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Conserved domains on  [gi|20455360|sp|Q9HA47|]
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RecName: Full=Uridine-cytidine kinase 1; Short=UCK 1; AltName: Full=Cytidine monophosphokinase 1; AltName: Full=Uridine monophosphokinase 1

Protein Classification

uridine-cytidine kinase( domain architecture ID 10113977)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
UMPK cd02023
Uridine monophosphate kinase (UMPK, EC 2.7.1.48), also known as uridine kinase or ...
 25-230 1.46e-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: 332.60  E-value: 1.46e-116
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20455360  25 LIGVSGGTASGKSTVCEKIMELLGQneveqrqRKVVILSQDRFYKVLTAEQKAKALKgqYNFDHPDAFDNDLMHRTLKNI 104
Cdd:cd02023   1 IIGIAGGSGSGKTTVAEEIIEQLGN-------PKVVIISQDSYYKDLSHEELEERKN--NNYDHPDAFDFDLLISHLQDL 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20455360 105 VEGKTVEVPTYDFVTHSRLPETTVVYPADVVLFEGILVFYSQEIRDMFHLRLFVDTDSDVRLSRRVLRDVR-RGRDLEQI 183
Cdd:cd02023  72 KNGKSVEIPVYDFKTHSRLKETVTVYPADVIILEGILALYDKELRDLMDLKIFVDTDADVRLIRRIERDIVeRGRDLESV 151

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 20455360 184 LTQYTTFVKPAFEEFCLPTKKYADVIIPRGVDNMVAINLIVQHIQDI 230
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 ...
 25-230 1.46e-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: 332.60  E-value: 1.46e-116
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20455360  25 LIGVSGGTASGKSTVCEKIMELLGQneveqrqRKVVILSQDRFYKVLTAEQKAKALKgqYNFDHPDAFDNDLMHRTLKNI 104
Cdd:cd02023   1 IIGIAGGSGSGKTTVAEEIIEQLGN-------PKVVIISQDSYYKDLSHEELEERKN--NNYDHPDAFDFDLLISHLQDL 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20455360 105 VEGKTVEVPTYDFVTHSRLPETTVVYPADVVLFEGILVFYSQEIRDMFHLRLFVDTDSDVRLSRRVLRDVR-RGRDLEQI 183
Cdd:cd02023  72 KNGKSVEIPVYDFKTHSRLKETVTVYPADVIILEGILALYDKELRDLMDLKIFVDTDADVRLIRRIERDIVeRGRDLESV 151

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 20455360 184 LTQYTTFVKPAFEEFCLPTKKYADVIIPRGVDNMVAINLIVQHIQDI 230
Cdd:cd02023 152 INQYLKFVKPMHEQFIEPTKRYADVIIPRGGDNHVAIDLIVQHIKSK 198
PRK05480 PRK05480
uridine/cytidine kinase; Provisional
 21-234 2.14e-91

uridine/cytidine kinase; Provisional


Pssm-ID: 235492 [Multi-domain]  Cd Length: 209  Bit Score: 269.34  E-value: 2.14e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20455360   21 QRPFLIGVSGGTASGKSTVCEKIMELLGQNeveqrqrKVVILSQDRFYK---VLTAEQKAKAlkgqyNFDHPDAFDNDLM 97
Cdd:PRK05480   4 KKPIIIGIAGGSGSGKTTVASTIYEELGDE-------SIAVIPQDSYYKdqsHLSFEERVKT-----NYDHPDAFDHDLL 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20455360   98 HRTLKNIVEGKTVEVPTYDFVTHSRLPETTVVYPADVVLFEGILVFYSQEIRDMFHLRLFVDTDSDVRLSRRVLRDVR-R 176
Cdd:PRK05480  72 IEHLKALKAGKAIEIPVYDYTEHTRSKETIRVEPKDVIILEGILLLEDERLRDLMDIKIFVDTPLDIRLIRRLKRDVNeR 151

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 20455360  177 GRDLEQILTQYTTFVKPAFEEFCLPTKKYADVIIPRGVDNMVAINLIVQHIQDILNGD 234
Cdd:PRK05480 152 GRSLESVINQYLSTVRPMHLQFIEPSKRYADIIIPEGGKNRVAIDILKAKIRQLLEKN 209
Udk COG0572
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway ...
 21-229 2.61e-77

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: 233.19  E-value: 2.61e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20455360  21 QRPFLIGVSGGTASGKSTVCEKIMELLGQNeveqrqrKVVILSQDRFYKVLtaEQKAKALKGQYNFDHPDAFDNDLMHRT 100
Cdd:COG0572   5 GKPRIIGIAGPSGSGKTTFARRLAEQLGAD-------KVVVISLDDYYKDR--EHLPLDERGKPNFDHPEAFDLDLLNEH 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20455360 101 LKNIVEGKTVEVPTYDFVTHSRLPETTVVYPADVVLFEGILVFYSQEIRDMFHLRLFVDTDSDVRLSRRVLRDVR-RGRD 179
Cdd:COG0572  76 LEPLKAGESVELPVYDFATGTRSGETVKVEPADVIIVEGIHALNDELLRDLLDLKIYVDADTDVRLIRRIVRDGEeRGRT 155

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 20455360 180 LEQILTQYTTFVKPAFEEFCLPTKKYADVIIPR-GVDNMVAINLIVQHIQD 229
Cdd:COG0572 156 AESVIEQYWATVRPGHEQYIEPTKEYADIVIPNgGPLNPVALDLLVARLLS 206
udk TIGR00235
uridine kinase; Model contains a number of longer eukaryotic proteins and starts bringing in ...
 21-232 5.13e-77

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: 232.66  E-value: 5.13e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20455360    21 QRPFLIGVSGGTASGKSTVCEKIMELLGQneveqrqRKVVILSQDRFYKVLtaEQKAKALKGQYNFDHPDAFDNDLMHRT 100
Cdd:TIGR00235   4 PKGIIIGIGGGSGSGKTTVARKIYEQLGK-------LEIVIISQDNYYKDQ--SHLEMAERKKTNFDHPDAFDNDLLYEH 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20455360   101 LKNIVEGKTVEVPTYDFVTHSRLPETTVVYPADVVLFEGILVFYSQEIRDMFHLRLFVDTDSDVRLSRRVLRDV-RRGRD 179
Cdd:TIGR00235  75 LKNLKNGSPIDVPVYDYVNHTRPKETVHIEPKDVVILEGIMPLFDERLRDLMDLKIFVDTPLDIRLIRRIERDInERGRS 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 20455360   180 LEQILTQYTTFVKPAFEEFCLPTKKYADVIIPRGVDNMVAINLIVQHIQDILN 232
Cdd:TIGR00235 155 LDSVIDQYRKTVRPMYEQFVEPTKQYADLIIPEGGRNEVAINVLDTKIKHLLE 207
PRK pfam00485
Phosphoribulokinase / Uridine kinase family; This family matches three types of P-loop ...
 25-219 4.43e-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: 186.45  E-value: 4.43e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20455360    25 LIGVSGGTASGKSTVCEKIMELLGQNEVEQRQRK-VVILSQDRFYKVLTAEQKAKALKGQYNFDHPDAFDNDLMHRTLKN 103
Cdd:pfam00485   1 VIGVAGSSGSGKTTVARRIVSIFGREGVPAVGIEgDSFHSTDRFYMDLHPEDRKRAGNNGYSFDGPEANDFDLLYEQFKE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20455360   104 IVEGKTVEVPTYDFVTHSRLPETTVVYPADVVLFEGILVFYSQEIRDMFHLRLFVDTDSDVRLSRRVLRDV-RRGRDLEQ 182
Cdd:pfam00485  81 LKEGGSVDKPIYNHVTHERDPTPELIEGADVLVIEGLHALYDERVAQLLDLKIYVDPDIDLELARKIQRDMaERGHSLEG 160

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 20455360   183 ILTQYtTFVKPAFEEFCLPTKKYADVIIPRGVDNMVA 219
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 ...
 25-230 1.46e-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: 332.60  E-value: 1.46e-116
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20455360  25 LIGVSGGTASGKSTVCEKIMELLGQneveqrqRKVVILSQDRFYKVLTAEQKAKALKgqYNFDHPDAFDNDLMHRTLKNI 104
Cdd:cd02023   1 IIGIAGGSGSGKTTVAEEIIEQLGN-------PKVVIISQDSYYKDLSHEELEERKN--NNYDHPDAFDFDLLISHLQDL 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20455360 105 VEGKTVEVPTYDFVTHSRLPETTVVYPADVVLFEGILVFYSQEIRDMFHLRLFVDTDSDVRLSRRVLRDVR-RGRDLEQI 183
Cdd:cd02023  72 KNGKSVEIPVYDFKTHSRLKETVTVYPADVIILEGILALYDKELRDLMDLKIFVDTDADVRLIRRIERDIVeRGRDLESV 151

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 20455360 184 LTQYTTFVKPAFEEFCLPTKKYADVIIPRGVDNMVAINLIVQHIQDI 230
Cdd:cd02023 152 INQYLKFVKPMHEQFIEPTKRYADVIIPRGGDNHVAIDLIVQHIKSK 198
PRK05480 PRK05480
uridine/cytidine kinase; Provisional
 21-234 2.14e-91

uridine/cytidine kinase; Provisional


Pssm-ID: 235492 [Multi-domain]  Cd Length: 209  Bit Score: 269.34  E-value: 2.14e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20455360   21 QRPFLIGVSGGTASGKSTVCEKIMELLGQNeveqrqrKVVILSQDRFYK---VLTAEQKAKAlkgqyNFDHPDAFDNDLM 97
Cdd:PRK05480   4 KKPIIIGIAGGSGSGKTTVASTIYEELGDE-------SIAVIPQDSYYKdqsHLSFEERVKT-----NYDHPDAFDHDLL 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20455360   98 HRTLKNIVEGKTVEVPTYDFVTHSRLPETTVVYPADVVLFEGILVFYSQEIRDMFHLRLFVDTDSDVRLSRRVLRDVR-R 176
Cdd:PRK05480  72 IEHLKALKAGKAIEIPVYDYTEHTRSKETIRVEPKDVIILEGILLLEDERLRDLMDIKIFVDTPLDIRLIRRLKRDVNeR 151

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 20455360  177 GRDLEQILTQYTTFVKPAFEEFCLPTKKYADVIIPRGVDNMVAINLIVQHIQDILNGD 234
Cdd:PRK05480 152 GRSLESVINQYLSTVRPMHLQFIEPSKRYADIIIPEGGKNRVAIDILKAKIRQLLEKN 209
Udk COG0572
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway ...
 21-229 2.61e-77

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: 233.19  E-value: 2.61e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20455360  21 QRPFLIGVSGGTASGKSTVCEKIMELLGQNeveqrqrKVVILSQDRFYKVLtaEQKAKALKGQYNFDHPDAFDNDLMHRT 100
Cdd:COG0572   5 GKPRIIGIAGPSGSGKTTFARRLAEQLGAD-------KVVVISLDDYYKDR--EHLPLDERGKPNFDHPEAFDLDLLNEH 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20455360 101 LKNIVEGKTVEVPTYDFVTHSRLPETTVVYPADVVLFEGILVFYSQEIRDMFHLRLFVDTDSDVRLSRRVLRDVR-RGRD 179
Cdd:COG0572  76 LEPLKAGESVELPVYDFATGTRSGETVKVEPADVIIVEGIHALNDELLRDLLDLKIYVDADTDVRLIRRIVRDGEeRGRT 155

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 20455360 180 LEQILTQYTTFVKPAFEEFCLPTKKYADVIIPR-GVDNMVAINLIVQHIQD 229
Cdd:COG0572 156 AESVIEQYWATVRPGHEQYIEPTKEYADIVIPNgGPLNPVALDLLVARLLS 206
udk TIGR00235
uridine kinase; Model contains a number of longer eukaryotic proteins and starts bringing in ...
 21-232 5.13e-77

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: 232.66  E-value: 5.13e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20455360    21 QRPFLIGVSGGTASGKSTVCEKIMELLGQneveqrqRKVVILSQDRFYKVLtaEQKAKALKGQYNFDHPDAFDNDLMHRT 100
Cdd:TIGR00235   4 PKGIIIGIGGGSGSGKTTVARKIYEQLGK-------LEIVIISQDNYYKDQ--SHLEMAERKKTNFDHPDAFDNDLLYEH 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20455360   101 LKNIVEGKTVEVPTYDFVTHSRLPETTVVYPADVVLFEGILVFYSQEIRDMFHLRLFVDTDSDVRLSRRVLRDV-RRGRD 179
Cdd:TIGR00235  75 LKNLKNGSPIDVPVYDYVNHTRPKETVHIEPKDVVILEGIMPLFDERLRDLMDLKIFVDTPLDIRLIRRIERDInERGRS 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 20455360   180 LEQILTQYTTFVKPAFEEFCLPTKKYADVIIPRGVDNMVAINLIVQHIQDILN 232
Cdd:TIGR00235 155 LDSVIDQYRKTVRPMYEQFVEPTKQYADLIIPEGGRNEVAINVLDTKIKHLLE 207
PRK pfam00485
Phosphoribulokinase / Uridine kinase family; This family matches three types of P-loop ...
 25-219 4.43e-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: 186.45  E-value: 4.43e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20455360    25 LIGVSGGTASGKSTVCEKIMELLGQNEVEQRQRK-VVILSQDRFYKVLTAEQKAKALKGQYNFDHPDAFDNDLMHRTLKN 103
Cdd:pfam00485   1 VIGVAGSSGSGKTTVARRIVSIFGREGVPAVGIEgDSFHSTDRFYMDLHPEDRKRAGNNGYSFDGPEANDFDLLYEQFKE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20455360   104 IVEGKTVEVPTYDFVTHSRLPETTVVYPADVVLFEGILVFYSQEIRDMFHLRLFVDTDSDVRLSRRVLRDV-RRGRDLEQ 182
Cdd:pfam00485  81 LKEGGSVDKPIYNHVTHERDPTPELIEGADVLVIEGLHALYDERVAQLLDLKIYVDPDIDLELARKIQRDMaERGHSLEG 160

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 20455360   183 ILTQYtTFVKPAFEEFCLPTKKYADVIIPRGVDNMVA 219
Cdd:pfam00485 161 VTDSI-LFRKPDYVNYIDPQFSYADLIIQRVPTNDTA 196
PTZ00301 PTZ00301
uridine kinase; Provisional
 26-233 9.69e-32

uridine kinase; Provisional


Pssm-ID: 140322 [Multi-domain]  Cd Length: 210  Bit Score: 116.64  E-value: 9.69e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20455360   26 IGVSGGTASGKSTVCEKImelLGQNEVEQRQRKVVILSQDRFYKvlTAEQKAKALKGQYNFDHPDAFDNDLMHRTLKNIV 105
Cdd:PTZ00301   6 IGISGASGSGKSSLSTNI---VSELMAHCGPVSIGVICEDFYYR--DQSNIPESERAYTNYDHPKSLEHDLLTTHLRELK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20455360  106 EGKTVEVPTYDFVTHSRLPETTVVYPADVVLFEGILVFYSQEIRDMFHLRLFVDTDSDVRLSRRVLRDVR-RGRDLEQIL 184
Cdd:PTZ00301  81 SGKTVQIPQYDYVHHTRSDTAVTMTPKSVLIVEGILLFTNAELRNEMDCLIFVDTPLDICLIRRAKRDMReRGRTFESVI 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 20455360  185 TQYTTFVKPAFEEFCLPTKKYADVIIPRGVDNMVAINLIVQHIQDILNG 233
Cdd:PTZ00301 161 EQYEATVRPMYYAYVEPSKVYADIIVPSWKDNSVAVGVLRAKLNHDLEN 209
UMPK_like cd02028
Uridine monophosphate kinase_like (UMPK_like) is a family of proteins highly similar to the ...
 25-198 1.26e-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: 94.29  E-value: 1.26e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20455360  25 LIGVSGGTASGKSTVCEKImellgQNEVEQRQRKVVILSQDRFYKVLTAEQKAkalkgQYNFDHPDAFDNDLMHRTLKNI 104
Cdd:cd02028   1 VVGIAGPSGSGKTTFAKKL-----SNQLRVNGIGPVVISLDDYYVPRKTPRDE-----DGNYDFESILDLDLLNKNLHDL 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20455360 105 VEGKTVEVPTYDFVTHSRLPETTVVYP-ADVVLFEGIlvfY--SQEIRDMFHLRLFVDT-DSDVRLSRRVLRDV-RRGRD 179
Cdd:cd02028  71 LNGKEVELPIYDFRTGKRRGYRKLKLPpSGVVILEGI---YalNERLRSLLDIRVAVSGgVHLNRLLRRVVRDIqFRGYS 147

                       170
                ....*....|....*....
gi 20455360 180 LEQILTQYTTFvkPAFEEF 198
Cdd:cd02028 148 AELTILMWPSV--PSGEEF 164
PRK cd02026
Phosphoribulokinase (PRK) is an enzyme involved in the Benson-Calvin cycle in chloroplasts or ...
 25-210 4.91e-23

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: 95.10  E-value: 4.91e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20455360  25 LIGVSGGTASGKSTVCEKIMELLGQNEVeqrqrkVVILSQDrfYKVLTAEQKAK----ALkgqynfdHPDAFDNDLMHRT 100
Cdd:cd02026   1 IIGVAGDSGCGKSTFLRRLTSLFGSDLV------TVICLDD--YHSLDRKGRKEtgitAL-------DPRANNFDLMYEQ 65

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20455360 101 LKNIVEGKTVEVPTYDFVTHS-RLPETtvVYPADVVLFEGILVFYSQEIRDMFHLRLFVDTDSDVRLSRRVLRDV-RRGR 178
Cdd:cd02026  66 LKALKEGQAIEKPIYNHVTGLiDPPEL--IKPTKIVVIEGLHPLYDERVRELLDFSVYLDISDEVKFAWKIQRDMaERGH 143

                       170       180       190
                ....*....|....*....|....*....|..
gi 20455360 179 DLEQILTQYTTfVKPAFEEFCLPTKKYADVII 210
Cdd:cd02026 144 SLEDVLASIEA-RKPDFEAYIDPQKQYADVVI 174
PRK07429 PRK07429
phosphoribulokinase; Provisional
 21-210 1.72e-22

phosphoribulokinase; Provisional


Pssm-ID: 180975  Cd Length: 327  Bit Score: 94.69  E-value: 1.72e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20455360   21 QRPFLIGVSGGTASGKSTVCEKIMELLGQneveqrQRKVVILSQDrfYKVLTAEQKAK----ALkgqynfdHPDAFDNDL 96
Cdd:PRK07429   6 DRPVLLGVAGDSGCGKTTFLRGLADLLGE------ELVTVICTDD--YHSYDRKQRKElgitAL-------DPRANNLDI 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20455360   97 MHRTLKNIVEGKTVEVPTYDFVTHSRLPETTVVyPADVVLFEGILVFYSQEIRDMFHLRLFVDTDSDVRLSRRVLRDV-R 175
Cdd:PRK07429  71 MYEHLKALKTGQPILKPIYNHETGTFDPPEYIE-PNKIVVVEGLHPLYDERVRELYDFKVYLDPPEEVKIAWKIKRDMaK 149

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 20455360  176 RGRDLEQILTQYTTfVKPAFEEFCLPTKKYADVII 210
Cdd:PRK07429 150 RGHTYEQVLAEIEA-REPDFEAYIRPQRQWADVVI 183
PLN02348 PLN02348
phosphoribulokinase
 21-210 1.08e-21

phosphoribulokinase


Pssm-ID: 215198  Cd Length: 395  Bit Score: 93.37  E-value: 1.08e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20455360   21 QRPFLIGVSGGTASGKSTVCEKIMELLG------------QNEVEQRQRKVVILsqDRFYKVLTAEQKAKALKGQynfdH 88
Cdd:PLN02348  47 DGTVVIGLAADSGCGKSTFMRRLTSVFGgaakppkggnpdSNTLISDTTTVICL--DDYHSLDRTGRKEKGVTAL----D 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20455360   89 PDAFDNDLMHRTLKNIVEGKTVEVPTYDFVThSRLPETTVVYPADVVLFEGILVFYSQEIRDMFHLRLFVDTDSDVRLSR 168
Cdd:PLN02348 121 PRANNFDLMYEQVKALKEGKAVEKPIYNHVT-GLLDPPELIEPPKILVIEGLHPMYDERVRDLLDFSIYLDISDDVKFAW 199

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 20455360  169 RVLRDV-RRGRDLEQILTQYTTfVKPAFEEFCLPTKKYADVII 210
Cdd:PLN02348 200 KIQRDMaERGHSLESIKASIEA-RKPDFDAYIDPQKQYADVVI 241
PLN02318 PLN02318
phosphoribulokinase/uridine kinase
 25-210 7.14e-17

phosphoribulokinase/uridine kinase


Pssm-ID: 177952 [Multi-domain]  Cd Length: 656  Bit Score: 80.29  E-value: 7.14e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20455360   25 LIGVSGGTASGKSTVCEKIMELLGQneveqrqrkVVILSQDRFykvltaEQKAKALKGqyNFDHPDAFDNDLMHRTLKNI 104
Cdd:PLN02318  67 LVGVAGPSGAGKTVFTEKVLNFMPS---------IAVISMDNY------NDSSRIIDG--NFDDPRLTDYDTLLDNIHDL 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20455360  105 VEGKTVEVPTYDFVTHSRLPETTVVYPAD-VVLFEGILVFySQEIRDMFHLRLFVDTDSDVRLSRRVLRDVRR-GRDLEQ 182
Cdd:PLN02318 130 KAGKSVQVPIYDFKSSSRVGYRTLEVPSSrIVIIEGIYAL-SEKLRPLLDLRVSVTGGVHFDLVKRVLRDIQRaGQEPEE 208

                        170       180
                 ....*....|....*....|....*...
gi 20455360  183 ILTQYTTFVKPAFEEFCLPTKKYADVII 210
Cdd:PLN02318 209 IIHQISETVYPMYKAFIEPDLQTAHIKI 236
CoaA COG1072
Panthothenate kinase [Coenzyme transport and metabolism]; Panthothenate kinase is part of the ...
 18-218 9.81e-15

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: 72.63  E-value: 9.81e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20455360  18 RPHQRPFLIGVSGGTASGKSTVCEKIMELLGQnevEQRQRKVVILSQDRF-YKvlTAEQKAKAL---KGqynFdhPDAFD 93
Cdd:COG1072  81 ADKKTPFIIGIAGSVAVGKSTTARLLQALLSR---WPEHPKVELVTTDGFlYP--NAVLERRGLmdrKG---F--PESYD 150

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20455360  94 NDLMHRTLKNIVEGK-TVEVPTYDFVTHSRLP-ETTVVYPADVVLFEGILVFYSQE-----IRDMFHLRLFVDTDSDVRL 166
Cdd:COG1072 151 RRGLLRFLARVKSGDpEVRAPVYSHLLYDIVPgAIVVVDQPDILIVEGNNVLQDEPnpwlfVSDFFDFSIYVDADEEDLR 230

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 20455360 167 SRRVLR--DVRR--------------GRDLEQILTQYTTFVK----PAFEEFCLPTKKYADVIIPRGVDNMV 218
Cdd:COG1072 231 EWYVERflKLREtafrdpdsyfhryaGLSEEEARAWAEEIWReinlPNLAENILPTRSRADLILRKGADHSV 302
NRK1 cd02024
Nicotinamide riboside kinase (NRK) is an enzyme involved in the metabolism of nicotinamide ...
 25-169 1.12e-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: 70.43  E-value: 1.12e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20455360  25 LIGVSGGTASGKSTVCEKIMELLGqneveqrqrKVVILSQDRFYKvlTAEQKAKALKGQYNFDHPDAFDNDLMHRTLKNI 104
Cdd:cd02024   1 IVGISGVTNSGKTTLAKLLQRILP---------NCCVIHQDDFFK--PEDEIPVDENGFKQWDVLEALDMEAMMSTLDYW 69

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 20455360 105 VEGKTVE--------VPTYDFVTHSRLPETTVVYPAD------VVLFEGILVFYSQEIRDMFHLRLFVDTDSDVRLSRR 169
Cdd:cd02024  70 RETGHFPkflrshgnENDPEKEFIEDAQIEETKADLLgaedlhILIVDGFLLYNYKPLVDLFDIRYFLRVPYETCKRRR 148
PanK cd02025
Pantothenate kinase (PanK) catalyzes the phosphorylation of pantothenic acid to form 4 ...
 25-218 2.61e-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: 61.56  E-value: 2.61e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20455360  25 LIGVSGGTASGKSTVCEKIMELLgqneveQRQ---RKVVILSQDRF-YKvlTAEQKAKALKGQYNFdhPDAFDNDLMHRT 100
Cdd:cd02025   1 IIGIAGSVAVGKSTTARVLQALL------SRWpdhPNVELITTDGFlYP--NKELIERGLMDRKGF--PESYDMEALLKF 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20455360 101 LKNIVEGK-TVEVPTYDFVTHSRLPET-TVVYPADVVLFEGILVF-----YSQEIRDMFHLRLFVDTDSDV----RLSRr 169
Cdd:cd02025  71 LKDIKSGKkNVKIPVYSHLTYDVIPGEkQTVDQPDILIIEGLNVLqtgqnPRLFVSDFFDFSIYVDADEDDiekwYIKR- 149

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 20455360 170 vLRDVRR--GRDLEQILTQYTTFVKPAFEEFC----------------LPTKKYADVIIPRGVDNMV 218
Cdd:cd02025 150 -FLKLREtaFSDPDSYFHRYAKMSEEEAIAFArevwkninlknlreniLPTRNRADLILEKGADHSI 215
PRK09270 PRK09270
nucleoside triphosphate hydrolase domain-containing protein; Reviewed
 21-189 2.13e-08

nucleoside triphosphate hydrolase domain-containing protein; Reviewed


Pssm-ID: 236442  Cd Length: 229  Bit Score: 53.40  E-value: 2.13e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20455360   21 QRPFLIGVSGGTASGKSTVCEKIMELLGQNEVEQRqrkvVILSQDRF--YKVLTAEQKAKALKGQynfdhPDAFD----N 94
Cdd:PRK09270  31 QRRTIVGIAGPPGAGKSTLAEFLEALLQQDGELPA----IQVPMDGFhlDNAVLDAHGLRPRKGA-----PETFDvaglA 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20455360   95 DLMHRtLKNivEGKTVEVPTYDFVTHSRLPETTVVYP-ADVVLFEGILVFYSQ----EIRDMFHLRLFVDTDSDVRLSRR 169
Cdd:PRK09270 102 ALLRR-LRA--GDDEVYWPVFDRSLEDPVADAIVVPPtARLVIVEGNYLLLDEepwrRLAGLFDFTIFLDAPAEVLRERL 178

                        170       180
                 ....*....|....*....|
gi 20455360  170 VLRDVRRGRDLEQILTQYTT 189
Cdd:PRK09270 179 VARKLAGGLSPEAAEAFVLR 198
PRK06696 PRK06696
uridine kinase; Validated
 22-210 5.14e-08

uridine kinase; Validated


Pssm-ID: 180660  Cd Length: 223  Bit Score: 52.29  E-value: 5.14e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20455360   22 RPFLIGVSGGTASGKSTVCEKIMEllgqnEVEQRQRKVVILSQDRFY--KVLTAEQKAKALKGQYNfdhpDAFDNDLMHR 99
Cdd:PRK06696  21 RPLRVAIDGITASGKTTFADELAE-----EIKKRGRPVIRASIDDFHnpRVIRYRRGRESAEGYYE----DAYDYTALRR 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20455360  100 TLKNIV--EG-KTVEVPTYDFVTHSRLPETTVVYPADVVLF-EGILVFySQEIRDMFHLRLFVDTDSDVRLSRRVLRDVR 175
Cdd:PRK06696  92 LLLDPLgpNGdRQYRTASHDLKTDIPVHNPPLLAAPNAVLIvDGTFLL-RPELRDLWDYKIFLDTDFEVSRRRGAKRDTE 170

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 20455360  176 RGRDLEQILTQYTTFVKPAFE---EFCLPtKKYADVII 210
Cdd:PRK06696 171 AFGSYEEAEKMYLARYHPAQKlyiAEANP-KERADVVI 207
PRK08233 PRK08233
hypothetical protein; Provisional
 23-231 1.65e-07

hypothetical protein; Provisional


Pssm-ID: 181310 [Multi-domain]  Cd Length: 182  Bit Score: 50.13  E-value: 1.65e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20455360   23 PFLIGVSGGTASGKSTVCEKIMELLgqneveqrqRKVVILSQDRFYKVLTAEQKAKALKGQYNFDhpdAFDNDLMHRTLK 102
Cdd:PRK08233   3 TKIITIAAVSGGGKTTLTERLTHKL---------KNSKALYFDRYDFDNCPEDICKWIDKGANYS---EWVLTPLIKDIQ 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20455360  103 NIVEGKTVEVPTYDfvthsrlpettvvYPadvvlfegiLVFYSQEIRDMFHLRLFVDTDSDVRLSRRVLRDVRR--GRDL 180
Cdd:PRK08233  71 ELIAKSNVDYIIVD-------------YP---------FAYLNSEMRQFIDVTIFIDTPLDIAMARRILRDFKEdtGNEI 128

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 20455360  181 EQILTQYTTFVKPAFEEFCLPTKKYADVIIprgvDNMVAINLIVQHIQDIL 231
Cdd:PRK08233 129 HNDLKHYLNYARPLYLEALHTVKPNADIVL----DGALSVEEIINQIEEEL 175
PLN02796 PLN02796
D-glycerate 3-kinase
 14-139 7.43e-06

D-glycerate 3-kinase


Pssm-ID: 215427  Cd Length: 347  Bit Score: 46.66  E-value: 7.43e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20455360   14 PEADRPHQRPFLIGVSGGTASGKSTVCEKIMELLgqnevEQRQRKVVILSQDRFYkvLTAE-QKAKALKGQYNF-----D 87
Cdd:PLN02796  91 KFKDGDEIPPLVIGISAPQGCGKTTLVFALVYLF-----NATGRRAASLSIDDFY--LTAAdQAKLAEANPGNAllelrG 163

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 20455360   88 HPDAFDNDLMHRTLKNI----VEGKTVEVPTYDFVTHS----RLPETT---VVYPADVVLFEG 139
Cdd:PLN02796 164 NAGSHDLALGVETLEALrklnKEGSKMKVPRYDKSAYGgrgdRADPSTwpeVEGPLDVVLFEG 226
CoaE COG0237
Dephospho-CoA kinase [Coenzyme transport and metabolism]; Dephospho-CoA kinase is part of the ...
 23-184 1.43e-03

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: 38.89  E-value: 1.43e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20455360  23 PFLIGVSGGTASGKSTVCeKIMELLGqneveqrqrkVVILSQDRFYKVLTAEQKA--KALK-----------GQYN---- 85
Cdd:COG0237   1 MLIIGLTGGIGSGKSTVA-RMFAELG----------APVIDADAIARELVEPGGPalAAIVeafgeeildadGSLDrkal 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20455360  86 ----FDHPDAFD--NDLMHRTLKNIVEgktvevptyDFVTHSRlpettvvyPADVVLFEGILVFYSQeIRDMFHLRLFVD 159
Cdd:COG0237  70 aeivFADPEALKklEAIVHPLVREEIE---------RRLAAAR--------GAPYVVLDIPLLFETG-LEKLVDRVIVVD 131

                       170       180
                ....*....|....*....|....*
gi 20455360 160 TDSDVRLsRRVLRdvRRGRDLEQIL 184
Cdd:COG0237 132 APEEVQI-ERLMA--RDGLSEEEAE 153
PLN03046 PLN03046
D-glycerate 3-kinase; Provisional
 23-139 1.51e-03

D-glycerate 3-kinase; Provisional


Pssm-ID: 178608  Cd Length: 460  Bit Score: 39.51  E-value: 1.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20455360   23 PFLIGVSGGTASGKSTVCEKIMELLgqnevEQRQRKVVILSQDRFYkvLTAEQKAK-----------ALKGQYNfDHPDA 91
Cdd:PLN03046 212 PLVIGFSAPQGCGKTTLVFALDYLF-----RVTGRKSATLSIDDFY--LTAEGQAElrernpgnallELRGNAG-SHDLQ 283

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 20455360   92 FDNDLMHRTLKNIVEGKTVEVPTYDFVTH---------SRLPEttVVYPADVVLFEG 139
Cdd:PLN03046 284 FSVETLEALSKLTKEGIKMKVPRYDKSAYsgrgdradpSTWPE--VEGPLEVILFEG 338
 
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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