NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|489126981|ref|WP_003036776|]
View 

MULTISPECIES: uridine kinase [Citrobacter]

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

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
PRK05480 PRK05480
uridine/cytidine kinase; Provisional
3-213 1.02e-146

uridine/cytidine kinase; Provisional


:

Pssm-ID: 235492 [Multi-domain]  Cd Length: 209  Bit Score: 406.47  E-value: 1.02e-146
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126981   3 DQSHQCVIIGIAGASASGKSLIASTLYRELreqvGDEHIGVIPEDSYYKDQSHLSMEERVKTNYDHPNAMDHSLLFQHLQ 82
Cdd:PRK05480   1 MMMKKPIIIGIAGGSGSGKTTVASTIYEEL----GDESIAVIPQDSYYKDQSHLSFEERVKTNYDHPDAFDHDLLIEHLK 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126981  83 TLKRGSAIELPVYSYVEHTRTQDTIHIEPKKVIILEGILLLTDARLRDEMNFSIFVDTPLDICLMRRIKRDVNERGRSMD 162
Cdd:PRK05480  77 ALKAGKAIEIPVYDYTEHTRSKETIRVEPKDVIILEGILLLEDERLRDLMDIKIFVDTPLDIRLIRRLKRDVNERGRSLE 156
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 489126981 163 SVMAQYQKTVRPMFLQFIEPSKQYADIIVPRGGKNRIAIDILKAKISQFFE 213
Cdd:PRK05480 157 SVINQYLSTVRPMHLQFIEPSKRYADIIIPEGGKNRVAIDILKAKIRQLLE 207
 
Name Accession Description Interval E-value
PRK05480 PRK05480
uridine/cytidine kinase; Provisional
3-213 1.02e-146

uridine/cytidine kinase; Provisional


Pssm-ID: 235492 [Multi-domain]  Cd Length: 209  Bit Score: 406.47  E-value: 1.02e-146
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126981   3 DQSHQCVIIGIAGASASGKSLIASTLYRELreqvGDEHIGVIPEDSYYKDQSHLSMEERVKTNYDHPNAMDHSLLFQHLQ 82
Cdd:PRK05480   1 MMMKKPIIIGIAGGSGSGKTTVASTIYEEL----GDESIAVIPQDSYYKDQSHLSFEERVKTNYDHPDAFDHDLLIEHLK 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126981  83 TLKRGSAIELPVYSYVEHTRTQDTIHIEPKKVIILEGILLLTDARLRDEMNFSIFVDTPLDICLMRRIKRDVNERGRSMD 162
Cdd:PRK05480  77 ALKAGKAIEIPVYDYTEHTRSKETIRVEPKDVIILEGILLLEDERLRDLMDIKIFVDTPLDIRLIRRLKRDVNERGRSLE 156
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 489126981 163 SVMAQYQKTVRPMFLQFIEPSKQYADIIVPRGGKNRIAIDILKAKISQFFE 213
Cdd:PRK05480 157 SVINQYLSTVRPMHLQFIEPSKRYADIIIPEGGKNRVAIDILKAKIRQLLE 207
udk TIGR00235
uridine kinase; Model contains a number of longer eukaryotic proteins and starts bringing in ...
1-213 5.07e-121

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: 341.68  E-value: 5.07e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126981    1 MTDQShqCVIIGIAGASASGKSliasTLYRELREQVGDEHIGVIPEDSYYKDQSHLSMEERVKTNYDHPNAMDHSLLFQH 80
Cdd:TIGR00235   1 MDKPK--GIIIGIGGGSGSGKT----TVARKIYEQLGKLEIVIISQDNYYKDQSHLEMAERKKTNFDHPDAFDNDLLYEH 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126981   81 LQTLKRGSAIELPVYSYVEHTRTQDTIHIEPKKVIILEGILLLTDARLRDEMNFSIFVDTPLDICLMRRIKRDVNERGRS 160
Cdd:TIGR00235  75 LKNLKNGSPIDVPVYDYVNHTRPKETVHIEPKDVVILEGIMPLFDERLRDLMDLKIFVDTPLDIRLIRRIERDINERGRS 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 489126981  161 MDSVMAQYQKTVRPMFLQFIEPSKQYADIIVPRGGKNRIAIDILKAKISQFFE 213
Cdd:TIGR00235 155 LDSVIDQYRKTVRPMYEQFVEPTKQYADLIIPEGGRNEVAINVLDTKIKHLLE 207
UMPK cd02023
Uridine monophosphate kinase (UMPK, EC 2.7.1.48), also known as uridine kinase or ...
10-208 3.81e-102

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: 293.31  E-value: 3.81e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126981  10 IIGIAGASASGKSliasTLYRELREQVGDEHIGVIPEDSYYKDQSHLSMEERVKTNYDHPNAMDHSLLFQHLQTLKRGSA 89
Cdd:cd02023    1 IIGIAGGSGSGKT----TVAEEIIEQLGNPKVVIISQDSYYKDLSHEELEERKNNNYDHPDAFDFDLLISHLQDLKNGKS 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126981  90 IELPVYSYVEHTRTQDTIHIEPKKVIILEGILLLTDARLRDEMNFSIFVDTPLDICLMRRIKRDVNERGRSMDSVMAQYQ 169
Cdd:cd02023   77 VEIPVYDFKTHSRLKETVTVYPADVIILEGILALYDKELRDLMDLKIFVDTDADVRLIRRIERDIVERGRDLESVINQYL 156
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 489126981 170 KTVRPMFLQFIEPSKQYADIIVPRGGKNRIAIDILKAKI 208
Cdd:cd02023  157 KFVKPMHEQFIEPTKRYADVIIPRGGDNHVAIDLIVQHI 195
Udk COG0572
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway ...
2-210 1.74e-98

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: 284.43  E-value: 1.74e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126981   2 TDQSHQCVIIGIAGASASGKSLIAstlyRELREQVGDEHIGVIPEDSYYKDQSHLSMEERVKTNYDHPNAMDHSLLFQHL 81
Cdd:COG0572    1 AARSGKPRIIGIAGPSGSGKTTFA----RRLAEQLGADKVVVISLDDYYKDREHLPLDERGKPNFDHPEAFDLDLLNEHL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126981  82 QTLKRGSAIELPVYSYVEHTRTQDTIHIEPKKVIILEGILLLTDARLRDEMNFSIFVDTPLDICLMRRIKRDVNERGRSM 161
Cdd:COG0572   77 EPLKAGESVELPVYDFATGTRSGETVKVEPADVIIVEGIHALNDELLRDLLDLKIYVDADTDVRLIRRIVRDGEERGRTA 156
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 489126981 162 DSVMAQYQKTVRPMFLQFIEPSKQYADIIVPRGG-KNRIAIDILKAKISQ 210
Cdd:COG0572  157 ESVIEQYWATVRPGHEQYIEPTKEYADIVIPNGGpLNPVALDLLVARLLS 206
PRK pfam00485
Phosphoribulokinase / Uridine kinase family; This family matches three types of P-loop ...
10-200 1.44e-49

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: 159.87  E-value: 1.44e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126981   10 IIGIAGASASGKS----LIASTLYRELREQVGDEHIGVIPEDSYYKDQSHLSMEERVKTNYDH--PNAMDHSLLFQHLQT 83
Cdd:pfam00485   1 VIGVAGSSGSGKTtvarRIVSIFGREGVPAVGIEGDSFHSTDRFYMDLHPEDRKRAGNNGYSFdgPEANDFDLLYEQFKE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126981   84 LKRGSAIELPVYSYVEHTRTQDTIHIEPKKVIILEGILLLTDARLRDEMNFSIFVDTPLDICLMRRIKRDVNERGRSMDS 163
Cdd:pfam00485  81 LKEGGSVDKPIYNHVTHERDPTPELIEGADVLVIEGLHALYDERVAQLLDLKIYVDPDIDLELARKIQRDMAERGHSLEG 160
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 489126981  164 VMAQYQKtVRPMFLQFIEPSKQYADIIVPRGGKNRIA 200
Cdd:pfam00485 161 VTDSILF-RKPDYVNYIDPQFSYADLIIQRVPTNDTA 196
 
Name Accession Description Interval E-value
PRK05480 PRK05480
uridine/cytidine kinase; Provisional
3-213 1.02e-146

uridine/cytidine kinase; Provisional


Pssm-ID: 235492 [Multi-domain]  Cd Length: 209  Bit Score: 406.47  E-value: 1.02e-146
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126981   3 DQSHQCVIIGIAGASASGKSLIASTLYRELreqvGDEHIGVIPEDSYYKDQSHLSMEERVKTNYDHPNAMDHSLLFQHLQ 82
Cdd:PRK05480   1 MMMKKPIIIGIAGGSGSGKTTVASTIYEEL----GDESIAVIPQDSYYKDQSHLSFEERVKTNYDHPDAFDHDLLIEHLK 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126981  83 TLKRGSAIELPVYSYVEHTRTQDTIHIEPKKVIILEGILLLTDARLRDEMNFSIFVDTPLDICLMRRIKRDVNERGRSMD 162
Cdd:PRK05480  77 ALKAGKAIEIPVYDYTEHTRSKETIRVEPKDVIILEGILLLEDERLRDLMDIKIFVDTPLDIRLIRRLKRDVNERGRSLE 156
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 489126981 163 SVMAQYQKTVRPMFLQFIEPSKQYADIIVPRGGKNRIAIDILKAKISQFFE 213
Cdd:PRK05480 157 SVINQYLSTVRPMHLQFIEPSKRYADIIIPEGGKNRVAIDILKAKIRQLLE 207
udk TIGR00235
uridine kinase; Model contains a number of longer eukaryotic proteins and starts bringing in ...
1-213 5.07e-121

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: 341.68  E-value: 5.07e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126981    1 MTDQShqCVIIGIAGASASGKSliasTLYRELREQVGDEHIGVIPEDSYYKDQSHLSMEERVKTNYDHPNAMDHSLLFQH 80
Cdd:TIGR00235   1 MDKPK--GIIIGIGGGSGSGKT----TVARKIYEQLGKLEIVIISQDNYYKDQSHLEMAERKKTNFDHPDAFDNDLLYEH 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126981   81 LQTLKRGSAIELPVYSYVEHTRTQDTIHIEPKKVIILEGILLLTDARLRDEMNFSIFVDTPLDICLMRRIKRDVNERGRS 160
Cdd:TIGR00235  75 LKNLKNGSPIDVPVYDYVNHTRPKETVHIEPKDVVILEGIMPLFDERLRDLMDLKIFVDTPLDIRLIRRIERDINERGRS 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 489126981  161 MDSVMAQYQKTVRPMFLQFIEPSKQYADIIVPRGGKNRIAIDILKAKISQFFE 213
Cdd:TIGR00235 155 LDSVIDQYRKTVRPMYEQFVEPTKQYADLIIPEGGRNEVAINVLDTKIKHLLE 207
UMPK cd02023
Uridine monophosphate kinase (UMPK, EC 2.7.1.48), also known as uridine kinase or ...
10-208 3.81e-102

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: 293.31  E-value: 3.81e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126981  10 IIGIAGASASGKSliasTLYRELREQVGDEHIGVIPEDSYYKDQSHLSMEERVKTNYDHPNAMDHSLLFQHLQTLKRGSA 89
Cdd:cd02023    1 IIGIAGGSGSGKT----TVAEEIIEQLGNPKVVIISQDSYYKDLSHEELEERKNNNYDHPDAFDFDLLISHLQDLKNGKS 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126981  90 IELPVYSYVEHTRTQDTIHIEPKKVIILEGILLLTDARLRDEMNFSIFVDTPLDICLMRRIKRDVNERGRSMDSVMAQYQ 169
Cdd:cd02023   77 VEIPVYDFKTHSRLKETVTVYPADVIILEGILALYDKELRDLMDLKIFVDTDADVRLIRRIERDIVERGRDLESVINQYL 156
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 489126981 170 KTVRPMFLQFIEPSKQYADIIVPRGGKNRIAIDILKAKI 208
Cdd:cd02023  157 KFVKPMHEQFIEPTKRYADVIIPRGGDNHVAIDLIVQHI 195
Udk COG0572
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway ...
2-210 1.74e-98

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: 284.43  E-value: 1.74e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126981   2 TDQSHQCVIIGIAGASASGKSLIAstlyRELREQVGDEHIGVIPEDSYYKDQSHLSMEERVKTNYDHPNAMDHSLLFQHL 81
Cdd:COG0572    1 AARSGKPRIIGIAGPSGSGKTTFA----RRLAEQLGADKVVVISLDDYYKDREHLPLDERGKPNFDHPEAFDLDLLNEHL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126981  82 QTLKRGSAIELPVYSYVEHTRTQDTIHIEPKKVIILEGILLLTDARLRDEMNFSIFVDTPLDICLMRRIKRDVNERGRSM 161
Cdd:COG0572   77 EPLKAGESVELPVYDFATGTRSGETVKVEPADVIIVEGIHALNDELLRDLLDLKIYVDADTDVRLIRRIVRDGEERGRTA 156
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 489126981 162 DSVMAQYQKTVRPMFLQFIEPSKQYADIIVPRGG-KNRIAIDILKAKISQ 210
Cdd:COG0572  157 ESVIEQYWATVRPGHEQYIEPTKEYADIVIPNGGpLNPVALDLLVARLLS 206
PTZ00301 PTZ00301
uridine kinase; Provisional
8-213 1.54e-74

uridine kinase; Provisional


Pssm-ID: 140322 [Multi-domain]  Cd Length: 210  Bit Score: 224.11  E-value: 1.54e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126981   8 CVIIGIAGASASGKSLIASTLYRELREQVGDEHIGVIPEDSYYKDQSHLSMEERVKTNYDHPNAMDHSLLFQHLQTLKRG 87
Cdd:PTZ00301   3 CTVIGISGASGSGKSSLSTNIVSELMAHCGPVSIGVICEDFYYRDQSNIPESERAYTNYDHPKSLEHDLLTTHLRELKSG 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126981  88 SAIELPVYSYVEHTRTQDTIHIEPKKVIILEGILLLTDARLRDEMNFSIFVDTPLDICLMRRIKRDVNERGRSMDSVMAQ 167
Cdd:PTZ00301  83 KTVQIPQYDYVHHTRSDTAVTMTPKSVLIVEGILLFTNAELRNEMDCLIFVDTPLDICLIRRAKRDMRERGRTFESVIEQ 162
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 489126981 168 YQKTVRPMFLQFIEPSKQYADIIVPRGGKNRIAIDILKAKISQFFE 213
Cdd:PTZ00301 163 YEATVRPMYYAYVEPSKVYADIIVPSWKDNSVAVGVLRAKLNHDLE 208
PRK pfam00485
Phosphoribulokinase / Uridine kinase family; This family matches three types of P-loop ...
10-200 1.44e-49

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: 159.87  E-value: 1.44e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126981   10 IIGIAGASASGKS----LIASTLYRELREQVGDEHIGVIPEDSYYKDQSHLSMEERVKTNYDH--PNAMDHSLLFQHLQT 83
Cdd:pfam00485   1 VIGVAGSSGSGKTtvarRIVSIFGREGVPAVGIEGDSFHSTDRFYMDLHPEDRKRAGNNGYSFdgPEANDFDLLYEQFKE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126981   84 LKRGSAIELPVYSYVEHTRTQDTIHIEPKKVIILEGILLLTDARLRDEMNFSIFVDTPLDICLMRRIKRDVNERGRSMDS 163
Cdd:pfam00485  81 LKEGGSVDKPIYNHVTHERDPTPELIEGADVLVIEGLHALYDERVAQLLDLKIYVDPDIDLELARKIQRDMAERGHSLEG 160
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 489126981  164 VMAQYQKtVRPMFLQFIEPSKQYADIIVPRGGKNRIA 200
Cdd:pfam00485 161 VTDSILF-RKPDYVNYIDPQFSYADLIIQRVPTNDTA 196
PRK07429 PRK07429
phosphoribulokinase; Provisional
1-210 7.00e-37

phosphoribulokinase; Provisional


Pssm-ID: 180975  Cd Length: 327  Bit Score: 130.90  E-value: 7.00e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126981   1 MTDQSHQCVIIGIAGASASGKSliasTLYRELREQVGDEHIGVIPEDSYYKdqshLSMEERVKTNYD--HPNAMDHSLLF 78
Cdd:PRK07429   1 MTSMPDRPVLLGVAGDSGCGKT----TFLRGLADLLGEELVTVICTDDYHS----YDRKQRKELGITalDPRANNLDIMY 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126981  79 QHLQTLKRGSAIELPVYSYveHTRTQDT-IHIEPKKVIILEGILLLTDARLRDEMNFSIFVDTPLDICLMRRIKRDVNER 157
Cdd:PRK07429  73 EHLKALKTGQPILKPIYNH--ETGTFDPpEYIEPNKIVVVEGLHPLYDERVRELYDFKVYLDPPEEVKIAWKIKRDMAKR 150
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 489126981 158 GRSMDSVMAQYQKTvRPMFLQFIEPSKQYADIIV----PRGGKNRIAIDILKAKISQ 210
Cdd:PRK07429 151 GHTYEQVLAEIEAR-EPDFEAYIRPQRQWADVVIqflpTQLIDNDEENKVLRVRLVL 206
PRK cd02026
Phosphoribulokinase (PRK) is an enzyme involved in the Benson-Calvin cycle in chloroplasts or ...
10-191 9.02e-35

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: 124.37  E-value: 9.02e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126981  10 IIGIAGASASGKSliasTLYRELREQVGDEHIGVIPEDSYYKdqshLSMEERVKTNYD--HPNAMDHSLLFQHLQTLKRG 87
Cdd:cd02026    1 IIGVAGDSGCGKS----TFLRRLTSLFGSDLVTVICLDDYHS----LDRKGRKETGITalDPRANNFDLMYEQLKALKEG 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126981  88 SAIELPVYSYVehTRTQDTIH-IEPKKVIILEGILLLTDARLRDEMNFSIFVDTPLDICLMRRIKRDVNERGRSMDSVMA 166
Cdd:cd02026   73 QAIEKPIYNHV--TGLIDPPElIKPTKIVVIEGLHPLYDERVRELLDFSVYLDISDEVKFAWKIQRDMAERGHSLEDVLA 150
                        170       180
                 ....*....|....*....|....*
gi 489126981 167 QYQKTvRPMFLQFIEPSKQYADIIV 191
Cdd:cd02026  151 SIEAR-KPDFEAYIDPQKQYADVVI 174
PLN02348 PLN02348
phosphoribulokinase
7-191 1.07e-27

phosphoribulokinase


Pssm-ID: 215198  Cd Length: 395  Bit Score: 108.01  E-value: 1.07e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126981   7 QCVIIGIAGASASGKSliasTLYRELREQVGDEHIG-----------------VIPEDSYYKDQSHLSMEERVkTNYDhP 69
Cdd:PLN02348  48 GTVVIGLAADSGCGKS----TFMRRLTSVFGGAAKPpkggnpdsntlisdtttVICLDDYHSLDRTGRKEKGV-TALD-P 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126981  70 NAMDHSLLFQHLQTLKRGSAIELPVYSYVehTRTQDTIH-IEPKKVIILEGILLLTDARLRDEMNFSIFVDTPLDICLMR 148
Cdd:PLN02348 122 RANNFDLMYEQVKALKEGKAVEKPIYNHV--TGLLDPPElIEPPKILVIEGLHPMYDERVRDLLDFSIYLDISDDVKFAW 199
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 489126981 149 RIKRDVNERGRSMDSVMAQYQKTvRPMFLQFIEPSKQYADIIV 191
Cdd:PLN02348 200 KIQRDMAERGHSLESIKASIEAR-KPDFDAYIDPQKQYADVVI 241
UMPK_like cd02028
Uridine monophosphate kinase_like (UMPK_like) is a family of proteins highly similar to the ...
10-191 3.94e-21

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: 86.21  E-value: 3.94e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126981  10 IIGIAGASASGKSLIASTLYRELREQVGDEHigVIPEDSYYKDQSHLSMEErvkTNYDHPNAMDHSLLFQHLQTLKRGSA 89
Cdd:cd02028    1 VVGIAGPSGSGKTTFAKKLSNQLRVNGIGPV--VISLDDYYVPRKTPRDED---GNYDFESILDLDLLNKNLHDLLNGKE 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126981  90 IELPVYSYVEHTRTQD-TIHIEPKKVIILEGILLLtDARLRDEMNFSIFVDTPLDIC-LMRRIKRDVNERGRSMDSVMAQ 167
Cdd:cd02028   76 VELPIYDFRTGKRRGYrKLKLPPSGVVILEGIYAL-NERLRSLLDIRVAVSGGVHLNrLLRRVVRDIQFRGYSAELTILM 154
                        170       180
                 ....*....|....*....|....
gi 489126981 168 YQktVRPMFLQFIEPSKQYADIIV 191
Cdd:cd02028  155 WP--SVPSGEEFIIPPLQEAAIVM 176
PLN02318 PLN02318
phosphoribulokinase/uridine kinase
9-189 2.89e-19

phosphoribulokinase/uridine kinase


Pssm-ID: 177952 [Multi-domain]  Cd Length: 656  Bit Score: 85.30  E-value: 2.89e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126981   9 VIIGIAGASASGKSLIAstlyrelrEQVGD--EHIGVIPEDSYyKDQSHLsmeerVKTNYDHPNAMDHSLLFQHLQTLKR 86
Cdd:PLN02318  66 ILVGVAGPSGAGKTVFT--------EKVLNfmPSIAVISMDNY-NDSSRI-----IDGNFDDPRLTDYDTLLDNIHDLKA 131
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126981  87 GSAIELPVYSYVEHTRT-QDTIHIEPKKVIILEGILLLTDaRLRDEMNFSIFVDTPLDICLMRRIKRDVNERGRSMDSVM 165
Cdd:PLN02318 132 GKSVQVPIYDFKSSSRVgYRTLEVPSSRIVIIEGIYALSE-KLRPLLDLRVSVTGGVHFDLVKRVLRDIQRAGQEPEEII 210
                        170       180
                 ....*....|....*....|....
gi 489126981 166 AQYQKTVRPMFLQFIEPSKQYADI 189
Cdd:PLN02318 211 HQISETVYPMYKAFIEPDLQTAHI 234
NRK1 cd02024
Nicotinamide riboside kinase (NRK) is an enzyme involved in the metabolism of nicotinamide ...
10-177 6.33e-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: 64.65  E-value: 6.33e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126981  10 IIGIAGASASGKsliaSTLYRELREQVGDehIGVIPEDSYYKDQSHLSMEERVKTNYDHPNAMDHSLLFQHLQTLKRGSA 89
Cdd:cd02024    1 IVGISGVTNSGK----TTLAKLLQRILPN--CCVIHQDDFFKPEDEIPVDENGFKQWDVLEALDMEAMMSTLDYWRETGH 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126981  90 IELPVYS--------------YVEHTRTQDTIHIEPKKVIILEGILLLTDARLRDEMNFSIFVDTPLDICLMRRIKRD-- 153
Cdd:cd02024   75 FPKFLRShgnendpekefiedAQIEETKADLLGAEDLHILIVDGFLLYNYKPLVDLFDIRYFLRVPYETCKRRREARTgy 154
                        170       180
                 ....*....|....*....|....
gi 489126981 154 VNERGRSMDSVmAQYQKTVRPMFL 177
Cdd:cd02024  155 VTLEGFWPDPP-GYFDGHVWPMYL 177
CoaA COG1072
Panthothenate kinase [Coenzyme transport and metabolism]; Panthothenate kinase is part of the ...
10-143 5.89e-11

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: 60.69  E-value: 5.89e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126981  10 IIGIAGASASGKSLIASTLYRELREQVGDEHIGVIPEDSYYKDQSHLsmEERvktnydhpNAMD----------HSLLfQ 79
Cdd:COG1072   88 IIGIAGSVAVGKSTTARLLQALLSRWPEHPKVELVTTDGFLYPNAVL--ERR--------GLMDrkgfpesydrRGLL-R 156
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489126981  80 HLQTLKRG-SAIELPVYSYVEHTRTQDTIHIEPK-KVIILEGI-LLLTDA----RLRDEMNFSIFVDTPLD 143
Cdd:COG1072  157 FLARVKSGdPEVRAPVYSHLLYDIVPGAIVVVDQpDILIVEGNnVLQDEPnpwlFVSDFFDFSIYVDADEE 227
PRK08233 PRK08233
hypothetical protein; Provisional
10-191 7.98e-08

hypothetical protein; Provisional


Pssm-ID: 181310 [Multi-domain]  Cd Length: 182  Bit Score: 50.51  E-value: 7.98e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126981  10 IIGIAGASASGKSLIASTLYRELREQVG----DEHIGVIPEDsyYKDQSHLSmeervkTNYdhpNAMDHSLLFQHLQTLK 85
Cdd:PRK08233   5 IITIAAVSGGGKTTLTERLTHKLKNSKAlyfdRYDFDNCPED--ICKWIDKG------ANY---SEWVLTPLIKDIQELI 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126981  86 RGSAIELpvysyvehtrtqdtihiepkkvIILEGILLLTDARLRDEMNFSIFVDTPLDICLMRRIKRDVNErgRSMDSV- 164
Cdd:PRK08233  74 AKSNVDY----------------------IIVDYPFAYLNSEMRQFIDVTIFIDTPLDIAMARRILRDFKE--DTGNEIh 129
                        170       180
                 ....*....|....*....|....*....
gi 489126981 165 --MAQYQKTVRPMFLQFIEPSKQYADIIV 191
Cdd:PRK08233 130 ndLKHYLNYARPLYLEALHTVKPNADIVL 158
PRK07667 PRK07667
uridine kinase; Provisional
10-191 1.08e-07

uridine kinase; Provisional


Pssm-ID: 169051  Cd Length: 193  Bit Score: 50.11  E-value: 1.08e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126981  10 IIGIAGASASGKSLIASTLYRELREQVGDEHIgvIPEDSYY---KDQSHLSMEERVKTNYDHpnaMDHSLLFQHL-QTLK 85
Cdd:PRK07667  19 ILGIDGLSRSGKTTFVANLKENMKQEGIPFHI--FHIDDYIverNKRYHTGFEEWYEYYYLQ---WDIEWLRQKFfRKLQ 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126981  86 RGSAIELPVYSYVEHTRTQDTIHIEPKKVIILEGILLLTDaRLRDEMNFSIFVDTPLDIclmrRIKRDVNERGRSMDSVM 165
Cdd:PRK07667  94 NETKLTLPFYHDETDTCEMKKVQIPIVGVIVIEGVFLQRK-EWRDFFHYMVYLDCPRET----RFLRESEETQKNLSKFK 168
                        170       180
                 ....*....|....*....|....*.
gi 489126981 166 AQYQKTvRPMFLQFIEPSKQyADIIV 191
Cdd:PRK07667 169 NRYWKA-EDYYLETESPKDR-ADLVI 192
PRK09270 PRK09270
nucleoside triphosphate hydrolase domain-containing protein; Reviewed
10-152 1.78e-07

nucleoside triphosphate hydrolase domain-containing protein; Reviewed


Pssm-ID: 236442  Cd Length: 229  Bit Score: 49.93  E-value: 1.78e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126981  10 IIGIAGASASGKSLIASTLYRELREQVGDEHIGViPEDSYYKDQSHLsmeERvktnydhpnamdHSLL------------ 77
Cdd:PRK09270  35 IVGIAGPPGAGKSTLAEFLEALLQQDGELPAIQV-PMDGFHLDNAVL---DA------------HGLRprkgapetfdva 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126981  78 -FQH-LQTLKRG-SAIELPVYSYVEHTRTQDTIHIEP-KKVIILEG-ILLLTD---ARLRDEMNFSIFVDTPLDICLMRR 149
Cdd:PRK09270  99 gLAAlLRRLRAGdDEVYWPVFDRSLEDPVADAIVVPPtARLVIVEGnYLLLDEepwRRLAGLFDFTIFLDAPAEVLRERL 178

                 ...
gi 489126981 150 IKR 152
Cdd:PRK09270 179 VAR 181
PanK cd02025
Pantothenate kinase (PanK) catalyzes the phosphorylation of pantothenic acid to form 4 ...
10-194 1.68e-06

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: 46.92  E-value: 1.68e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126981  10 IIGIAGASASGKSLIASTLYRELREQVGDEHIGVIPEDSYYKDQSHLsMEERVKTNYDHPNAMDHSLLFQHLQTLKRG-S 88
Cdd:cd02025    1 IIGIAGSVAVGKSTTARVLQALLSRWPDHPNVELITTDGFLYPNKEL-IERGLMDRKGFPESYDMEALLKFLKDIKSGkK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126981  89 AIELPVYSYVEHTRTQDTI-HIEPKKVIILEGILLLTDARLR-----DEMNFSIFVDTPLDICLMRRIKRDVNER---GR 159
Cdd:cd02025   80 NVKIPVYSHLTYDVIPGEKqTVDQPDILIIEGLNVLQTGQNPrlfvsDFFDFSIYVDADEDDIEKWYIKRFLKLRetaFS 159
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 489126981 160 SMDSVMAQYQK---------------TV-RPMFLQFIEPSKQYADIIVPRG 194
Cdd:cd02025  160 DPDSYFHRYAKmseeeaiafarevwkNInLKNLRENILPTRNRADLILEKG 210
PRK06696 PRK06696
uridine kinase; Validated
104-191 1.33e-05

uridine kinase; Validated


Pssm-ID: 180660  Cd Length: 223  Bit Score: 44.58  E-value: 1.33e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126981 104 QDTIHIEPKKVIILEGILLLTDaRLRDEMNFSIFVDTPLDICLMRRIKRDVNERGrSMDSVMAQYQKTVRPMFLQFIE-- 181
Cdd:PRK06696 120 NPPLLAAPNAVLIVDGTFLLRP-ELRDLWDYKIFLDTDFEVSRRRGAKRDTEAFG-SYEEAEKMYLARYHPAQKLYIAea 197
                         90
                 ....*....|.
gi 489126981 182 -PsKQYADIIV 191
Cdd:PRK06696 198 nP-KERADVVI 207
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH