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Conserved domains on  [gi|13507680|ref|NP_109649|]
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uridine-cytidine kinase 2 isoform a [Mus musculus]

Protein Classification

uridine-cytidine kinase( domain architecture ID 10113977)

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

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 ...
 22-228 3.12e-116

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: 331.06  E-value: 3.12e-116
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507680  22 LIGVSGGTASGKSSVCAKIVQLLGQnevdyhqKQVVILSQDSFYRVLTSEQKAKALKgqFNFDHPDAFDNELIFKTLKEI 101
Cdd:cd02023   1 IIGIAGGSGSGKTTVAEEIIEQLGN-------PKVVIISQDSYYKDLSHEELEERKN--NNYDHPDAFDFDLLISHLQDL 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507680 102 TEGKTVQIPVYDFVSHSRKEETVTIYPADVVLFEGILAFYSQEVRDLFQMKLFVDTDADTRLSRRVLRDISERGRDLEQI 181
Cdd:cd02023  72 KNGKSVEIPVYDFKTHSRLKETVTVYPADVIILEGILALYDKELRDLMDLKIFVDTDADVRLIRRIERDIVERGRDLESV 151

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 13507680 182 LSQYITFVKPAFEEFCLPTKKYADVIIPRGADNLVAINLIVQHIQDI 228
Cdd:cd02023 152 INQYLKFVKPMHEQFIEPTKRYADVIIPRGGDNHVAIDLIVQHIKSK 198
 
Name Accession Description Interval E-value
UMPK cd02023
Uridine monophosphate kinase (UMPK, EC 2.7.1.48), also known as uridine kinase or ...
 22-228 3.12e-116

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: 331.06  E-value: 3.12e-116
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507680  22 LIGVSGGTASGKSSVCAKIVQLLGQnevdyhqKQVVILSQDSFYRVLTSEQKAKALKgqFNFDHPDAFDNELIFKTLKEI 101
Cdd:cd02023   1 IIGIAGGSGSGKTTVAEEIIEQLGN-------PKVVIISQDSYYKDLSHEELEERKN--NNYDHPDAFDFDLLISHLQDL 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507680 102 TEGKTVQIPVYDFVSHSRKEETVTIYPADVVLFEGILAFYSQEVRDLFQMKLFVDTDADTRLSRRVLRDISERGRDLEQI 181
Cdd:cd02023  72 KNGKSVEIPVYDFKTHSRLKETVTVYPADVIILEGILALYDKELRDLMDLKIFVDTDADVRLIRRIERDIVERGRDLESV 151

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 13507680 182 LSQYITFVKPAFEEFCLPTKKYADVIIPRGADNLVAINLIVQHIQDI 228
Cdd:cd02023 152 INQYLKFVKPMHEQFIEPTKRYADVIIPRGGDNHVAIDLIVQHIKSK 198
PRK05480 PRK05480
uridine/cytidine kinase; Provisional
 20-231 1.17e-91

uridine/cytidine kinase; Provisional


Pssm-ID: 235492 [Multi-domain]  Cd Length: 209  Bit Score: 269.34  E-value: 1.17e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507680   20 PFLIGVSGGTASGKSSVCAKIVQLLGQNevdyhqkQVVILSQDSFYR---VLTSEQKAKalkgqFNFDHPDAFDNELIFK 96
Cdd:PRK05480   6 PIIIGIAGGSGSGKTTVASTIYEELGDE-------SIAVIPQDSYYKdqsHLSFEERVK-----TNYDHPDAFDHDLLIE 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507680   97 TLKEITEGKTVQIPVYDFVSHSRKEETVTIYPADVVLFEGILAFYSQEVRDLFQMKLFVDTDADTRLSRRVLRDISERGR 176
Cdd:PRK05480  74 HLKALKAGKAIEIPVYDYTEHTRSKETIRVEPKDVIILEGILLLEDERLRDLMDIKIFVDTPLDIRLIRRLKRDVNERGR 153

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 13507680  177 DLEQILSQYITFVKPAFEEFCLPTKKYADVIIPRGADNLVAINLIVQHIQDILNG 231
Cdd:PRK05480 154 SLESVINQYLSTVRPMHLQFIEPSKRYADIIIPEGGKNRVAIDILKAKIRQLLEK 208
Udk COG0572
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway ...
 15-227 1.03e-81

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: 243.98  E-value: 1.03e-81
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507680  15 PNGGEPFLIGVSGGTASGKSSVCAKIVQLLGQNEVdyhqkqvVILSQDSFYRVLtsEQKAKALKGQFNFDHPDAFDNELI 94
Cdd:COG0572   2 ARSGKPRIIGIAGPSGSGKTTFARRLAEQLGADKV-------VVISLDDYYKDR--EHLPLDERGKPNFDHPEAFDLDLL 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507680  95 FKTLKEITEGKTVQIPVYDFVSHSRKEETVTIYPADVVLFEGILAFYSQEVRDLFQMKLFVDTDADTRLSRRVLRDISER 174
Cdd:COG0572  73 NEHLEPLKAGESVELPVYDFATGTRSGETVKVEPADVIIVEGIHALNDELLRDLLDLKIYVDADTDVRLIRRIVRDGEER 152

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 13507680 175 GRDLEQILSQYITFVKPAFEEFCLPTKKYADVIIPR-GADNLVAINLIVQHIQD 227
Cdd:COG0572 153 GRTAESVIEQYWATVRPGHEQYIEPTKEYADIVIPNgGPLNPVALDLLVARLLS 206
udk TIGR00235
uridine kinase; Model contains a number of longer eukaryotic proteins and starts bringing in ...
 20-230 1.81e-81

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: 243.45  E-value: 1.81e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507680    20 PFLIGVSGGTASGKSSVCAKIVQLLGQNEVdyhqkqvVILSQDSFYRVLtsEQKAKALKGQFNFDHPDAFDNELIFKTLK 99
Cdd:TIGR00235   6 GIIIGIGGGSGSGKTTVARKIYEQLGKLEI-------VIISQDNYYKDQ--SHLEMAERKKTNFDHPDAFDNDLLYEHLK 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507680   100 EITEGKTVQIPVYDFVSHSRKEETVTIYPADVVLFEGILAFYSQEVRDLFQMKLFVDTDADTRLSRRVLRDISERGRDLE 179
Cdd:TIGR00235  77 NLKNGSPIDVPVYDYVNHTRPKETVHIEPKDVVILEGIMPLFDERLRDLMDLKIFVDTPLDIRLIRRIERDINERGRSLD 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 13507680   180 QILSQYITFVKPAFEEFCLPTKKYADVIIPRGADNLVAINLIVQHIQDILN 230
Cdd:TIGR00235 157 SVIDQYRKTVRPMYEQFVEPTKQYADLIIPEGGRNEVAINVLDTKIKHLLE 207
PRK pfam00485
Phosphoribulokinase / Uridine kinase family; This family matches three types of P-loop ...
 22-217 3.38e-62

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: 193.77  E-value: 3.38e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507680    22 LIGVSGGTASGKSSVCAKIVQLLGQNEVDYHQKQ-VVILSQDSFYRVLTSEQKAKALKGQFNFDHPDAFDNELIFKTLKE 100
Cdd:pfam00485   1 VIGVAGSSGSGKTTVARRIVSIFGREGVPAVGIEgDSFHSTDRFYMDLHPEDRKRAGNNGYSFDGPEANDFDLLYEQFKE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507680   101 ITEGKTVQIPVYDFVSHSRKEETVTIYPADVVLFEGILAFYSQEVRDLFQMKLFVDTDADTRLSRRVLRDISERGRDLEQ 180
Cdd:pfam00485  81 LKEGGSVDKPIYNHVTHERDPTPELIEGADVLVIEGLHALYDERVAQLLDLKIYVDPDIDLELARKIQRDMAERGHSLEG 160

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 13507680   181 ILSQYItFVKPAFEEFCLPTKKYADVIIPRGADNLVA 217
Cdd:pfam00485 161 VTDSIL-FRKPDYVNYIDPQFSYADLIIQRVPTNDTA 196
 
Name Accession Description Interval E-value
UMPK cd02023
Uridine monophosphate kinase (UMPK, EC 2.7.1.48), also known as uridine kinase or ...
 22-228 3.12e-116

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: 331.06  E-value: 3.12e-116
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507680  22 LIGVSGGTASGKSSVCAKIVQLLGQnevdyhqKQVVILSQDSFYRVLTSEQKAKALKgqFNFDHPDAFDNELIFKTLKEI 101
Cdd:cd02023   1 IIGIAGGSGSGKTTVAEEIIEQLGN-------PKVVIISQDSYYKDLSHEELEERKN--NNYDHPDAFDFDLLISHLQDL 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507680 102 TEGKTVQIPVYDFVSHSRKEETVTIYPADVVLFEGILAFYSQEVRDLFQMKLFVDTDADTRLSRRVLRDISERGRDLEQI 181
Cdd:cd02023  72 KNGKSVEIPVYDFKTHSRLKETVTVYPADVIILEGILALYDKELRDLMDLKIFVDTDADVRLIRRIERDIVERGRDLESV 151

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 13507680 182 LSQYITFVKPAFEEFCLPTKKYADVIIPRGADNLVAINLIVQHIQDI 228
Cdd:cd02023 152 INQYLKFVKPMHEQFIEPTKRYADVIIPRGGDNHVAIDLIVQHIKSK 198
PRK05480 PRK05480
uridine/cytidine kinase; Provisional
 20-231 1.17e-91

uridine/cytidine kinase; Provisional


Pssm-ID: 235492 [Multi-domain]  Cd Length: 209  Bit Score: 269.34  E-value: 1.17e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507680   20 PFLIGVSGGTASGKSSVCAKIVQLLGQNevdyhqkQVVILSQDSFYR---VLTSEQKAKalkgqFNFDHPDAFDNELIFK 96
Cdd:PRK05480   6 PIIIGIAGGSGSGKTTVASTIYEELGDE-------SIAVIPQDSYYKdqsHLSFEERVK-----TNYDHPDAFDHDLLIE 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507680   97 TLKEITEGKTVQIPVYDFVSHSRKEETVTIYPADVVLFEGILAFYSQEVRDLFQMKLFVDTDADTRLSRRVLRDISERGR 176
Cdd:PRK05480  74 HLKALKAGKAIEIPVYDYTEHTRSKETIRVEPKDVIILEGILLLEDERLRDLMDIKIFVDTPLDIRLIRRLKRDVNERGR 153

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 13507680  177 DLEQILSQYITFVKPAFEEFCLPTKKYADVIIPRGADNLVAINLIVQHIQDILNG 231
Cdd:PRK05480 154 SLESVINQYLSTVRPMHLQFIEPSKRYADIIIPEGGKNRVAIDILKAKIRQLLEK 208
Udk COG0572
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway ...
 15-227 1.03e-81

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: 243.98  E-value: 1.03e-81
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507680  15 PNGGEPFLIGVSGGTASGKSSVCAKIVQLLGQNEVdyhqkqvVILSQDSFYRVLtsEQKAKALKGQFNFDHPDAFDNELI 94
Cdd:COG0572   2 ARSGKPRIIGIAGPSGSGKTTFARRLAEQLGADKV-------VVISLDDYYKDR--EHLPLDERGKPNFDHPEAFDLDLL 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507680  95 FKTLKEITEGKTVQIPVYDFVSHSRKEETVTIYPADVVLFEGILAFYSQEVRDLFQMKLFVDTDADTRLSRRVLRDISER 174
Cdd:COG0572  73 NEHLEPLKAGESVELPVYDFATGTRSGETVKVEPADVIIVEGIHALNDELLRDLLDLKIYVDADTDVRLIRRIVRDGEER 152

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 13507680 175 GRDLEQILSQYITFVKPAFEEFCLPTKKYADVIIPR-GADNLVAINLIVQHIQD 227
Cdd:COG0572 153 GRTAESVIEQYWATVRPGHEQYIEPTKEYADIVIPNgGPLNPVALDLLVARLLS 206
udk TIGR00235
uridine kinase; Model contains a number of longer eukaryotic proteins and starts bringing in ...
 20-230 1.81e-81

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: 243.45  E-value: 1.81e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507680    20 PFLIGVSGGTASGKSSVCAKIVQLLGQNEVdyhqkqvVILSQDSFYRVLtsEQKAKALKGQFNFDHPDAFDNELIFKTLK 99
Cdd:TIGR00235   6 GIIIGIGGGSGSGKTTVARKIYEQLGKLEI-------VIISQDNYYKDQ--SHLEMAERKKTNFDHPDAFDNDLLYEHLK 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507680   100 EITEGKTVQIPVYDFVSHSRKEETVTIYPADVVLFEGILAFYSQEVRDLFQMKLFVDTDADTRLSRRVLRDISERGRDLE 179
Cdd:TIGR00235  77 NLKNGSPIDVPVYDYVNHTRPKETVHIEPKDVVILEGIMPLFDERLRDLMDLKIFVDTPLDIRLIRRIERDINERGRSLD 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 13507680   180 QILSQYITFVKPAFEEFCLPTKKYADVIIPRGADNLVAINLIVQHIQDILN 230
Cdd:TIGR00235 157 SVIDQYRKTVRPMYEQFVEPTKQYADLIIPEGGRNEVAINVLDTKIKHLLE 207
PRK pfam00485
Phosphoribulokinase / Uridine kinase family; This family matches three types of P-loop ...
 22-217 3.38e-62

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: 193.77  E-value: 3.38e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507680    22 LIGVSGGTASGKSSVCAKIVQLLGQNEVDYHQKQ-VVILSQDSFYRVLTSEQKAKALKGQFNFDHPDAFDNELIFKTLKE 100
Cdd:pfam00485   1 VIGVAGSSGSGKTTVARRIVSIFGREGVPAVGIEgDSFHSTDRFYMDLHPEDRKRAGNNGYSFDGPEANDFDLLYEQFKE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507680   101 ITEGKTVQIPVYDFVSHSRKEETVTIYPADVVLFEGILAFYSQEVRDLFQMKLFVDTDADTRLSRRVLRDISERGRDLEQ 180
Cdd:pfam00485  81 LKEGGSVDKPIYNHVTHERDPTPELIEGADVLVIEGLHALYDERVAQLLDLKIYVDPDIDLELARKIQRDMAERGHSLEG 160

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 13507680   181 ILSQYItFVKPAFEEFCLPTKKYADVIIPRGADNLVA 217
Cdd:pfam00485 161 VTDSIL-FRKPDYVNYIDPQFSYADLIIQRVPTNDTA 196
PTZ00301 PTZ00301
uridine kinase; Provisional
 23-231 5.20e-39

uridine kinase; Provisional


Pssm-ID: 140322 [Multi-domain]  Cd Length: 210  Bit Score: 135.13  E-value: 5.20e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507680   23 IGVSGGTASGKSSVCAKIVQLL----GQNEVDyhqkqvvILSQDSFYR----VLTSEQKAKalkgqfNFDHPDAFDNELI 94
Cdd:PTZ00301   6 IGISGASGSGKSSLSTNIVSELmahcGPVSIG-------VICEDFYYRdqsnIPESERAYT------NYDHPKSLEHDLL 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507680   95 FKTLKEITEGKTVQIPVYDFVSHSRKEETVTIYPADVVLFEGILAFYSQEVRDLFQMKLFVDTDADTRLSRRVLRDISER 174
Cdd:PTZ00301  73 TTHLRELKSGKTVQIPQYDYVHHTRSDTAVTMTPKSVLIVEGILLFTNAELRNEMDCLIFVDTPLDICLIRRAKRDMRER 152

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 13507680  175 GRDLEQILSQYITFVKPAFEEFCLPTKKYADVIIPRGADNLVAINLIVQHIQDILNG 231
Cdd:PTZ00301 153 GRTFESVIEQYEATVRPMYYAYVEPSKVYADIIVPSWKDNSVAVGVLRAKLNHDLEN 209
PRK cd02026
Phosphoribulokinase (PRK) is an enzyme involved in the Benson-Calvin cycle in chloroplasts or ...
 22-208 5.53e-26

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: 102.42  E-value: 5.53e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507680  22 LIGVSGGTASGKSSVCAKIVQLLGQNEV------DYHqkqvvilsqdSFYRVLTSEQKAKALkgqfnfdHPDAFDNELIF 95
Cdd:cd02026   1 IIGVAGDSGCGKSTFLRRLTSLFGSDLVtvicldDYH----------SLDRKGRKETGITAL-------DPRANNFDLMY 63

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507680  96 KTLKEITEGKTVQIPVYDFVSHS-RKEETvtIYPADVVLFEGILAFYSQEVRDLFQMKLFVDTDADTRLSRRVLRDISER 174
Cdd:cd02026  64 EQLKALKEGQAIEKPIYNHVTGLiDPPEL--IKPTKIVVIEGLHPLYDERVRELLDFSVYLDISDEVKFAWKIQRDMAER 141

                       170       180       190
                ....*....|....*....|....*....|....
gi 13507680 175 GRDLEQILSQyITFVKPAFEEFCLPTKKYADVII 208
Cdd:cd02026 142 GHSLEDVLAS-IEARKPDFEAYIDPQKQYADVVI 174
UMPK_like cd02028
Uridine monophosphate kinase_like (UMPK_like) is a family of proteins highly similar to the ...
 22-196 1.94e-24

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: 96.22  E-value: 1.94e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507680  22 LIGVSGGTASGKSSVCAKIVQLLGQNEVdyhqkQVVILSQDSFYRVLTSEQKAkalkgQFNFDHPDAFDNELIFKTLKEI 101
Cdd:cd02028   1 VVGIAGPSGSGKTTFAKKLSNQLRVNGI-----GPVVISLDDYYVPRKTPRDE-----DGNYDFESILDLDLLNKNLHDL 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507680 102 TEGKTVQIPVYDFVSHSRK-EETVTIYPADVVLFEGILAFySQEVRDLFQMKLFVDT-DADTRLSRRVLRDISERGRDLE 179
Cdd:cd02028  71 LNGKEVELPIYDFRTGKRRgYRKLKLPPSGVVILEGIYAL-NERLRSLLDIRVAVSGgVHLNRLLRRVVRDIQFRGYSAE 149

                       170
                ....*....|....*..
gi 13507680 180 QILSQYITFvkPAFEEF 196
Cdd:cd02028 150 LTILMWPSV--PSGEEF 164
PRK07429 PRK07429
phosphoribulokinase; Provisional
 20-208 1.95e-24

phosphoribulokinase; Provisional


Pssm-ID: 180975  Cd Length: 327  Bit Score: 99.70  E-value: 1.95e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507680   20 PFLIGVSGGTASGKSSVCAKIVQLLGQNEV------DYHQkqvvilsqdsfyrvLTSEQKAK----ALkgqfnfdHPDAF 89
Cdd:PRK07429   8 PVLLGVAGDSGCGKTTFLRGLADLLGEELVtvictdDYHS--------------YDRKQRKElgitAL-------DPRAN 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507680   90 DNELIFKTLKEITEGKTVQIPVYDfvsHSRK--EETVTIYPADVVLFEGILAFYSQEVRDLFQMKLFVDTDADTRLSRRV 167
Cdd:PRK07429  67 NLDIMYEHLKALKTGQPILKPIYN---HETGtfDPPEYIEPNKIVVVEGLHPLYDERVRELYDFKVYLDPPEEVKIAWKI 143

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 13507680  168 LRDISERGRDLEQILSQyITFVKPAFEEFCLPTKKYADVII 208
Cdd:PRK07429 144 KRDMAKRGHTYEQVLAE-IEAREPDFEAYIRPQRQWADVVI 183
PLN02348 PLN02348
phosphoribulokinase
 17-208 1.91e-23

phosphoribulokinase


Pssm-ID: 215198  Cd Length: 395  Bit Score: 97.99  E-value: 1.91e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507680   17 GGEPFLIGVSGGTASGKSSVCAKIVQLLG------------QNEVDYHQKQVVILsqDSFYRVLTSEQKAKALKGQfnfd 84
Cdd:PLN02348  46 DDGTVVIGLAADSGCGKSTFMRRLTSVFGgaakppkggnpdSNTLISDTTTVICL--DDYHSLDRTGRKEKGVTAL---- 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507680   85 HPDAFDNELIFKTLKEITEGKTVQIPVYDFVShSRKEETVTIYPADVVLFEGILAFYSQEVRDLFQMKLFVDTDADTRLS 164
Cdd:PLN02348 120 DPRANNFDLMYEQVKALKEGKAVEKPIYNHVT-GLLDPPELIEPPKILVIEGLHPMYDERVRDLLDFSIYLDISDDVKFA 198

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 13507680  165 RRVLRDISERGRDLEQILSQyITFVKPAFEEFCLPTKKYADVII 208
Cdd:PLN02348 199 WKIQRDMAERGHSLESIKAS-IEARKPDFDAYIDPQKQYADVVI 241
PLN02318 PLN02318
phosphoribulokinase/uridine kinase
 22-208 2.48e-16

phosphoribulokinase/uridine kinase


Pssm-ID: 177952 [Multi-domain]  Cd Length: 656  Bit Score: 78.36  E-value: 2.48e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507680   22 LIGVSGGTASGKSSVCAKIVQLLgqnevdyhqKQVVILSQDSFyrvltsEQKAKALKGqfNFDHPDAFDNELIFKTLKEI 101
Cdd:PLN02318  67 LVGVAGPSGAGKTVFTEKVLNFM---------PSIAVISMDNY------NDSSRIIDG--NFDDPRLTDYDTLLDNIHDL 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507680  102 TEGKTVQIPVYDFVSHSR-KEETVTIYPADVVLFEGILAFySQEVRDLFQMKLFVDTDADTRLSRRVLRDISERGRDLEQ 180
Cdd:PLN02318 130 KAGKSVQVPIYDFKSSSRvGYRTLEVPSSRIVIIEGIYAL-SEKLRPLLDLRVSVTGGVHFDLVKRVLRDIQRAGQEPEE 208

                        170       180
                 ....*....|....*....|....*...
gi 13507680  181 ILSQYITFVKPAFEEFCLPTKKYADVII 208
Cdd:PLN02318 209 IIHQISETVYPMYKAFIEPDLQTAHIKI 236
CoaA COG1072
Panthothenate kinase [Coenzyme transport and metabolism]; Panthothenate kinase is part of the ...
 7-216 1.46e-14

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: 71.86  E-value: 1.46e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507680   7 QTLQNHQQPNGGEPFLIGVSGGTASGKSSVCAKIVQLLGQnevDYHQKQVVILSQDSF-Y--RVLtseqKAKAL---KGq 80
Cdd:COG1072  73 ATSAFLGQADKKTPFIIGIAGSVAVGKSTTARLLQALLSR---WPEHPKVELVTTDGFlYpnAVL----ERRGLmdrKG- 144

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507680  81 FnfdhPDAFDNELIFKTLKEITEGK-TVQIPVYDFVSH-SRKEETVTIYPADVVLFEGI--L---AFYSQEVRDLFQMKL 153
Cdd:COG1072 145 F----PESYDRRGLLRFLARVKSGDpEVRAPVYSHLLYdIVPGAIVVVDQPDILIVEGNnvLqdePNPWLFVSDFFDFSI 220

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507680 154 FVDTDADTRLSRRV-----LRDISER----------GRDLEQILSQYITFVK----PAFEEFCLPTKKYADVIIPRGADN 214
Cdd:COG1072 221 YVDADEEDLREWYVerflkLRETAFRdpdsyfhryaGLSEEEARAWAEEIWReinlPNLAENILPTRSRADLILRKGADH 300


                ..
gi 13507680 215 LV 216
Cdd:COG1072 301 SV 302
PanK cd02025
Pantothenate kinase (PanK) catalyzes the phosphorylation of pantothenic acid to form 4 ...
 22-216 1.36e-11

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: 62.33  E-value: 1.36e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507680  22 LIGVSGGTASGKSsVCAKIVQLLGQNEVDyhQKQVVILSQDSF-YRVLTSEQKAKALKGQFnfdhPDAFDNELIFKTLKE 100
Cdd:cd02025   1 IIGIAGSVAVGKS-TTARVLQALLSRWPD--HPNVELITTDGFlYPNKELIERGLMDRKGF----PESYDMEALLKFLKD 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507680 101 ITEGK-TVQIPVYDFVSHSR-KEETVTIYPADVVLFEGILAF-----YSQEVRDLFQMKLFVDTDADtRLSR----RVLR 169
Cdd:cd02025  74 IKSGKkNVKIPVYSHLTYDViPGEKQTVDQPDILIIEGLNVLqtgqnPRLFVSDFFDFSIYVDADED-DIEKwyikRFLK 152

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13507680 170 DISERGRDLEQILSQY--------ITFVK--------PAFEEFCLPTKKYADVIIPRGADNLV 216
Cdd:cd02025 153 LRETAFSDPDSYFHRYakmseeeaIAFARevwkninlKNLRENILPTRNRADLILEKGADHSI 215
NRK1 cd02024
Nicotinamide riboside kinase (NRK) is an enzyme involved in the metabolism of nicotinamide ...
 22-166 1.04e-10

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: 59.26  E-value: 1.04e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507680  22 LIGVSGGTASGKSSVCAKIVQLLGQnevdyhqkqVVILSQDSFYRvlTSEQKAKALKGQFNFDHPDAFDNELIFKTLKEI 101
Cdd:cd02024   1 IVGISGVTNSGKTTLAKLLQRILPN---------CCVIHQDDFFK--PEDEIPVDENGFKQWDVLEALDMEAMMSTLDYW 69

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13507680 102 TEGKTVQIPV--------YDFVSHSRKEETVTIYPAD------VVLFEGILAFYSQEVRDLFQMKLFVDTDADTRLSRR 166
Cdd:cd02024  70 RETGHFPKFLrshgnendPEKEFIEDAQIEETKADLLgaedlhILIVDGFLLYNYKPLVDLFDIRYFLRVPYETCKRRR 148
PRK08233 PRK08233
hypothetical protein; Provisional
 121-229 1.33e-09

hypothetical protein; Provisional


Pssm-ID: 181310 [Multi-domain]  Cd Length: 182  Bit Score: 55.90  E-value: 1.33e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507680  121 EETVTIYPADVVLFEGILAFYSQEVRDLFQMKLFVDTDADTRLSRRVLRDISER-GRDLEQILSQYITFVKPAFEEFCLP 199
Cdd:PRK08233  70 QELIAKSNVDYIIVDYPFAYLNSEMRQFIDVTIFIDTPLDIAMARRILRDFKEDtGNEIHNDLKHYLNYARPLYLEALHT 149

                         90       100       110
                 ....*....|....*....|....*....|
gi 13507680  200 TKKYADVIIprgaDNLVAINLIVQHIQDIL 229
Cdd:PRK08233 150 VKPNADIVL----DGALSVEEIINQIEEEL 175
PLN02796 PLN02796
D-glycerate 3-kinase
 6-144 4.92e-04

D-glycerate 3-kinase


Pssm-ID: 215427  Cd Length: 347  Bit Score: 40.88  E-value: 4.92e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507680    6 EQTLQNHQQP-NGGE---PFLIGVSGGTASGKSSVCAKIVQLLgqnevDYHQKQVVILSQDSFYrvLTSE-QKAKALKGQ 80
Cdd:PLN02796  82 EDQLEAHRSKfKDGDeipPLVIGISAPQGCGKTTLVFALVYLF-----NATGRRAASLSIDDFY--LTAAdQAKLAEANP 154

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507680   81 FNF---------DHPDAFDNELIfKTLKEIT-EGKTVQIPVYDFVSHS----RKE----ETVTiYPADVVLFEG-ILAFY 141
Cdd:PLN02796 155 GNAllelrgnagSHDLALGVETL-EALRKLNkEGSKMKVPRYDKSAYGgrgdRADpstwPEVE-GPLDVVLFEGwMLGFK 232


                 ...
gi 13507680  142 SQE 144
Cdd:PLN02796 233 PLG 235
PRK07667 PRK07667
uridine kinase; Provisional
 95-208 1.15e-03

uridine kinase; Provisional


Pssm-ID: 169051  Cd Length: 193  Bit Score: 38.94  E-value: 1.15e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507680   95 FKTLKEITEgktVQIPVYDFVSHSRKEETVTIYPADVVLFEGILaFYSQEVRDLFQMKLFVDTDADTRLSrRVLRDISER 174
Cdd:PRK07667  89 FRKLQNETK---LTLPFYHDETDTCEMKKVQIPIVGVIVIEGVF-LQRKEWRDFFHYMVYLDCPRETRFL-RESEETQKN 163

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 13507680  175 grdleqiLSQYITFVKPAfEEFCLPT---KKYADVII 208
Cdd:PRK07667 164 -------LSKFKNRYWKA-EDYYLETespKDRADLVI 192
CoaE pfam01121
Dephospho-CoA kinase; This family catalyzes the phosphorylation of the 3'-hydroxyl group of ...
 22-184 2.96e-03

Dephospho-CoA kinase; This family catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form Coenzyme A EC:2.7.1.24. This enzyme uses ATP in its reaction.


Pssm-ID: 426062  Cd Length: 180  Bit Score: 37.69  E-value: 2.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507680    22 LIGVSGGTASGKSSVCAKIVQlLGQNEVDYHQ--KQVV-----ILSQ--DSFYRVLTSEQKA--KALKGQFNFDHPDAfd 90
Cdd:pfam01121   2 IVGLTGGIGSGKSTVANYFRD-LGVPIIDADAiaRQVVepggpALSRivRHFGPTILDADGQldRRALRELVFSNPER-- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507680    91 nelifktlKEITEGKtvqipVYDFVSHSRKEETVTIYPADVVLFEGILAFYSQeVRDLFQMKLFVDTDADTRLSRRVLRD 170
Cdd:pfam01121  79 --------KKWLNGI-----LHPLIRREIFKQIATLTAAPYVVLDIPLLFESG-LHKLCHRVLVVDAPPELQVERLVARD 144

                         170
                  ....*....|....
gi 13507680   171 ISERGRDLEQILSQ 184
Cdd:pfam01121 145 GLSREEAQARIAAQ 158
 
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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