 
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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