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Conserved domains on  [gi|544826489|ref|WP_021242480|]
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MULTISPECIES: type I pantothenate kinase [Enterobacteriaceae]

Protein Classification

nucleoside/nucleotide kinase family protein( domain architecture ID 106737)

nucleoside/nucleotide kinase family protein may catalyze the reversible phosphate group transfer from nucleoside triphosphates to nucleosides/nucleotides, nucleoside monophosphates, or sugars

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
NK super family cl17190
Nucleoside/nucleotide kinase (NK) is a protein superfamily consisting of multiple families of ...
 27-316 0e+00

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.


The actual alignment was detected with superfamily member TIGR00554:

Pssm-ID: 450170  Cd Length: 290  Bit Score: 567.32  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544826489   27 VPMTLTEGEIARLKGINEDLSLEEVAEIYLPLSRLLNFYISSNLRRQAVLEQFLGTNGQRIPYIISIAGSVAVGKSTTAR 106
Cdd:TIGR00554   1 VPLKLSEDDIAPLKGFNEDLSLDEVAEIYLPLSRLINFYIDENLHRQAVLEQFLGRNGAKIPYIISIAGSVAVGKSTSAR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544826489  107 VLQALLSRWPEHRSVELITTDGFLHPNEVLKERGLMKKKGFPLSYDMHRLVKFVSDLKSGVPHVTAPVYSHLIYDRIPGG 186
Cdd:TIGR00554  81 ILQALLSHWPEERKVDLITTDGFLHPLNKLKEDGLLKKKGFPESYDMHKLIKFLADLKSGKPNVTAPIYSHLIYDIIPDG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544826489  187 DKTVVQPDILILEGLNVLQSGMDYPHDPHHVFVSDFVDFSIYVDAPEDLLQNWYINRFLKFREGAFTDPDSYFHHYAQLS 266
Cdd:TIGR00554 161 DDTVDKPDILILEGLNVLQSGMDKPHDPDHTFVSDFVDFSIYVDAEEDLLKEWYIKRFLKFREGAFNDPDSYFHHYAKLS 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 544826489  267 EEEAINVATGLWNEINYVNLKENILPTRERASLILTKSEKHAVDQIRLRK 316
Cdd:TIGR00554 241 KEEAIATAMKIWDEINGLNLKQNILPTRERANLILKKGANHAVEEIKLRK 290
 
Name Accession Description Interval E-value
panK_bact TIGR00554
pantothenate kinase, bacterial type; Shown to be a homodimer in E. coli. This enzyme catalyzes ...
 27-316 0e+00

pantothenate kinase, bacterial type; Shown to be a homodimer in E. coli. This enzyme catalyzes the rate-limiting step in the biosynthesis of coenzyme A. It is very well conserved from E. coli to B. subtilis, but differs considerably from known eukaryotic forms, described in a separate model. [Biosynthesis of cofactors, prosthetic groups, and carriers, Pantothenate and coenzyme A]


Pssm-ID: 273134  Cd Length: 290  Bit Score: 567.32  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544826489   27 VPMTLTEGEIARLKGINEDLSLEEVAEIYLPLSRLLNFYISSNLRRQAVLEQFLGTNGQRIPYIISIAGSVAVGKSTTAR 106
Cdd:TIGR00554   1 VPLKLSEDDIAPLKGFNEDLSLDEVAEIYLPLSRLINFYIDENLHRQAVLEQFLGRNGAKIPYIISIAGSVAVGKSTSAR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544826489  107 VLQALLSRWPEHRSVELITTDGFLHPNEVLKERGLMKKKGFPLSYDMHRLVKFVSDLKSGVPHVTAPVYSHLIYDRIPGG 186
Cdd:TIGR00554  81 ILQALLSHWPEERKVDLITTDGFLHPLNKLKEDGLLKKKGFPESYDMHKLIKFLADLKSGKPNVTAPIYSHLIYDIIPDG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544826489  187 DKTVVQPDILILEGLNVLQSGMDYPHDPHHVFVSDFVDFSIYVDAPEDLLQNWYINRFLKFREGAFTDPDSYFHHYAQLS 266
Cdd:TIGR00554 161 DDTVDKPDILILEGLNVLQSGMDKPHDPDHTFVSDFVDFSIYVDAEEDLLKEWYIKRFLKFREGAFNDPDSYFHHYAKLS 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 544826489  267 EEEAINVATGLWNEINYVNLKENILPTRERASLILTKSEKHAVDQIRLRK 316
Cdd:TIGR00554 241 KEEAIATAMKIWDEINGLNLKQNILPTRERANLILKKGANHAVEEIKLRK 290
CoaA COG1072
Panthothenate kinase [Coenzyme transport and metabolism]; Panthothenate kinase is part of the ...
 1-316 0e+00

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: 525.63  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544826489   1 MSKKEQtlMTPYLHFNRSQWAALRDSVPMTLTEGEIARLKGINEDLSLEEVAEIYLPLSRLLNFYISSNLRRQAVLEQFL 80
Cdd:COG1072    1 MSDTDE--LSPYVEFSREEWAALRASTPLTLTEEELERLRGLNDPISLDEVEDIYLPLSRLLNLYVAATQRLHRATSAFL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544826489  81 GTNGQRIPYIISIAGSVAVGKSTTARVLQALLSRWPEHRSVELITTDGFLHPNEVLKERGLMKKKGFPLSYDMHRLVKFV 160
Cdd:COG1072   79 GQADKKTPFIIGIAGSVAVGKSTTARLLQALLSRWPEHPKVELVTTDGFLYPNAVLERRGLMDRKGFPESYDRRGLLRFL 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544826489 161 SDLKSGVPHVTAPVYSHLIYDRIPGGDKTVVQPDILILEGLNVLQSGMdyphdPHHVFVSDFVDFSIYVDAPEDLLQNWY 240
Cdd:COG1072  159 ARVKSGDPEVRAPVYSHLLYDIVPGAIVVVDQPDILIVEGNNVLQDEP-----NPWLFVSDFFDFSIYVDADEEDLREWY 233

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 544826489 241 INRFLKFREGAFTDPDSYFHHYAQLSEEEAINVATGLWNEINYVNLKENILPTRERASLILTKSEKHAVDQIRLRK 316
Cdd:COG1072  234 VERFLKLRETAFRDPDSYFHRYAGLSEEEARAWAEEIWREINLPNLAENILPTRSRADLILRKGADHSVERVRLRK 309
PanK cd02025
Pantothenate kinase (PanK) catalyzes the phosphorylation of pantothenic acid to form 4 ...
 90-314 7.78e-135

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: 381.27  E-value: 7.78e-135
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544826489  90 IISIAGSVAVGKSTTARVLQALLSRWPEHRSVELITTDGFLHPNEVLKERGLMKKKGFPLSYDMHRLVKFVSDLKSGVPH 169
Cdd:cd02025    1 IIGIAGSVAVGKSTTARVLQALLSRWPDHPNVELITTDGFLYPNKELIERGLMDRKGFPESYDMEALLKFLKDIKSGKKN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544826489 170 VTAPVYSHLIYDRIPGGDKTVVQPDILILEGLNVLQSGMDYphdphHVFVSDFVDFSIYVDAPEDLLQNWYINRFLKFRE 249
Cdd:cd02025   81 VKIPVYSHLTYDVIPGEKQTVDQPDILIIEGLNVLQTGQNP-----RLFVSDFFDFSIYVDADEDDIEKWYIKRFLKLRE 155

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 544826489 250 GAFTDPDSYFHHYAQLSEEEAINVATGLWNEINYVNLKENILPTRERASLILTKSEKHAVDQIRL 314
Cdd:cd02025  156 TAFSDPDSYFHRYAKMSEEEAIAFAREVWKNINLKNLRENILPTRNRADLILEKGADHSIEEVYL 220
PRK09270 PRK09270
nucleoside triphosphate hydrolase domain-containing protein; Reviewed
 89-301 3.99e-21

nucleoside triphosphate hydrolase domain-containing protein; Reviewed


Pssm-ID: 236442  Cd Length: 229  Bit Score: 89.61  E-value: 3.99e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544826489  89 YIISIAGSVAVGKSTTARVLQALLSRWPEHRSVELiTTDGFLHPNEVLKERGLMKKKGFPLSYDMHRLVKFVSDLKSGVP 168
Cdd:PRK09270  34 TIVGIAGPPGAGKSTLAEFLEALLQQDGELPAIQV-PMDGFHLDNAVLDAHGLRPRKGAPETFDVAGLAALLRRLRAGDD 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544826489 169 HVTAPVyshliYDR---IPGGDKTVVQPD--ILILEGlNVLQSGmDYPHDPhhvfVSDFVDFSIYVDAPEDLLQNWYINR 243
Cdd:PRK09270 113 EVYWPV-----FDRsleDPVADAIVVPPTarLVIVEG-NYLLLD-EEPWRR----LAGLFDFTIFLDAPAEVLRERLVAR 181

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 544826489 244 FLKFRegaftdpdsyfhhyaqLSEEEAINVATGlwNEINYVNLkenILPTRERASLIL 301
Cdd:PRK09270 182 KLAGG----------------LSPEAAEAFVLR--NDGPNARL---VLETSRPADLVL 218
PRK pfam00485
Phosphoribulokinase / Uridine kinase family; This family matches three types of P-loop ...
 90-248 1.47e-11

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: 62.41  E-value: 1.47e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544826489   90 IISIAGSVAVGKSTTARVLQALLSRWPEHRS----VELITTDGFLHPNEVLKERGlMKKKGF----PLSYDMHRLVKFVS 161
Cdd:pfam00485   1 VIGVAGSSGSGKTTVARRIVSIFGREGVPAVgiegDSFHSTDRFYMDLHPEDRKR-AGNNGYsfdgPEANDFDLLYEQFK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544826489  162 DLKSGVpHVTAPVYSHLIYDRIPGGDKtVVQPDILILEGLnvlqsgmdypHDPHHVFVSDFVDFSIYVDAPEDLLQNWYI 241
Cdd:pfam00485  80 ELKEGG-SVDKPIYNHVTHERDPTPEL-IEGADVLVIEGL----------HALYDERVAQLLDLKIYVDPDIDLELARKI 147


                  ....*..
gi 544826489  242 NRFLKFR 248
Cdd:pfam00485 148 QRDMAER 154
 
Name Accession Description Interval E-value
panK_bact TIGR00554
pantothenate kinase, bacterial type; Shown to be a homodimer in E. coli. This enzyme catalyzes ...
 27-316 0e+00

pantothenate kinase, bacterial type; Shown to be a homodimer in E. coli. This enzyme catalyzes the rate-limiting step in the biosynthesis of coenzyme A. It is very well conserved from E. coli to B. subtilis, but differs considerably from known eukaryotic forms, described in a separate model. [Biosynthesis of cofactors, prosthetic groups, and carriers, Pantothenate and coenzyme A]


Pssm-ID: 273134  Cd Length: 290  Bit Score: 567.32  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544826489   27 VPMTLTEGEIARLKGINEDLSLEEVAEIYLPLSRLLNFYISSNLRRQAVLEQFLGTNGQRIPYIISIAGSVAVGKSTTAR 106
Cdd:TIGR00554   1 VPLKLSEDDIAPLKGFNEDLSLDEVAEIYLPLSRLINFYIDENLHRQAVLEQFLGRNGAKIPYIISIAGSVAVGKSTSAR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544826489  107 VLQALLSRWPEHRSVELITTDGFLHPNEVLKERGLMKKKGFPLSYDMHRLVKFVSDLKSGVPHVTAPVYSHLIYDRIPGG 186
Cdd:TIGR00554  81 ILQALLSHWPEERKVDLITTDGFLHPLNKLKEDGLLKKKGFPESYDMHKLIKFLADLKSGKPNVTAPIYSHLIYDIIPDG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544826489  187 DKTVVQPDILILEGLNVLQSGMDYPHDPHHVFVSDFVDFSIYVDAPEDLLQNWYINRFLKFREGAFTDPDSYFHHYAQLS 266
Cdd:TIGR00554 161 DDTVDKPDILILEGLNVLQSGMDKPHDPDHTFVSDFVDFSIYVDAEEDLLKEWYIKRFLKFREGAFNDPDSYFHHYAKLS 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 544826489  267 EEEAINVATGLWNEINYVNLKENILPTRERASLILTKSEKHAVDQIRLRK 316
Cdd:TIGR00554 241 KEEAIATAMKIWDEINGLNLKQNILPTRERANLILKKGANHAVEEIKLRK 290
CoaA COG1072
Panthothenate kinase [Coenzyme transport and metabolism]; Panthothenate kinase is part of the ...
 1-316 0e+00

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: 525.63  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544826489   1 MSKKEQtlMTPYLHFNRSQWAALRDSVPMTLTEGEIARLKGINEDLSLEEVAEIYLPLSRLLNFYISSNLRRQAVLEQFL 80
Cdd:COG1072    1 MSDTDE--LSPYVEFSREEWAALRASTPLTLTEEELERLRGLNDPISLDEVEDIYLPLSRLLNLYVAATQRLHRATSAFL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544826489  81 GTNGQRIPYIISIAGSVAVGKSTTARVLQALLSRWPEHRSVELITTDGFLHPNEVLKERGLMKKKGFPLSYDMHRLVKFV 160
Cdd:COG1072   79 GQADKKTPFIIGIAGSVAVGKSTTARLLQALLSRWPEHPKVELVTTDGFLYPNAVLERRGLMDRKGFPESYDRRGLLRFL 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544826489 161 SDLKSGVPHVTAPVYSHLIYDRIPGGDKTVVQPDILILEGLNVLQSGMdyphdPHHVFVSDFVDFSIYVDAPEDLLQNWY 240
Cdd:COG1072  159 ARVKSGDPEVRAPVYSHLLYDIVPGAIVVVDQPDILIVEGNNVLQDEP-----NPWLFVSDFFDFSIYVDADEEDLREWY 233

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 544826489 241 INRFLKFREGAFTDPDSYFHHYAQLSEEEAINVATGLWNEINYVNLKENILPTRERASLILTKSEKHAVDQIRLRK 316
Cdd:COG1072  234 VERFLKLRETAFRDPDSYFHRYAGLSEEEARAWAEEIWREINLPNLAENILPTRSRADLILRKGADHSVERVRLRK 309
PanK cd02025
Pantothenate kinase (PanK) catalyzes the phosphorylation of pantothenic acid to form 4 ...
 90-314 7.78e-135

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: 381.27  E-value: 7.78e-135
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544826489  90 IISIAGSVAVGKSTTARVLQALLSRWPEHRSVELITTDGFLHPNEVLKERGLMKKKGFPLSYDMHRLVKFVSDLKSGVPH 169
Cdd:cd02025    1 IIGIAGSVAVGKSTTARVLQALLSRWPDHPNVELITTDGFLYPNKELIERGLMDRKGFPESYDMEALLKFLKDIKSGKKN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544826489 170 VTAPVYSHLIYDRIPGGDKTVVQPDILILEGLNVLQSGMDYphdphHVFVSDFVDFSIYVDAPEDLLQNWYINRFLKFRE 249
Cdd:cd02025   81 VKIPVYSHLTYDVIPGEKQTVDQPDILIIEGLNVLQTGQNP-----RLFVSDFFDFSIYVDADEDDIEKWYIKRFLKLRE 155

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 544826489 250 GAFTDPDSYFHHYAQLSEEEAINVATGLWNEINYVNLKENILPTRERASLILTKSEKHAVDQIRL 314
Cdd:cd02025  156 TAFSDPDSYFHRYAKMSEEEAIAFAREVWKNINLKNLRENILPTRNRADLILEKGADHSIEEVYL 220
PRK09270 PRK09270
nucleoside triphosphate hydrolase domain-containing protein; Reviewed
 89-301 3.99e-21

nucleoside triphosphate hydrolase domain-containing protein; Reviewed


Pssm-ID: 236442  Cd Length: 229  Bit Score: 89.61  E-value: 3.99e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544826489  89 YIISIAGSVAVGKSTTARVLQALLSRWPEHRSVELiTTDGFLHPNEVLKERGLMKKKGFPLSYDMHRLVKFVSDLKSGVP 168
Cdd:PRK09270  34 TIVGIAGPPGAGKSTLAEFLEALLQQDGELPAIQV-PMDGFHLDNAVLDAHGLRPRKGAPETFDVAGLAALLRRLRAGDD 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544826489 169 HVTAPVyshliYDR---IPGGDKTVVQPD--ILILEGlNVLQSGmDYPHDPhhvfVSDFVDFSIYVDAPEDLLQNWYINR 243
Cdd:PRK09270 113 EVYWPV-----FDRsleDPVADAIVVPPTarLVIVEG-NYLLLD-EEPWRR----LAGLFDFTIFLDAPAEVLRERLVAR 181

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 544826489 244 FLKFRegaftdpdsyfhhyaqLSEEEAINVATGlwNEINYVNLkenILPTRERASLIL 301
Cdd:PRK09270 182 KLAGG----------------LSPEAAEAFVLR--NDGPNARL---VLETSRPADLVL 218
Udk COG0572
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway ...
 88-314 3.51e-18

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: 81.04  E-value: 3.51e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544826489  88 PYIISIAGSVAVGKSTTARVLQALLSRwpehRSVELITTDGFLHPNEVLK--ERGlmkKKGF--PLSYDMHRLVKFVSDL 163
Cdd:COG0572    7 PRIIGIAGPSGSGKTTFARRLAEQLGA----DKVVVISLDDYYKDREHLPldERG---KPNFdhPEAFDLDLLNEHLEPL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544826489 164 KSGVPhVTAPVYSHLIYDRIpgGDKTVVQP-DILILEGLNVLqsgmdypHDPhhvFVSDFVDFSIYVDAPEDLLQNWYIN 242
Cdd:COG0572   80 KAGES-VELPVYDFATGTRS--GETVKVEPaDVIIVEGIHAL-------NDE---LLRDLLDLKIYVDADTDVRLIRRIV 146

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 544826489 243 RFLKFREGAFTDP-DSYFHHYaqlseEEAinvatglwneinyvnLKENILPTRERASLILTKSEKHAVDQIRL 314
Cdd:COG0572  147 RDGEERGRTAESViEQYWATV-----RPG---------------HEQYIEPTKEYADIVIPNGGPLNPVALDL 199
UMPK cd02023
Uridine monophosphate kinase (UMPK, EC 2.7.1.48), also known as uridine kinase or ...
 90-235 3.51e-12

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: 64.11  E-value: 3.51e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544826489  90 IISIAGSVAVGKSTTARVLQALLsrwpEHRSVELITTDGFLHPN--EVLKERglmkKKG---FPLSYDMHRLVKFVSDLK 164
Cdd:cd02023    1 IIGIAGGSGSGKTTVAEEIIEQL----GNPKVVIISQDSYYKDLshEELEER----KNNnydHPDAFDFDLLISHLQDLK 72

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 544826489 165 SGVPhVTAPVYSHLIYDRIPggDKTVVQP-DILILEGLNVLqsgmdypHDPHhvfVSDFVDFSIYVDAPEDL 235
Cdd:cd02023   73 NGKS-VEIPVYDFKTHSRLK--ETVTVYPaDVIILEGILAL-------YDKE---LRDLMDLKIFVDTDADV 131
PRK pfam00485
Phosphoribulokinase / Uridine kinase family; This family matches three types of P-loop ...
 90-248 1.47e-11

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: 62.41  E-value: 1.47e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544826489   90 IISIAGSVAVGKSTTARVLQALLSRWPEHRS----VELITTDGFLHPNEVLKERGlMKKKGF----PLSYDMHRLVKFVS 161
Cdd:pfam00485   1 VIGVAGSSGSGKTTVARRIVSIFGREGVPAVgiegDSFHSTDRFYMDLHPEDRKR-AGNNGYsfdgPEANDFDLLYEQFK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544826489  162 DLKSGVpHVTAPVYSHLIYDRIPGGDKtVVQPDILILEGLnvlqsgmdypHDPHHVFVSDFVDFSIYVDAPEDLLQNWYI 241
Cdd:pfam00485  80 ELKEGG-SVDKPIYNHVTHERDPTPEL-IEGADVLVIEGL----------HALYDERVAQLLDLKIYVDPDIDLELARKI 147


                  ....*..
gi 544826489  242 NRFLKFR 248
Cdd:pfam00485 148 QRDMAER 154
PRK05480 PRK05480
uridine/cytidine kinase; Provisional
 88-235 5.25e-11

uridine/cytidine kinase; Provisional


Pssm-ID: 235492 [Multi-domain]  Cd Length: 209  Bit Score: 60.94  E-value: 5.25e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544826489  88 PYIISIAGSVAVGKSTTARVLQALLsrwPEHrSVELITTDGFLHPNEVL--KERglmKKKGF--PLSYDMHRLVKFVSDL 163
Cdd:PRK05480   6 PIIIGIAGGSGSGKTTVASTIYEEL---GDE-SIAVIPQDSYYKDQSHLsfEER---VKTNYdhPDAFDHDLLIEHLKAL 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 544826489 164 KSGVPhVTAPVYSHLIYDRIpggDKTV-VQP-DILILEGLNVLqsgmdypHDPHhvfVSDFVDFSIYVDAPEDL 235
Cdd:PRK05480  79 KAGKA-IEIPVYDYTEHTRS---KETIrVEPkDVIILEGILLL-------EDER---LRDLMDIKIFVDTPLDI 138
PRK cd02026
Phosphoribulokinase (PRK) is an enzyme involved in the Benson-Calvin cycle in chloroplasts or ...
 90-248 5.49e-08

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: 53.11  E-value: 5.49e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544826489  90 IISIAGSVAVGKSTTARVLQALLSrwPEhrSVELITTDGFlHPNEvLKERglmKKKGF----PLSYDMHRLVKFVSDLKS 165
Cdd:cd02026    1 IIGVAGDSGCGKSTFLRRLTSLFG--SD--LVTVICLDDY-HSLD-RKGR---KETGItaldPRANNFDLMYEQLKALKE 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544826489 166 GVPhVTAPVYSHLIydRIPGGDKTVVQPDILILEGLNVLqsgmdYPHDphhvfVSDFVDFSIYVDAPEDLLQNWYINRFL 245
Cdd:cd02026   72 GQA-IEKPIYNHVT--GLIDPPELIKPTKIVVIEGLHPL-----YDER-----VRELLDFSVYLDISDEVKFAWKIQRDM 138


                 ...
gi 544826489 246 KFR 248
Cdd:cd02026  139 AER 141
PRK07429 PRK07429
phosphoribulokinase; Provisional
 88-243 1.35e-07

phosphoribulokinase; Provisional


Pssm-ID: 180975  Cd Length: 327  Bit Score: 52.32  E-value: 1.35e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544826489  88 PYIISIAGSVAVGKSTTARVLQALLSrwPEHRSVelITTDGFlHpNEVLKERglmKKKGF----PLSYDMHRLVKFVSDL 163
Cdd:PRK07429   8 PVLLGVAGDSGCGKTTFLRGLADLLG--EELVTV--ICTDDY-H-SYDRKQR---KELGItaldPRANNLDIMYEHLKAL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544826489 164 KSGVPhVTAPVYSHliydripgGDKTVVQP------DILILEGLNVLqsgmdypHDPHhvfVSDFVDFSIYVDAPEDLLQ 237
Cdd:PRK07429  79 KTGQP-ILKPIYNH--------ETGTFDPPeyiepnKIVVVEGLHPL-------YDER---VRELYDFKVYLDPPEEVKI 139


                 ....*.
gi 544826489 238 NWYINR 243
Cdd:PRK07429 140 AWKIKR 145
PLN02348 PLN02348
phosphoribulokinase
 88-243 5.49e-06

phosphoribulokinase


Pssm-ID: 215198  Cd Length: 395  Bit Score: 47.53  E-value: 5.49e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544826489  88 PYIISIAGSVAVGKSTTARVLQALLS---------RWPEHRSVELITT-----DGFLHPNEVLKERGLM----KKKGFPL 149
Cdd:PLN02348  49 TVVIGLAADSGCGKSTFMRRLTSVFGgaakppkggNPDSNTLISDTTTvicldDYHSLDRTGRKEKGVTaldpRANNFDL 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544826489 150 SYDMhrlvkfVSDLKSGVPhVTAPVYSHL--IYDripgGDKTVVQPDILILEGLnvlqsgmdypHDPHHVFVSDFVDFSI 227
Cdd:PLN02348 129 MYEQ------VKALKEGKA-VEKPIYNHVtgLLD----PPELIEPPKILVIEGL----------HPMYDERVRDLLDFSI 187

                        170
                 ....*....|....*.
gi 544826489 228 YVDAPEDLLQNWYINR 243
Cdd:PLN02348 188 YLDISDDVKFAWKIQR 203
PRK06696 PRK06696
uridine kinase; Validated
 74-234 2.10e-05

uridine kinase; Validated


Pssm-ID: 180660  Cd Length: 223  Bit Score: 44.97  E-value: 2.10e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544826489  74 AVLEQFLGTNGQRiPYIISIAGSVAVGKSTTARVLQALLSRWpeHRSVELITTDGFLHPNEVLKERGLMKKKGF------ 147
Cdd:PRK06696   9 ELAEHILTLNLTR-PLRVAIDGITASGKTTFADELAEEIKKR--GRPVIRASIDDFHNPRVIRYRRGRESAEGYyedayd 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544826489 148 ----------PLSYDMHRLVKFVS-DLKSGVPHVTAPVyshliydripggdktVVQPD-ILILEGLnvlqsgmdYPHDPH 215
Cdd:PRK06696  86 ytalrrllldPLGPNGDRQYRTAShDLKTDIPVHNPPL---------------LAAPNaVLIVDGT--------FLLRPE 142

                        170
                 ....*....|....*....
gi 544826489 216 hvfVSDFVDFSIYVDAPED 234
Cdd:PRK06696 143 ---LRDLWDYKIFLDTDFE 158
NK cd02019
Nucleoside/nucleotide kinase (NK) is a protein superfamily consisting of multiple families of ...
 90-126 1.39e-04

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: 39.63  E-value: 1.39e-04
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 544826489  90 IISIAGSVAVGKSTTARVLQALLsrwpEHRSVELITT 126
Cdd:cd02019    1 IIAITGGSGSGKSTVAKKLAEQL----GGRSVVVLDE 33
UMPK_like cd02028
Uridine monophosphate kinase_like (UMPK_like) is a family of proteins highly similar to the ...
 90-232 4.66e-03

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: 37.28  E-value: 4.66e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544826489  90 IISIAGSVAVGKSTTARVLQALLSrwPEHRSVELITTDGFLHPNEVlkERGLMKKKGFPLSYDMHRLVKFVSDLKSGVPh 169
Cdd:cd02028    1 VVGIAGPSGSGKTTFAKKLSNQLR--VNGIGPVVISLDDYYVPRKT--PRDEDGNYDFESILDLDLLNKNLHDLLNGKE- 75

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 544826489 170 VTAPVYSHLIYDRIpgGDKTVVQP--DILILEGLnvlqsgmdypHDPHHVfVSDFVDFSIYVDAP 232
Cdd:cd02028   76 VELPIYDFRTGKRR--GYRKLKLPpsGVVILEGI----------YALNER-LRSLLDIRVAVSGG 127
 
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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