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Conserved domains on  [gi|446459232|ref|WP_000537086|]
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MULTISPECIES: uridine kinase [Bacillus]

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

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List of domain hits

 Name Accession Description Interval E-value
PRK05480 PRK05480
uridine/cytidine kinase; Provisional
 19-209 1.74e-127

uridine/cytidine kinase; Provisional


:

Pssm-ID: 235492 [Multi-domain]  Cd Length: 209  Bit Score: 357.93  E-value: 1.74e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459232  19 KTSVTKAIFDHFKGHSILILEQDYYYKDQSHLPMEERLKTNYDHPLAFDNDLLIEHLQQLLAYKQVDKPVYDYTLHTRSE 98
Cdd:PRK05480  19 KTTVASTIYEELGDESIAVIPQDSYYKDQSHLSFEERVKTNYDHPDAFDHDLLIEHLKALKAGKAIEIPVYDYTEHTRSK 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459232  99 EIIPVEPKDVIILEGILILEDPRLCELMDIKLFVDTDADLRILRRMQRDIKERGRTMDSVIDQYVNVVRPMHNQFIEPSK 178
Cdd:PRK05480  99 ETIRVEPKDVIILEGILLLEDERLRDLMDIKIFVDTPLDIRLIRRLKRDVNERGRSLESVINQYLSTVRPMHLQFIEPSK 178

                        170       180       190
                 ....*....|....*....|....*....|.
gi 446459232 179 KFADIIIPEGGQNHVAIDSMVTKIATILEQK 209
Cdd:PRK05480 179 RYADIIIPEGGKNRVAIDILKAKIRQLLEKN 209
 
Name Accession Description Interval E-value
PRK05480 PRK05480
uridine/cytidine kinase; Provisional
 19-209 1.74e-127

uridine/cytidine kinase; Provisional


Pssm-ID: 235492 [Multi-domain]  Cd Length: 209  Bit Score: 357.93  E-value: 1.74e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459232  19 KTSVTKAIFDHFKGHSILILEQDYYYKDQSHLPMEERLKTNYDHPLAFDNDLLIEHLQQLLAYKQVDKPVYDYTLHTRSE 98
Cdd:PRK05480  19 KTTVASTIYEELGDESIAVIPQDSYYKDQSHLSFEERVKTNYDHPDAFDHDLLIEHLKALKAGKAIEIPVYDYTEHTRSK 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459232  99 EIIPVEPKDVIILEGILILEDPRLCELMDIKLFVDTDADLRILRRMQRDIKERGRTMDSVIDQYVNVVRPMHNQFIEPSK 178
Cdd:PRK05480  99 ETIRVEPKDVIILEGILLLEDERLRDLMDIKIFVDTPLDIRLIRRLKRDVNERGRSLESVINQYLSTVRPMHLQFIEPSK 178

                        170       180       190
                 ....*....|....*....|....*....|.
gi 446459232 179 KFADIIIPEGGQNHVAIDSMVTKIATILEQK 209
Cdd:PRK05480 179 RYADIIIPEGGKNRVAIDILKAKIRQLLEKN 209
UMPK cd02023
Uridine monophosphate kinase (UMPK, EC 2.7.1.48), also known as uridine kinase or ...
 15-205 6.90e-97

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: 280.21  E-value: 6.90e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459232  15 SGSGKTSVTKAIFDHFKGHSILILEQDYYYKDQSHLPMEERLKTNYDHPLAFDNDLLIEHLQQLLAYKQVDKPVYDYTLH 94
Cdd:cd02023    8 SGSGKTTVAEEIIEQLGNPKVVIISQDSYYKDLSHEELEERKNNNYDHPDAFDFDLLISHLQDLKNGKSVEIPVYDFKTH 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459232  95 TRSEEIIPVEPKDVIILEGILILEDPRLCELMDIKLFVDTDADLRILRRMQRDIKERGRTMDSVIDQYVNVVRPMHNQFI 174
Cdd:cd02023   88 SRLKETVTVYPADVIILEGILALYDKELRDLMDLKIFVDTDADVRLIRRIERDIVERGRDLESVINQYLKFVKPMHEQFI 167

                        170       180       190
                 ....*....|....*....|....*....|.
gi 446459232 175 EPSKKFADIIIPEGGQNHVAIDSMVTKIATI 205
Cdd:cd02023  168 EPTKRYADVIIPRGGDNHVAIDLIVQHIKSK 198
udk TIGR00235
uridine kinase; Model contains a number of longer eukaryotic proteins and starts bringing in ...
 1-207 4.17e-96

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: 278.50  E-value: 4.17e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459232    1 MGTNKPVVIGIAGGSGSGKTSVTKAIFDHFKGHSILILEQDYYYKDQSHLPMEERLKTNYDHPLAFDNDLLIEHLQQLLA 80
Cdd:TIGR00235   1 MDKPKGIIIGIGGGSGSGKTTVARKIYEQLGKLEIVIISQDNYYKDQSHLEMAERKKTNFDHPDAFDNDLLYEHLKNLKN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459232   81 YKQVDKPVYDYTLHTRSEEIIPVEPKDVIILEGILILEDPRLCELMDIKLFVDTDADLRILRRMQRDIKERGRTMDSVID 160
Cdd:TIGR00235  81 GSPIDVPVYDYVNHTRPKETVHIEPKDVVILEGIMPLFDERLRDLMDLKIFVDTPLDIRLIRRIERDINERGRSLDSVID 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 446459232  161 QYVNVVRPMHNQFIEPSKKFADIIIPEGGQNHVAIDSMVTKIATILE 207
Cdd:TIGR00235 161 QYRKTVRPMYEQFVEPTKQYADLIIPEGGRNEVAINVLDTKIKHLLE 207
Udk COG0572
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway ...
 16-202 2.89e-85

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: 250.91  E-value: 2.89e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459232  16 GSGKTSVTKAIFDHFKGHSILILEQDYYYKDQSHLPMEERLKTNYDHPLAFDNDLLIEHLQQLLAYKQVDKPVYDYTLHT 95
Cdd:COG0572   17 GSGKTTFARRLAEQLGADKVVVISLDDYYKDREHLPLDERGKPNFDHPEAFDLDLLNEHLEPLKAGESVELPVYDFATGT 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459232  96 RSEEIIPVEPKDVIILEGILILEDPRLCELMDIKLFVDTDADLRILRRMQRDIKERGRTMDSVIDQYVNVVRPMHNQFIE 175
Cdd:COG0572   97 RSGETVKVEPADVIIVEGIHALNDELLRDLLDLKIYVDADTDVRLIRRIVRDGEERGRTAESVIEQYWATVRPGHEQYIE 176

                        170       180
                 ....*....|....*....|....*...
gi 446459232 176 PSKKFADIIIPEGG-QNHVAIDSMVTKI 202
Cdd:COG0572  177 PTKEYADIVIPNGGpLNPVALDLLVARL 204
PRK pfam00485
Phosphoribulokinase / Uridine kinase family; This family matches three types of P-loop ...
 19-194 2.82e-35

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: 123.28  E-value: 2.82e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459232   19 KTSVTKAIFDHF--------KGHSILILEQDYYYKDQSHLPMEERLKTNYDH--PLAFDNDLLIEHLQQLLAYKQVDKPV 88
Cdd:pfam00485  12 KTTVARRIVSIFgregvpavGIEGDSFHSTDRFYMDLHPEDRKRAGNNGYSFdgPEANDFDLLYEQFKELKEGGSVDKPI 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459232   89 YDYTLHTRSEEIIPVEPKDVIILEGILILEDPRLCELMDIKLFVDTDADLRILRRMQRDIKERGRTMDSVIDQYvNVVRP 168
Cdd:pfam00485  92 YNHVTHERDPTPELIEGADVLVIEGLHALYDERVAQLLDLKIYVDPDIDLELARKIQRDMAERGHSLEGVTDSI-LFRKP 170

                         170       180
                  ....*....|....*....|....*.
gi 446459232  169 MHNQFIEPSKKFADIIIPEGGQNHVA 194
Cdd:pfam00485 171 DYVNYIDPQFSYADLIIQRVPTNDTA 196
 
Name Accession Description Interval E-value
PRK05480 PRK05480
uridine/cytidine kinase; Provisional
 19-209 1.74e-127

uridine/cytidine kinase; Provisional


Pssm-ID: 235492 [Multi-domain]  Cd Length: 209  Bit Score: 357.93  E-value: 1.74e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459232  19 KTSVTKAIFDHFKGHSILILEQDYYYKDQSHLPMEERLKTNYDHPLAFDNDLLIEHLQQLLAYKQVDKPVYDYTLHTRSE 98
Cdd:PRK05480  19 KTTVASTIYEELGDESIAVIPQDSYYKDQSHLSFEERVKTNYDHPDAFDHDLLIEHLKALKAGKAIEIPVYDYTEHTRSK 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459232  99 EIIPVEPKDVIILEGILILEDPRLCELMDIKLFVDTDADLRILRRMQRDIKERGRTMDSVIDQYVNVVRPMHNQFIEPSK 178
Cdd:PRK05480  99 ETIRVEPKDVIILEGILLLEDERLRDLMDIKIFVDTPLDIRLIRRLKRDVNERGRSLESVINQYLSTVRPMHLQFIEPSK 178

                        170       180       190
                 ....*....|....*....|....*....|.
gi 446459232 179 KFADIIIPEGGQNHVAIDSMVTKIATILEQK 209
Cdd:PRK05480 179 RYADIIIPEGGKNRVAIDILKAKIRQLLEKN 209
UMPK cd02023
Uridine monophosphate kinase (UMPK, EC 2.7.1.48), also known as uridine kinase or ...
 15-205 6.90e-97

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: 280.21  E-value: 6.90e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459232  15 SGSGKTSVTKAIFDHFKGHSILILEQDYYYKDQSHLPMEERLKTNYDHPLAFDNDLLIEHLQQLLAYKQVDKPVYDYTLH 94
Cdd:cd02023    8 SGSGKTTVAEEIIEQLGNPKVVIISQDSYYKDLSHEELEERKNNNYDHPDAFDFDLLISHLQDLKNGKSVEIPVYDFKTH 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459232  95 TRSEEIIPVEPKDVIILEGILILEDPRLCELMDIKLFVDTDADLRILRRMQRDIKERGRTMDSVIDQYVNVVRPMHNQFI 174
Cdd:cd02023   88 SRLKETVTVYPADVIILEGILALYDKELRDLMDLKIFVDTDADVRLIRRIERDIVERGRDLESVINQYLKFVKPMHEQFI 167

                        170       180       190
                 ....*....|....*....|....*....|.
gi 446459232 175 EPSKKFADIIIPEGGQNHVAIDSMVTKIATI 205
Cdd:cd02023  168 EPTKRYADVIIPRGGDNHVAIDLIVQHIKSK 198
udk TIGR00235
uridine kinase; Model contains a number of longer eukaryotic proteins and starts bringing in ...
 1-207 4.17e-96

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: 278.50  E-value: 4.17e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459232    1 MGTNKPVVIGIAGGSGSGKTSVTKAIFDHFKGHSILILEQDYYYKDQSHLPMEERLKTNYDHPLAFDNDLLIEHLQQLLA 80
Cdd:TIGR00235   1 MDKPKGIIIGIGGGSGSGKTTVARKIYEQLGKLEIVIISQDNYYKDQSHLEMAERKKTNFDHPDAFDNDLLYEHLKNLKN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459232   81 YKQVDKPVYDYTLHTRSEEIIPVEPKDVIILEGILILEDPRLCELMDIKLFVDTDADLRILRRMQRDIKERGRTMDSVID 160
Cdd:TIGR00235  81 GSPIDVPVYDYVNHTRPKETVHIEPKDVVILEGIMPLFDERLRDLMDLKIFVDTPLDIRLIRRIERDINERGRSLDSVID 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 446459232  161 QYVNVVRPMHNQFIEPSKKFADIIIPEGGQNHVAIDSMVTKIATILE 207
Cdd:TIGR00235 161 QYRKTVRPMYEQFVEPTKQYADLIIPEGGRNEVAINVLDTKIKHLLE 207
Udk COG0572
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway ...
 16-202 2.89e-85

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: 250.91  E-value: 2.89e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459232  16 GSGKTSVTKAIFDHFKGHSILILEQDYYYKDQSHLPMEERLKTNYDHPLAFDNDLLIEHLQQLLAYKQVDKPVYDYTLHT 95
Cdd:COG0572   17 GSGKTTFARRLAEQLGADKVVVISLDDYYKDREHLPLDERGKPNFDHPEAFDLDLLNEHLEPLKAGESVELPVYDFATGT 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459232  96 RSEEIIPVEPKDVIILEGILILEDPRLCELMDIKLFVDTDADLRILRRMQRDIKERGRTMDSVIDQYVNVVRPMHNQFIE 175
Cdd:COG0572   97 RSGETVKVEPADVIIVEGIHALNDELLRDLLDLKIYVDADTDVRLIRRIVRDGEERGRTAESVIEQYWATVRPGHEQYIE 176

                        170       180
                 ....*....|....*....|....*...
gi 446459232 176 PSKKFADIIIPEGG-QNHVAIDSMVTKI 202
Cdd:COG0572  177 PTKEYADIVIPNGGpLNPVALDLLVARL 204
PTZ00301 PTZ00301
uridine kinase; Provisional
 34-207 2.72e-55

uridine kinase; Provisional


Pssm-ID: 140322 [Multi-domain]  Cd Length: 210  Bit Score: 175.19  E-value: 2.72e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459232  34 SILILEQDYYYKDQSHLPMEERLKTNYDHPLAFDNDLLIEHLQQLLAYKQVDKPVYDYTLHTRSEEIIPVEPKDVIILEG 113
Cdd:PTZ00301  35 SIGVICEDFYYRDQSNIPESERAYTNYDHPKSLEHDLLTTHLRELKSGKTVQIPQYDYVHHTRSDTAVTMTPKSVLIVEG 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459232 114 ILILEDPRLCELMDIKLFVDTDADLRILRRMQRDIKERGRTMDSVIDQYVNVVRPMHNQFIEPSKKFADIIIPEGGQNHV 193
Cdd:PTZ00301 115 ILLFTNAELRNEMDCLIFVDTPLDICLIRRAKRDMRERGRTFESVIEQYEATVRPMYYAYVEPSKVYADIIVPSWKDNSV 194

                        170
                 ....*....|....
gi 446459232 194 AIDSMVTKIATILE 207
Cdd:PTZ00301 195 AVGVLRAKLNHDLE 208
PRK pfam00485
Phosphoribulokinase / Uridine kinase family; This family matches three types of P-loop ...
 19-194 2.82e-35

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: 123.28  E-value: 2.82e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459232   19 KTSVTKAIFDHF--------KGHSILILEQDYYYKDQSHLPMEERLKTNYDH--PLAFDNDLLIEHLQQLLAYKQVDKPV 88
Cdd:pfam00485  12 KTTVARRIVSIFgregvpavGIEGDSFHSTDRFYMDLHPEDRKRAGNNGYSFdgPEANDFDLLYEQFKELKEGGSVDKPI 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459232   89 YDYTLHTRSEEIIPVEPKDVIILEGILILEDPRLCELMDIKLFVDTDADLRILRRMQRDIKERGRTMDSVIDQYvNVVRP 168
Cdd:pfam00485  92 YNHVTHERDPTPELIEGADVLVIEGLHALYDERVAQLLDLKIYVDPDIDLELARKIQRDMAERGHSLEGVTDSI-LFRKP 170

                         170       180
                  ....*....|....*....|....*.
gi 446459232  169 MHNQFIEPSKKFADIIIPEGGQNHVA 194
Cdd:pfam00485 171 DYVNYIDPQFSYADLIIQRVPTNDTA 196
PRK07429 PRK07429
phosphoribulokinase; Provisional
 62-185 6.67e-21

phosphoribulokinase; Provisional


Pssm-ID: 180975  Cd Length: 327  Bit Score: 88.53  E-value: 6.67e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459232  62 HPLAFDNDLLIEHLQQLLAYKQVDKPVYDYTlhtrSEEIIP---VEPKDVIILEGILILEDPRLCELMDIKLFVDTDADL 138
Cdd:PRK07429  62 DPRANNLDIMYEHLKALKTGQPILKPIYNHE----TGTFDPpeyIEPNKIVVVEGLHPLYDERVRELYDFKVYLDPPEEV 137

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 446459232 139 RILRRMQRDIKERGRTMDSVIDQyVNVVRPMHNQFIEPSKKFADIII 185
Cdd:PRK07429 138 KIAWKIKRDMAKRGHTYEQVLAE-IEAREPDFEAYIRPQRQWADVVI 183
PRK cd02026
Phosphoribulokinase (PRK) is an enzyme involved in the Benson-Calvin cycle in chloroplasts or ...
 62-185 1.38e-20

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: 86.62  E-value: 1.38e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459232  62 HPLAFDNDLLIEHLQQLLAYKQVDKPVYDYTLHT-RSEEIIpvEPKDVIILEGILILEDPRLCELMDIKLFVDTDADLRI 140
Cdd:cd02026   53 DPRANNFDLMYEQLKALKEGQAIEKPIYNHVTGLiDPPELI--KPTKIVVIEGLHPLYDERVRELLDFSVYLDISDEVKF 130

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 446459232 141 LRRMQRDIKERGRTMDSVIDQyVNVVRPMHNQFIEPSKKFADIII 185
Cdd:cd02026  131 AWKIQRDMAERGHSLEDVLAS-IEARKPDFEAYIDPQKQYADVVI 174
UMPK_like cd02028
Uridine monophosphate kinase_like (UMPK_like) is a family of proteins highly similar to the ...
 19-185 2.04e-18

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: 78.89  E-value: 2.04e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459232  19 KTSVTK--AIFDHFKGHSILILEQDYYYKDqshLPMEERLKTNYDHPLAFDNDLLIEHLQQLLAYKQVDKPVYDYTLHTR 96
Cdd:cd02028   12 KTTFAKklSNQLRVNGIGPVVISLDDYYVP---RKTPRDEDGNYDFESILDLDLLNKNLHDLLNGKEVELPIYDFRTGKR 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459232  97 -SEEIIPVEPKDVIILEGILILeDPRLCELMDIKLFVDT-DADLRILRRMQRDIKERGRTMDSVIDQYVnVVRPMHNQFI 174
Cdd:cd02028   89 rGYRKLKLPPSGVVILEGIYAL-NERLRSLLDIRVAVSGgVHLNRLLRRVVRDIQFRGYSAELTILMWP-SVPSGEEFII 166

                        170
                 ....*....|.
gi 446459232 175 EPSKKFADIII 185
Cdd:cd02028  167 PPLQEAAIVMF 177
PLN02318 PLN02318
phosphoribulokinase/uridine kinase
 59-185 1.43e-15

phosphoribulokinase/uridine kinase


Pssm-ID: 177952 [Multi-domain]  Cd Length: 656  Bit Score: 74.51  E-value: 1.43e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459232  59 NYDHPLAFDNDLLIEHLQQLLAYKQVDKPVYDYTLHTR-SEEIIPVEPKDVIILEGILILEDpRLCELMDIKLFVDTDAD 137
Cdd:PLN02318 110 NFDDPRLTDYDTLLDNIHDLKAGKSVQVPIYDFKSSSRvGYRTLEVPSSRIVIIEGIYALSE-KLRPLLDLRVSVTGGVH 188

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 446459232 138 LRILRRMQRDIKERGRTMDSVIDQYVNVVRPMHNQFIEPSKKFADIII 185
Cdd:PLN02318 189 FDLVKRVLRDIQRAGQEPEEIIHQISETVYPMYKAFIEPDLQTAHIKI 236
PLN02348 PLN02348
phosphoribulokinase
 5-185 9.46e-15

phosphoribulokinase


Pssm-ID: 215198  Cd Length: 395  Bit Score: 71.80  E-value: 9.46e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459232   5 KPVVIGIAGGSGSGKTSVTKAIFDHFKGH------------------SILILEQDYYYKDQSHlpMEERLKTNYDhPLAF 66
Cdd:PLN02348  48 GTVVIGLAADSGCGKSTFMRRLTSVFGGAakppkggnpdsntlisdtTTVICLDDYHSLDRTG--RKEKGVTALD-PRAN 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459232  67 DNDLLIEHLQQLLAYKQVDKPVYDYT--LHTRSEEIipvEPKDVIILEGILILEDPRLCELMDIKLFVDTDADLRILRRM 144
Cdd:PLN02348 125 NFDLMYEQVKALKEGKAVEKPIYNHVtgLLDPPELI---EPPKILVIEGLHPMYDERVRDLLDFSIYLDISDDVKFAWKI 201

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 446459232 145 QRDIKERGRTMDSvIDQYVNVVRPMHNQFIEPSKKFADIII 185
Cdd:PLN02348 202 QRDMAERGHSLES-IKASIEARKPDFDAYIDPQKQYADVVI 241
NRK1 cd02024
Nicotinamide riboside kinase (NRK) is an enzyme involved in the metabolism of nicotinamide ...
 19-147 2.89e-10

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


Pssm-ID: 238982 [Multi-domain]  Cd Length: 187  Bit Score: 57.33  E-value: 2.89e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459232  19 KTSVTKAIFDHFKGHSILilEQDYYYKDQSHLPMEERLKTNYDHPLAFDNDLLIEHLQQLLAYKQVDK------------ 86
Cdd:cd02024   12 KTTLAKLLQRILPNCCVI--HQDDFFKPEDEIPVDENGFKQWDVLEALDMEAMMSTLDYWRETGHFPKflrshgnendpe 89

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446459232  87 --PVYDYTLHTRSEEIIPVEPKDVIILEGILILEDPRLCELMDIKLFVDTDADLRILRRMQRD 147
Cdd:cd02024   90 keFIEDAQIEETKADLLGAEDLHILIVDGFLLYNYKPLVDLFDIRYFLRVPYETCKRRREART 152
PRK08233 PRK08233
hypothetical protein; Provisional
 4-185 1.84e-04

hypothetical protein; Provisional


Pssm-ID: 181310 [Multi-domain]  Cd Length: 182  Bit Score: 40.88  E-value: 1.84e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459232   4 NKPVVIGIAGGSGSGKTSVTKAIFDHFKghSILILEQDYYYKDQSHLPMEERLK--TNYDhplAFDNDLLIEHLQQLLAY 81
Cdd:PRK08233   1 KKTKIITIAAVSGGGKTTLTERLTHKLK--NSKALYFDRYDFDNCPEDICKWIDkgANYS---EWVLTPLIKDIQELIAK 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459232  82 KQVDKPVYDYTLhtrseeiipvepkdviileGILileDPRLCELMDIKLFVDTDADLRILRRMQRDIKErgRTMDSVID- 160
Cdd:PRK08233  76 SNVDYIIVDYPF-------------------AYL---NSEMRQFIDVTIFIDTPLDIAMARRILRDFKE--DTGNEIHNd 131

                        170       180
                 ....*....|....*....|....*..
gi 446459232 161 --QYVNVVRPMHNQFIEPSKKFADIII 185
Cdd:PRK08233 132 lkHYLNYARPLYLEALHTVKPNADIVL 158
PanK cd02025
Pantothenate kinase (PanK) catalyzes the phosphorylation of pantothenic acid to form 4 ...
 82-192 1.57e-03

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: 38.45  E-value: 1.57e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459232  82 KQVDKPVYDYTLHTR-SEEIIPVEPKDVIILEGILILEDPRLCELM-----DIKLFVDTDADL---RILRRMQRDIKERG 152
Cdd:cd02025   79 KNVKIPVYSHLTYDViPGEKQTVDQPDILIIEGLNVLQTGQNPRLFvsdffDFSIYVDADEDDiekWYIKRFLKLRETAF 158

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 446459232 153 RTMDSVIDQYV----------------NVVRPMHNQFIEPSKKFADIIIpEGGQNH 192
Cdd:cd02025  159 SDPDSYFHRYAkmseeeaiafarevwkNINLKNLRENILPTRNRADLIL-EKGADH 213
PRK_like cd02029
Phosphoribulokinase-like (PRK-like) is a family of proteins similar to phosphoribulokinase ...
 20-183 2.10e-03

Phosphoribulokinase-like (PRK-like) is a family of proteins similar to phosphoribulokinase (PRK), the enzyme involved in the Benson-Calvin cycle in chloroplasts or photosynthetic prokaryotes. PRK 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: 238987  Cd Length: 277  Bit Score: 38.24  E-value: 2.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459232  20 TSVTKAIFDH-FKGHSI--LILEQDYYYKdQSHLPMEERLKT------NYDH--PLAFDNDLLiehLQQLLAYKQVDKPV 88
Cdd:cd02029   12 TTTVKRAFEHiFAREGIhpAVVEGDSFHR-YERMEMKMAIAEaldagrNFSHfgPEANLFDLL---EELFRTYGETGRGR 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459232  89 YDYTLHTRSE--------------EIIPvEPKDVIILEGI---LILEDPRLCELMDIKLFVDTDADLRILRRMQRDIKER 151
Cdd:cd02029   88 SRYYLHSDEEaapfnqepgtftpwEDLP-EDTDLLFYEGLhggVVTEGYNVAQHADLLVGVVPIINLEWIQKIHRDTAER 166

                        170       180       190
                 ....*....|....*....|....*....|....
gi 446459232 152 GRTMDSVIDqyvNVVRPMHN--QFIEPSKKFADI 183
Cdd:cd02029  167 GYSAEAVMD---TILRRMPDyiNYICPQFSRTDI 197
 
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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