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Conserved domains on  [gi|298552909|emb|CBN62650|]
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unnamed protein product [Drosophila melanogaster]

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 ...
 29-236 2.50e-110

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: 316.03  E-value: 2.50e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298552909  29 LIGVAGGTASGKSTVCKKIMEQLGQaemdhtqRQVVSISQDSFYRELTPAEKAKAQKglFNFDHPDAFNEELMYSTLQNI 108
Cdd:cd02023    1 IIGIAGGSGSGKTTVAEEIIEQLGN-------PKVVIISQDSYYKDLSHEELEERKN--NNYDHPDAFDFDLLISHLQDL 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298552909 109 LKGHKVEIPSYDYRTNSLDFENVlVIYPADVVLFEGILVFYFPKIRELFHMKLFVDTDSDTRLARRVPRDINERGRDLDA 188
Cdd:cd02023   72 KNGKSVEIPVYDFKTHSRLKETV-TVYPADVIILEGILALYDKELRDLMDLKIFVDTDADVRLIRRIERDIVERGRDLES 150

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 298552909 189 VLTQYMTFVKPAFEEFCSPTKKFADVIIPRGADNTVAIDLIVHHIGEI 236
Cdd:cd02023  151 VINQYLKFVKPMHEQFIEPTKRYADVIIPRGGDNHVAIDLIVQHIKSK 198
 
Name Accession Description Interval E-value
UMPK cd02023
Uridine monophosphate kinase (UMPK, EC 2.7.1.48), also known as uridine kinase or ...
 29-236 2.50e-110

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: 316.03  E-value: 2.50e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298552909  29 LIGVAGGTASGKSTVCKKIMEQLGQaemdhtqRQVVSISQDSFYRELTPAEKAKAQKglFNFDHPDAFNEELMYSTLQNI 108
Cdd:cd02023    1 IIGIAGGSGSGKTTVAEEIIEQLGN-------PKVVIISQDSYYKDLSHEELEERKN--NNYDHPDAFDFDLLISHLQDL 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298552909 109 LKGHKVEIPSYDYRTNSLDFENVlVIYPADVVLFEGILVFYFPKIRELFHMKLFVDTDSDTRLARRVPRDINERGRDLDA 188
Cdd:cd02023   72 KNGKSVEIPVYDFKTHSRLKETV-TVYPADVIILEGILALYDKELRDLMDLKIFVDTDADVRLIRRIERDIVERGRDLES 150

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 298552909 189 VLTQYMTFVKPAFEEFCSPTKKFADVIIPRGADNTVAIDLIVHHIGEI 236
Cdd:cd02023  151 VINQYLKFVKPMHEQFIEPTKRYADVIIPRGGDNHVAIDLIVQHIKSK 198
PRK05480 PRK05480
uridine/cytidine kinase; Provisional
 22-238 3.84e-84

uridine/cytidine kinase; Provisional


Pssm-ID: 235492 [Multi-domain]  Cd Length: 209  Bit Score: 250.08  E-value: 3.84e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298552909  22 DEVKSPFLIGVAGGTASGKSTVCKKIMEQLGqaemDHtqrQVVSISQDSFYR---ELTPAEKAKaqkglFNFDHPDAFNE 98
Cdd:PRK05480   1 MMMKKPIIIGIAGGSGSGKTTVASTIYEELG----DE---SIAVIPQDSYYKdqsHLSFEERVK-----TNYDHPDAFDH 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298552909  99 ELMYSTLQNILKGHKVEIPSYDYrTNSLDFENVLVIYPADVVLFEGILVFYFPKIRELFHMKLFVDTDSDTRLARRVPRD 178
Cdd:PRK05480  69 DLLIEHLKALKAGKAIEIPVYDY-TEHTRSKETIRVEPKDVIILEGILLLEDERLRDLMDIKIFVDTPLDIRLIRRLKRD 147

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 298552909 179 INERGRDLDAVLTQYMTFVKPAFEEFCSPTKKFADVIIPRGADNTVAIDLIVHHIGEILA 238
Cdd:PRK05480 148 VNERGRSLESVINQYLSTVRPMHLQFIEPSKRYADIIIPEGGKNRVAIDILKAKIRQLLE 207
udk TIGR00235
uridine kinase; Model contains a number of longer eukaryotic proteins and starts bringing in ...
 25-237 2.61e-72

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: 219.95  E-value: 2.61e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298552909   25 KSPFLIGVAGGTASGKSTVCKKIMEQLGQAEmdhtqrqVVSISQDSFYRELtpAEKAKAQKGLFNFDHPDAFNEELMYST 104
Cdd:TIGR00235   4 PKGIIIGIGGGSGSGKTTVARKIYEQLGKLE-------IVIISQDNYYKDQ--SHLEMAERKKTNFDHPDAFDNDLLYEH 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298552909  105 LQNILKGHKVEIPSYDYRTNSLDFENVlVIYPADVVLFEGILVFYFPKIRELFHMKLFVDTDSDTRLARRVPRDINERGR 184
Cdd:TIGR00235  75 LKNLKNGSPIDVPVYDYVNHTRPKETV-HIEPKDVVILEGIMPLFDERLRDLMDLKIFVDTPLDIRLIRRIERDINERGR 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 298552909  185 DLDAVLTQYMTFVKPAFEEFCSPTKKFADVIIPRGADNTVAIDLIVHHIGEIL 237
Cdd:TIGR00235 154 SLDSVIDQYRKTVRPMYEQFVEPTKQYADLIIPEGGRNEVAINVLDTKIKHLL 206
Udk COG0572
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway ...
 25-233 4.27e-72

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: 219.33  E-value: 4.27e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298552909  25 KSPFLIGVAGGTASGKSTVCKKIMEQLGQaemdhtqRQVVSISQDSFY--RELTPAEkakaQKGLFNFDHPDAFNEELMY 102
Cdd:COG0572    5 GKPRIIGIAGPSGSGKTTFARRLAEQLGA-------DKVVVISLDDYYkdREHLPLD----ERGKPNFDHPEAFDLDLLN 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298552909 103 STLQNILKGHKVEIPSYDYRTNSLDFEnVLVIYPADVVLFEGILVFYFPKIRELFHMKLFVDTDSDTRLARRVPRDINER 182
Cdd:COG0572   74 EHLEPLKAGESVELPVYDFATGTRSGE-TVKVEPADVIIVEGIHALNDELLRDLLDLKIYVDADTDVRLIRRIVRDGEER 152

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 298552909 183 GRDLDAVLTQYMTFVKPAFEEFCSPTKKFADVIIPRG-ADNTVAIDLIVHHI 233
Cdd:COG0572  153 GRTAESVIEQYWATVRPGHEQYIEPTKEYADIVIPNGgPLNPVALDLLVARL 204
PRK pfam00485
Phosphoribulokinase / Uridine kinase family; This family matches three types of P-loop ...
 29-225 4.94e-52

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: 167.96  E-value: 4.94e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298552909   29 LIGVAGGTASGKSTVCKKIMEQLGQAEMDHTQRQVVSI-SQDSFYRELTPAEKAKAQKGLFNFDHPDAFNEELMYSTLQN 107
Cdd:pfam00485   1 VIGVAGSSGSGKTTVARRIVSIFGREGVPAVGIEGDSFhSTDRFYMDLHPEDRKRAGNNGYSFDGPEANDFDLLYEQFKE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298552909  108 ILKGHKVEIPSYDYRTNSLDFENVLvIYPADVVLFEGILVFYFPKIRELFHMKLFVDTDSDTRLARRVPRDINERGRDLD 187
Cdd:pfam00485  81 LKEGGSVDKPIYNHVTHERDPTPEL-IEGADVLVIEGLHALYDERVAQLLDLKIYVDPDIDLELARKIQRDMAERGHSLE 159

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 298552909  188 AVLTQYMtFVKPAFEEFCSPTKKFADVIIPRGADNTVA 225
Cdd:pfam00485 160 GVTDSIL-FRKPDYVNYIDPQFSYADLIIQRVPTNDTA 196
 
Name Accession Description Interval E-value
UMPK cd02023
Uridine monophosphate kinase (UMPK, EC 2.7.1.48), also known as uridine kinase or ...
 29-236 2.50e-110

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: 316.03  E-value: 2.50e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298552909  29 LIGVAGGTASGKSTVCKKIMEQLGQaemdhtqRQVVSISQDSFYRELTPAEKAKAQKglFNFDHPDAFNEELMYSTLQNI 108
Cdd:cd02023    1 IIGIAGGSGSGKTTVAEEIIEQLGN-------PKVVIISQDSYYKDLSHEELEERKN--NNYDHPDAFDFDLLISHLQDL 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298552909 109 LKGHKVEIPSYDYRTNSLDFENVlVIYPADVVLFEGILVFYFPKIRELFHMKLFVDTDSDTRLARRVPRDINERGRDLDA 188
Cdd:cd02023   72 KNGKSVEIPVYDFKTHSRLKETV-TVYPADVIILEGILALYDKELRDLMDLKIFVDTDADVRLIRRIERDIVERGRDLES 150

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 298552909 189 VLTQYMTFVKPAFEEFCSPTKKFADVIIPRGADNTVAIDLIVHHIGEI 236
Cdd:cd02023  151 VINQYLKFVKPMHEQFIEPTKRYADVIIPRGGDNHVAIDLIVQHIKSK 198
PRK05480 PRK05480
uridine/cytidine kinase; Provisional
 22-238 3.84e-84

uridine/cytidine kinase; Provisional


Pssm-ID: 235492 [Multi-domain]  Cd Length: 209  Bit Score: 250.08  E-value: 3.84e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298552909  22 DEVKSPFLIGVAGGTASGKSTVCKKIMEQLGqaemDHtqrQVVSISQDSFYR---ELTPAEKAKaqkglFNFDHPDAFNE 98
Cdd:PRK05480   1 MMMKKPIIIGIAGGSGSGKTTVASTIYEELG----DE---SIAVIPQDSYYKdqsHLSFEERVK-----TNYDHPDAFDH 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298552909  99 ELMYSTLQNILKGHKVEIPSYDYrTNSLDFENVLVIYPADVVLFEGILVFYFPKIRELFHMKLFVDTDSDTRLARRVPRD 178
Cdd:PRK05480  69 DLLIEHLKALKAGKAIEIPVYDY-TEHTRSKETIRVEPKDVIILEGILLLEDERLRDLMDIKIFVDTPLDIRLIRRLKRD 147

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 298552909 179 INERGRDLDAVLTQYMTFVKPAFEEFCSPTKKFADVIIPRGADNTVAIDLIVHHIGEILA 238
Cdd:PRK05480 148 VNERGRSLESVINQYLSTVRPMHLQFIEPSKRYADIIIPEGGKNRVAIDILKAKIRQLLE 207
udk TIGR00235
uridine kinase; Model contains a number of longer eukaryotic proteins and starts bringing in ...
 25-237 2.61e-72

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: 219.95  E-value: 2.61e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298552909   25 KSPFLIGVAGGTASGKSTVCKKIMEQLGQAEmdhtqrqVVSISQDSFYRELtpAEKAKAQKGLFNFDHPDAFNEELMYST 104
Cdd:TIGR00235   4 PKGIIIGIGGGSGSGKTTVARKIYEQLGKLE-------IVIISQDNYYKDQ--SHLEMAERKKTNFDHPDAFDNDLLYEH 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298552909  105 LQNILKGHKVEIPSYDYRTNSLDFENVlVIYPADVVLFEGILVFYFPKIRELFHMKLFVDTDSDTRLARRVPRDINERGR 184
Cdd:TIGR00235  75 LKNLKNGSPIDVPVYDYVNHTRPKETV-HIEPKDVVILEGIMPLFDERLRDLMDLKIFVDTPLDIRLIRRIERDINERGR 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 298552909  185 DLDAVLTQYMTFVKPAFEEFCSPTKKFADVIIPRGADNTVAIDLIVHHIGEIL 237
Cdd:TIGR00235 154 SLDSVIDQYRKTVRPMYEQFVEPTKQYADLIIPEGGRNEVAINVLDTKIKHLL 206
Udk COG0572
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway ...
 25-233 4.27e-72

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: 219.33  E-value: 4.27e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298552909  25 KSPFLIGVAGGTASGKSTVCKKIMEQLGQaemdhtqRQVVSISQDSFY--RELTPAEkakaQKGLFNFDHPDAFNEELMY 102
Cdd:COG0572    5 GKPRIIGIAGPSGSGKTTFARRLAEQLGA-------DKVVVISLDDYYkdREHLPLD----ERGKPNFDHPEAFDLDLLN 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298552909 103 STLQNILKGHKVEIPSYDYRTNSLDFEnVLVIYPADVVLFEGILVFYFPKIRELFHMKLFVDTDSDTRLARRVPRDINER 182
Cdd:COG0572   74 EHLEPLKAGESVELPVYDFATGTRSGE-TVKVEPADVIIVEGIHALNDELLRDLLDLKIYVDADTDVRLIRRIVRDGEER 152

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 298552909 183 GRDLDAVLTQYMTFVKPAFEEFCSPTKKFADVIIPRG-ADNTVAIDLIVHHI 233
Cdd:COG0572  153 GRTAESVIEQYWATVRPGHEQYIEPTKEYADIVIPNGgPLNPVALDLLVARL 204
PRK pfam00485
Phosphoribulokinase / Uridine kinase family; This family matches three types of P-loop ...
 29-225 4.94e-52

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: 167.96  E-value: 4.94e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298552909   29 LIGVAGGTASGKSTVCKKIMEQLGQAEMDHTQRQVVSI-SQDSFYRELTPAEKAKAQKGLFNFDHPDAFNEELMYSTLQN 107
Cdd:pfam00485   1 VIGVAGSSGSGKTTVARRIVSIFGREGVPAVGIEGDSFhSTDRFYMDLHPEDRKRAGNNGYSFDGPEANDFDLLYEQFKE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298552909  108 ILKGHKVEIPSYDYRTNSLDFENVLvIYPADVVLFEGILVFYFPKIRELFHMKLFVDTDSDTRLARRVPRDINERGRDLD 187
Cdd:pfam00485  81 LKEGGSVDKPIYNHVTHERDPTPEL-IEGADVLVIEGLHALYDERVAQLLDLKIYVDPDIDLELARKIQRDMAERGHSLE 159

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 298552909  188 AVLTQYMtFVKPAFEEFCSPTKKFADVIIPRGADNTVA 225
Cdd:pfam00485 160 GVTDSIL-FRKPDYVNYIDPQFSYADLIIQRVPTNDTA 196
PTZ00301 PTZ00301
uridine kinase; Provisional
 30-229 4.72e-30

uridine kinase; Provisional


Pssm-ID: 140322 [Multi-domain]  Cd Length: 210  Bit Score: 111.63  E-value: 4.72e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298552909  30 IGVAGGTASGKSTVCKKIMEQLgqaeMDHTQRQVVSI-SQDSFYREltPAEKAKAQKGLFNFDHPDAFNEELMYSTLQNI 108
Cdd:PTZ00301   6 IGISGASGSGKSSLSTNIVSEL----MAHCGPVSIGViCEDFYYRD--QSNIPESERAYTNYDHPKSLEHDLLTTHLREL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298552909 109 LKGHKVEIPSYDYRTNSLDfENVLVIYPADVVLFEGILVFYFPKIRELFHMKLFVDTDSDTRLARRVPRDINERGRDLDA 188
Cdd:PTZ00301  80 KSGKTVQIPQYDYVHHTRS-DTAVTMTPKSVLIVEGILLFTNAELRNEMDCLIFVDTPLDICLIRRAKRDMRERGRTFES 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 298552909 189 VLTQYMTFVKPAFEEFCSPTKKFADVIIPRGADNTVAIDLI 229
Cdd:PTZ00301 159 VIEQYEATVRPMYYAYVEPSKVYADIIVPSWKDNSVAVGVL 199
PRK07429 PRK07429
phosphoribulokinase; Provisional
 26-216 8.24e-25

phosphoribulokinase; Provisional


Pssm-ID: 180975  Cd Length: 327  Bit Score: 100.47  E-value: 8.24e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298552909  26 SPFLIGVAGGTASGKSTVCKKIMEQLGQAEMDHtqrqvvsISQDSFYREltpAEKAKAQKGLFNFdHPDAFNEELMYSTL 105
Cdd:PRK07429   7 RPVLLGVAGDSGCGKTTFLRGLADLLGEELVTV-------ICTDDYHSY---DRKQRKELGITAL-DPRANNLDIMYEHL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298552909 106 QNILKGHKVEIPSYDYRTNSLDF-ENvlvIYPADVVLFEGILVFYFPKIRELFHMKLFVDTDSDTRLARRVPRDINERGR 184
Cdd:PRK07429  76 KALKTGQPILKPIYNHETGTFDPpEY---IEPNKIVVVEGLHPLYDERVRELYDFKVYLDPPEEVKIAWKIKRDMAKRGH 152

                        170       180       190
                 ....*....|....*....|....*....|..
gi 298552909 185 DLDAVLTQyMTFVKPAFEEFCSPTKKFADVII 216
Cdd:PRK07429 153 TYEQVLAE-IEAREPDFEAYIRPQRQWADVVI 183
PRK cd02026
Phosphoribulokinase (PRK) is an enzyme involved in the Benson-Calvin cycle in chloroplasts or ...
 29-216 1.15e-22

Phosphoribulokinase (PRK) is an enzyme involved in the Benson-Calvin cycle in chloroplasts or photosynthetic prokaryotes. This enzyme catalyzes the phosphorylation of D-ribulose 5-phosphate to form D-ribulose 1, 5-biphosphate, using ATP and NADPH produced by the primary reactions of photosynthesis.


Pssm-ID: 238984 [Multi-domain]  Cd Length: 273  Bit Score: 93.56  E-value: 1.15e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298552909  29 LIGVAGGTASGKSTVCKKIMEQLGqAEMdhtqrqVVSISQDSFYREltpAEKAKAQKGLFNFDhPDAFNEELMYSTLQNI 108
Cdd:cd02026    1 IIGVAGDSGCGKSTFLRRLTSLFG-SDL------VTVICLDDYHSL---DRKGRKETGITALD-PRANNFDLMYEQLKAL 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298552909 109 LKGHKVEIPSYDYRTNSLD-FENvlvIYPADVVLFEGILVFYFPKIRELFHMKLFVDTDSDTRLARRVPRDINERGRDLD 187
Cdd:cd02026   70 KEGQAIEKPIYNHVTGLIDpPEL---IKPTKIVVIEGLHPLYDERVRELLDFSVYLDISDEVKFAWKIQRDMAERGHSLE 146

                        170       180
                 ....*....|....*....|....*....
gi 298552909 188 AVLTQyMTFVKPAFEEFCSPTKKFADVII 216
Cdd:cd02026  147 DVLAS-IEARKPDFEAYIDPQKQYADVVI 174
UMPK_like cd02028
Uridine monophosphate kinase_like (UMPK_like) is a family of proteins highly similar to the ...
 29-204 1.85e-22

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


Pssm-ID: 238986 [Multi-domain]  Cd Length: 179  Bit Score: 90.83  E-value: 1.85e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298552909  29 LIGVAGGTASGKSTVCKKIMEQLGQaemdhTQRQVVSISQDSFYRELTPAEKAKaqkglFNFDHPDAFNEELMYSTLQNI 108
Cdd:cd02028    1 VVGIAGPSGSGKTTFAKKLSNQLRV-----NGIGPVVISLDDYYVPRKTPRDED-----GNYDFESILDLDLLNKNLHDL 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298552909 109 LKGHKVEIPSYDYRTNSLDFENVLVIYPADVVLFEGIlvfY--FPKIRELFHMKLFVDT-DSDTRLARRVPRDINERGRd 185
Cdd:cd02028   71 LNGKEVELPIYDFRTGKRRGYRKLKLPPSGVVILEGI---YalNERLRSLLDIRVAVSGgVHLNRLLRRVVRDIQFRGY- 146

                        170
                 ....*....|....*....
gi 298552909 186 lDAVLTQYMTFVKPAFEEF 204
Cdd:cd02028  147 -SAELTILMWPSVPSGEEF 164
PLN02348 PLN02348
phosphoribulokinase
 23-216 9.11e-20

phosphoribulokinase


Pssm-ID: 215198  Cd Length: 395  Bit Score: 87.59  E-value: 9.11e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298552909  23 EVKSPFLIGVAGGTASGKSTVCKKIMEQLG-QAEMDHTQ----RQVVS-----ISQDSFYRELTPAEKAKAQKGLfnfdH 92
Cdd:PLN02348  45 ADDGTVVIGLAADSGCGKSTFMRRLTSVFGgAAKPPKGGnpdsNTLISdtttvICLDDYHSLDRTGRKEKGVTAL----D 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298552909  93 PDAFNEELMYSTLQNILKGHKVEIPSYDYRTNSLDFENVlvIYPADVVLFEGILVFYFPKIRELFHMKLFVDTDSDTRLA 172
Cdd:PLN02348 121 PRANNFDLMYEQVKALKEGKAVEKPIYNHVTGLLDPPEL--IEPPKILVIEGLHPMYDERVRDLLDFSIYLDISDDVKFA 198

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 298552909 173 RRVPRDINERGRDLDAVLTQyMTFVKPAFEEFCSPTKKFADVII 216
Cdd:PLN02348 199 WKIQRDMAERGHSLESIKAS-IEARKPDFDAYIDPQKQYADVVI 241
NRK1 cd02024
Nicotinamide riboside kinase (NRK) is an enzyme involved in the metabolism of nicotinamide ...
 29-178 1.39e-16

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: 75.44  E-value: 1.39e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298552909  29 LIGVAGGTASGKSTVCKKIMEQLGQAemdhtqrqvVSISQDSFYRelTPAEKAKAQKGLFNFDHPDAFNEELMYSTLQNI 108
Cdd:cd02024    1 IVGISGVTNSGKTTLAKLLQRILPNC---------CVIHQDDFFK--PEDEIPVDENGFKQWDVLEALDMEAMMSTLDYW 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298552909 109 LKG--------HKVEIPSYDYRTNSLDFENVLVIY-----PADVVLFEGILVFYFPKIRELFHMKLFVDTDSDTRLARRV 175
Cdd:cd02024   70 RETghfpkflrSHGNENDPEKEFIEDAQIEETKADllgaeDLHILIVDGFLLYNYKPLVDLFDIRYFLRVPYETCKRRRE 149


                 ...
gi 298552909 176 PRD 178
Cdd:cd02024  150 ART 152
PRK08233 PRK08233
hypothetical protein; Provisional
 25-237 1.85e-09

hypothetical protein; Provisional


Pssm-ID: 181310 [Multi-domain]  Cd Length: 182  Bit Score: 55.52  E-value: 1.85e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298552909  25 KSPFLIGVAGGTASGKSTVCKKIMEQLGQAEMDHTqrqvvsisqDSFYRELTPAEKAKAQKGLFNFDhpdafneELMYST 104
Cdd:PRK08233   1 KKTKIITIAAVSGGGKTTLTERLTHKLKNSKALYF---------DRYDFDNCPEDICKWIDKGANYS-------EWVLTP 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298552909 105 LQNILKgHKVEIPSYDYrtnsldfenVLVIYPadvvlfegiLVFYFPKIRELFHMKLFVDTDSDTRLARRVPRDINER-G 183
Cdd:PRK08233  65 LIKDIQ-ELIAKSNVDY---------IIVDYP---------FAYLNSEMRQFIDVTIFIDTPLDIAMARRILRDFKEDtG 125

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 298552909 184 RDLDAVLTQYMTFVKPAFEEFCSPTKKFADVIIprgaDNTVAIDLIVHHIGEIL 237
Cdd:PRK08233 126 NEIHNDLKHYLNYARPLYLEALHTVKPNADIVL----DGALSVEEIINQIEEEL 175
PLN02318 PLN02318
phosphoribulokinase/uridine kinase
 29-216 5.13e-08

phosphoribulokinase/uridine kinase


Pssm-ID: 177952 [Multi-domain]  Cd Length: 656  Bit Score: 53.32  E-value: 5.13e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298552909  29 LIGVAGGTASGKSTVCKKIMEQLgqaemdhtqRQVVSISQDSFyreltpAEKAKAQKGlfNFDHPDAFNEELMYSTLQNI 108
Cdd:PLN02318  67 LVGVAGPSGAGKTVFTEKVLNFM---------PSIAVISMDNY------NDSSRIIDG--NFDDPRLTDYDTLLDNIHDL 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298552909 109 LKGHKVEIPSYDYRTNSLDFENVLVIYPADVVLFEGILVFYfPKIRELFHMKLFVDTDSDTRLARRVPRDINERGRDLDA 188
Cdd:PLN02318 130 KAGKSVQVPIYDFKSSSRVGYRTLEVPSSRIVIIEGIYALS-EKLRPLLDLRVSVTGGVHFDLVKRVLRDIQRAGQEPEE 208

                        170       180
                 ....*....|....*....|....*...
gi 298552909 189 VLTQYMTFVKPAFEEFCSPTKKFADVII 216
Cdd:PLN02318 209 IIHQISETVYPMYKAFIEPDLQTAHIKI 236
PRK06696 PRK06696
uridine kinase; Validated
 27-224 7.60e-08

uridine kinase; Validated


Pssm-ID: 180660  Cd Length: 223  Bit Score: 51.52  E-value: 7.60e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298552909  27 PFLIGVAGGTASGKSTVCKKIMEQLGQAemdhtQRQVVSISQDSFYReltPAEKAKAQ-----KGLFNfdhpDAFNeelm 101
Cdd:PRK06696  22 PLRVAIDGITASGKTTFADELAEEIKKR-----GRPVIRASIDDFHN---PRVIRYRRgresaEGYYE----DAYD---- 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298552909 102 YSTLQNIL------KGH-KVEIPSYDYRTNSlDFENVLVIYPADVVLF-EGILVFYfPKIRELFHMKLFVDTDSDTRLAR 173
Cdd:PRK06696  86 YTALRRLLldplgpNGDrQYRTASHDLKTDI-PVHNPPLLAAPNAVLIvDGTFLLR-PELRDLWDYKIFLDTDFEVSRRR 163

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 298552909 174 RVPRDINERGRDlDAVLTQYMTFVKPAFE---EFCSPtKKFADVIIprgaDNTV 224
Cdd:PRK06696 164 GAKRDTEAFGSY-EEAEKMYLARYHPAQKlyiAEANP-KERADVVI----DNSD 211
PanK cd02025
Pantothenate kinase (PanK) catalyzes the phosphorylation of pantothenic acid to form 4 ...
 29-224 5.96e-07

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: 48.85  E-value: 5.96e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298552909  29 LIGVAGGTASGKSTVCkKIMEQLGQAEMDHtqRQVVSISQDSFyreLTPAEKAKaQKGLFN---FdhPDAFNEELMYSTL 105
Cdd:cd02025    1 IIGIAGSVAVGKSTTA-RVLQALLSRWPDH--PNVELITTDGF---LYPNKELI-ERGLMDrkgF--PESYDMEALLKFL 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298552909 106 QNILKGHK-VEIPSYDYRTNSLDFENVLVIYPADVVLFEGILVFYFPK-----IRELFHMKLFVDTDSD---TRLARRVP 176
Cdd:cd02025   72 KDIKSGKKnVKIPVYSHLTYDVIPGEKQTVDQPDILIIEGLNVLQTGQnprlfVSDFFDFSIYVDADEDdieKWYIKRFL 151

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 298552909 177 RDINERGRDLDAVLTQYMTFVKPAFEEFCS----------------PTKKFADVIIPRGADNTV 224
Cdd:cd02025  152 KLRETAFSDPDSYFHRYAKMSEEEAIAFARevwkninlknlrenilPTRNRADLILEKGADHSI 215
CoaA COG1072
Panthothenate kinase [Coenzyme transport and metabolism]; Panthothenate kinase is part of the ...
 25-177 6.72e-07

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: 49.52  E-value: 6.72e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298552909  25 KSPFLIGVAGGTASGKSTVCkKIMEQLGQAEMDHtqRQVVSISQDSF-Y--RELTpAEKAKAQKGlFnfdhPDAFNEELM 101
Cdd:COG1072   84 KTPFIIGIAGSVAVGKSTTA-RLLQALLSRWPEH--PKVELVTTDGFlYpnAVLE-RRGLMDRKG-F----PESYDRRGL 154

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298552909 102 YSTLQNILKG-HKVEIPSYDYRTnsldfENVL-----VIYPADVVLFEGILVFYFPK-----IRELFHMKLFVDTDSDTR 170
Cdd:COG1072  155 LRFLARVKSGdPEVRAPVYSHLL-----YDIVpgaivVVDQPDILIVEGNNVLQDEPnpwlfVSDFFDFSIYVDADEEDL 229


                 ....*..
gi 298552909 171 LARRVPR 177
Cdd:COG1072  230 REWYVER 236
PRK07667 PRK07667
uridine kinase; Provisional
 105-173 2.71e-03

uridine kinase; Provisional


Pssm-ID: 169051  Cd Length: 193  Bit Score: 37.79  E-value: 2.71e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 298552909 105 LQNilkGHKVEIPSYDYRTNSLDFENVLvIYPADVVLFEGILVfYFPKIRELFHMKLFVDTDSDTRLAR 173
Cdd:PRK07667  92 LQN---ETKLTLPFYHDETDTCEMKKVQ-IPIVGVIVIEGVFL-QRKEWRDFFHYMVYLDCPRETRFLR 155
NK cd02019
Nucleoside/nucleotide kinase (NK) is a protein superfamily consisting of multiple families of ...
 29-56 4.85e-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: 35.00  E-value: 4.85e-03
                         10        20
                 ....*....|....*....|....*...
gi 298552909  29 LIGVAGGTASGKSTVCKKIMEQLGQAEM 56
Cdd:cd02019    1 IIAITGGSGSGKSTVAKKLAEQLGGRSV 28
CoaE COG0237
Dephospho-CoA kinase [Coenzyme transport and metabolism]; Dephospho-CoA kinase is part of the ...
 27-52 5.94e-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: 36.97  E-value: 5.94e-03
                         10        20
                 ....*....|....*....|....*.
gi 298552909  27 PFLIGVAGGTASGKSTVCkKIMEQLG 52
Cdd:COG0237    1 MLIIGLTGGIGSGKSTVA-RMFAELG 25
 
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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