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Conserved domains on  [gi|499722569|ref|WP_011403303|]
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MULTISPECIES: uridine kinase [Salinibacter]

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
 26-214 3.60e-106

uridine/cytidine kinase; Provisional


:

Pssm-ID: 235492 [Multi-domain]  Cd Length: 209  Bit Score: 304.39  E-value: 3.60e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499722569  26 KTTVLNHILEEFGSDPIAILDHDAYYHDLSHLSREKRAQFNFDHPDALETSLMREHLDRLIEGEAIEKPVYDFTTHTRRE 105
Cdd:PRK05480  19 KTTVASTIYEELGDESIAVIPQDSYYKDQSHLSFEERVKTNYDHPDAFDHDLLIEHLKALKAGKAIEIPVYDYTEHTRSK 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499722569 106 ETETVEPRPVIIIEGILVLAESALEERMDIKIYVDAADDIRLMRRIRRDMQERDRSIEGILRQYERTVRPMHLEFVEPSK 185
Cdd:PRK05480  99 ETIRVEPKDVIILEGILLLEDERLRDLMDIKIFVDTPLDIRLIRRLKRDVNERGRSLESVINQYLSTVRPMHLQFIEPSK 178

                        170       180
                 ....*....|....*....|....*....
gi 499722569 186 READIIIPRGGHNEVAIQMVMSRIQELLR 214
Cdd:PRK05480 179 RYADIIIPEGGKNRVAIDILKAKIRQLLE 207
 
Name Accession Description Interval E-value
PRK05480 PRK05480
uridine/cytidine kinase; Provisional
 26-214 3.60e-106

uridine/cytidine kinase; Provisional


Pssm-ID: 235492 [Multi-domain]  Cd Length: 209  Bit Score: 304.39  E-value: 3.60e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499722569  26 KTTVLNHILEEFGSDPIAILDHDAYYHDLSHLSREKRAQFNFDHPDALETSLMREHLDRLIEGEAIEKPVYDFTTHTRRE 105
Cdd:PRK05480  19 KTTVASTIYEELGDESIAVIPQDSYYKDQSHLSFEERVKTNYDHPDAFDHDLLIEHLKALKAGKAIEIPVYDYTEHTRSK 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499722569 106 ETETVEPRPVIIIEGILVLAESALEERMDIKIYVDAADDIRLMRRIRRDMQERDRSIEGILRQYERTVRPMHLEFVEPSK 185
Cdd:PRK05480  99 ETIRVEPKDVIILEGILLLEDERLRDLMDIKIFVDTPLDIRLIRRLKRDVNERGRSLESVINQYLSTVRPMHLQFIEPSK 178

                        170       180
                 ....*....|....*....|....*....
gi 499722569 186 READIIIPRGGHNEVAIQMVMSRIQELLR 214
Cdd:PRK05480 179 RYADIIIPEGGKNRVAIDILKAKIRQLLE 207
UMPK cd02023
Uridine monophosphate kinase (UMPK, EC 2.7.1.48), also known as uridine kinase or ...
 22-212 2.00e-85

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: 251.32  E-value: 2.00e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499722569  22 SGSGKTTVLNHILEEFGSDPIAILDHDAYYHDLSHLSREKRAQFNFDHPDALETSLMREHLDRLIEGEAIEKPVYDFTTH 101
Cdd:cd02023    8 SGSGKTTVAEEIIEQLGNPKVVIISQDSYYKDLSHEELEERKNNNYDHPDAFDFDLLISHLQDLKNGKSVEIPVYDFKTH 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499722569 102 TRREETETVEPRPVIIIEGILVLAESALEERMDIKIYVDAADDIRLMRRIRRDMQERDRSIEGILRQYERTVRPMHLEFV 181
Cdd:cd02023   88 SRLKETVTVYPADVIILEGILALYDKELRDLMDLKIFVDTDADVRLIRRIERDIVERGRDLESVINQYLKFVKPMHEQFI 167

                        170       180       190
                 ....*....|....*....|....*....|.
gi 499722569 182 EPSKREADIIIPRGGHNEVAIQMVMSRIQEL 212
Cdd:cd02023  168 EPTKRYADVIIPRGGDNHVAIDLIVQHIKSK 198
Udk COG0572
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway ...
 24-211 6.81e-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: 6.81e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499722569  24 SGKTTVLNHILEEFGSDPIAILDHDAYYHDLSHLSREKRAQFNFDHPDALETSLMREHLDRLIEGEAIEKPVYDFTTHTR 103
Cdd:COG0572   18 SGKTTFARRLAEQLGADKVVVISLDDYYKDREHLPLDERGKPNFDHPEAFDLDLLNEHLEPLKAGESVELPVYDFATGTR 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499722569 104 REETETVEPRPVIIIEGILVLAESALEERMDIKIYVDAADDIRLMRRIRRDMQERDRSIEGILRQYERTVRPMHLEFVEP 183
Cdd:COG0572   98 SGETVKVEPADVIIVEGIHALNDELLRDLLDLKIYVDADTDVRLIRRIVRDGEERGRTAESVIEQYWATVRPGHEQYIEP 177

                        170       180
                 ....*....|....*....|....*....
gi 499722569 184 SKREADIIIPRGG-HNEVAIQMVMSRIQE 211
Cdd:COG0572  178 TKEYADIVIPNGGpLNPVALDLLVARLLS 206
udk TIGR00235
uridine kinase; Model contains a number of longer eukaryotic proteins and starts bringing in ...
 8-214 9.61e-78

uridine kinase; Model contains a number of longer eukaryotic proteins and starts bringing in phosphoribulokinase hits at scores of 160 and below [Purines, pyrimidines, nucleosides, and nucleotides, Salvage of nucleosides and nucleotides]


Pssm-ID: 272977  Cd Length: 207  Bit Score: 232.28  E-value: 9.61e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499722569    8 MPMNPPVVIGIAGGSGSGKTTVLNHILEEFGSDPIAILDHDAYYHDLSHLSREKRAQFNFDHPDALETSLMREHLDRLIE 87
Cdd:TIGR00235   1 MDKPKGIIIGIGGGSGSGKTTVARKIYEQLGKLEIVIISQDNYYKDQSHLEMAERKKTNFDHPDAFDNDLLYEHLKNLKN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499722569   88 GEAIEKPVYDFTTHTRREETETVEPRPVIIIEGILVLAESALEERMDIKIYVDAADDIRLMRRIRRDMQERDRSIEGILR 167
Cdd:TIGR00235  81 GSPIDVPVYDYVNHTRPKETVHIEPKDVVILEGIMPLFDERLRDLMDLKIFVDTPLDIRLIRRIERDINERGRSLDSVID 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 499722569  168 QYERTVRPMHLEFVEPSKREADIIIPRGGHNEVAIQMVMSRIQELLR 214
Cdd:TIGR00235 161 QYRKTVRPMYEQFVEPTKQYADLIIPEGGRNEVAINVLDTKIKHLLE 207
PRK pfam00485
Phosphoribulokinase / Uridine kinase family; This family matches three types of P-loop ...
 26-201 6.05e-38

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: 130.60  E-value: 6.05e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499722569   26 KTTVLNHILEEFGSDP--------IAILDHDAYYHDLSHLSREKR--AQFNFDHPDALETSLMREHLDRLIEGEAIEKPV 95
Cdd:pfam00485  12 KTTVARRIVSIFGREGvpavgiegDSFHSTDRFYMDLHPEDRKRAgnNGYSFDGPEANDFDLLYEQFKELKEGGSVDKPI 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499722569   96 YDFTTHTRREETETVEPRPVIIIEGILVLAESALEERMDIKIYVDAADDIRLMRRIRRDMQERDRSIEGILRQYERtVRP 175
Cdd:pfam00485  92 YNHVTHERDPTPELIEGADVLVIEGLHALYDERVAQLLDLKIYVDPDIDLELARKIQRDMAERGHSLEGVTDSILF-RKP 170

                         170       180
                  ....*....|....*....|....*.
gi 499722569  176 MHLEFVEPSKREADIIIPRGGHNEVA 201
Cdd:pfam00485 171 DYVNYIDPQFSYADLIIQRVPTNDTA 196
 
Name Accession Description Interval E-value
PRK05480 PRK05480
uridine/cytidine kinase; Provisional
 26-214 3.60e-106

uridine/cytidine kinase; Provisional


Pssm-ID: 235492 [Multi-domain]  Cd Length: 209  Bit Score: 304.39  E-value: 3.60e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499722569  26 KTTVLNHILEEFGSDPIAILDHDAYYHDLSHLSREKRAQFNFDHPDALETSLMREHLDRLIEGEAIEKPVYDFTTHTRRE 105
Cdd:PRK05480  19 KTTVASTIYEELGDESIAVIPQDSYYKDQSHLSFEERVKTNYDHPDAFDHDLLIEHLKALKAGKAIEIPVYDYTEHTRSK 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499722569 106 ETETVEPRPVIIIEGILVLAESALEERMDIKIYVDAADDIRLMRRIRRDMQERDRSIEGILRQYERTVRPMHLEFVEPSK 185
Cdd:PRK05480  99 ETIRVEPKDVIILEGILLLEDERLRDLMDIKIFVDTPLDIRLIRRLKRDVNERGRSLESVINQYLSTVRPMHLQFIEPSK 178

                        170       180
                 ....*....|....*....|....*....
gi 499722569 186 READIIIPRGGHNEVAIQMVMSRIQELLR 214
Cdd:PRK05480 179 RYADIIIPEGGKNRVAIDILKAKIRQLLE 207
UMPK cd02023
Uridine monophosphate kinase (UMPK, EC 2.7.1.48), also known as uridine kinase or ...
 22-212 2.00e-85

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: 251.32  E-value: 2.00e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499722569  22 SGSGKTTVLNHILEEFGSDPIAILDHDAYYHDLSHLSREKRAQFNFDHPDALETSLMREHLDRLIEGEAIEKPVYDFTTH 101
Cdd:cd02023    8 SGSGKTTVAEEIIEQLGNPKVVIISQDSYYKDLSHEELEERKNNNYDHPDAFDFDLLISHLQDLKNGKSVEIPVYDFKTH 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499722569 102 TRREETETVEPRPVIIIEGILVLAESALEERMDIKIYVDAADDIRLMRRIRRDMQERDRSIEGILRQYERTVRPMHLEFV 181
Cdd:cd02023   88 SRLKETVTVYPADVIILEGILALYDKELRDLMDLKIFVDTDADVRLIRRIERDIVERGRDLESVINQYLKFVKPMHEQFI 167

                        170       180       190
                 ....*....|....*....|....*....|.
gi 499722569 182 EPSKREADIIIPRGGHNEVAIQMVMSRIQEL 212
Cdd:cd02023  168 EPTKRYADVIIPRGGDNHVAIDLIVQHIKSK 198
Udk COG0572
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway ...
 24-211 6.81e-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: 6.81e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499722569  24 SGKTTVLNHILEEFGSDPIAILDHDAYYHDLSHLSREKRAQFNFDHPDALETSLMREHLDRLIEGEAIEKPVYDFTTHTR 103
Cdd:COG0572   18 SGKTTFARRLAEQLGADKVVVISLDDYYKDREHLPLDERGKPNFDHPEAFDLDLLNEHLEPLKAGESVELPVYDFATGTR 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499722569 104 REETETVEPRPVIIIEGILVLAESALEERMDIKIYVDAADDIRLMRRIRRDMQERDRSIEGILRQYERTVRPMHLEFVEP 183
Cdd:COG0572   98 SGETVKVEPADVIIVEGIHALNDELLRDLLDLKIYVDADTDVRLIRRIVRDGEERGRTAESVIEQYWATVRPGHEQYIEP 177

                        170       180
                 ....*....|....*....|....*....
gi 499722569 184 SKREADIIIPRGG-HNEVAIQMVMSRIQE 211
Cdd:COG0572  178 TKEYADIVIPNGGpLNPVALDLLVARLLS 206
udk TIGR00235
uridine kinase; Model contains a number of longer eukaryotic proteins and starts bringing in ...
 8-214 9.61e-78

uridine kinase; Model contains a number of longer eukaryotic proteins and starts bringing in phosphoribulokinase hits at scores of 160 and below [Purines, pyrimidines, nucleosides, and nucleotides, Salvage of nucleosides and nucleotides]


Pssm-ID: 272977  Cd Length: 207  Bit Score: 232.28  E-value: 9.61e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499722569    8 MPMNPPVVIGIAGGSGSGKTTVLNHILEEFGSDPIAILDHDAYYHDLSHLSREKRAQFNFDHPDALETSLMREHLDRLIE 87
Cdd:TIGR00235   1 MDKPKGIIIGIGGGSGSGKTTVARKIYEQLGKLEIVIISQDNYYKDQSHLEMAERKKTNFDHPDAFDNDLLYEHLKNLKN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499722569   88 GEAIEKPVYDFTTHTRREETETVEPRPVIIIEGILVLAESALEERMDIKIYVDAADDIRLMRRIRRDMQERDRSIEGILR 167
Cdd:TIGR00235  81 GSPIDVPVYDYVNHTRPKETVHIEPKDVVILEGIMPLFDERLRDLMDLKIFVDTPLDIRLIRRIERDINERGRSLDSVID 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 499722569  168 QYERTVRPMHLEFVEPSKREADIIIPRGGHNEVAIQMVMSRIQELLR 214
Cdd:TIGR00235 161 QYRKTVRPMYEQFVEPTKQYADLIIPEGGRNEVAINVLDTKIKHLLE 207
PTZ00301 PTZ00301
uridine kinase; Provisional
 26-213 1.41e-43

uridine kinase; Provisional


Pssm-ID: 140322 [Multi-domain]  Cd Length: 210  Bit Score: 145.53  E-value: 1.41e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499722569  26 KTTVLNHILEEFGSDPIAILDHDAYYHDLSHLSREKRAQFNFDHPDALETSLMREHLDRLIEGEAIEKPVYDFTTHTRRE 105
Cdd:PTZ00301  20 STNIVSELMAHCGPVSIGVICEDFYYRDQSNIPESERAYTNYDHPKSLEHDLLTTHLRELKSGKTVQIPQYDYVHHTRSD 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499722569 106 ETETVEPRPVIIIEGILVLAESALEERMDIKIYVDAADDIRLMRRIRRDMQERDRSIEGILRQYERTVRPMHLEFVEPSK 185
Cdd:PTZ00301 100 TAVTMTPKSVLIVEGILLFTNAELRNEMDCLIFVDTPLDICLIRRAKRDMRERGRTFESVIEQYEATVRPMYYAYVEPSK 179

                        170       180
                 ....*....|....*....|....*...
gi 499722569 186 READIIIPRGGHNEVAIQMVMSRIQELL 213
Cdd:PTZ00301 180 VYADIIVPSWKDNSVAVGVLRAKLNHDL 207
PRK pfam00485
Phosphoribulokinase / Uridine kinase family; This family matches three types of P-loop ...
 26-201 6.05e-38

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: 130.60  E-value: 6.05e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499722569   26 KTTVLNHILEEFGSDP--------IAILDHDAYYHDLSHLSREKR--AQFNFDHPDALETSLMREHLDRLIEGEAIEKPV 95
Cdd:pfam00485  12 KTTVARRIVSIFGREGvpavgiegDSFHSTDRFYMDLHPEDRKRAgnNGYSFDGPEANDFDLLYEQFKELKEGGSVDKPI 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499722569   96 YDFTTHTRREETETVEPRPVIIIEGILVLAESALEERMDIKIYVDAADDIRLMRRIRRDMQERDRSIEGILRQYERtVRP 175
Cdd:pfam00485  92 YNHVTHERDPTPELIEGADVLVIEGLHALYDERVAQLLDLKIYVDPDIDLELARKIQRDMAERGHSLEGVTDSILF-RKP 170

                         170       180
                  ....*....|....*....|....*.
gi 499722569  176 MHLEFVEPSKREADIIIPRGGHNEVA 201
Cdd:pfam00485 171 DYVNYIDPQFSYADLIIQRVPTNDTA 196
PRK07429 PRK07429
phosphoribulokinase; Provisional
 26-192 8.45e-28

phosphoribulokinase; Provisional


Pssm-ID: 180975  Cd Length: 327  Bit Score: 107.40  E-value: 8.45e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499722569  26 KTTVLNHILEEFGSDPIAILDHDAYYHdlshLSREKRAQFNFD--HPDALETSLMREHLDRLIEGEAIEKPVYDFTTHTR 103
Cdd:PRK07429  21 KTTFLRGLADLLGEELVTVICTDDYHS----YDRKQRKELGITalDPRANNLDIMYEHLKALKTGQPILKPIYNHETGTF 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499722569 104 rEETETVEPRPVIIIEGILVLAESALEERMDIKIYVDAADDIRLMRRIRRDMQERDRSIEGILRQYERTvRPMHLEFVEP 183
Cdd:PRK07429  97 -DPPEYIEPNKIVVVEGLHPLYDERVRELYDFKVYLDPPEEVKIAWKIKRDMAKRGHTYEQVLAEIEAR-EPDFEAYIRP 174


                 ....*....
gi 499722569 184 SKREADIII 192
Cdd:PRK07429 175 QRQWADVVI 183
PRK cd02026
Phosphoribulokinase (PRK) is an enzyme involved in the Benson-Calvin cycle in chloroplasts or ...
 26-192 1.22e-27

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: 105.88  E-value: 1.22e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499722569  26 KTTVLNHILEEFGSDPIAILDHDAYYHdlshLSREKRAQFNFD--HPDALETSLMREHLDRLIEGEAIEKPVYDFTTHTR 103
Cdd:cd02026   12 KSTFLRRLTSLFGSDLVTVICLDDYHS----LDRKGRKETGITalDPRANNFDLMYEQLKALKEGQAIEKPIYNHVTGLI 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499722569 104 rEETETVEPRPVIIIEGILVLAESALEERMDIKIYVDAADDIRLMRRIRRDMQERDRSIEGILRQYERTvRPMHLEFVEP 183
Cdd:cd02026   88 -DPPELIKPTKIVVIEGLHPLYDERVRELLDFSVYLDISDEVKFAWKIQRDMAERGHSLEDVLASIEAR-KPDFEAYIDP 165


                 ....*....
gi 499722569 184 SKREADIII 192
Cdd:cd02026  166 QKQYADVVI 174
PLN02348 PLN02348
phosphoribulokinase
 51-192 1.62e-23

phosphoribulokinase


Pssm-ID: 215198  Cd Length: 395  Bit Score: 96.84  E-value: 1.62e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499722569  51 YHDLSHLSREKRAQFNFDhPDALETSLMREHLDRLIEGEAIEKPVYDFTTHTRrEETETVEPRPVIIIEGILVLAESALE 130
Cdd:PLN02348 103 YHSLDRTGRKEKGVTALD-PRANNFDLMYEQVKALKEGKAVEKPIYNHVTGLL-DPPELIEPPKILVIEGLHPMYDERVR 180

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499722569 131 ERMDIKIYVDAADDIRLMRRIRRDMQERDRSIEGILRQYErTVRPMHLEFVEPSKREADIII 192
Cdd:PLN02348 181 DLLDFSIYLDISDDVKFAWKIQRDMAERGHSLESIKASIE-ARKPDFDAYIDPQKQYADVVI 241
UMPK_like cd02028
Uridine monophosphate kinase_like (UMPK_like) is a family of proteins highly similar to the ...
 26-192 4.12e-17

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


Pssm-ID: 238986 [Multi-domain]  Cd Length: 179  Bit Score: 75.80  E-value: 4.12e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499722569  26 KTTV---LNHILEEFGSDPIAIlDHDAYYHDLShlsREKRAQFNFDHPDALETSLMREHLDRLIEGEAIEKPVYDFTTHT 102
Cdd:cd02028   12 KTTFakkLSNQLRVNGIGPVVI-SLDDYYVPRK---TPRDEDGNYDFESILDLDLLNKNLHDLLNGKEVELPIYDFRTGK 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499722569 103 RR-EETETVEPRPVIIIEGILVLAEsALEERMDIKIYVDAA-DDIRLMRRIRRDMQERDRSIEGILRQYerTVRPMHLEF 180
Cdd:cd02028   88 RRgYRKLKLPPSGVVILEGIYALNE-RLRSLLDIRVAVSGGvHLNRLLRRVVRDIQFRGYSAELTILMW--PSVPSGEEF 164

                        170
                 ....*....|..
gi 499722569 181 VEPSKREADIII 192
Cdd:cd02028  165 IIPPLQEAAIVM 176
PLN02318 PLN02318
phosphoribulokinase/uridine kinase
 66-192 9.43e-14

phosphoribulokinase/uridine kinase


Pssm-ID: 177952 [Multi-domain]  Cd Length: 656  Bit Score: 69.50  E-value: 9.43e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499722569  66 NFDHPDALETSLMREHLDRLIEGEAIEKPVYDFTTHTRR-EETETVEPRPVIIIEGILVLAESaLEERMDIKIYVDAADD 144
Cdd:PLN02318 110 NFDDPRLTDYDTLLDNIHDLKAGKSVQVPIYDFKSSSRVgYRTLEVPSSRIVIIEGIYALSEK-LRPLLDLRVSVTGGVH 188

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 499722569 145 IRLMRRIRRDMQERDRSIEGILRQYERTVRPMHLEFVEPSKREADIII 192
Cdd:PLN02318 189 FDLVKRVLRDIQRAGQEPEEIIHQISETVYPMYKAFIEPDLQTAHIKI 236
PRK08233 PRK08233
hypothetical protein; Provisional
 116-192 6.90e-05

hypothetical protein; Provisional


Pssm-ID: 181310 [Multi-domain]  Cd Length: 182  Bit Score: 42.04  E-value: 6.90e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499722569 116 IIIEGILVLAESALEERMDIKIYVDAADDIRLMRRIRRDMQERDRS-IEGILRQYERTVRPMHLEFVEPSKREADIII 192
Cdd:PRK08233  81 IIVDYPFAYLNSEMRQFIDVTIFIDTPLDIAMARRILRDFKEDTGNeIHNDLKHYLNYARPLYLEALHTVKPNADIVL 158
CoaE COG0237
Dephospho-CoA kinase [Coenzyme transport and metabolism]; Dephospho-CoA kinase is part of the ...
 26-154 5.66e-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: 36.58  E-value: 5.66e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499722569  26 KTTVLNhILEEFGsdpIAILDHDAYYHDLS-----------------------HLSREKRAQFNFDHPDALEtslmrehl 82
Cdd:COG0237   14 KSTVAR-MFAELG---APVIDADAIARELVepggpalaaiveafgeeildadgSLDRKALAEIVFADPEALK-------- 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499722569  83 dRLiegEAIekpvydftTH-----TRREETETVEPRPVIIIEGILvLAESALEERMDIKIYVDAADDIRLMRRIRRD 154
Cdd:COG0237   82 -KL---EAI--------VHplvreEIERRLAAARGAPYVVLDIPL-LFETGLEKLVDRVIVVDAPEEVQIERLMARD 145
 
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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