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Conserved domains on  [gi|158186618|ref|NP_001101301|]
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uridine-cytidine kinase 1 [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 ...
 31-236 8.11e-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: 8.11e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186618  31 LIGVSGGTASGKSTVCEKIMELLGQNEVdrrqrklVILSQDCFYKVLTAEQKAKALKgqYNFDHPDAFDNDLMHKTLKNI 110
Cdd:cd02023    1 IIGIAGGSGSGKTTVAEEIIEQLGNPKV-------VIISQDSYYKDLSHEELEERKN--NNYDHPDAFDFDLLISHLQDL 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186618 111 VEGKTVEVPTYDFVTHSRLPETTVVYPADVVLFEGILVFYTQEIRDMFHLRLFVDTDSDVRLSRRVLRDVQ-RGRDLEQI 189
Cdd:cd02023   72 KNGKSVEIPVYDFKTHSRLKETVTVYPADVIILEGILALYDKELRDLMDLKIFVDTDADVRLIRRIERDIVeRGRDLESV 151

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 158186618 190 LTQYTAFVKPAFEEFCLPTKKYADVIIPRGVDNMVAINLIVQHIQDI 236
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 ...
 31-236 8.11e-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: 8.11e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186618  31 LIGVSGGTASGKSTVCEKIMELLGQNEVdrrqrklVILSQDCFYKVLTAEQKAKALKgqYNFDHPDAFDNDLMHKTLKNI 110
Cdd:cd02023    1 IIGIAGGSGSGKTTVAEEIIEQLGNPKV-------VIISQDSYYKDLSHEELEERKN--NNYDHPDAFDFDLLISHLQDL 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186618 111 VEGKTVEVPTYDFVTHSRLPETTVVYPADVVLFEGILVFYTQEIRDMFHLRLFVDTDSDVRLSRRVLRDVQ-RGRDLEQI 189
Cdd:cd02023   72 KNGKSVEIPVYDFKTHSRLKETVTVYPADVIILEGILALYDKELRDLMDLKIFVDTDADVRLIRRIERDIVeRGRDLESV 151

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 158186618 190 LTQYTAFVKPAFEEFCLPTKKYADVIIPRGVDNMVAINLIVQHIQDI 236
Cdd:cd02023  152 INQYLKFVKPMHEQFIEPTKRYADVIIPRGGDNHVAIDLIVQHIKSK 198
PRK05480 PRK05480
uridine/cytidine kinase; Provisional
 28-240 9.00e-93

uridine/cytidine kinase; Provisional


Pssm-ID: 235492 [Multi-domain]  Cd Length: 209  Bit Score: 272.80  E-value: 9.00e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186618  28 RPFLIGVSGGTASGKSTVCEKIMELLGQNEVdrrqrklVILSQDCFYK---VLTAEQKAKAlkgqyNFDHPDAFDNDLMH 104
Cdd:PRK05480   5 KPIIIGIAGGSGSGKTTVASTIYEELGDESI-------AVIPQDSYYKdqsHLSFEERVKT-----NYDHPDAFDHDLLI 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186618 105 KTLKNIVEGKTVEVPTYDFVTHSRLPETTVVYPADVVLFEGILVFYTQEIRDMFHLRLFVDTDSDVRLSRRVLRDVQ-RG 183
Cdd:PRK05480  73 EHLKALKAGKAIEIPVYDYTEHTRSKETIRVEPKDVIILEGILLLEDERLRDLMDIKIFVDTPLDIRLIRRLKRDVNeRG 152

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 158186618 184 RDLEQILTQYTAFVKPAFEEFCLPTKKYADVIIPRGVDNMVAINLIVQHIQDILNGD 240
Cdd:PRK05480 153 RSLESVINQYLSTVRPMHLQFIEPSKRYADIIIPEGGKNRVAIDILKAKIRQLLEKN 209
udk TIGR00235
uridine kinase; Model contains a number of longer eukaryotic proteins and starts bringing in ...
 27-238 2.64e-80

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: 241.14  E-value: 2.64e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186618   27 PRPFLIGVSGGTASGKSTVCEKIMELLGQNEVdrrqrklVILSQDCFYKVLtaEQKAKALKGQYNFDHPDAFDNDLMHKT 106
Cdd:TIGR00235   4 PKGIIIGIGGGSGSGKTTVARKIYEQLGKLEI-------VIISQDNYYKDQ--SHLEMAERKKTNFDHPDAFDNDLLYEH 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186618  107 LKNIVEGKTVEVPTYDFVTHSRLPETTVVYPADVVLFEGILVFYTQEIRDMFHLRLFVDTDSDVRLSRRVLRDVQ-RGRD 185
Cdd:TIGR00235  75 LKNLKNGSPIDVPVYDYVNHTRPKETVHIEPKDVVILEGIMPLFDERLRDLMDLKIFVDTPLDIRLIRRIERDINeRGRS 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 158186618  186 LEQILTQYTAFVKPAFEEFCLPTKKYADVIIPRGVDNMVAINLIVQHIQDILN 238
Cdd:TIGR00235 155 LDSVIDQYRKTVRPMYEQFVEPTKQYADLIIPEGGRNEVAINVLDTKIKHLLE 207
Udk COG0572
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway ...
 27-235 9.23e-79

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: 237.43  E-value: 9.23e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186618  27 PRPFLIGVSGGTASGKSTVCEKIMELLGQNEVdrrqrklVILSQDCFYKVLtaEQKAKALKGQYNFDHPDAFDNDLMHKT 106
Cdd:COG0572    5 GKPRIIGIAGPSGSGKTTFARRLAEQLGADKV-------VVISLDDYYKDR--EHLPLDERGKPNFDHPEAFDLDLLNEH 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186618 107 LKNIVEGKTVEVPTYDFVTHSRLPETTVVYPADVVLFEGILVFYTQEIRDMFHLRLFVDTDSDVRLSRRVLRDVQ-RGRD 185
Cdd:COG0572   76 LEPLKAGESVELPVYDFATGTRSGETVKVEPADVIIVEGIHALNDELLRDLLDLKIYVDADTDVRLIRRIVRDGEeRGRT 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 158186618 186 LEQILTQYTAFVKPAFEEFCLPTKKYADVIIPR-GVDNMVAINLIVQHIQD 235
Cdd:COG0572  156 AESVIEQYWATVRPGHEQYIEPTKEYADIVIPNgGPLNPVALDLLVARLLS 206
PRK pfam00485
Phosphoribulokinase / Uridine kinase family; This family matches three types of P-loop ...
 31-225 8.40e-59

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: 186.06  E-value: 8.40e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186618   31 LIGVSGGTASGKSTVCEKIMELLGQNEVDRRQRKL-VILSQDCFYKVLTAEQKAKALKGQYNFDHPDAFDNDLMHKTLKN 109
Cdd:pfam00485   1 VIGVAGSSGSGKTTVARRIVSIFGREGVPAVGIEGdSFHSTDRFYMDLHPEDRKRAGNNGYSFDGPEANDFDLLYEQFKE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186618  110 IVEGKTVEVPTYDFVTHSRLPETTVVYPADVVLFEGILVFYTQEIRDMFHLRLFVDTDSDVRLSRRVLRDV-QRGRDLEQ 188
Cdd:pfam00485  81 LKEGGSVDKPIYNHVTHERDPTPELIEGADVLVIEGLHALYDERVAQLLDLKIYVDPDIDLELARKIQRDMaERGHSLEG 160

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 158186618  189 ILTQYtAFVKPAFEEFCLPTKKYADVIIPRGVDNMVA 225
Cdd:pfam00485 161 VTDSI-LFRKPDYVNYIDPQFSYADLIIQRVPTNDTA 196
 
Name Accession Description Interval E-value
UMPK cd02023
Uridine monophosphate kinase (UMPK, EC 2.7.1.48), also known as uridine kinase or ...
 31-236 8.11e-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: 8.11e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186618  31 LIGVSGGTASGKSTVCEKIMELLGQNEVdrrqrklVILSQDCFYKVLTAEQKAKALKgqYNFDHPDAFDNDLMHKTLKNI 110
Cdd:cd02023    1 IIGIAGGSGSGKTTVAEEIIEQLGNPKV-------VIISQDSYYKDLSHEELEERKN--NNYDHPDAFDFDLLISHLQDL 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186618 111 VEGKTVEVPTYDFVTHSRLPETTVVYPADVVLFEGILVFYTQEIRDMFHLRLFVDTDSDVRLSRRVLRDVQ-RGRDLEQI 189
Cdd:cd02023   72 KNGKSVEIPVYDFKTHSRLKETVTVYPADVIILEGILALYDKELRDLMDLKIFVDTDADVRLIRRIERDIVeRGRDLESV 151

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 158186618 190 LTQYTAFVKPAFEEFCLPTKKYADVIIPRGVDNMVAINLIVQHIQDI 236
Cdd:cd02023  152 INQYLKFVKPMHEQFIEPTKRYADVIIPRGGDNHVAIDLIVQHIKSK 198
PRK05480 PRK05480
uridine/cytidine kinase; Provisional
 28-240 9.00e-93

uridine/cytidine kinase; Provisional


Pssm-ID: 235492 [Multi-domain]  Cd Length: 209  Bit Score: 272.80  E-value: 9.00e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186618  28 RPFLIGVSGGTASGKSTVCEKIMELLGQNEVdrrqrklVILSQDCFYK---VLTAEQKAKAlkgqyNFDHPDAFDNDLMH 104
Cdd:PRK05480   5 KPIIIGIAGGSGSGKTTVASTIYEELGDESI-------AVIPQDSYYKdqsHLSFEERVKT-----NYDHPDAFDHDLLI 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186618 105 KTLKNIVEGKTVEVPTYDFVTHSRLPETTVVYPADVVLFEGILVFYTQEIRDMFHLRLFVDTDSDVRLSRRVLRDVQ-RG 183
Cdd:PRK05480  73 EHLKALKAGKAIEIPVYDYTEHTRSKETIRVEPKDVIILEGILLLEDERLRDLMDIKIFVDTPLDIRLIRRLKRDVNeRG 152

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 158186618 184 RDLEQILTQYTAFVKPAFEEFCLPTKKYADVIIPRGVDNMVAINLIVQHIQDILNGD 240
Cdd:PRK05480 153 RSLESVINQYLSTVRPMHLQFIEPSKRYADIIIPEGGKNRVAIDILKAKIRQLLEKN 209
udk TIGR00235
uridine kinase; Model contains a number of longer eukaryotic proteins and starts bringing in ...
 27-238 2.64e-80

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: 241.14  E-value: 2.64e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186618   27 PRPFLIGVSGGTASGKSTVCEKIMELLGQNEVdrrqrklVILSQDCFYKVLtaEQKAKALKGQYNFDHPDAFDNDLMHKT 106
Cdd:TIGR00235   4 PKGIIIGIGGGSGSGKTTVARKIYEQLGKLEI-------VIISQDNYYKDQ--SHLEMAERKKTNFDHPDAFDNDLLYEH 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186618  107 LKNIVEGKTVEVPTYDFVTHSRLPETTVVYPADVVLFEGILVFYTQEIRDMFHLRLFVDTDSDVRLSRRVLRDVQ-RGRD 185
Cdd:TIGR00235  75 LKNLKNGSPIDVPVYDYVNHTRPKETVHIEPKDVVILEGIMPLFDERLRDLMDLKIFVDTPLDIRLIRRIERDINeRGRS 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 158186618  186 LEQILTQYTAFVKPAFEEFCLPTKKYADVIIPRGVDNMVAINLIVQHIQDILN 238
Cdd:TIGR00235 155 LDSVIDQYRKTVRPMYEQFVEPTKQYADLIIPEGGRNEVAINVLDTKIKHLLE 207
Udk COG0572
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway ...
 27-235 9.23e-79

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: 237.43  E-value: 9.23e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186618  27 PRPFLIGVSGGTASGKSTVCEKIMELLGQNEVdrrqrklVILSQDCFYKVLtaEQKAKALKGQYNFDHPDAFDNDLMHKT 106
Cdd:COG0572    5 GKPRIIGIAGPSGSGKTTFARRLAEQLGADKV-------VVISLDDYYKDR--EHLPLDERGKPNFDHPEAFDLDLLNEH 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186618 107 LKNIVEGKTVEVPTYDFVTHSRLPETTVVYPADVVLFEGILVFYTQEIRDMFHLRLFVDTDSDVRLSRRVLRDVQ-RGRD 185
Cdd:COG0572   76 LEPLKAGESVELPVYDFATGTRSGETVKVEPADVIIVEGIHALNDELLRDLLDLKIYVDADTDVRLIRRIVRDGEeRGRT 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 158186618 186 LEQILTQYTAFVKPAFEEFCLPTKKYADVIIPR-GVDNMVAINLIVQHIQD 235
Cdd:COG0572  156 AESVIEQYWATVRPGHEQYIEPTKEYADIVIPNgGPLNPVALDLLVARLLS 206
PRK pfam00485
Phosphoribulokinase / Uridine kinase family; This family matches three types of P-loop ...
 31-225 8.40e-59

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: 186.06  E-value: 8.40e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186618   31 LIGVSGGTASGKSTVCEKIMELLGQNEVDRRQRKL-VILSQDCFYKVLTAEQKAKALKGQYNFDHPDAFDNDLMHKTLKN 109
Cdd:pfam00485   1 VIGVAGSSGSGKTTVARRIVSIFGREGVPAVGIEGdSFHSTDRFYMDLHPEDRKRAGNNGYSFDGPEANDFDLLYEQFKE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186618  110 IVEGKTVEVPTYDFVTHSRLPETTVVYPADVVLFEGILVFYTQEIRDMFHLRLFVDTDSDVRLSRRVLRDV-QRGRDLEQ 188
Cdd:pfam00485  81 LKEGGSVDKPIYNHVTHERDPTPELIEGADVLVIEGLHALYDERVAQLLDLKIYVDPDIDLELARKIQRDMaERGHSLEG 160

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 158186618  189 ILTQYtAFVKPAFEEFCLPTKKYADVIIPRGVDNMVA 225
Cdd:pfam00485 161 VTDSI-LFRKPDYVNYIDPQFSYADLIIQRVPTNDTA 196
PTZ00301 PTZ00301
uridine kinase; Provisional
 32-239 4.32e-31

uridine kinase; Provisional


Pssm-ID: 140322 [Multi-domain]  Cd Length: 210  Bit Score: 115.10  E-value: 4.32e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186618  32 IGVSGGTASGKSTVCEKIM-ELLGQNEVDRrqrkLVILSQDCFYKvlTAEQKAKALKGQYNFDHPDAFDNDLMHKTLKNI 110
Cdd:PTZ00301   6 IGISGASGSGKSSLSTNIVsELMAHCGPVS----IGVICEDFYYR--DQSNIPESERAYTNYDHPKSLEHDLLTTHLREL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186618 111 VEGKTVEVPTYDFVTHSRLPETTVVYPADVVLFEGILVFYTQEIRDMFHLRLFVDTDSDVRLSRRVLRDV-QRGRDLEQI 189
Cdd:PTZ00301  80 KSGKTVQIPQYDYVHHTRSDTAVTMTPKSVLIVEGILLFTNAELRNEMDCLIFVDTPLDICLIRRAKRDMrERGRTFESV 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 158186618 190 LTQYTAFVKPAFEEFCLPTKKYADVIIPRGVDNMVAINLIVQHIQDILNG 239
Cdd:PTZ00301 160 IEQYEATVRPMYYAYVEPSKVYADIIVPSWKDNSVAVGVLRAKLNHDLEN 209
PRK cd02026
Phosphoribulokinase (PRK) is an enzyme involved in the Benson-Calvin cycle in chloroplasts or ...
 31-216 7.95e-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: 102.80  E-value: 7.95e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186618  31 LIGVSGGTASGKSTVCEKIMELLGQNEV-----------DRRQRKlvilsqdcfykvltaEQKAKALkgqynfdHPDAFD 99
Cdd:cd02026    1 IIGVAGDSGCGKSTFLRRLTSLFGSDLVtviclddyhslDRKGRK---------------ETGITAL-------DPRANN 58

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186618 100 NDLMHKTLKNIVEGKTVEVPTYDFVTHS-RLPETtvVYPADVVLFEGILVFYTQEIRDMFHLRLFVDTDSDVRLSRRVLR 178
Cdd:cd02026   59 FDLMYEQLKALKEGQAIEKPIYNHVTGLiDPPEL--IKPTKIVVIEGLHPLYDERVRELLDFSVYLDISDEVKFAWKIQR 136

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 158186618 179 DV-QRGRDLEQILTQYTAfVKPAFEEFCLPTKKYADVII 216
Cdd:cd02026  137 DMaERGHSLEDVLASIEA-RKPDFEAYIDPQKQYADVVI 174
PRK07429 PRK07429
phosphoribulokinase; Provisional
 28-216 1.62e-23

phosphoribulokinase; Provisional


Pssm-ID: 180975  Cd Length: 327  Bit Score: 97.77  E-value: 1.62e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186618  28 RPFLIGVSGGTASGKSTVCEKIMELLGQNEV-----------DRRQRKlvilsqdcfykvltaEQKAKALkgqynfdHPD 96
Cdd:PRK07429   7 RPVLLGVAGDSGCGKTTFLRGLADLLGEELVtvictddyhsyDRKQRK---------------ELGITAL-------DPR 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186618  97 AFDNDLMHKTLKNIVEGKTVEVPTYDFVTHSRLPETTVVyPADVVLFEGILVFYTQEIRDMFHLRLFVDTDSDVRLSRRV 176
Cdd:PRK07429  65 ANNLDIMYEHLKALKTGQPILKPIYNHETGTFDPPEYIE-PNKIVVVEGLHPLYDERVRELYDFKVYLDPPEEVKIAWKI 143

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 158186618 177 LRDVQ-RGRDLEQILTQYTAfVKPAFEEFCLPTKKYADVII 216
Cdd:PRK07429 144 KRDMAkRGHTYEQVLAEIEA-REPDFEAYIRPQRQWADVVI 183
UMPK_like cd02028
Uridine monophosphate kinase_like (UMPK_like) is a family of proteins highly similar to the ...
 31-204 9.72e-23

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


Pssm-ID: 238986 [Multi-domain]  Cd Length: 179  Bit Score: 91.98  E-value: 9.72e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186618  31 LIGVSGGTASGKSTVCEKImellgQNEVDRRQRKLVILSQDCFYKVLTAEQKAkalkgQYNFDHPDAFDNDLMHKTLKNI 110
Cdd:cd02028    1 VVGIAGPSGSGKTTFAKKL-----SNQLRVNGIGPVVISLDDYYVPRKTPRDE-----DGNYDFESILDLDLLNKNLHDL 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186618 111 VEGKTVEVPTYDFVTHSRLPETTVVYP-ADVVLFEGIlvfY--TQEIRDMFHLRLFVDT-DSDVRLSRRVLRDVQ-RGRD 185
Cdd:cd02028   71 LNGKEVELPIYDFRTGKRRGYRKLKLPpSGVVILEGI---YalNERLRSLLDIRVAVSGgVHLNRLLRRVVRDIQfRGYS 147

                        170
                 ....*....|....*....
gi 158186618 186 LEQILTQYTAFvkPAFEEF 204
Cdd:cd02028  148 AELTILMWPSV--PSGEEF 164
PLN02348 PLN02348
phosphoribulokinase
 27-216 9.73e-22

phosphoribulokinase


Pssm-ID: 215198  Cd Length: 395  Bit Score: 93.76  E-value: 9.73e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186618  27 PRPFLIGVSGGTASGKSTVCEKIMELLGQNEVDRR-----QRKLV-----ILSQDCFYKVLTAEQKAKALKGQynfdHPD 96
Cdd:PLN02348  47 DGTVVIGLAADSGCGKSTFMRRLTSVFGGAAKPPKggnpdSNTLIsdtttVICLDDYHSLDRTGRKEKGVTAL----DPR 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186618  97 AFDNDLMHKTLKNIVEGKTVEVPTYDFVThSRLPETTVVYPADVVLFEGILVFYTQEIRDMFHLRLFVDTDSDVRLSRRV 176
Cdd:PLN02348 123 ANNFDLMYEQVKALKEGKAVEKPIYNHVT-GLLDPPELIEPPKILVIEGLHPMYDERVRDLLDFSIYLDISDDVKFAWKI 201

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 158186618 177 LRDV-QRGRDLEQILTQYTAfVKPAFEEFCLPTKKYADVII 216
Cdd:PLN02348 202 QRDMaERGHSLESIKASIEA-RKPDFDAYIDPQKQYADVVI 241
PLN02318 PLN02318
phosphoribulokinase/uridine kinase
 31-216 8.45e-17

phosphoribulokinase/uridine kinase


Pssm-ID: 177952 [Multi-domain]  Cd Length: 656  Bit Score: 80.29  E-value: 8.45e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186618  31 LIGVSGGTASGKSTVCEKIMELLgqnevdrrqRKLVILSQDCFykvltaEQKAKALKGqyNFDHPDAFDNDLMHKTLKNI 110
Cdd:PLN02318  67 LVGVAGPSGAGKTVFTEKVLNFM---------PSIAVISMDNY------NDSSRIIDG--NFDDPRLTDYDTLLDNIHDL 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186618 111 VEGKTVEVPTYDFVTHSRLPETTVVYPAD-VVLFEGILVFyTQEIRDMFHLRLFVDTDSDVRLSRRVLRDVQR-GRDLEQ 188
Cdd:PLN02318 130 KAGKSVQVPIYDFKSSSRVGYRTLEVPSSrIVIIEGIYAL-SEKLRPLLDLRVSVTGGVHFDLVKRVLRDIQRaGQEPEE 208

                        170       180
                 ....*....|....*....|....*...
gi 158186618 189 ILTQYTAFVKPAFEEFCLPTKKYADVII 216
Cdd:PLN02318 209 IIHQISETVYPMYKAFIEPDLQTAHIKI 236
NRK1 cd02024
Nicotinamide riboside kinase (NRK) is an enzyme involved in the metabolism of nicotinamide ...
 31-175 2.28e-14

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: 69.66  E-value: 2.28e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186618  31 LIGVSGGTASGKSTVCEKIMELLGqnevdrrqrKLVILSQDCFYKvlTAEQKAKALKGQYNFDHPDAFDNDLMHKTLKNI 110
Cdd:cd02024    1 IVGISGVTNSGKTTLAKLLQRILP---------NCCVIHQDDFFK--PEDEIPVDENGFKQWDVLEALDMEAMMSTLDYW 69

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 158186618 111 VEGKTVE--------VPTYDFVTHSRLPETTVVYPAD------VVLFEGILVFYTQEIRDMFHLRLFVDTDSDVRLSRR 175
Cdd:cd02024   70 RETGHFPkflrshgnENDPEKEFIEDAQIEETKADLLgaedlhILIVDGFLLYNYKPLVDLFDIRYFLRVPYETCKRRR 148
CoaA COG1072
Panthothenate kinase [Coenzyme transport and metabolism]; Panthothenate kinase is part of the ...
 24-224 7.18e-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: 70.32  E-value: 7.18e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186618  24 RPQPRPFLIGVSGGTASGKSTVCEKIMELLGQnevDRRQRKLVILSQDCF-YKvlTAEQKAKAL---KGqynFdhPDAFD 99
Cdd:COG1072   81 ADKKTPFIIGIAGSVAVGKSTTARLLQALLSR---WPEHPKVELVTTDGFlYP--NAVLERRGLmdrKG---F--PESYD 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186618 100 NDLMHKTLKNIVEGK-TVEVPTYDFVTHSRLP-ETTVVYPADVVLFEGILVFYTQE-----IRDMFHLRLFVDTDSDVRL 172
Cdd:COG1072  151 RRGLLRFLARVKSGDpEVRAPVYSHLLYDIVPgAIVVVDQPDILIVEGNNVLQDEPnpwlfVSDFFDFSIYVDADEEDLR 230

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186618 173 SRRvlrdVQRGRDLEQiltqyTAFVKPA-----------------------------FEEFCLPTKKYADVIIPRGVDNM 223
Cdd:COG1072  231 EWY----VERFLKLRE-----TAFRDPDsyfhryaglseeearawaeeiwreinlpnLAENILPTRSRADLILRKGADHS 301


                 .
gi 158186618 224 V 224
Cdd:COG1072  302 V 302
PanK cd02025
Pantothenate kinase (PanK) catalyzes the phosphorylation of pantothenic acid to form 4 ...
 31-224 4.44e-12

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: 63.87  E-value: 4.44e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186618  31 LIGVSGGTASGKSTVCeKIMELLGQNEVDRRQRKLVilSQDCF-YKvlTAEQKAKALKGQYNFdhPDAFDNDLMHKTLKN 109
Cdd:cd02025    1 IIGIAGSVAVGKSTTA-RVLQALLSRWPDHPNVELI--TTDGFlYP--NKELIERGLMDRKGF--PESYDMEALLKFLKD 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186618 110 IVEGK-TVEVPTYDFVTHSRLPET-TVVYPADVVLFEGILVFYTQE-----IRDMFHLRLFVDTDSDV----RLSR-RVL 177
Cdd:cd02025   74 IKSGKkNVKIPVYSHLTYDVIPGEkQTVDQPDILIIEGLNVLQTGQnprlfVSDFFDFSIYVDADEDDiekwYIKRfLKL 153

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 158186618 178 RDvQRGRDLEQILTQYTAFVKPAFEEFC----------------LPTKKYADVIIPRGVDNMV 224
Cdd:cd02025  154 RE-TAFSDPDSYFHRYAKMSEEEAIAFArevwkninlknlreniLPTRNRADLILEKGADHSI 215
PRK09270 PRK09270
nucleoside triphosphate hydrolase domain-containing protein; Reviewed
 5-194 3.57e-08

nucleoside triphosphate hydrolase domain-containing protein; Reviewed


Pssm-ID: 236442  Cd Length: 229  Bit Score: 53.01  E-value: 3.57e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186618   5 PEMASAGGGGSESAAPEADRPQPRpFLIGVSGGTASGKSTVCEKIMELLGQnevdRRQRKLVILSQDCF--YKVLTAEQK 82
Cdd:PRK09270  10 EEIEAVHKPLLRRLAALQAEPQRR-TIVGIAGPPGAGKSTLAEFLEALLQQ----DGELPAIQVPMDGFhlDNAVLDAHG 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186618  83 AKALKGQynfdhPDAFDNDLMHKTLKNIVEG-KTVEVPTYDFVTHSRLPETTVVYP-ADVVLFEGILVFYTQ----EIRD 156
Cdd:PRK09270  85 LRPRKGA-----PETFDVAGLAALLRRLRAGdDEVYWPVFDRSLEDPVADAIVVPPtARLVIVEGNYLLLDEepwrRLAG 159

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 158186618 157 MFHLRLFVDTDSDVRLSRRVLRDVQRGRDLEQILTQYT 194
Cdd:PRK09270 160 LFDFTIFLDAPAEVLRERLVARKLAGGLSPEAAEAFVL 197
PRK08233 PRK08233
hypothetical protein; Provisional
 29-237 6.75e-07

hypothetical protein; Provisional


Pssm-ID: 181310 [Multi-domain]  Cd Length: 182  Bit Score: 48.59  E-value: 6.75e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186618  29 PFLIGVSGGTASGKSTVCEKIMELLgqnevdrrqRKLVILSQDCFYKVLTAEQKAKALKGQYNFDhpdAFDNDLMHKTLK 108
Cdd:PRK08233   3 TKIITIAAVSGGGKTTLTERLTHKL---------KNSKALYFDRYDFDNCPEDICKWIDKGANYS---EWVLTPLIKDIQ 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186618 109 NIVEGKTVEVPTYDfvthsrlpettvvYPadvvlfegiLVFYTQEIRDMFHLRLFVDTDSDVRLSRRVLRDV--QRGRDL 186
Cdd:PRK08233  71 ELIAKSNVDYIIVD-------------YP---------FAYLNSEMRQFIDVTIFIDTPLDIAMARRILRDFkeDTGNEI 128

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 158186618 187 EQILTQYTAFVKPAFEEFCLPTKKYADVIIprgvDNMVAINLIVQHIQDIL 237
Cdd:PRK08233 129 HNDLKHYLNYARPLYLEALHTVKPNADIVL----DGALSVEEIINQIEEEL 175
PRK06696 PRK06696
uridine kinase; Validated
 27-216 8.20e-07

uridine kinase; Validated


Pssm-ID: 180660  Cd Length: 223  Bit Score: 48.82  E-value: 8.20e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186618  27 PRPFLIGVSGGTASGKSTVCEKIMEllgqnEVDRRQRKLVILSQDCFY--KVLTAEQKAKALKGQYNfdhpDAFDND-LM 103
Cdd:PRK06696  20 TRPLRVAIDGITASGKTTFADELAE-----EIKKRGRPVIRASIDDFHnpRVIRYRRGRESAEGYYE----DAYDYTaLR 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186618 104 HKTLKNIVEGKTVEVPT--YDFVTHSRLPETTVVYPADVVLF-EGILVFyTQEIRDMFHLRLFVDTDSDVRLSRRVLRDV 180
Cdd:PRK06696  91 RLLLDPLGPNGDRQYRTasHDLKTDIPVHNPPLLAAPNAVLIvDGTFLL-RPELRDLWDYKIFLDTDFEVSRRRGAKRDT 169

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 158186618 181 QRGRDLEQILTQYTAFVKPAFE---EFCLPtKKYADVII 216
Cdd:PRK06696 170 EAFGSYEEAEKMYLARYHPAQKlyiAEANP-KERADVVI 207
PLN02796 PLN02796
D-glycerate 3-kinase
 20-145 3.01e-06

D-glycerate 3-kinase


Pssm-ID: 215427  Cd Length: 347  Bit Score: 47.81  E-value: 3.01e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186618  20 PEADRPQPRPFLIGVSGGTASGKSTVCEKIMELLgqnevDRRQRKLVILSQDCFYkvLTAE-QKAKALKGQYNF-----D 93
Cdd:PLN02796  91 KFKDGDEIPPLVIGISAPQGCGKTTLVFALVYLF-----NATGRRAASLSIDDFY--LTAAdQAKLAEANPGNAllelrG 163

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 158186618  94 HPDAFDNDLMHKTLKNI----VEGKTVEVPTYDFVTHS----RLPETT---VVYPADVVLFEG 145
Cdd:PLN02796 164 NAGSHDLALGVETLEALrklnKEGSKMKVPRYDKSAYGgrgdRADPSTwpeVEGPLDVVLFEG 226
PRK07667 PRK07667
uridine kinase; Provisional
 102-216 3.10e-03

uridine kinase; Provisional


Pssm-ID: 169051  Cd Length: 193  Bit Score: 37.79  E-value: 3.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186618 102 LMHKTLKNIVEGKTVEVPTYDFVTHSRLPETTVVYPADVVLFEGILVfYTQEIRDMFHLRLFVDTDSDVRLSrRVLRDVQ 181
Cdd:PRK07667  84 LRQKFFRKLQNETKLTLPFYHDETDTCEMKKVQIPIVGVIVIEGVFL-QRKEWRDFFHYMVYLDCPRETRFL-RESEETQ 161

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 158186618 182 rgRDLEQILTQYTafvkPAfEEFCLPT---KKYADVII 216
Cdd:PRK07667 162 --KNLSKFKNRYW----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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