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Conserved domains on  [gi|972781896|ref|NP_001305448|]
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uridine-cytidine kinase 1 isoform e [Homo sapiens]

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

 Zoom to residue level

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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 ...
 25-207 5.75e-95

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: 277.13  E-value: 5.75e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972781896  25 LIGVSGGTASGKSTVCEKIMELLGQneveqrqRKVVILSQDRFYKVLTAEQKAKALKgqYNFDHPDAFDNDLMHRTLKNI 104
Cdd:cd02023    1 IIGIAGGSGSGKTTVAEEIIEQLGN-------PKVVIISQDSYYKDLSHEELEERKN--NNYDHPDAFDFDLLISHLQDL 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972781896 105 VEGKTVEVPTYDFVTHS-----------------------SQEIRDMFHLRLFVDTDSDVRLSRRVLRDVR-RGRDLEQI 160
Cdd:cd02023   72 KNGKSVEIPVYDFKTHSrlketvtvypadviilegilalyDKELRDLMDLKIFVDTDADVRLIRRIERDIVeRGRDLESV 151

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 972781896 161 LTQYTTFVKPAFEEFCLPTKKYADVIIPRGVDNMVAINLIVQHIQDI 207
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 ...
 25-207 5.75e-95

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: 277.13  E-value: 5.75e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972781896  25 LIGVSGGTASGKSTVCEKIMELLGQneveqrqRKVVILSQDRFYKVLTAEQKAKALKgqYNFDHPDAFDNDLMHRTLKNI 104
Cdd:cd02023    1 IIGIAGGSGSGKTTVAEEIIEQLGN-------PKVVIISQDSYYKDLSHEELEERKN--NNYDHPDAFDFDLLISHLQDL 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972781896 105 VEGKTVEVPTYDFVTHS-----------------------SQEIRDMFHLRLFVDTDSDVRLSRRVLRDVR-RGRDLEQI 160
Cdd:cd02023   72 KNGKSVEIPVYDFKTHSrlketvtvypadviilegilalyDKELRDLMDLKIFVDTDADVRLIRRIERDIVeRGRDLESV 151

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 972781896 161 LTQYTTFVKPAFEEFCLPTKKYADVIIPRGVDNMVAINLIVQHIQDI 207
Cdd:cd02023  152 INQYLKFVKPMHEQFIEPTKRYADVIIPRGGDNHVAIDLIVQHIKSK 198
PRK05480 PRK05480
uridine/cytidine kinase; Provisional
 21-211 5.61e-73

uridine/cytidine kinase; Provisional


Pssm-ID: 235492 [Multi-domain]  Cd Length: 209  Bit Score: 221.57  E-value: 5.61e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972781896  21 QRPFLIGVSGGTASGKSTVCEKIMELLGQNeveqrqrKVVILSQDRFYK---VLTAEQKAKAlkgqyNFDHPDAFDNDLM 97
Cdd:PRK05480   4 KKPIIIGIAGGSGSGKTTVASTIYEELGDE-------SIAVIPQDSYYKdqsHLSFEERVKT-----NYDHPDAFDHDLL 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972781896  98 HRTLKNIVEGKTVEVPTYDFVTHS-----------------------SQEIRDMFHLRLFVDTDSDVRLSRRVLRDVR-R 153
Cdd:PRK05480  72 IEHLKALKAGKAIEIPVYDYTEHTrsketirvepkdviilegillleDERLRDLMDIKIFVDTPLDIRLIRRLKRDVNeR 151

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 972781896 154 GRDLEQILTQYTTFVKPAFEEFCLPTKKYADVIIPRGVDNMVAINLIVQHIQDILNGD 211
Cdd:PRK05480 152 GRSLESVINQYLSTVRPMHLQFIEPSKRYADIIIPEGGKNRVAIDILKAKIRQLLEKN 209
Udk COG0572
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway ...
 21-206 2.32e-61

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: 191.98  E-value: 2.32e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972781896  21 QRPFLIGVSGGTASGKSTVCEKIMELLGQNeveqrqrKVVILSQDRFYKVLtaEQKAKALKGQYNFDHPDAFDNDLMHRT 100
Cdd:COG0572    5 GKPRIIGIAGPSGSGKTTFARRLAEQLGAD-------KVVVISLDDYYKDR--EHLPLDERGKPNFDHPEAFDLDLLNEH 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972781896 101 LKNIVEGKTVEVPTYDFVTHS-----------------------SQEIRDMFHLRLFVDTDSDVRLSRRVLRDVR-RGRD 156
Cdd:COG0572   76 LEPLKAGESVELPVYDFATGTrsgetvkvepadviivegihalnDELLRDLLDLKIYVDADTDVRLIRRIVRDGEeRGRT 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 972781896 157 LEQILTQYTTFVKPAFEEFCLPTKKYADVIIPR-GVDNMVAINLIVQHIQD 206
Cdd:COG0572  156 AESVIEQYWATVRPGHEQYIEPTKEYADIVIPNgGPLNPVALDLLVARLLS 206
udk TIGR00235
uridine kinase; Model contains a number of longer eukaryotic proteins and starts bringing in ...
 21-209 5.57e-61

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: 191.06  E-value: 5.57e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972781896   21 QRPFLIGVSGGTASGKSTVCEKIMELLGQneveqrqRKVVILSQDRFYKVLtaEQKAKALKGQYNFDHPDAFDNDLMHRT 100
Cdd:TIGR00235   4 PKGIIIGIGGGSGSGKTTVARKIYEQLGK-------LEIVIISQDNYYKDQ--SHLEMAERKKTNFDHPDAFDNDLLYEH 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972781896  101 LKNIVEGKTVEVPTYDFVTHSSQE-----------------------IRDMFHLRLFVDTDSDVRLSRRVLRDV-RRGRD 156
Cdd:TIGR00235  75 LKNLKNGSPIDVPVYDYVNHTRPKetvhiepkdvvilegimplfderLRDLMDLKIFVDTPLDIRLIRRIERDInERGRS 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 972781896  157 LEQILTQYTTFVKPAFEEFCLPTKKYADVIIPRGVDNMVAINLIVQHIQDILN 209
Cdd:TIGR00235 155 LDSVIDQYRKTVRPMYEQFVEPTKQYADLIIPEGGRNEVAINVLDTKIKHLLE 207
PRK pfam00485
Phosphoribulokinase / Uridine kinase family; This family matches three types of P-loop ...
 25-196 2.79e-44

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: 147.93  E-value: 2.79e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972781896   25 LIGVSGGTASGKSTVCEKIMELLGQNEVEQRQRK-VVILSQDRFYKVLTAEQKAKALKGQYNFDHPDAFDNDLMHRTLKN 103
Cdd:pfam00485   1 VIGVAGSSGSGKTTVARRIVSIFGREGVPAVGIEgDSFHSTDRFYMDLHPEDRKRAGNNGYSFDGPEANDFDLLYEQFKE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972781896  104 IVEGKTVEVPTYDFVTHSS-----------------------QEIRDMFHLRLFVDTDSDVRLSRRVLRDV-RRGRDLEQ 159
Cdd:pfam00485  81 LKEGGSVDKPIYNHVTHERdptpeliegadvlvieglhalydERVAQLLDLKIYVDPDIDLELARKIQRDMaERGHSLEG 160

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 972781896  160 ILTQYtTFVKPAFEEFCLPTKKYADVIIPRGVDNMVA 196
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 ...
 25-207 5.75e-95

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: 277.13  E-value: 5.75e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972781896  25 LIGVSGGTASGKSTVCEKIMELLGQneveqrqRKVVILSQDRFYKVLTAEQKAKALKgqYNFDHPDAFDNDLMHRTLKNI 104
Cdd:cd02023    1 IIGIAGGSGSGKTTVAEEIIEQLGN-------PKVVIISQDSYYKDLSHEELEERKN--NNYDHPDAFDFDLLISHLQDL 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972781896 105 VEGKTVEVPTYDFVTHS-----------------------SQEIRDMFHLRLFVDTDSDVRLSRRVLRDVR-RGRDLEQI 160
Cdd:cd02023   72 KNGKSVEIPVYDFKTHSrlketvtvypadviilegilalyDKELRDLMDLKIFVDTDADVRLIRRIERDIVeRGRDLESV 151

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 972781896 161 LTQYTTFVKPAFEEFCLPTKKYADVIIPRGVDNMVAINLIVQHIQDI 207
Cdd:cd02023  152 INQYLKFVKPMHEQFIEPTKRYADVIIPRGGDNHVAIDLIVQHIKSK 198
PRK05480 PRK05480
uridine/cytidine kinase; Provisional
 21-211 5.61e-73

uridine/cytidine kinase; Provisional


Pssm-ID: 235492 [Multi-domain]  Cd Length: 209  Bit Score: 221.57  E-value: 5.61e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972781896  21 QRPFLIGVSGGTASGKSTVCEKIMELLGQNeveqrqrKVVILSQDRFYK---VLTAEQKAKAlkgqyNFDHPDAFDNDLM 97
Cdd:PRK05480   4 KKPIIIGIAGGSGSGKTTVASTIYEELGDE-------SIAVIPQDSYYKdqsHLSFEERVKT-----NYDHPDAFDHDLL 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972781896  98 HRTLKNIVEGKTVEVPTYDFVTHS-----------------------SQEIRDMFHLRLFVDTDSDVRLSRRVLRDVR-R 153
Cdd:PRK05480  72 IEHLKALKAGKAIEIPVYDYTEHTrsketirvepkdviilegillleDERLRDLMDIKIFVDTPLDIRLIRRLKRDVNeR 151

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 972781896 154 GRDLEQILTQYTTFVKPAFEEFCLPTKKYADVIIPRGVDNMVAINLIVQHIQDILNGD 211
Cdd:PRK05480 152 GRSLESVINQYLSTVRPMHLQFIEPSKRYADIIIPEGGKNRVAIDILKAKIRQLLEKN 209
Udk COG0572
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway ...
 21-206 2.32e-61

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: 191.98  E-value: 2.32e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972781896  21 QRPFLIGVSGGTASGKSTVCEKIMELLGQNeveqrqrKVVILSQDRFYKVLtaEQKAKALKGQYNFDHPDAFDNDLMHRT 100
Cdd:COG0572    5 GKPRIIGIAGPSGSGKTTFARRLAEQLGAD-------KVVVISLDDYYKDR--EHLPLDERGKPNFDHPEAFDLDLLNEH 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972781896 101 LKNIVEGKTVEVPTYDFVTHS-----------------------SQEIRDMFHLRLFVDTDSDVRLSRRVLRDVR-RGRD 156
Cdd:COG0572   76 LEPLKAGESVELPVYDFATGTrsgetvkvepadviivegihalnDELLRDLLDLKIYVDADTDVRLIRRIVRDGEeRGRT 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 972781896 157 LEQILTQYTTFVKPAFEEFCLPTKKYADVIIPR-GVDNMVAINLIVQHIQD 206
Cdd:COG0572  156 AESVIEQYWATVRPGHEQYIEPTKEYADIVIPNgGPLNPVALDLLVARLLS 206
udk TIGR00235
uridine kinase; Model contains a number of longer eukaryotic proteins and starts bringing in ...
 21-209 5.57e-61

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: 191.06  E-value: 5.57e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972781896   21 QRPFLIGVSGGTASGKSTVCEKIMELLGQneveqrqRKVVILSQDRFYKVLtaEQKAKALKGQYNFDHPDAFDNDLMHRT 100
Cdd:TIGR00235   4 PKGIIIGIGGGSGSGKTTVARKIYEQLGK-------LEIVIISQDNYYKDQ--SHLEMAERKKTNFDHPDAFDNDLLYEH 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972781896  101 LKNIVEGKTVEVPTYDFVTHSSQE-----------------------IRDMFHLRLFVDTDSDVRLSRRVLRDV-RRGRD 156
Cdd:TIGR00235  75 LKNLKNGSPIDVPVYDYVNHTRPKetvhiepkdvvilegimplfderLRDLMDLKIFVDTPLDIRLIRRIERDInERGRS 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 972781896  157 LEQILTQYTTFVKPAFEEFCLPTKKYADVIIPRGVDNMVAINLIVQHIQDILN 209
Cdd:TIGR00235 155 LDSVIDQYRKTVRPMYEQFVEPTKQYADLIIPEGGRNEVAINVLDTKIKHLLE 207
PRK pfam00485
Phosphoribulokinase / Uridine kinase family; This family matches three types of P-loop ...
 25-196 2.79e-44

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: 147.93  E-value: 2.79e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972781896   25 LIGVSGGTASGKSTVCEKIMELLGQNEVEQRQRK-VVILSQDRFYKVLTAEQKAKALKGQYNFDHPDAFDNDLMHRTLKN 103
Cdd:pfam00485   1 VIGVAGSSGSGKTTVARRIVSIFGREGVPAVGIEgDSFHSTDRFYMDLHPEDRKRAGNNGYSFDGPEANDFDLLYEQFKE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972781896  104 IVEGKTVEVPTYDFVTHSS-----------------------QEIRDMFHLRLFVDTDSDVRLSRRVLRDV-RRGRDLEQ 159
Cdd:pfam00485  81 LKEGGSVDKPIYNHVTHERdptpeliegadvlvieglhalydERVAQLLDLKIYVDPDIDLELARKIQRDMaERGHSLEG 160

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 972781896  160 ILTQYtTFVKPAFEEFCLPTKKYADVIIPRGVDNMVA 196
Cdd:pfam00485 161 VTDSI-LFRKPDYVNYIDPQFSYADLIIQRVPTNDTA 196
PTZ00301 PTZ00301
uridine kinase; Provisional
 26-210 6.17e-21

uridine kinase; Provisional


Pssm-ID: 140322 [Multi-domain]  Cd Length: 210  Bit Score: 87.75  E-value: 6.17e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972781896  26 IGVSGGTASGKSTVCEKImelLGQNEVEQRQRKVVILSQDRFYKvlTAEQKAKALKGQYNFDHPDAFDNDLMHRTLKNIV 105
Cdd:PTZ00301   6 IGISGASGSGKSSLSTNI---VSELMAHCGPVSIGVICEDFYYR--DQSNIPESERAYTNYDHPKSLEHDLLTTHLRELK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972781896 106 EGKTVEVPTYDFVTH-----------------------SSQEIRDMFHLRLFVDTDSDVRLSRRVLRDVR-RGRDLEQIL 161
Cdd:PTZ00301  81 SGKTVQIPQYDYVHHtrsdtavtmtpksvlivegillfTNAELRNEMDCLIFVDTPLDICLIRRAKRDMReRGRTFESVI 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 972781896 162 TQYTTFVKPAFEEFCLPTKKYADVIIPRGVDNMVAINLIVQHIQDILNG 210
Cdd:PTZ00301 161 EQYEATVRPMYYAYVEPSKVYADIIVPSWKDNSVAVGVLRAKLNHDLEN 209
UMPK_like cd02028
Uridine monophosphate kinase_like (UMPK_like) is a family of proteins highly similar to the ...
 25-175 1.92e-17

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: 77.35  E-value: 1.92e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972781896  25 LIGVSGGTASGKSTVCEKImellgQNEVEQRQRKVVILSQDRFYKVLTAEQKAkalkgQYNFDHPDAFDNDLMHRTLKNI 104
Cdd:cd02028    1 VVGIAGPSGSGKTTFAKKL-----SNQLRVNGIGPVVISLDDYYVPRKTPRDE-----DGNYDFESILDLDLLNKNLHDL 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972781896 105 VEGKTVEVPTYDFVTHSSQEIRDM------------FH-----LRLFVDT-------DSDVRLSRRVLRDV-RRGRDLEQ 159
Cdd:cd02028   71 LNGKEVELPIYDFRTGKRRGYRKLklppsgvvilegIYalnerLRSLLDIrvavsggVHLNRLLRRVVRDIqFRGYSAEL 150

                        170
                 ....*....|....*.
gi 972781896 160 ILTQYTTFvkPAFEEF 175
Cdd:cd02028  151 TILMWPSV--PSGEEF 164
PRK cd02026
Phosphoribulokinase (PRK) is an enzyme involved in the Benson-Calvin cycle in chloroplasts or ...
 25-187 3.76e-16

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: 75.84  E-value: 3.76e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972781896  25 LIGVSGGTASGKSTVCEKIMELLGQNEVeqrqrkVVILSQDrfYKVLTAEQKAK----ALkgqynfdHPDAFDNDLMHRT 100
Cdd:cd02026    1 IIGVAGDSGCGKSTFLRRLTSLFGSDLV------TVICLDD--YHSLDRKGRKEtgitAL-------DPRANNFDLMYEQ 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972781896 101 LKNIVEGKTVEVPTYDFVT--------------------H--SSQEIRDMFHLRLFVDTDSDVRLSRRVLRDV-RRGRDL 157
Cdd:cd02026   66 LKALKEGQAIEKPIYNHVTglidppelikptkivvieglHplYDERVRELLDFSVYLDISDEVKFAWKIQRDMaERGHSL 145

                        170       180       190
                 ....*....|....*....|....*....|
gi 972781896 158 EQILTQYTTfVKPAFEEFCLPTKKYADVII 187
Cdd:cd02026  146 EDVLASIEA-RKPDFEAYIDPQKQYADVVI 174
PRK07429 PRK07429
phosphoribulokinase; Provisional
 21-187 5.30e-16

phosphoribulokinase; Provisional


Pssm-ID: 180975  Cd Length: 327  Bit Score: 75.82  E-value: 5.30e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972781896  21 QRPFLIGVSGGTASGKSTVCEKIMELLGQneveqrQRKVVILSQDrfYKVLTAEQKAK----ALkgqynfdHPDAFDNDL 96
Cdd:PRK07429   6 DRPVLLGVAGDSGCGKTTFLRGLADLLGE------ELVTVICTDD--YHSYDRKQRKElgitAL-------DPRANNLDI 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972781896  97 MHRTLKNIVEGKTVEVPTYD----------------FV------THSSQEIRDMFHLRLFVDTDSDVRLSRRVLRDV-RR 153
Cdd:PRK07429  71 MYEHLKALKTGQPILKPIYNhetgtfdppeyiepnkIVvveglhPLYDERVRELYDFKVYLDPPEEVKIAWKIKRDMaKR 150

                        170       180       190
                 ....*....|....*....|....*....|....
gi 972781896 154 GRDLEQILTQYTTfVKPAFEEFCLPTKKYADVII 187
Cdd:PRK07429 151 GHTYEQVLAEIEA-REPDFEAYIRPQRQWADVVI 183
PLN02348 PLN02348
phosphoribulokinase
 21-187 4.10e-15

phosphoribulokinase


Pssm-ID: 215198  Cd Length: 395  Bit Score: 74.11  E-value: 4.10e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972781896  21 QRPFLIGVSGGTASGKSTVCEKIMELLG------------QNEVEQRQRKVVILsqDRFYKVLTAEQKAKALKGQynfdH 88
Cdd:PLN02348  47 DGTVVIGLAADSGCGKSTFMRRLTSVFGgaakppkggnpdSNTLISDTTTVICL--DDYHSLDRTGRKEKGVTAL----D 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972781896  89 PDAFDNDLMHRTLKNIVEGKTVEVPTYDFVT--------------------HS--SQEIRDMFHLRLFVDTDSDVRLSRR 146
Cdd:PLN02348 121 PRANNFDLMYEQVKALKEGKAVEKPIYNHVTglldppelieppkilvieglHPmyDERVRDLLDFSIYLDISDDVKFAWK 200

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 972781896 147 VLRDV-RRGRDLEQILTQYTTfVKPAFEEFCLPTKKYADVII 187
Cdd:PLN02348 201 IQRDMaERGHSLESIKASIEA-RKPDFDAYIDPQKQYADVVI 241
PLN02318 PLN02318
phosphoribulokinase/uridine kinase
 25-187 2.72e-11

phosphoribulokinase/uridine kinase


Pssm-ID: 177952 [Multi-domain]  Cd Length: 656  Bit Score: 62.95  E-value: 2.72e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972781896  25 LIGVSGGTASGKSTVCEKIMELLGQneveqrqrkVVILSQDRFykvltaEQKAKALKGqyNFDHPDAFDNDLMHRTLKNI 104
Cdd:PLN02318  67 LVGVAGPSGAGKTVFTEKVLNFMPS---------IAVISMDNY------NDSSRIIDG--NFDDPRLTDYDTLLDNIHDL 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972781896 105 VEGKTVEVPTYDFVTHS-----------------------SQEIRDMFHLRLFVDTDSDVRLSRRVLRDVRR-GRDLEQI 160
Cdd:PLN02318 130 KAGKSVQVPIYDFKSSSrvgyrtlevpssriviiegiyalSEKLRPLLDLRVSVTGGVHFDLVKRVLRDIQRaGQEPEEI 209

                        170       180
                 ....*....|....*....|....*..
gi 972781896 161 LTQYTTFVKPAFEEFCLPTKKYADVII 187
Cdd:PLN02318 210 IHQISETVYPMYKAFIEPDLQTAHIKI 236
PRK08233 PRK08233
hypothetical protein; Provisional
 23-208 3.78e-10

hypothetical protein; Provisional


Pssm-ID: 181310 [Multi-domain]  Cd Length: 182  Bit Score: 57.45  E-value: 3.78e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972781896  23 PFLIGVSGGTASGKSTVCEKIMELLgqneveqrqRKVVILSQDRFYKVLTAEQKAKALKGQYNFDhpdAFDNDLMHRTLK 102
Cdd:PRK08233   3 TKIITIAAVSGGGKTTLTERLTHKL---------KNSKALYFDRYDFDNCPEDICKWIDKGANYS---EWVLTPLIKDIQ 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972781896 103 NIVEGKTVEVPTYDF-VTHSSQEIRDMFHLRLFVDTDSDVRLSRRVLRDVRR--GRDLEQILTQYTTFVKPAFEEFCLPT 179
Cdd:PRK08233  71 ELIAKSNVDYIIVDYpFAYLNSEMRQFIDVTIFIDTPLDIAMARRILRDFKEdtGNEIHNDLKHYLNYARPLYLEALHTV 150

                        170       180
                 ....*....|....*....|....*....
gi 972781896 180 KKYADVIIprgvDNMVAINLIVQHIQDIL 208
Cdd:PRK08233 151 KPNADIVL----DGALSVEEIINQIEEEL 175
NRK1 cd02024
Nicotinamide riboside kinase (NRK) is an enzyme involved in the metabolism of nicotinamide ...
 25-124 7.20e-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: 56.95  E-value: 7.20e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972781896  25 LIGVSGGTASGKSTVCEKIMELLGqneveqrqrKVVILSQDRFYKvlTAEQKAKALKGQYNFDHPDAFDNDLMHRTLKNI 104
Cdd:cd02024    1 IVGISGVTNSGKTTLAKLLQRILP---------NCCVIHQDDFFK--PEDEIPVDENGFKQWDVLEALDMEAMMSTLDYW 69

                         90       100
                 ....*....|....*....|
gi 972781896 105 VEGKTVEvptyDFVTHSSQE 124
Cdd:cd02024   70 RETGHFP----KFLRSHGNE 85
CoaA COG1072
Panthothenate kinase [Coenzyme transport and metabolism]; Panthothenate kinase is part of the ...
 18-195 9.49e-08

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: 51.83  E-value: 9.49e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972781896  18 RPHQRPFLIGVSGGTASGKSTVCEKIMELLGQnevEQRQRKVVILSQDRF-YKvlTAEQKAKAL---KGqynFdhPDAFD 93
Cdd:COG1072   81 ADKKTPFIIGIAGSVAVGKSTTARLLQALLSR---WPEHPKVELVTTDGFlYP--NAVLERRGLmdrKG---F--PESYD 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972781896  94 NDLMHRTLKNIVEGK-TVEVPTYDFVTH-----------------------------SSQEIRDMFHLRLFVDTDSDVRL 143
Cdd:COG1072  151 RRGLLRFLARVKSGDpEVRAPVYSHLLYdivpgaivvvdqpdilivegnnvlqdepnPWLFVSDFFDFSIYVDADEEDLR 230

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 972781896 144 SRRVLR--DVRR--------------GRDLEQILTQYTTFVK----PAFEEFCLPTKKYADVIIPRGVDNMV 195
Cdd:COG1072  231 EWYVERflKLREtafrdpdsyfhryaGLSEEEARAWAEEIWReinlPNLAENILPTRSRADLILRKGADHSV 302
PRK09270 PRK09270
nucleoside triphosphate hydrolase domain-containing protein; Reviewed
 21-166 2.20e-04

nucleoside triphosphate hydrolase domain-containing protein; Reviewed


Pssm-ID: 236442  Cd Length: 229  Bit Score: 41.46  E-value: 2.20e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972781896  21 QRPFLIGVSGGTASGKSTVCEKIMELLGQNEVEQRqrkvVILSQDRFY---KVLtAEQKAKALKGQynfdhPDAFD---- 93
Cdd:PRK09270  31 QRRTIVGIAGPPGAGKSTLAEFLEALLQQDGELPA----IQVPMDGFHldnAVL-DAHGLRPRKGA-----PETFDvagl 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972781896  94 NDLMHRtLKNivEGKTVEVPTYDFVTHSS----------------------------QEIRDMFHLRLFVDTDSDVRLSR 145
Cdd:PRK09270 101 AALLRR-LRA--GDDEVYWPVFDRSLEDPvadaivvpptarlvivegnyllldeepwRRLAGLFDFTIFLDAPAEVLRER 177

                        170       180
                 ....*....|....*....|.
gi 972781896 146 RVLRDVRRGRDLEQILTQYTT 166
Cdd:PRK09270 178 LVARKLAGGLSPEAAEAFVLR 198
PanK cd02025
Pantothenate kinase (PanK) catalyzes the phosphorylation of pantothenic acid to form 4 ...
 25-195 3.88e-04

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: 40.37  E-value: 3.88e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972781896  25 LIGVSGGTASGKSTVCEKIMELLgqneveQRQ---RKVVILSQDRF-YKvlTAEQKAKALKGQYNFdhPDAFDNDLMHRT 100
Cdd:cd02025    1 IIGIAGSVAVGKSTTARVLQALL------SRWpdhPNVELITTDGFlYP--NKELIERGLMDRKGF--PESYDMEALLKF 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972781896 101 LKNIVEGK-TVEVP-----TYDFVTHSSQEIR------------------------DMFHLRLFVDTDSDV----RLSRr 146
Cdd:cd02025   71 LKDIKSGKkNVKIPvyshlTYDVIPGEKQTVDqpdiliieglnvlqtgqnprlfvsDFFDFSIYVDADEDDiekwYIKR- 149

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 972781896 147 vLRDVRR--GRDLEQILTQYTTFVKPAFEEFC----------------LPTKKYADVIIPRGVDNMV 195
Cdd:cd02025  150 -FLKLREtaFSDPDSYFHRYAKMSEEEAIAFArevwkninlknlreniLPTRNRADLILEKGADHSI 215
CoaE COG0237
Dephospho-CoA kinase [Coenzyme transport and metabolism]; Dephospho-CoA kinase is part of the ...
 23-161 8.15e-04

Dephospho-CoA kinase [Coenzyme transport and metabolism]; Dephospho-CoA kinase is part of the Pathway/BioSystem: Pantothenate/CoA biosynthesis


Pssm-ID: 440007  Cd Length: 193  Bit Score: 39.28  E-value: 8.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972781896  23 PFLIGVSGGTASGKSTVCeKIMELLGqneveqrqrkVVILSQDRFYKVLTAEQKA--KALK-----------GQYN---- 85
Cdd:COG0237    1 MLIIGLTGGIGSGKSTVA-RMFAELG----------APVIDADAIARELVEPGGPalAAIVeafgeeildadGSLDrkal 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972781896  86 ----FDHPDAFD--NDLMH--------RTLKNIVEGKTV--EVPTYdFVTHSsqeiRDMFHLRLFVDTDSDVRLsRRVLR 149
Cdd:COG0237   70 aeivFADPEALKklEAIVHplvreeieRRLAAARGAPYVvlDIPLL-FETGL----EKLVDRVIVVDAPEEVQI-ERLMA 143

                        170
                 ....*....|..
gi 972781896 150 dvRRGRDLEQIL 161
Cdd:COG0237  144 --RDGLSEEEAE 153
PLN02796 PLN02796
D-glycerate 3-kinase
 14-116 4.13e-03

D-glycerate 3-kinase


Pssm-ID: 215427  Cd Length: 347  Bit Score: 37.80  E-value: 4.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972781896  14 PEADRPHQRPFLIGVSGGTASGKSTVCEKIMELLgqnevEQRQRKVVILSQDRFYkvLTAE-QKAKALKGQYNF-----D 87
Cdd:PLN02796  91 KFKDGDEIPPLVIGISAPQGCGKTTLVFALVYLF-----NATGRRAASLSIDDFY--LTAAdQAKLAEANPGNAllelrG 163

                         90       100       110
                 ....*....|....*....|....*....|...
gi 972781896  88 HPDAFDNDLMHRTLKNI----VEGKTVEVPTYD 116
Cdd:PLN02796 164 NAGSHDLALGVETLEALrklnKEGSKMKVPRYD 196
NK cd02019
Nucleoside/nucleotide kinase (NK) is a protein superfamily consisting of multiple families of ...
 25-53 9.05e-03

Nucleoside/nucleotide kinase (NK) is a protein superfamily consisting of multiple families of enzymes that share structural similarity and are functionally related to the catalysis of the reversible phosphate group transfer from nucleoside triphosphates to nucleosides/nucleotides, nucleoside monophosphates, or sugars. Members of this family play a wide variety of essential roles in nucleotide metabolism, the biosynthesis of coenzymes and aromatic compounds, as well as the metabolism of sugar and sulfate.


Pssm-ID: 238977 [Multi-domain]  Cd Length: 69  Bit Score: 34.23  E-value: 9.05e-03
                         10        20
                 ....*....|....*....|....*....
gi 972781896  25 LIGVSGGTASGKSTVCEKIMELLGQNEVE 53
Cdd:cd02019    1 IIAITGGSGSGKSTVAKKLAEQLGGRSVV 29
DPCK cd02022
Dephospho-coenzyme A kinase (DPCK, EC 2.7.1.24) catalyzes the phosphorylation of ...
 25-187 9.94e-03

Dephospho-coenzyme A kinase (DPCK, EC 2.7.1.24) catalyzes the phosphorylation of dephosphocoenzyme A (dCoA) to yield CoA, which is the final step in CoA biosynthesis.


Pssm-ID: 238980  Cd Length: 179  Bit Score: 35.96  E-value: 9.94e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972781896  25 LIGVSGGTASGKSTVCEKIMEL---------LGQNEVEQRQRKVVILSqDRFYKVLTAEQKA---KALkGQYNFDHPDAF 92
Cdd:cd02022    1 IIGLTGGIGSGKSTVAKLLKELgipvidadkIAHEVYEPGGPALQAIV-EAFGPDILLEDGEldrKKL-GEIVFADPEKR 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972781896  93 D--NDLMH--------RTLKNIVEGKTV--EVPTYdFVTHssqeIRDMFHLRLFVDTDSDVRLSRRVLRDVRRGRDLEQI 160
Cdd:cd02022   79 KklEAITHplirkeieEQLAEARKEKVVvlDIPLL-FETG----LEKLVDRVIVVDAPPEIQIERLMKRDGLSEEEAEAR 153

                        170       180
                 ....*....|....*....|....*...
gi 972781896 161 L-TQYTTFVKpafeefclptKKYADVII 187
Cdd:cd02022  154 IaSQMPLEEK----------RARADFVI 171
 
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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