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Conserved domains on  [gi|283806560|ref|NP_001164538|]
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uridine-cytidine kinase 2-A [Danio rerio]

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 ...
 24-229 1.76e-115

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: 329.13  E-value: 1.76e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283806560  24 LIGVAGGTASGKSSVCGKIMELLGQnkidhhqRQVAILSQDSFYRVLTPEQKAKALKgqFNFDHPDAFDNELIVKTLCEI 103
Cdd:cd02023    1 IIGIAGGSGSGKTTVAEEIIEQLGN-------PKVVIISQDSYYKDLSHEELEERKN--NNYDHPDAFDFDLLISHLQDL 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283806560 104 MEGRTVQIPVYDFVTHSRKEETVTVYPADVVLFEGILMFYSQEIRDLFQMKLFVDTDADTRLSRRVLRDISERGRDLEQV 183
Cdd:cd02023   72 KNGKSVEIPVYDFKTHSRLKETVTVYPADVIILEGILALYDKELRDLMDLKIFVDTDADVRLIRRIERDIVERGRDLESV 151

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 283806560 184 LNQYITFVKPAFEEFCLPTKKYADVIIPRGADNLVAINLIVQHIQD 229
Cdd:cd02023  152 INQYLKFVKPMHEQFIEPTKRYADVIIPRGGDNHVAIDLIVQHIKS 197
 
Name Accession Description Interval E-value
UMPK cd02023
Uridine monophosphate kinase (UMPK, EC 2.7.1.48), also known as uridine kinase or ...
 24-229 1.76e-115

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: 329.13  E-value: 1.76e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283806560  24 LIGVAGGTASGKSSVCGKIMELLGQnkidhhqRQVAILSQDSFYRVLTPEQKAKALKgqFNFDHPDAFDNELIVKTLCEI 103
Cdd:cd02023    1 IIGIAGGSGSGKTTVAEEIIEQLGN-------PKVVIISQDSYYKDLSHEELEERKN--NNYDHPDAFDFDLLISHLQDL 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283806560 104 MEGRTVQIPVYDFVTHSRKEETVTVYPADVVLFEGILMFYSQEIRDLFQMKLFVDTDADTRLSRRVLRDISERGRDLEQV 183
Cdd:cd02023   72 KNGKSVEIPVYDFKTHSRLKETVTVYPADVIILEGILALYDKELRDLMDLKIFVDTDADVRLIRRIERDIVERGRDLESV 151

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 283806560 184 LNQYITFVKPAFEEFCLPTKKYADVIIPRGADNLVAINLIVQHIQD 229
Cdd:cd02023  152 INQYLKFVKPMHEQFIEPTKRYADVIIPRGGDNHVAIDLIVQHIKS 197
PRK05480 PRK05480
uridine/cytidine kinase; Provisional
 21-233 8.52e-94

uridine/cytidine kinase; Provisional


Pssm-ID: 235492 [Multi-domain]  Cd Length: 209  Bit Score: 274.73  E-value: 8.52e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283806560  21 QPFLIGVAGGTASGKSSVCGKIMELLGQNKIdhhqrqvAILSQDSFYR---VLTPEQKAKalkgqFNFDHPDAFDNELIV 97
Cdd:PRK05480   5 KPIIIGIAGGSGSGKTTVASTIYEELGDESI-------AVIPQDSYYKdqsHLSFEERVK-----TNYDHPDAFDHDLLI 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283806560  98 KTLCEIMEGRTVQIPVYDFVTHSRKEETVTVYPADVVLFEGILMFYSQEIRDLFQMKLFVDTDADTRLSRRVLRDISERG 177
Cdd:PRK05480  73 EHLKALKAGKAIEIPVYDYTEHTRSKETIRVEPKDVIILEGILLLEDERLRDLMDIKIFVDTPLDIRLIRRLKRDVNERG 152

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 283806560 178 RDLEQVLNQYITFVKPAFEEFCLPTKKYADVIIPRGADNLVAINLIVQHIQDFLNG 233
Cdd:PRK05480 153 RSLESVINQYLSTVRPMHLQFIEPSKRYADIIIPEGGKNRVAIDILKAKIRQLLEK 208
Udk COG0572
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway ...
 21-229 2.09e-80

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: 240.51  E-value: 2.09e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283806560  21 QPFLIGVAGGTASGKSSVCGKIMELLGQNKidhhqrqVAILSQDSFYRVLtpEQKAKALKGQFNFDHPDAFDNELIVKTL 100
Cdd:COG0572    6 KPRIIGIAGPSGSGKTTFARRLAEQLGADK-------VVVISLDDYYKDR--EHLPLDERGKPNFDHPEAFDLDLLNEHL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283806560 101 CEIMEGRTVQIPVYDFVTHSRKEETVTVYPADVVLFEGILMFYSQEIRDLFQMKLFVDTDADTRLSRRVLRDISERGRDL 180
Cdd:COG0572   77 EPLKAGESVELPVYDFATGTRSGETVKVEPADVIIVEGIHALNDELLRDLLDLKIYVDADTDVRLIRRIVRDGEERGRTA 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 283806560 181 EQVLNQYITFVKPAFEEFCLPTKKYADVIIPR-GADNLVAINLIVQHIQD 229
Cdd:COG0572  157 ESVIEQYWATVRPGHEQYIEPTKEYADIVIPNgGPLNPVALDLLVARLLS 206
udk TIGR00235
uridine kinase; Model contains a number of longer eukaryotic proteins and starts bringing in ...
 22-232 1.05e-78

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: 236.52  E-value: 1.05e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283806560   22 PFLIGVAGGTASGKSSVCGKIMELLGQNKIdhhqrqvAILSQDSFYRVLtpEQKAKALKGQFNFDHPDAFDNELIVKTLC 101
Cdd:TIGR00235   6 GIIIGIGGGSGSGKTTVARKIYEQLGKLEI-------VIISQDNYYKDQ--SHLEMAERKKTNFDHPDAFDNDLLYEHLK 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283806560  102 EIMEGRTVQIPVYDFVTHSRKEETVTVYPADVVLFEGILMFYSQEIRDLFQMKLFVDTDADTRLSRRVLRDISERGRDLE 181
Cdd:TIGR00235  77 NLKNGSPIDVPVYDYVNHTRPKETVHIEPKDVVILEGIMPLFDERLRDLMDLKIFVDTPLDIRLIRRIERDINERGRSLD 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 283806560  182 QVLNQYITFVKPAFEEFCLPTKKYADVIIPRGADNLVAINLIVQHIQDFLN 232
Cdd:TIGR00235 157 SVIDQYRKTVRPMYEQFVEPTKQYADLIIPEGGRNEVAINVLDTKIKHLLE 207
PRK pfam00485
Phosphoribulokinase / Uridine kinase family; This family matches three types of P-loop ...
 24-219 2.32e-57

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: 181.44  E-value: 2.32e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283806560   24 LIGVAGGTASGKSSVCGKIMELLGQ-NKIDHHQRQVAILSQDSFYRVLTPEQKAKALKGQFNFDHPDAFDNELIVKTLCE 102
Cdd:pfam00485   1 VIGVAGSSGSGKTTVARRIVSIFGReGVPAVGIEGDSFHSTDRFYMDLHPEDRKRAGNNGYSFDGPEANDFDLLYEQFKE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283806560  103 IMEGRTVQIPVYDFVTHSRKEETVTVYPADVVLFEGILMFYSQEIRDLFQMKLFVDTDADTRLSRRVLRDISERGRDLEQ 182
Cdd:pfam00485  81 LKEGGSVDKPIYNHVTHERDPTPELIEGADVLVIEGLHALYDERVAQLLDLKIYVDPDIDLELARKIQRDMAERGHSLEG 160

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 283806560  183 VLNQYItFVKPAFEEFCLPTKKYADVIIPRGADNLVA 219
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 ...
 24-229 1.76e-115

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: 329.13  E-value: 1.76e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283806560  24 LIGVAGGTASGKSSVCGKIMELLGQnkidhhqRQVAILSQDSFYRVLTPEQKAKALKgqFNFDHPDAFDNELIVKTLCEI 103
Cdd:cd02023    1 IIGIAGGSGSGKTTVAEEIIEQLGN-------PKVVIISQDSYYKDLSHEELEERKN--NNYDHPDAFDFDLLISHLQDL 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283806560 104 MEGRTVQIPVYDFVTHSRKEETVTVYPADVVLFEGILMFYSQEIRDLFQMKLFVDTDADTRLSRRVLRDISERGRDLEQV 183
Cdd:cd02023   72 KNGKSVEIPVYDFKTHSRLKETVTVYPADVIILEGILALYDKELRDLMDLKIFVDTDADVRLIRRIERDIVERGRDLESV 151

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 283806560 184 LNQYITFVKPAFEEFCLPTKKYADVIIPRGADNLVAINLIVQHIQD 229
Cdd:cd02023  152 INQYLKFVKPMHEQFIEPTKRYADVIIPRGGDNHVAIDLIVQHIKS 197
PRK05480 PRK05480
uridine/cytidine kinase; Provisional
 21-233 8.52e-94

uridine/cytidine kinase; Provisional


Pssm-ID: 235492 [Multi-domain]  Cd Length: 209  Bit Score: 274.73  E-value: 8.52e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283806560  21 QPFLIGVAGGTASGKSSVCGKIMELLGQNKIdhhqrqvAILSQDSFYR---VLTPEQKAKalkgqFNFDHPDAFDNELIV 97
Cdd:PRK05480   5 KPIIIGIAGGSGSGKTTVASTIYEELGDESI-------AVIPQDSYYKdqsHLSFEERVK-----TNYDHPDAFDHDLLI 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283806560  98 KTLCEIMEGRTVQIPVYDFVTHSRKEETVTVYPADVVLFEGILMFYSQEIRDLFQMKLFVDTDADTRLSRRVLRDISERG 177
Cdd:PRK05480  73 EHLKALKAGKAIEIPVYDYTEHTRSKETIRVEPKDVIILEGILLLEDERLRDLMDIKIFVDTPLDIRLIRRLKRDVNERG 152

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 283806560 178 RDLEQVLNQYITFVKPAFEEFCLPTKKYADVIIPRGADNLVAINLIVQHIQDFLNG 233
Cdd:PRK05480 153 RSLESVINQYLSTVRPMHLQFIEPSKRYADIIIPEGGKNRVAIDILKAKIRQLLEK 208
Udk COG0572
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway ...
 21-229 2.09e-80

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: 240.51  E-value: 2.09e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283806560  21 QPFLIGVAGGTASGKSSVCGKIMELLGQNKidhhqrqVAILSQDSFYRVLtpEQKAKALKGQFNFDHPDAFDNELIVKTL 100
Cdd:COG0572    6 KPRIIGIAGPSGSGKTTFARRLAEQLGADK-------VVVISLDDYYKDR--EHLPLDERGKPNFDHPEAFDLDLLNEHL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283806560 101 CEIMEGRTVQIPVYDFVTHSRKEETVTVYPADVVLFEGILMFYSQEIRDLFQMKLFVDTDADTRLSRRVLRDISERGRDL 180
Cdd:COG0572   77 EPLKAGESVELPVYDFATGTRSGETVKVEPADVIIVEGIHALNDELLRDLLDLKIYVDADTDVRLIRRIVRDGEERGRTA 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 283806560 181 EQVLNQYITFVKPAFEEFCLPTKKYADVIIPR-GADNLVAINLIVQHIQD 229
Cdd:COG0572  157 ESVIEQYWATVRPGHEQYIEPTKEYADIVIPNgGPLNPVALDLLVARLLS 206
udk TIGR00235
uridine kinase; Model contains a number of longer eukaryotic proteins and starts bringing in ...
 22-232 1.05e-78

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: 236.52  E-value: 1.05e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283806560   22 PFLIGVAGGTASGKSSVCGKIMELLGQNKIdhhqrqvAILSQDSFYRVLtpEQKAKALKGQFNFDHPDAFDNELIVKTLC 101
Cdd:TIGR00235   6 GIIIGIGGGSGSGKTTVARKIYEQLGKLEI-------VIISQDNYYKDQ--SHLEMAERKKTNFDHPDAFDNDLLYEHLK 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283806560  102 EIMEGRTVQIPVYDFVTHSRKEETVTVYPADVVLFEGILMFYSQEIRDLFQMKLFVDTDADTRLSRRVLRDISERGRDLE 181
Cdd:TIGR00235  77 NLKNGSPIDVPVYDYVNHTRPKETVHIEPKDVVILEGIMPLFDERLRDLMDLKIFVDTPLDIRLIRRIERDINERGRSLD 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 283806560  182 QVLNQYITFVKPAFEEFCLPTKKYADVIIPRGADNLVAINLIVQHIQDFLN 232
Cdd:TIGR00235 157 SVIDQYRKTVRPMYEQFVEPTKQYADLIIPEGGRNEVAINVLDTKIKHLLE 207
PRK pfam00485
Phosphoribulokinase / Uridine kinase family; This family matches three types of P-loop ...
 24-219 2.32e-57

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: 181.44  E-value: 2.32e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283806560   24 LIGVAGGTASGKSSVCGKIMELLGQ-NKIDHHQRQVAILSQDSFYRVLTPEQKAKALKGQFNFDHPDAFDNELIVKTLCE 102
Cdd:pfam00485   1 VIGVAGSSGSGKTTVARRIVSIFGReGVPAVGIEGDSFHSTDRFYMDLHPEDRKRAGNNGYSFDGPEANDFDLLYEQFKE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283806560  103 IMEGRTVQIPVYDFVTHSRKEETVTVYPADVVLFEGILMFYSQEIRDLFQMKLFVDTDADTRLSRRVLRDISERGRDLEQ 182
Cdd:pfam00485  81 LKEGGSVDKPIYNHVTHERDPTPELIEGADVLVIEGLHALYDERVAQLLDLKIYVDPDIDLELARKIQRDMAERGHSLEG 160

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 283806560  183 VLNQYItFVKPAFEEFCLPTKKYADVIIPRGADNLVA 219
Cdd:pfam00485 161 VTDSIL-FRKPDYVNYIDPQFSYADLIIQRVPTNDTA 196
PTZ00301 PTZ00301
uridine kinase; Provisional
 25-223 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 283806560  25 IGVAGGTASGKSSVCGKIMELL----GQNKIdhhqrqvAILSQDSFYRVLT--PEQKakalKGQFNFDHPDAFDNELIVK 98
Cdd:PTZ00301   6 IGISGASGSGKSSLSTNIVSELmahcGPVSI-------GVICEDFYYRDQSniPESE----RAYTNYDHPKSLEHDLLTT 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283806560  99 TLCEIMEGRTVQIPVYDFVTHSRKEETVTVYPADVVLFEGILMFYSQEIRDLFQMKLFVDTDADTRLSRRVLRDISERGR 178
Cdd:PTZ00301  75 HLRELKSGKTVQIPQYDYVHHTRSDTAVTMTPKSVLIVEGILLFTNAELRNEMDCLIFVDTPLDICLIRRAKRDMRERGR 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 283806560 179 DLEQVLNQYITFVKPAFEEFCLPTKKYADVIIPRGADNLVAINLI 223
Cdd:PTZ00301 155 TFESVIEQYEATVRPMYYAYVEPSKVYADIIVPSWKDNSVAVGVL 199
UMPK_like cd02028
Uridine monophosphate kinase_like (UMPK_like) is a family of proteins highly similar to the ...
 24-198 1.29e-22

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


Pssm-ID: 238986 [Multi-domain]  Cd Length: 179  Bit Score: 91.21  E-value: 1.29e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283806560  24 LIGVAGGTASGKSSVCGKIMELLGQNkidhhQRQVAILSQDSFYRVLTPEQKAkalkgQFNFDHPDAFDNELIVKTLCEI 103
Cdd:cd02028    1 VVGIAGPSGSGKTTFAKKLSNQLRVN-----GIGPVVISLDDYYVPRKTPRDE-----DGNYDFESILDLDLLNKNLHDL 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283806560 104 MEGRTVQIPVYDFVTHSRK-EETVTVYPADVVLFEGIlmfY--SQEIRDLFQMKLFVDT-DADTRLSRRVLRDISERGRD 179
Cdd:cd02028   71 LNGKEVELPIYDFRTGKRRgYRKLKLPPSGVVILEGI---YalNERLRSLLDIRVAVSGgVHLNRLLRRVVRDIQFRGYS 147

                        170
                 ....*....|....*....
gi 283806560 180 LEQVLNQYITFvkPAFEEF 198
Cdd:cd02028  148 AELTILMWPSV--PSGEEF 164
PRK cd02026
Phosphoribulokinase (PRK) is an enzyme involved in the Benson-Calvin cycle in chloroplasts or ...
 24-210 3.50e-22

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: 92.40  E-value: 3.50e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283806560  24 LIGVAGGTASGKSSVCGKIMELLGQNkidhhqrQVAILSQDSFYRVltpEQKAKALKGQFNFDhPDAFDNELIVKTLCEI 103
Cdd:cd02026    1 IIGVAGDSGCGKSTFLRRLTSLFGSD-------LVTVICLDDYHSL---DRKGRKETGITALD-PRANNFDLMYEQLKAL 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283806560 104 MEGRTVQIPVYDFVTHS-RKEETVTvyPADVVLFEGILMFYSQEIRDLFQMKLFVDTDADTRLSRRVLRDISERGRDLEQ 182
Cdd:cd02026   70 KEGQAIEKPIYNHVTGLiDPPELIK--PTKIVVIEGLHPLYDERVRELLDFSVYLDISDEVKFAWKIQRDMAERGHSLED 147

                        170       180
                 ....*....|....*....|....*...
gi 283806560 183 VLNQyITFVKPAFEEFCLPTKKYADVII 210
Cdd:cd02026  148 VLAS-IEARKPDFEAYIDPQKQYADVVI 174
PRK07429 PRK07429
phosphoribulokinase; Provisional
 22-210 4.62e-21

phosphoribulokinase; Provisional


Pssm-ID: 180975  Cd Length: 327  Bit Score: 90.45  E-value: 4.62e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283806560  22 PFLIGVAGGTASGKSSVCGKIMELLGQNKidhhqrqVAILSQDSFYRvLTPEQKAK----ALkgqfnfdHPDAFDNELIV 97
Cdd:PRK07429   8 PVLLGVAGDSGCGKTTFLRGLADLLGEEL-------VTVICTDDYHS-YDRKQRKElgitAL-------DPRANNLDIMY 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283806560  98 KTLCEIMEGRTVQIPVYDFVTHSRkEETVTVYPADVVLFEGILMFYSQEIRDLFQMKLFVDTDADTRLSRRVLRDISERG 177
Cdd:PRK07429  73 EHLKALKTGQPILKPIYNHETGTF-DPPEYIEPNKIVVVEGLHPLYDERVRELYDFKVYLDPPEEVKIAWKIKRDMAKRG 151

                        170       180       190
                 ....*....|....*....|....*....|...
gi 283806560 178 RDLEQVLNQyITFVKPAFEEFCLPTKKYADVII 210
Cdd:PRK07429 152 HTYEQVLAE-IEAREPDFEAYIRPQRQWADVVI 183
PLN02348 PLN02348
phosphoribulokinase
 21-210 3.52e-19

phosphoribulokinase


Pssm-ID: 215198  Cd Length: 395  Bit Score: 85.67  E-value: 3.52e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283806560  21 QPFLIGVAGGTASGKSSVCGKIMELLG------------QNKIDHHQRQVAILsqDSFYRVLTPEQKAKALKGQfnfdHP 88
Cdd:PLN02348  48 GTVVIGLAADSGCGKSTFMRRLTSVFGgaakppkggnpdSNTLISDTTTVICL--DDYHSLDRTGRKEKGVTAL----DP 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283806560  89 DAFDNELIVKTLCEIMEGRTVQIPVYDFVThSRKEETVTVYPADVVLFEGILMFYSQEIRDLFQMKLFVDTDADTRLSRR 168
Cdd:PLN02348 122 RANNFDLMYEQVKALKEGKAVEKPIYNHVT-GLLDPPELIEPPKILVIEGLHPMYDERVRDLLDFSIYLDISDDVKFAWK 200

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 283806560 169 VLRDISERGRDLEQVLNQyITFVKPAFEEFCLPTKKYADVII 210
Cdd:PLN02348 201 IQRDMAERGHSLESIKAS-IEARKPDFDAYIDPQKQYADVVI 241
PLN02318 PLN02318
phosphoribulokinase/uridine kinase
 24-210 5.56e-16

phosphoribulokinase/uridine kinase


Pssm-ID: 177952 [Multi-domain]  Cd Length: 656  Bit Score: 77.21  E-value: 5.56e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283806560  24 LIGVAGGTASGKSSVCGKIMELLgqnkidhhqRQVAILSQDSFyrvltpEQKAKALKGqfNFDHPDAFDNELIVKTLCEI 103
Cdd:PLN02318  67 LVGVAGPSGAGKTVFTEKVLNFM---------PSIAVISMDNY------NDSSRIIDG--NFDDPRLTDYDTLLDNIHDL 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283806560 104 MEGRTVQIPVYDFVTHSR-KEETVTVYPADVVLFEGILMFySQEIRDLFQMKLFVDTDADTRLSRRVLRDISERGRDLEQ 182
Cdd:PLN02318 130 KAGKSVQVPIYDFKSSSRvGYRTLEVPSSRIVIIEGIYAL-SEKLRPLLDLRVSVTGGVHFDLVKRVLRDIQRAGQEPEE 208

                        170       180
                 ....*....|....*....|....*...
gi 283806560 183 VLNQYITFVKPAFEEFCLPTKKYADVII 210
Cdd:PLN02318 209 IIHQISETVYPMYKAFIEPDLQTAHIKI 236
CoaA COG1072
Panthothenate kinase [Coenzyme transport and metabolism]; Panthothenate kinase is part of the ...
 22-218 5.15e-13

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: 67.62  E-value: 5.15e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283806560  22 PFLIGVAGGTASGKSSVCGKIMELLGQnkiDHHQRQVAILSQDSF-Y--RVLtpeqKAKAL---KGqFnfdhPDAFDNEL 95
Cdd:COG1072   86 PFIIGIAGSVAVGKSTTARLLQALLSR---WPEHPKVELVTTDGFlYpnAVL----ERRGLmdrKG-F----PESYDRRG 153

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283806560  96 IVKTLCEIMEGR-TVQIPVYDFVTH-SRKEETVTVYPADVVLFEGI--L---MFYSQEIRDLFQMKLFVDTDADTRLSR- 167
Cdd:COG1072  154 LLRFLARVKSGDpEVRAPVYSHLLYdIVPGAIVVVDQPDILIVEGNnvLqdePNPWLFVSDFFDFSIYVDADEEDLREWy 233

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 283806560 168 --RVLRDISERGRDLEQVLNQY--------ITFVK--------PAFEEFCLPTKKYADVIIPRGADNLV 218
Cdd:COG1072  234 veRFLKLRETAFRDPDSYFHRYaglseeeaRAWAEeiwreinlPNLAENILPTRSRADLILRKGADHSV 302
PanK cd02025
Pantothenate kinase (PanK) catalyzes the phosphorylation of pantothenic acid to form 4 ...
 24-218 1.27e-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: 1.27e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283806560  24 LIGVAGGTASGKSsVCGKIMELLGQNKIDHhqRQVAILSQDSF-YRVLTPEQKAKALKGQFnfdhPDAFDNELIVKTLCE 102
Cdd:cd02025    1 IIGIAGSVAVGKS-TTARVLQALLSRWPDH--PNVELITTDGFlYPNKELIERGLMDRKGF----PESYDMEALLKFLKD 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283806560 103 IMEG-RTVQIPVYDFVTHSR-KEETVTVYPADVVLFEGILMF-----YSQEIRDLFQMKLFVDTDADtRLSR----RVLR 171
Cdd:cd02025   74 IKSGkKNVKIPVYSHLTYDViPGEKQTVDQPDILIIEGLNVLqtgqnPRLFVSDFFDFSIYVDADED-DIEKwyikRFLK 152

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 283806560 172 DISERGRDLEQVLNQY--------ITFVK--------PAFEEFCLPTKKYADVIIPRGADNLV 218
Cdd:cd02025  153 LRETAFSDPDSYFHRYakmseeeaIAFARevwkninlKNLRENILPTRNRADLILEKGADHSI 215
NRK1 cd02024
Nicotinamide riboside kinase (NRK) is an enzyme involved in the metabolism of nicotinamide ...
 24-168 2.80e-11

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: 60.80  E-value: 2.80e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283806560  24 LIGVAGGTASGKSSVCGKIMELLGQnkidhhqrqVAILSQDSFYRvlTPEQKAKALKGQFNFDHPDAFDNELIVKTLCEI 103
Cdd:cd02024    1 IVGISGVTNSGKTTLAKLLQRILPN---------CCVIHQDDFFK--PEDEIPVDENGFKQWDVLEALDMEAMMSTLDYW 69

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 283806560 104 MEGRTVQIPV--------YDFVTHSRKEETVTVYPAD------VVLFEGILMFYSQEIRDLFQMKLFVDTDADTRLSRR 168
Cdd:cd02024   70 RETGHFPKFLrshgnendPEKEFIEDAQIEETKADLLgaedlhILIVDGFLLYNYKPLVDLFDIRYFLRVPYETCKRRR 148
PRK08233 PRK08233
hypothetical protein; Provisional
 22-231 6.95e-10

hypothetical protein; Provisional


Pssm-ID: 181310 [Multi-domain]  Cd Length: 182  Bit Score: 56.68  E-value: 6.95e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283806560  22 PFLIGVAGGTASGKSSVCGKIMELLGQNKIDHHqrqvailsqDSFYRVLTPEQKAKALKGQFNFDhpdAFDNELIVKTLC 101
Cdd:PRK08233   3 TKIITIAAVSGGGKTTLTERLTHKLKNSKALYF---------DRYDFDNCPEDICKWIDKGANYS---EWVLTPLIKDIQ 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283806560 102 EIMEGRTVQIPVYDfvthsrkeetvtvYPadvvlfegiLMFYSQEIRDLFQMKLFVDTDADTRLSRRVLRDISER-GRDL 180
Cdd:PRK08233  71 ELIAKSNVDYIIVD-------------YP---------FAYLNSEMRQFIDVTIFIDTPLDIAMARRILRDFKEDtGNEI 128

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 283806560 181 EQVLNQYITFVKPAFEEFCLPTKKYADVIIprgaDNLVAINLIVQHIQDFL 231
Cdd:PRK08233 129 HNDLKHYLNYARPLYLEALHTVKPNADIVL----DGALSVEEIINQIEEEL 175
PRK06696 PRK06696
uridine kinase; Validated
 22-210 1.22e-05

uridine kinase; Validated


Pssm-ID: 180660  Cd Length: 223  Bit Score: 44.97  E-value: 1.22e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283806560  22 PFLIGVAGGTASGKSSVCGKIMELlgqnkIDHHQRQVAILSQDSFY--RVLTPEQKAKALKGQFNfdhpDAFD----NEL 95
Cdd:PRK06696  22 PLRVAIDGITASGKTTFADELAEE-----IKKRGRPVIRASIDDFHnpRVIRYRRGRESAEGYYE----DAYDytalRRL 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283806560  96 IVKTLCEIMEGRTVQIpVYDFVTHSRKEETVTVYPADVVLF-EGILMFySQEIRDLFQMKLFVDTDADTRLSRRVLRDIS 174
Cdd:PRK06696  93 LLDPLGPNGDRQYRTA-SHDLKTDIPVHNPPLLAAPNAVLIvDGTFLL-RPELRDLWDYKIFLDTDFEVSRRRGAKRDTE 170

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 283806560 175 ERG--RDLEQV-LNQYItfvkPAFE---EFCLPtKKYADVII 210
Cdd:PRK06696 171 AFGsyEEAEKMyLARYH----PAQKlyiAEANP-KERADVVI 207
PRK07667 PRK07667
uridine kinase; Provisional
 111-210 6.93e-04

uridine kinase; Provisional


Pssm-ID: 169051  Cd Length: 193  Bit Score: 39.71  E-value: 6.93e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283806560 111 IPVYDFVTHSRKEETVTVYPADVVLFEGILMfYSQEIRDLFQMKLFVDTDADTRLsrrvLRDISERGRDLEQVLNQYItf 190
Cdd:PRK07667 100 LPFYHDETDTCEMKKVQIPIVGVIVIEGVFL-QRKEWRDFFHYMVYLDCPRETRF----LRESEETQKNLSKFKNRYW-- 172

                         90       100
                 ....*....|....*....|...
gi 283806560 191 vkPAfEEFCLPT---KKYADVII 210
Cdd:PRK07667 173 --KA-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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