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Conserved domains on  [gi|1958672567|ref|XP_038946718|]
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uridine-cytidine kinase 2 isoform X1 [Rattus norvegicus]

Protein Classification

uridine-cytidine kinase( domain architecture ID 10113977)

uridine-cytidine kinase (UCK) catalyzes the phosphorylation of uridine and cytidine as well as the pharmacological activation of several cytotoxic pyrimidine ribonucleoside analogues

CATH:  3.40.50.300
EC:  2.7.1.48
Gene Ontology:  GO:0044206|GO:0043771|GO:0005524|GO:0004849|GO:0044211
SCOP:  4003940

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
UMPK cd02023
Uridine monophosphate kinase (UMPK, EC 2.7.1.48), also known as uridine kinase or ...
 38-234 5.15e-107

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: 307.94  E-value: 5.15e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672567  38 GMSSVCAKIVQLLGQnevdyhqKQVVILSQDSFYRVLTSEQKAKALKgqFNFDHPDAFDNELIFKTLKEITEGKTVQIPV 117
Cdd:cd02023    11 GKTTVAEEIIEQLGN-------PKVVIISQDSYYKDLSHEELEERKN--NNYDHPDAFDFDLLISHLQDLKNGKSVEIPV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672567 118 YDFVSHSRKEETVTIYPADVVLFEGILAFYSQEVRDLFQMKLFVDTDADTRLSRRVLRDISERGRDLEQILSQYITFVKP 197
Cdd:cd02023    82 YDFKTHSRLKETVTVYPADVIILEGILALYDKELRDLMDLKIFVDTDADVRLIRRIERDIVERGRDLESVINQYLKFVKP 161

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1958672567 198 AFEEFCLPTKKYADVIIPRGADNLVAINLIVQHIQDI 234
Cdd:cd02023   162 MHEQFIEPTKRYADVIIPRGGDNHVAIDLIVQHIKSK 198
 
Name Accession Description Interval E-value
UMPK cd02023
Uridine monophosphate kinase (UMPK, EC 2.7.1.48), also known as uridine kinase or ...
 38-234 5.15e-107

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: 307.94  E-value: 5.15e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672567  38 GMSSVCAKIVQLLGQnevdyhqKQVVILSQDSFYRVLTSEQKAKALKgqFNFDHPDAFDNELIFKTLKEITEGKTVQIPV 117
Cdd:cd02023    11 GKTTVAEEIIEQLGN-------PKVVIISQDSYYKDLSHEELEERKN--NNYDHPDAFDFDLLISHLQDLKNGKSVEIPV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672567 118 YDFVSHSRKEETVTIYPADVVLFEGILAFYSQEVRDLFQMKLFVDTDADTRLSRRVLRDISERGRDLEQILSQYITFVKP 197
Cdd:cd02023    82 YDFKTHSRLKETVTVYPADVIILEGILALYDKELRDLMDLKIFVDTDADVRLIRRIERDIVERGRDLESVINQYLKFVKP 161

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1958672567 198 AFEEFCLPTKKYADVIIPRGADNLVAINLIVQHIQDI 234
Cdd:cd02023   162 MHEQFIEPTKRYADVIIPRGGDNHVAIDLIVQHIKSK 198
PRK05480 PRK05480
uridine/cytidine kinase; Provisional
 38-237 1.01e-81

uridine/cytidine kinase; Provisional


Pssm-ID: 235492 [Multi-domain]  Cd Length: 209  Bit Score: 244.30  E-value: 1.01e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672567  38 GMSSVCAKIVQLLGQNevdyhqkQVVILSQDSFYR---VLTSEQKAKalkgqFNFDHPDAFDNELIFKTLKEITEGKTVQ 114
Cdd:PRK05480   18 GKTTVASTIYEELGDE-------SIAVIPQDSYYKdqsHLSFEERVK-----TNYDHPDAFDHDLLIEHLKALKAGKAIE 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672567 115 IPVYDFVSHSRKEETVTIYPADVVLFEGILAFYSQEVRDLFQMKLFVDTDADTRLSRRVLRDISERGRDLEQILSQYITF 194
Cdd:PRK05480   86 IPVYDYTEHTRSKETIRVEPKDVIILEGILLLEDERLRDLMDIKIFVDTPLDIRLIRRLKRDVNERGRSLESVINQYLST 165

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1958672567 195 VKPAFEEFCLPTKKYADVIIPRGADNLVAINLIVQHIQDILNG 237
Cdd:PRK05480  166 VRPMHLQFIEPSKRYADIIIPEGGKNRVAIDILKAKIRQLLEK 208
udk TIGR00235
uridine kinase; Model contains a number of longer eukaryotic proteins and starts bringing in ...
 29-236 1.14e-73

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: 223.80  E-value: 1.14e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672567  29 GAACGrwrgGMSSVCAKIVQLLGQNEVdyhqkqvVILSQDSFYRVLtsEQKAKALKGQFNFDHPDAFDNELIFKTLKEIT 108
Cdd:TIGR00235  13 GGSGS----GKTTVARKIYEQLGKLEI-------VIISQDNYYKDQ--SHLEMAERKKTNFDHPDAFDNDLLYEHLKNLK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672567 109 EGKTVQIPVYDFVSHSRKEETVTIYPADVVLFEGILAFYSQEVRDLFQMKLFVDTDADTRLSRRVLRDISERGRDLEQIL 188
Cdd:TIGR00235  80 NGSPIDVPVYDYVNHTRPKETVHIEPKDVVILEGIMPLFDERLRDLMDLKIFVDTPLDIRLIRRIERDINERGRSLDSVI 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1958672567 189 SQYITFVKPAFEEFCLPTKKYADVIIPRGADNLVAINLIVQHIQDILN 236
Cdd:TIGR00235 160 DQYRKTVRPMYEQFVEPTKQYADLIIPEGGRNEVAINVLDTKIKHLLE 207
Udk COG0572
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway ...
 40-233 1.15e-68

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: 210.85  E-value: 1.15e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672567  40 SSVCAKIVQLLGQNEVdyhqkqvVILSQDSFYRVLtsEQKAKALKGQFNFDHPDAFDNELIFKTLKEITEGKTVQIPVYD 119
Cdd:COG0572    21 TTFARRLAEQLGADKV-------VVISLDDYYKDR--EHLPLDERGKPNFDHPEAFDLDLLNEHLEPLKAGESVELPVYD 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672567 120 FVSHSRKEETVTIYPADVVLFEGILAFYSQEVRDLFQMKLFVDTDADTRLSRRVLRDISERGRDLEQILSQYITFVKPAF 199
Cdd:COG0572    92 FATGTRSGETVKVEPADVIIVEGIHALNDELLRDLLDLKIYVDADTDVRLIRRIVRDGEERGRTAESVIEQYWATVRPGH 171

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1958672567 200 EEFCLPTKKYADVIIPRG-ADNLVAINLIVQHIQD 233
Cdd:COG0572   172 EQYIEPTKEYADIVIPNGgPLNPVALDLLVARLLS 206
PRK pfam00485
Phosphoribulokinase / Uridine kinase family; This family matches three types of P-loop ...
 38-223 1.79e-56

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: 179.52  E-value: 1.79e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672567  38 GMSSVCAKIVQLLGQNEVDYHQKQ-VVILSQDSFYRVLTSEQKAKALKGQFNFDHPDAFDNELIFKTLKEITEGKTVQIP 116
Cdd:pfam00485  11 GKTTVARRIVSIFGREGVPAVGIEgDSFHSTDRFYMDLHPEDRKRAGNNGYSFDGPEANDFDLLYEQFKELKEGGSVDKP 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672567 117 VYDFVSHSRKEETVTIYPADVVLFEGILAFYSQEVRDLFQMKLFVDTDADTRLSRRVLRDISERGRDLEQILSQYItFVK 196
Cdd:pfam00485  91 IYNHVTHERDPTPELIEGADVLVIEGLHALYDERVAQLLDLKIYVDPDIDLELARKIQRDMAERGHSLEGVTDSIL-FRK 169

                         170       180
                  ....*....|....*....|....*..
gi 1958672567 197 PAFEEFCLPTKKYADVIIPRGADNLVA 223
Cdd:pfam00485 170 PDYVNYIDPQFSYADLIIQRVPTNDTA 196
 
Name Accession Description Interval E-value
UMPK cd02023
Uridine monophosphate kinase (UMPK, EC 2.7.1.48), also known as uridine kinase or ...
 38-234 5.15e-107

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: 307.94  E-value: 5.15e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672567  38 GMSSVCAKIVQLLGQnevdyhqKQVVILSQDSFYRVLTSEQKAKALKgqFNFDHPDAFDNELIFKTLKEITEGKTVQIPV 117
Cdd:cd02023    11 GKTTVAEEIIEQLGN-------PKVVIISQDSYYKDLSHEELEERKN--NNYDHPDAFDFDLLISHLQDLKNGKSVEIPV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672567 118 YDFVSHSRKEETVTIYPADVVLFEGILAFYSQEVRDLFQMKLFVDTDADTRLSRRVLRDISERGRDLEQILSQYITFVKP 197
Cdd:cd02023    82 YDFKTHSRLKETVTVYPADVIILEGILALYDKELRDLMDLKIFVDTDADVRLIRRIERDIVERGRDLESVINQYLKFVKP 161

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1958672567 198 AFEEFCLPTKKYADVIIPRGADNLVAINLIVQHIQDI 234
Cdd:cd02023   162 MHEQFIEPTKRYADVIIPRGGDNHVAIDLIVQHIKSK 198
PRK05480 PRK05480
uridine/cytidine kinase; Provisional
 38-237 1.01e-81

uridine/cytidine kinase; Provisional


Pssm-ID: 235492 [Multi-domain]  Cd Length: 209  Bit Score: 244.30  E-value: 1.01e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672567  38 GMSSVCAKIVQLLGQNevdyhqkQVVILSQDSFYR---VLTSEQKAKalkgqFNFDHPDAFDNELIFKTLKEITEGKTVQ 114
Cdd:PRK05480   18 GKTTVASTIYEELGDE-------SIAVIPQDSYYKdqsHLSFEERVK-----TNYDHPDAFDHDLLIEHLKALKAGKAIE 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672567 115 IPVYDFVSHSRKEETVTIYPADVVLFEGILAFYSQEVRDLFQMKLFVDTDADTRLSRRVLRDISERGRDLEQILSQYITF 194
Cdd:PRK05480   86 IPVYDYTEHTRSKETIRVEPKDVIILEGILLLEDERLRDLMDIKIFVDTPLDIRLIRRLKRDVNERGRSLESVINQYLST 165

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1958672567 195 VKPAFEEFCLPTKKYADVIIPRGADNLVAINLIVQHIQDILNG 237
Cdd:PRK05480  166 VRPMHLQFIEPSKRYADIIIPEGGKNRVAIDILKAKIRQLLEK 208
udk TIGR00235
uridine kinase; Model contains a number of longer eukaryotic proteins and starts bringing in ...
 29-236 1.14e-73

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: 223.80  E-value: 1.14e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672567  29 GAACGrwrgGMSSVCAKIVQLLGQNEVdyhqkqvVILSQDSFYRVLtsEQKAKALKGQFNFDHPDAFDNELIFKTLKEIT 108
Cdd:TIGR00235  13 GGSGS----GKTTVARKIYEQLGKLEI-------VIISQDNYYKDQ--SHLEMAERKKTNFDHPDAFDNDLLYEHLKNLK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672567 109 EGKTVQIPVYDFVSHSRKEETVTIYPADVVLFEGILAFYSQEVRDLFQMKLFVDTDADTRLSRRVLRDISERGRDLEQIL 188
Cdd:TIGR00235  80 NGSPIDVPVYDYVNHTRPKETVHIEPKDVVILEGIMPLFDERLRDLMDLKIFVDTPLDIRLIRRIERDINERGRSLDSVI 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1958672567 189 SQYITFVKPAFEEFCLPTKKYADVIIPRGADNLVAINLIVQHIQDILN 236
Cdd:TIGR00235 160 DQYRKTVRPMYEQFVEPTKQYADLIIPEGGRNEVAINVLDTKIKHLLE 207
Udk COG0572
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway ...
 40-233 1.15e-68

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: 210.85  E-value: 1.15e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672567  40 SSVCAKIVQLLGQNEVdyhqkqvVILSQDSFYRVLtsEQKAKALKGQFNFDHPDAFDNELIFKTLKEITEGKTVQIPVYD 119
Cdd:COG0572    21 TTFARRLAEQLGADKV-------VVISLDDYYKDR--EHLPLDERGKPNFDHPEAFDLDLLNEHLEPLKAGESVELPVYD 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672567 120 FVSHSRKEETVTIYPADVVLFEGILAFYSQEVRDLFQMKLFVDTDADTRLSRRVLRDISERGRDLEQILSQYITFVKPAF 199
Cdd:COG0572    92 FATGTRSGETVKVEPADVIIVEGIHALNDELLRDLLDLKIYVDADTDVRLIRRIVRDGEERGRTAESVIEQYWATVRPGH 171

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1958672567 200 EEFCLPTKKYADVIIPRG-ADNLVAINLIVQHIQD 233
Cdd:COG0572   172 EQYIEPTKEYADIVIPNGgPLNPVALDLLVARLLS 206
PRK pfam00485
Phosphoribulokinase / Uridine kinase family; This family matches three types of P-loop ...
 38-223 1.79e-56

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: 179.52  E-value: 1.79e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672567  38 GMSSVCAKIVQLLGQNEVDYHQKQ-VVILSQDSFYRVLTSEQKAKALKGQFNFDHPDAFDNELIFKTLKEITEGKTVQIP 116
Cdd:pfam00485  11 GKTTVARRIVSIFGREGVPAVGIEgDSFHSTDRFYMDLHPEDRKRAGNNGYSFDGPEANDFDLLYEQFKELKEGGSVDKP 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672567 117 VYDFVSHSRKEETVTIYPADVVLFEGILAFYSQEVRDLFQMKLFVDTDADTRLSRRVLRDISERGRDLEQILSQYItFVK 196
Cdd:pfam00485  91 IYNHVTHERDPTPELIEGADVLVIEGLHALYDERVAQLLDLKIYVDPDIDLELARKIQRDMAERGHSLEGVTDSIL-FRK 169

                         170       180
                  ....*....|....*....|....*..
gi 1958672567 197 PAFEEFCLPTKKYADVIIPRGADNLVA 223
Cdd:pfam00485 170 PDYVNYIDPQFSYADLIIQRVPTNDTA 196
PTZ00301 PTZ00301
uridine kinase; Provisional
 88-237 5.19e-36

uridine kinase; Provisional


Pssm-ID: 140322 [Multi-domain]  Cd Length: 210  Bit Score: 127.43  E-value: 5.19e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672567  88 NFDHPDAFDNELIFKTLKEITEGKTVQIPVYDFVSHSRKEETVTIYPADVVLFEGILAFYSQEVRDLFQMKLFVDTDADT 167
Cdd:PTZ00301   60 NYDHPKSLEHDLLTTHLRELKSGKTVQIPQYDYVHHTRSDTAVTMTPKSVLIVEGILLFTNAELRNEMDCLIFVDTPLDI 139

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672567 168 RLSRRVLRDISERGRDLEQILSQYITFVKPAFEEFCLPTKKYADVIIPRGADNLVAINLIVQHIQDILNG 237
Cdd:PTZ00301  140 CLIRRAKRDMRERGRTFESVIEQYEATVRPMYYAYVEPSKVYADIIVPSWKDNSVAVGVLRAKLNHDLEN 209
PLN02348 PLN02348
phosphoribulokinase
 91-214 7.17e-23

phosphoribulokinase


Pssm-ID: 215198  Cd Length: 395  Bit Score: 96.45  E-value: 7.17e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672567  91 HPDAFDNELIFKTLKEITEGKTVQIPVYDFVShSRKEETVTIYPADVVLFEGILAFYSQEVRDLFQMKLFVDTDADTRLS 170
Cdd:PLN02348  120 DPRANNFDLMYEQVKALKEGKAVEKPIYNHVT-GLLDPPELIEPPKILVIEGLHPMYDERVRDLLDFSIYLDISDDVKFA 198

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1958672567 171 RRVLRDISERGRDLEQILSQyITFVKPAFEEFCLPTKKYADVII 214
Cdd:PLN02348  199 WKIQRDMAERGHSLESIKAS-IEARKPDFDAYIDPQKQYADVVI 241
PRK cd02026
Phosphoribulokinase (PRK) is an enzyme involved in the Benson-Calvin cycle in chloroplasts or ...
 91-214 5.04e-21

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: 89.32  E-value: 5.04e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672567  91 HPDAFDNELIFKTLKEITEGKTVQIPVYDFVSHS-RKEETvtIYPADVVLFEGILAFYSQEVRDLFQMKLFVDTDADTRL 169
Cdd:cd02026    53 DPRANNFDLMYEQLKALKEGQAIEKPIYNHVTGLiDPPEL--IKPTKIVVIEGLHPLYDERVRELLDFSVYLDISDEVKF 130

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1958672567 170 SRRVLRDISERGRDLEQILSQyITFVKPAFEEFCLPTKKYADVII 214
Cdd:cd02026   131 AWKIQRDMAERGHSLEDVLAS-IEARKPDFEAYIDPQKQYADVVI 174
UMPK_like cd02028
Uridine monophosphate kinase_like (UMPK_like) is a family of proteins highly similar to the ...
 61-202 5.91e-19

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: 81.58  E-value: 5.91e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672567  61 QVVILSQDSFYRVLTSEQKAkalkgQFNFDHPDAFDNELIFKTLKEITEGKTVQIPVYDFVSHSRK-EETVTIYPADVVL 139
Cdd:cd02028    29 GPVVISLDDYYVPRKTPRDE-----DGNYDFESILDLDLLNKNLHDLLNGKEVELPIYDFRTGKRRgYRKLKLPPSGVVI 103

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958672567 140 FEGILAFySQEVRDLFQMKLFVDT-DADTRLSRRVLRDISERGRDLEQILSQYITFvkPAFEEF 202
Cdd:cd02028   104 LEGIYAL-NERLRSLLDIRVAVSGgVHLNRLLRRVVRDIQFRGYSAELTILMWPSV--PSGEEF 164
PRK07429 PRK07429
phosphoribulokinase; Provisional
 24-214 8.93e-18

phosphoribulokinase; Provisional


Pssm-ID: 180975  Cd Length: 327  Bit Score: 81.21  E-value: 8.93e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672567  24 RPRKLG----AACGRwrggmSSVCAKIVQLLGQNEV------DYHQkqvvilsqdsfyrvLTSEQKAK----ALkgqfnf 89
Cdd:PRK07429    7 RPVLLGvagdSGCGK-----TTFLRGLADLLGEELVtvictdDYHS--------------YDRKQRKElgitAL------ 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672567  90 dHPDAFDNELIFKTLKEITEGKTVQIPVYDfvsHSRK--EETVTIYPADVVLFEGILAFYSQEVRDLFQMKLFVDTDADT 167
Cdd:PRK07429   62 -DPRANNLDIMYEHLKALKTGQPILKPIYN---HETGtfDPPEYIEPNKIVVVEGLHPLYDERVRELYDFKVYLDPPEEV 137

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1958672567 168 RLSRRVLRDISERGRDLEQILSQyITFVKPAFEEFCLPTKKYADVII 214
Cdd:PRK07429  138 KIAWKIKRDMAKRGHTYEQVLAE-IEAREPDFEAYIRPQRQWADVVI 183
PLN02318 PLN02318
phosphoribulokinase/uridine kinase
 88-214 8.82e-15

phosphoribulokinase/uridine kinase


Pssm-ID: 177952 [Multi-domain]  Cd Length: 656  Bit Score: 73.74  E-value: 8.82e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672567  88 NFDHPDAFDNELIFKTLKEITEGKTVQIPVYDFVSHSR-KEETVTIYPADVVLFEGILAFySQEVRDLFQMKLFVDTDAD 166
Cdd:PLN02318  110 NFDDPRLTDYDTLLDNIHDLKAGKSVQVPIYDFKSSSRvGYRTLEVPSSRIVIIEGIYAL-SEKLRPLLDLRVSVTGGVH 188

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1958672567 167 TRLSRRVLRDISERGRDLEQILSQYITFVKPAFEEFCLPTKKYADVII 214
Cdd:PLN02318  189 FDLVKRVLRDIQRAGQEPEEIIHQISETVYPMYKAFIEPDLQTAHIKI 236
PRK08233 PRK08233
hypothetical protein; Provisional
 127-235 7.68e-10

hypothetical protein; Provisional


Pssm-ID: 181310 [Multi-domain]  Cd Length: 182  Bit Score: 56.68  E-value: 7.68e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672567 127 EETVTIYPADVVLFEGILAFYSQEVRDLFQMKLFVDTDADTRLSRRVLRDISER-GRDLEQILSQYITFVKPAFEEFCLP 205
Cdd:PRK08233   70 QELIAKSNVDYIIVDYPFAYLNSEMRQFIDVTIFIDTPLDIAMARRILRDFKEDtGNEIHNDLKHYLNYARPLYLEALHT 149

                          90       100       110
                  ....*....|....*....|....*....|
gi 1958672567 206 TKKYADVIIprgaDNLVAINLIVQHIQDIL 235
Cdd:PRK08233  150 VKPNADIVL----DGALSVEEIINQIEEEL 175
PanK cd02025
Pantothenate kinase (PanK) catalyzes the phosphorylation of pantothenic acid to form 4 ...
 41-222 1.90e-07

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: 50.39  E-value: 1.90e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672567  41 SVCAKIVQLLGQNEVDyhQKQVVILSQDSF-YRVLTSEQKAKALKGQFnfdhPDAFDNELIFKTLKEITEGK-TVQIPVY 118
Cdd:cd02025    13 STTARVLQALLSRWPD--HPNVELITTDGFlYPNKELIERGLMDRKGF----PESYDMEALLKFLKDIKSGKkNVKIPVY 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672567 119 DFVSHSR-KEETVTIYPADVVLFEGILAF-----YSQEVRDLFQMKLFVDTDADtRLSR----RVLRDISERGRDLEQIL 188
Cdd:cd02025    87 SHLTYDViPGEKQTVDQPDILIIEGLNVLqtgqnPRLFVSDFFDFSIYVDADED-DIEKwyikRFLKLRETAFSDPDSYF 165

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1958672567 189 SQY--------ITFVK--------PAFEEFCLPTKKYADVIIPRGADNLV 222
Cdd:cd02025   166 HRYakmseeeaIAFARevwkninlKNLRENILPTRNRADLILEKGADHSI 215
CoaA COG1072
Panthothenate kinase [Coenzyme transport and metabolism]; Panthothenate kinase is part of the ...
 92-222 2.82e-06

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: 47.59  E-value: 2.82e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672567  92 PDAFDNELIFKTLKEITEGK-TVQIPVYDFVSH-SRKEETVTIYPADVVLFEGI--L---AFYSQEVRDLFQMKLFVDTD 164
Cdd:COG1072   146 PESYDRRGLLRFLARVKSGDpEVRAPVYSHLLYdIVPGAIVVVDQPDILIVEGNnvLqdePNPWLFVSDFFDFSIYVDAD 225

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958672567 165 ADTRLSRRV-----LRDISER----------GRDLEQILSQYITFVK----PAFEEFCLPTKKYADVIIPRGADNLV 222
Cdd:COG1072   226 EEDLREWYVerflkLRETAFRdpdsyfhryaGLSEEEARAWAEEIWReinlPNLAENILPTRSRADLILRKGADHSV 302
NRK1 cd02024
Nicotinamide riboside kinase (NRK) is an enzyme involved in the metabolism of nicotinamide ...
 63-172 6.93e-06

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: 45.39  E-value: 6.93e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672567  63 VILSQDSFYRvlTSEQKAKALKGQFNFDHPDAFDNELIFKTLKEITEGKTVQIPV--------YDFVSHSRKEETVTIYP 134
Cdd:cd02024    27 CVIHQDDFFK--PEDEIPVDENGFKQWDVLEALDMEAMMSTLDYWRETGHFPKFLrshgnendPEKEFIEDAQIEETKAD 104

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1958672567 135 AD------VVLFEGILAFYSQEVRDLFQMKLFVDTDADTRLSRR 172
Cdd:cd02024   105 LLgaedlhILIVDGFLLYNYKPLVDLFDIRYFLRVPYETCKRRR 148
PRK07667 PRK07667
uridine kinase; Provisional
 101-214 1.75e-03

uridine kinase; Provisional


Pssm-ID: 169051  Cd Length: 193  Bit Score: 38.56  E-value: 1.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672567 101 FKTLKEITEgktVQIPVYDFVSHSRKEETVTIYPADVVLFEGILaFYSQEVRDLFQMKLFVDTDADTRLSrRVLRDISER 180
Cdd:PRK07667   89 FRKLQNETK---LTLPFYHDETDTCEMKKVQIPIVGVIVIEGVF-LQRKEWRDFFHYMVYLDCPRETRFL-RESEETQKN 163

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1958672567 181 grdleqiLSQYITFVKPAfEEFCLPT---KKYADVII 214
Cdd:PRK07667  164 -------LSKFKNRYWKA-EDYYLETespKDRADLVI 192
 
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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