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Conserved domains on  [gi|488193132|ref|WP_002264340|]
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uridine kinase [Streptococcus mutans]

Protein Classification

uridine-cytidine kinase( domain architecture ID 10792545)

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

EC:  2.7.1.48
Gene Ontology:  GO:0005737|GO:0044206|GO:0005829|GO:0016310|GO:0043771|GO:0005524|GO:0004849|GO:0044211
PubMed:  27239701

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
PRK05480 PRK05480
uridine/cytidine kinase; Provisional
 1-207 9.82e-120

uridine/cytidine kinase; Provisional


:

Pssm-ID: 235492 [Multi-domain]  Cd Length: 209  Bit Score: 338.29  E-value: 9.82e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488193132   1 MRKKPIIIGVTGGSGSGKTSVSRAILANFPNAKIAMIEHDSYYKDQSHLTFEERVTINYDHPLAFETDLLINHLKELIAD 80
Cdd:PRK05480   2 MMKKPIIIGIAGGSGSGKTTVASTIYEELGDESIAVIPQDSYYKDQSHLSFEERVKTNYDHPDAFDHDLLIEHLKALKAG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488193132  81 RPVDIPIYDYTQHTRSEKSYRQEPQDVFIVEGILVLEDQRLRDLMDIKLFVDTDDDIRIIRRIKRDMQERGRSLDSIIEQ 160
Cdd:PRK05480  82 KAIEIPVYDYTEHTRSKETIRVEPKDVIILEGILLLEDERLRDLMDIKIFVDTPLDIRLIRRLKRDVNERGRSLESVINQ 161

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 488193132 161 YTRVVKPMYHQFIEPTKRYADIVVPEGVSNLVAIDLINTKVASILNE 207
Cdd:PRK05480 162 YLSTVRPMHLQFIEPSKRYADIIIPEGGKNRVAIDILKAKIRQLLEK 208
 
Name Accession Description Interval E-value
PRK05480 PRK05480
uridine/cytidine kinase; Provisional
 1-207 9.82e-120

uridine/cytidine kinase; Provisional


Pssm-ID: 235492 [Multi-domain]  Cd Length: 209  Bit Score: 338.29  E-value: 9.82e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488193132   1 MRKKPIIIGVTGGSGSGKTSVSRAILANFPNAKIAMIEHDSYYKDQSHLTFEERVTINYDHPLAFETDLLINHLKELIAD 80
Cdd:PRK05480   2 MMKKPIIIGIAGGSGSGKTTVASTIYEELGDESIAVIPQDSYYKDQSHLSFEERVKTNYDHPDAFDHDLLIEHLKALKAG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488193132  81 RPVDIPIYDYTQHTRSEKSYRQEPQDVFIVEGILVLEDQRLRDLMDIKLFVDTDDDIRIIRRIKRDMQERGRSLDSIIEQ 160
Cdd:PRK05480  82 KAIEIPVYDYTEHTRSKETIRVEPKDVIILEGILLLEDERLRDLMDIKIFVDTPLDIRLIRRLKRDVNERGRSLESVINQ 161

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 488193132 161 YTRVVKPMYHQFIEPTKRYADIVVPEGVSNLVAIDLINTKVASILNE 207
Cdd:PRK05480 162 YLSTVRPMHLQFIEPSKRYADIIIPEGGKNRVAIDILKAKIRQLLEK 208
UMPK cd02023
Uridine monophosphate kinase (UMPK, EC 2.7.1.48), also known as uridine kinase or ...
 7-204 9.70e-90

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: 261.72  E-value: 9.70e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488193132   7 IIGVTGGSGSGKTSVSRAILANFPNAKIAMIEHDSYYKDQSHLTFEERVTINYDHPLAFETDLLINHLKELIADRPVDIP 86
Cdd:cd02023    1 IIGIAGGSGSGKTTVAEEIIEQLGNPKVVIISQDSYYKDLSHEELEERKNNNYDHPDAFDFDLLISHLQDLKNGKSVEIP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488193132  87 IYDYTQHTRSEKSYRQEPQDVFIVEGILVLEDQRLRDLMDIKLFVDTDDDIRIIRRIKRDMQERGRSLDSIIEQYTRVVK 166
Cdd:cd02023   81 VYDFKTHSRLKETVTVYPADVIILEGILALYDKELRDLMDLKIFVDTDADVRLIRRIERDIVERGRDLESVINQYLKFVK 160

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 488193132 167 PMYHQFIEPTKRYADIVVPEGVSNLVAIDLINTKVASI 204
Cdd:cd02023  161 PMHEQFIEPTKRYADVIIPRGGDNHVAIDLIVQHIKSK 198
udk TIGR00235
uridine kinase; Model contains a number of longer eukaryotic proteins and starts bringing in ...
 3-206 2.43e-85

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: 251.15  E-value: 2.43e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488193132    3 KKPIIIGVTGGSGSGKTSVSRAILANFPNAKIAMIEHDSYYKDQSHLTFEERVTINYDHPLAFETDLLINHLKELIADRP 82
Cdd:TIGR00235   4 PKGIIIGIGGGSGSGKTTVARKIYEQLGKLEIVIISQDNYYKDQSHLEMAERKKTNFDHPDAFDNDLLYEHLKNLKNGSP 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488193132   83 VDIPIYDYTQHTRSEKSYRQEPQDVFIVEGILVLEDQRLRDLMDIKLFVDTDDDIRIIRRIKRDMQERGRSLDSIIEQYT 162
Cdd:TIGR00235  84 IDVPVYDYVNHTRPKETVHIEPKDVVILEGIMPLFDERLRDLMDLKIFVDTPLDIRLIRRIERDINERGRSLDSVIDQYR 163

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 488193132  163 RVVKPMYHQFIEPTKRYADIVVPEGVSNLVAIDLINTKVASILN 206
Cdd:TIGR00235 164 KTVRPMYEQFVEPTKQYADLIIPEGGRNEVAINVLDTKIKHLLE 207
Udk COG0572
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway ...
 1-203 3.93e-81

Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway/BioSystem: Pyrimidine salvage


Pssm-ID: 440337 [Multi-domain]  Cd Length: 206  Bit Score: 240.13  E-value: 3.93e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488193132   1 MRKKPIIIGVTGGSGSGKTSVSRAILANFPNAKIAMIEHDSYYKDQSHLTFEERVTINYDHPLAFETDLLINHLKELIAD 80
Cdd:COG0572    3 RSGKPRIIGIAGPSGSGKTTFARRLAEQLGADKVVVISLDDYYKDREHLPLDERGKPNFDHPEAFDLDLLNEHLEPLKAG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488193132  81 RPVDIPIYDYTQHTRSEKSYRQEPQDVFIVEGILVLEDQRLRDLMDIKLFVDTDDDIRIIRRIKRDMQERGRSLDSIIEQ 160
Cdd:COG0572   83 ESVELPVYDFATGTRSGETVKVEPADVIIVEGIHALNDELLRDLLDLKIYVDADTDVRLIRRIVRDGEERGRTAESVIEQ 162

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 488193132 161 YTRVVKPMYHQFIEPTKRYADIVVPEG-VSNLVAIDLINTKVAS 203
Cdd:COG0572  163 YWATVRPGHEQYIEPTKEYADIVIPNGgPLNPVALDLLVARLLS 206
PRK pfam00485
Phosphoribulokinase / Uridine kinase family; This family matches three types of P-loop ...
 7-193 2.45e-39

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: 133.68  E-value: 2.45e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488193132    7 IIGVTGGSGSGKTSVSRAILANF--PNAKIAMIEHDSY------YKDqshLTFEER-----VTINYDHPLAFETDLLINH 73
Cdd:pfam00485   1 VIGVAGSSGSGKTTVARRIVSIFgrEGVPAVGIEGDSFhstdrfYMD---LHPEDRkragnNGYSFDGPEANDFDLLYEQ 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488193132   74 LKELIADRPVDIPIYDYTQHTRSEKSYRQEPQDVFIVEGILVLEDQRLRDLMDIKLFVDTDDDIRIIRRIKRDMQERGRS 153
Cdd:pfam00485  78 FKELKEGGSVDKPIYNHVTHERDPTPELIEGADVLVIEGLHALYDERVAQLLDLKIYVDPDIDLELARKIQRDMAERGHS 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 488193132  154 LDSIIEQYTRvVKPMYHQFIEPTKRYADIVVPEGVSNLVA 193
Cdd:pfam00485 158 LEGVTDSILF-RKPDYVNYIDPQFSYADLIIQRVPTNDTA 196
 
Name Accession Description Interval E-value
PRK05480 PRK05480
uridine/cytidine kinase; Provisional
 1-207 9.82e-120

uridine/cytidine kinase; Provisional


Pssm-ID: 235492 [Multi-domain]  Cd Length: 209  Bit Score: 338.29  E-value: 9.82e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488193132   1 MRKKPIIIGVTGGSGSGKTSVSRAILANFPNAKIAMIEHDSYYKDQSHLTFEERVTINYDHPLAFETDLLINHLKELIAD 80
Cdd:PRK05480   2 MMKKPIIIGIAGGSGSGKTTVASTIYEELGDESIAVIPQDSYYKDQSHLSFEERVKTNYDHPDAFDHDLLIEHLKALKAG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488193132  81 RPVDIPIYDYTQHTRSEKSYRQEPQDVFIVEGILVLEDQRLRDLMDIKLFVDTDDDIRIIRRIKRDMQERGRSLDSIIEQ 160
Cdd:PRK05480  82 KAIEIPVYDYTEHTRSKETIRVEPKDVIILEGILLLEDERLRDLMDIKIFVDTPLDIRLIRRLKRDVNERGRSLESVINQ 161

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 488193132 161 YTRVVKPMYHQFIEPTKRYADIVVPEGVSNLVAIDLINTKVASILNE 207
Cdd:PRK05480 162 YLSTVRPMHLQFIEPSKRYADIIIPEGGKNRVAIDILKAKIRQLLEK 208
UMPK cd02023
Uridine monophosphate kinase (UMPK, EC 2.7.1.48), also known as uridine kinase or ...
 7-204 9.70e-90

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: 261.72  E-value: 9.70e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488193132   7 IIGVTGGSGSGKTSVSRAILANFPNAKIAMIEHDSYYKDQSHLTFEERVTINYDHPLAFETDLLINHLKELIADRPVDIP 86
Cdd:cd02023    1 IIGIAGGSGSGKTTVAEEIIEQLGNPKVVIISQDSYYKDLSHEELEERKNNNYDHPDAFDFDLLISHLQDLKNGKSVEIP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488193132  87 IYDYTQHTRSEKSYRQEPQDVFIVEGILVLEDQRLRDLMDIKLFVDTDDDIRIIRRIKRDMQERGRSLDSIIEQYTRVVK 166
Cdd:cd02023   81 VYDFKTHSRLKETVTVYPADVIILEGILALYDKELRDLMDLKIFVDTDADVRLIRRIERDIVERGRDLESVINQYLKFVK 160

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 488193132 167 PMYHQFIEPTKRYADIVVPEGVSNLVAIDLINTKVASI 204
Cdd:cd02023  161 PMHEQFIEPTKRYADVIIPRGGDNHVAIDLIVQHIKSK 198
udk TIGR00235
uridine kinase; Model contains a number of longer eukaryotic proteins and starts bringing in ...
 3-206 2.43e-85

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: 251.15  E-value: 2.43e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488193132    3 KKPIIIGVTGGSGSGKTSVSRAILANFPNAKIAMIEHDSYYKDQSHLTFEERVTINYDHPLAFETDLLINHLKELIADRP 82
Cdd:TIGR00235   4 PKGIIIGIGGGSGSGKTTVARKIYEQLGKLEIVIISQDNYYKDQSHLEMAERKKTNFDHPDAFDNDLLYEHLKNLKNGSP 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488193132   83 VDIPIYDYTQHTRSEKSYRQEPQDVFIVEGILVLEDQRLRDLMDIKLFVDTDDDIRIIRRIKRDMQERGRSLDSIIEQYT 162
Cdd:TIGR00235  84 IDVPVYDYVNHTRPKETVHIEPKDVVILEGIMPLFDERLRDLMDLKIFVDTPLDIRLIRRIERDINERGRSLDSVIDQYR 163

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 488193132  163 RVVKPMYHQFIEPTKRYADIVVPEGVSNLVAIDLINTKVASILN 206
Cdd:TIGR00235 164 KTVRPMYEQFVEPTKQYADLIIPEGGRNEVAINVLDTKIKHLLE 207
Udk COG0572
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway ...
 1-203 3.93e-81

Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway/BioSystem: Pyrimidine salvage


Pssm-ID: 440337 [Multi-domain]  Cd Length: 206  Bit Score: 240.13  E-value: 3.93e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488193132   1 MRKKPIIIGVTGGSGSGKTSVSRAILANFPNAKIAMIEHDSYYKDQSHLTFEERVTINYDHPLAFETDLLINHLKELIAD 80
Cdd:COG0572    3 RSGKPRIIGIAGPSGSGKTTFARRLAEQLGADKVVVISLDDYYKDREHLPLDERGKPNFDHPEAFDLDLLNEHLEPLKAG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488193132  81 RPVDIPIYDYTQHTRSEKSYRQEPQDVFIVEGILVLEDQRLRDLMDIKLFVDTDDDIRIIRRIKRDMQERGRSLDSIIEQ 160
Cdd:COG0572   83 ESVELPVYDFATGTRSGETVKVEPADVIIVEGIHALNDELLRDLLDLKIYVDADTDVRLIRRIVRDGEERGRTAESVIEQ 162

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 488193132 161 YTRVVKPMYHQFIEPTKRYADIVVPEG-VSNLVAIDLINTKVAS 203
Cdd:COG0572  163 YWATVRPGHEQYIEPTKEYADIVIPNGgPLNPVALDLLVARLLS 206
PTZ00301 PTZ00301
uridine kinase; Provisional
 7-205 1.57e-49

uridine kinase; Provisional


Pssm-ID: 140322 [Multi-domain]  Cd Length: 210  Bit Score: 160.17  E-value: 1.57e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488193132   7 IIGVTGGSGSGKTSVSRAILANF-----PNaKIAMIEHDSYYKDQSHLTFEERVTINYDHPLAFETDLLINHLKELIADR 81
Cdd:PTZ00301   5 VIGISGASGSGKSSLSTNIVSELmahcgPV-SIGVICEDFYYRDQSNIPESERAYTNYDHPKSLEHDLLTTHLRELKSGK 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488193132  82 PVDIPIYDYTQHTRSEKSYRQEPQDVFIVEGILVLEDQRLRDLMDIKLFVDTDDDIRIIRRIKRDMQERGRSLDSIIEQY 161
Cdd:PTZ00301  84 TVQIPQYDYVHHTRSDTAVTMTPKSVLIVEGILLFTNAELRNEMDCLIFVDTPLDICLIRRAKRDMRERGRTFESVIEQY 163

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 488193132 162 TRVVKPMYHQFIEPTKRYADIVVPEGVSNLVAIDLINTKVASIL 205
Cdd:PTZ00301 164 EATVRPMYYAYVEPSKVYADIIVPSWKDNSVAVGVLRAKLNHDL 207
PRK pfam00485
Phosphoribulokinase / Uridine kinase family; This family matches three types of P-loop ...
 7-193 2.45e-39

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: 133.68  E-value: 2.45e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488193132    7 IIGVTGGSGSGKTSVSRAILANF--PNAKIAMIEHDSY------YKDqshLTFEER-----VTINYDHPLAFETDLLINH 73
Cdd:pfam00485   1 VIGVAGSSGSGKTTVARRIVSIFgrEGVPAVGIEGDSFhstdrfYMD---LHPEDRkragnNGYSFDGPEANDFDLLYEQ 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488193132   74 LKELIADRPVDIPIYDYTQHTRSEKSYRQEPQDVFIVEGILVLEDQRLRDLMDIKLFVDTDDDIRIIRRIKRDMQERGRS 153
Cdd:pfam00485  78 FKELKEGGSVDKPIYNHVTHERDPTPELIEGADVLVIEGLHALYDERVAQLLDLKIYVDPDIDLELARKIQRDMAERGHS 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 488193132  154 LDSIIEQYTRvVKPMYHQFIEPTKRYADIVVPEGVSNLVA 193
Cdd:pfam00485 158 LEGVTDSILF-RKPDYVNYIDPQFSYADLIIQRVPTNDTA 196
PRK07429 PRK07429
phosphoribulokinase; Provisional
 1-184 3.30e-23

phosphoribulokinase; Provisional


Pssm-ID: 180975  Cd Length: 327  Bit Score: 94.69  E-value: 3.30e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488193132   1 MRKKPIIIGVTGGSGSGKTSVSRAILANFPNAKIAMIEHDSYYKdqshLTFEERVTINYD--HPLAFETDLLINHLKELI 78
Cdd:PRK07429   4 MPDRPVLLGVAGDSGCGKTTFLRGLADLLGEELVTVICTDDYHS----YDRKQRKELGITalDPRANNLDIMYEHLKALK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488193132  79 ADRPVDIPIYDYTQHT--RSEksyRQEPQDVFIVEGILVLEDQRLRDLMDIKLFVDTDDDIRIIRRIKRDMQERGRSLDS 156
Cdd:PRK07429  80 TGQPILKPIYNHETGTfdPPE---YIEPNKIVVVEGLHPLYDERVRELYDFKVYLDPPEEVKIAWKIKRDMAKRGHTYEQ 156

                        170       180
                 ....*....|....*....|....*...
gi 488193132 157 IIEQYTRvVKPMYHQFIEPTKRYADIVV 184
Cdd:PRK07429 157 VLAEIEA-REPDFEAYIRPQRQWADVVI 183
PRK cd02026
Phosphoribulokinase (PRK) is an enzyme involved in the Benson-Calvin cycle in chloroplasts or ...
 7-184 7.41e-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: 90.09  E-value: 7.41e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488193132   7 IIGVTGGSGSGKTSVSRAILANFPNAKIAMIEHDSYYKdqshLTFEERVT--INYDHPLAFETDLLINHLKELIADRPVD 84
Cdd:cd02026    1 IIGVAGDSGCGKSTFLRRLTSLFGSDLVTVICLDDYHS----LDRKGRKEtgITALDPRANNFDLMYEQLKALKEGQAIE 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488193132  85 IPIYDYTQHTrSEKSYRQEPQDVFIVEGILVLEDQRLRDLMDIKLFVDTDDDIRIIRRIKRDMQERGRSLDSIIEQY-TR 163
Cdd:cd02026   77 KPIYNHVTGL-IDPPELIKPTKIVVIEGLHPLYDERVRELLDFSVYLDISDEVKFAWKIQRDMAERGHSLEDVLASIeAR 155

                        170       180
                 ....*....|....*....|.
gi 488193132 164 vvKPMYHQFIEPTKRYADIVV 184
Cdd:cd02026  156 --KPDFEAYIDPQKQYADVVI 174
PLN02318 PLN02318
phosphoribulokinase/uridine kinase
 6-184 2.57e-21

phosphoribulokinase/uridine kinase


Pssm-ID: 177952 [Multi-domain]  Cd Length: 656  Bit Score: 91.07  E-value: 2.57e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488193132   6 IIIGVTGGSGSGKTSVSRAILANFPNakIAMIEHDSYyKDQSHLtfeerVTINYDHPLAFETDLLINHLKELIADRPVDI 85
Cdd:PLN02318  66 ILVGVAGPSGAGKTVFTEKVLNFMPS--IAVISMDNY-NDSSRI-----IDGNFDDPRLTDYDTLLDNIHDLKAGKSVQV 137

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488193132  86 PIYDYTQHTRSekSYRQEP---QDVFIVEGILVLEdQRLRDLMDIKLFVDTDDDIRIIRRIKRDMQERGRSLDSIIEQYT 162
Cdd:PLN02318 138 PIYDFKSSSRV--GYRTLEvpsSRIVIIEGIYALS-EKLRPLLDLRVSVTGGVHFDLVKRVLRDIQRAGQEPEEIIHQIS 214

                        170       180
                 ....*....|....*....|..
gi 488193132 163 RVVKPMYHQFIEPTKRYADIVV 184
Cdd:PLN02318 215 ETVYPMYKAFIEPDLQTAHIKI 236
PLN02348 PLN02348
phosphoribulokinase
 2-184 4.86e-18

phosphoribulokinase


Pssm-ID: 215198  Cd Length: 395  Bit Score: 81.04  E-value: 4.86e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488193132   2 RKKPIIIGVTGGSGSGKTSVSRAILANF-------------PNAKIA----MIEHDSYYKDQSHLTFEERVTINydHPLA 64
Cdd:PLN02348  46 DDGTVVIGLAADSGCGKSTFMRRLTSVFggaakppkggnpdSNTLISdtttVICLDDYHSLDRTGRKEKGVTAL--DPRA 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488193132  65 FETDLLINHLKELIADRPVDIPIYDYTQHTRsEKSYRQEPQDVFIVEGILVLEDQRLRDLMDIKLFVDTDDDIRIIRRIK 144
Cdd:PLN02348 124 NNFDLMYEQVKALKEGKAVEKPIYNHVTGLL-DPPELIEPPKILVIEGLHPMYDERVRDLLDFSIYLDISDDVKFAWKIQ 202

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 488193132 145 RDMQERGRSLDSI---IEQYtrvvKPMYHQFIEPTKRYADIVV 184
Cdd:PLN02348 203 RDMAERGHSLESIkasIEAR----KPDFDAYIDPQKQYADVVI 241
UMPK_like cd02028
Uridine monophosphate kinase_like (UMPK_like) is a family of proteins highly similar to the ...
 7-184 5.12e-16

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: 72.34  E-value: 5.12e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488193132   7 IIGVTGGSGSGKTSvSRAILANFPNA---KIAMIEHDSYYKDqshLTFEERVTINYDHPLAFETDLLINHLKELIADRPV 83
Cdd:cd02028    1 VVGIAGPSGSGKTT-FAKKLSNQLRVngiGPVVISLDDYYVP---RKTPRDEDGNYDFESILDLDLLNKNLHDLLNGKEV 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488193132  84 DIPIYDYTQHTR-SEKSYRQEPQDVFIVEGILVLEDqRLRDLMDIKLFVDTDDDIRIIRRIKR-DMQERGRSLDSIIEQY 161
Cdd:cd02028   77 ELPIYDFRTGKRrGYRKLKLPPSGVVILEGIYALNE-RLRSLLDIRVAVSGGVHLNRLLRRVVrDIQFRGYSAELTILMW 155

                        170       180
                 ....*....|....*....|...
gi 488193132 162 TRVvkPMYHQFIEPTKRYADIVV 184
Cdd:cd02028  156 PSV--PSGEEFIIPPLQEAAIVM 176
NRK1 cd02024
Nicotinamide riboside kinase (NRK) is an enzyme involved in the metabolism of nicotinamide ...
 7-131 1.44e-11

Nicotinamide riboside kinase (NRK) is an enzyme involved in the metabolism of nicotinamide adenine dinucleotide (NAD+). This enzyme catalyzes the phosphorylation of nicotinamide riboside (NR) to form nicotinamide mononucleotide (NMN). It defines the NR salvage pathway of NAD+ biosynthesis in addition to the pathways through nicotinic acid mononucleotide (NaMN). This enzyme can also phosphorylate the anticancer drug tiazofurin, which is an analog of nicotinamide riboside.


Pssm-ID: 238982 [Multi-domain]  Cd Length: 187  Bit Score: 60.80  E-value: 1.44e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488193132   7 IIGVTGGSGSGKTSVSRAILANFPNAKIamIEHDSYYKDQSHLTFEERVTINYDHPLAF-------------ETDLLINH 73
Cdd:cd02024    1 IVGISGVTNSGKTTLAKLLQRILPNCCV--IHQDDFFKPEDEIPVDENGFKQWDVLEALdmeammstldywrETGHFPKF 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 488193132  74 LKEL-IADRPVDIPIYDYTQHTRSEKSYRQEPQDVFIVEGILVLEDQRLRDLMDIKLFV 131
Cdd:cd02024   79 LRSHgNENDPEKEFIEDAQIEETKADLLGAEDLHILIVDGFLLYNYKPLVDLFDIRYFL 137
CoaA COG1072
Panthothenate kinase [Coenzyme transport and metabolism]; Panthothenate kinase is part of the ...
 2-133 6.32e-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: 48.75  E-value: 6.32e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488193132   2 RKKPIIIGVTGGSGSGKTSVSR---AILANFPNA-KIAMIEHDSYYKDQSHLtfEERVTIN-------YDhplafeTDLL 70
Cdd:COG1072   83 KKTPFIIGIAGSVAVGKSTTARllqALLSRWPEHpKVELVTTDGFLYPNAVL--ERRGLMDrkgfpesYD------RRGL 154

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488193132  71 INHLKELIADRP-VDIPIYDYTQHTRSEKSYRQEPQ-DVFIVEGILVLEDQR-----LRDLMDIKLFVDT 133
Cdd:COG1072  155 LRFLARVKSGDPeVRAPVYSHLLYDIVPGAIVVVDQpDILIVEGNNVLQDEPnpwlfVSDFFDFSIYVDA 224
PRK08233 PRK08233
hypothetical protein; Provisional
 3-184 6.99e-06

hypothetical protein; Provisional


Pssm-ID: 181310 [Multi-domain]  Cd Length: 182  Bit Score: 44.73  E-value: 6.99e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488193132   3 KKPIIIGVTGGSGSGKTSVSRAILANFPNAKIamIEHDSYYKDQSHLTFEERVT--INYDhplAFETDLLINHLKELIAD 80
Cdd:PRK08233   1 KKTKIITIAAVSGGGKTTLTERLTHKLKNSKA--LYFDRYDFDNCPEDICKWIDkgANYS---EWVLTPLIKDIQELIAK 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488193132  81 RPVDIPIYDYTqhtrseksyrqepqdvfivegiLVLEDQRLRDLMDIKLFVDTDDDIRIIRRIKRDMQER-GRSLDSIIE 159
Cdd:PRK08233  76 SNVDYIIVDYP----------------------FAYLNSEMRQFIDVTIFIDTPLDIAMARRILRDFKEDtGNEIHNDLK 133

                        170       180
                 ....*....|....*....|....*
gi 488193132 160 QYTRVVKPMYHQFIEPTKRYADIVV 184
Cdd:PRK08233 134 HYLNYARPLYLEALHTVKPNADIVL 158
PanK cd02025
Pantothenate kinase (PanK) catalyzes the phosphorylation of pantothenic acid to form 4 ...
 7-132 7.51e-05

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: 42.30  E-value: 7.51e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488193132   7 IIGVTGGSGSGKTSVSR---AILANFP-NAKIAMIEHDSY-YKDQshlTFEERVTINYD-HPLAFETDLLINHLKELIAD 80
Cdd:cd02025    1 IIGIAGSVAVGKSTTARvlqALLSRWPdHPNVELITTDGFlYPNK---ELIERGLMDRKgFPESYDMEALLKFLKDIKSG 77

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 488193132  81 RP-VDIPIYDYTQH--TRSEKSYRQEPqDVFIVEGILVLEDQRLR-----DLMDIKLFVD 132
Cdd:cd02025   78 KKnVKIPVYSHLTYdvIPGEKQTVDQP-DILIIEGLNVLQTGQNPrlfvsDFFDFSIYVD 136
PRK15453 PRK15453
phosphoribulokinase; Provisional
 1-44 4.89e-04

phosphoribulokinase; Provisional


Pssm-ID: 237970  Cd Length: 290  Bit Score: 40.18  E-value: 4.89e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 488193132   1 MRKKPIIIGVTGGSGSGKTSVSRAILANFPNAKI--AMIEHDSYYK 44
Cdd:PRK15453   1 MSAKHPIIAVTGSSGAGTTTVKRAFEKIFRRENInaAVVEGDSFHR 46
PRK06696 PRK06696
uridine kinase; Validated
 5-133 3.65e-03

uridine kinase; Validated


Pssm-ID: 180660  Cd Length: 223  Bit Score: 37.26  E-value: 3.65e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488193132   5 PIIIGVTGGSGSGKTS---------------VSRAILANFPNAKIamIEH-------DSYYKDQSHLT-FEERVTinydH 61
Cdd:PRK06696  22 PLRVAIDGITASGKTTfadelaeeikkrgrpVIRASIDDFHNPRV--IRYrrgresaEGYYEDAYDYTaLRRLLL----D 95

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488193132  62 PLAFETDLL---INHlkELIADRPVDIPiydytqhtrseksYRQEPQD-VFIVEGILVLEDQrLRDLMDIKLFVDT 133
Cdd:PRK06696  96 PLGPNGDRQyrtASH--DLKTDIPVHNP-------------PLLAAPNaVLIVDGTFLLRPE-LRDLWDYKIFLDT 155
YejR COG0523
Zinc metallochaperone YeiR/ZagA and related GTPases, G3E family [General function prediction ...
 1-40 4.66e-03

Zinc metallochaperone YeiR/ZagA and related GTPases, G3E family [General function prediction only];


Pssm-ID: 440289 [Multi-domain]  Cd Length: 318  Bit Score: 37.07  E-value: 4.66e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 488193132   1 MRKKPIIIgVTGGSGSGKTSVSRAILANFPNAKIAMIEHD 40
Cdd:COG0523    1 DKRIPVTV-LTGFLGAGKTTLLNHLLANPEGRRIAVIVNE 39
CoaE COG0237
Dephospho-CoA kinase [Coenzyme transport and metabolism]; Dephospho-CoA kinase is part of the ...
 5-23 9.57e-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: 35.81  E-value: 9.57e-03
                         10
                 ....*....|....*....
gi 488193132   5 PIIIGVTGGSGSGKTSVSR 23
Cdd:COG0237    1 MLIIGLTGGIGSGKSTVAR 19
Gmk COG0194
Guanylate kinase [Nucleotide transport and metabolism];
4-31 9.93e-03

Guanylate kinase [Nucleotide transport and metabolism];


Pssm-ID: 439964  Cd Length: 190  Bit Score: 35.43  E-value: 9.93e-03
                         10        20
                 ....*....|....*....|....*...
gi 488193132   4 KPIIIGVTGGSGSGKTSVSRAILANFPN 31
Cdd:COG0194    1 RGKLIVLSGPSGAGKTTLVKALLERDPD 28
 
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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