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Conserved domains on  [gi|696365843|ref|WP_032940924|]
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MULTISPECIES: type I pantothenate kinase [Citrobacter]

Protein Classification

type I pantothenate kinase( domain architecture ID 10794612)

type I pantothenate kinase catalyzes the phosphorylation of (R)-pantothenate to form (R)-4'-phosphopantothenate, the first of five steps in coenzyme A biosynthesis

Graphical summary

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List of domain hits

 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: 589.66  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696365843   27 VPMTLTEEEIARLKGINEDLSLEEVAEIYLPLSRLLNFYISSNLRRQAVLEQFLGTNGERIPYIISIAGSVAVGKSTTAR 106
Cdd:TIGR00554   1 VPLKLSEDDIAPLKGFNEDLSLDEVAEIYLPLSRLINFYIDENLHRQAVLEQFLGRNGAKIPYIISIAGSVAVGKSTSAR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696365843  107 VLQALLSRWPEHRKVELITTDGFLHPNQVLKDRGLMKKKGFPQSYDMHRLVKFVSDLKSGVPNVTAPVYSHLIYDVIPDG 186
Cdd:TIGR00554  81 ILQALLSHWPEERKVDLITTDGFLHPLNKLKEDGLLKKKGFPESYDMHKLIKFLADLKSGKPNVTAPIYSHLIYDIIPDG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696365843  187 DKTVAQPDILILEGLNVLQSGMDYPHDPHHVFVSDFVDFSIYVDAPEELLQTWYINRFLKFREGAFTNPDSYFHNYAKLS 266
Cdd:TIGR00554 161 DDTVDKPDILILEGLNVLQSGMDKPHDPDHTFVSDFVDFSIYVDAEEDLLKEWYIKRFLKFREGAFNDPDSYFHHYAKLS 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 696365843  267 EDEAINTATSLWKEINWLNLKQNILPTRERASLIMTKSANHAVEEVRLRK 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: 589.66  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696365843   27 VPMTLTEEEIARLKGINEDLSLEEVAEIYLPLSRLLNFYISSNLRRQAVLEQFLGTNGERIPYIISIAGSVAVGKSTTAR 106
Cdd:TIGR00554   1 VPLKLSEDDIAPLKGFNEDLSLDEVAEIYLPLSRLINFYIDENLHRQAVLEQFLGRNGAKIPYIISIAGSVAVGKSTSAR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696365843  107 VLQALLSRWPEHRKVELITTDGFLHPNQVLKDRGLMKKKGFPQSYDMHRLVKFVSDLKSGVPNVTAPVYSHLIYDVIPDG 186
Cdd:TIGR00554  81 ILQALLSHWPEERKVDLITTDGFLHPLNKLKEDGLLKKKGFPESYDMHKLIKFLADLKSGKPNVTAPIYSHLIYDIIPDG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696365843  187 DKTVAQPDILILEGLNVLQSGMDYPHDPHHVFVSDFVDFSIYVDAPEELLQTWYINRFLKFREGAFTNPDSYFHNYAKLS 266
Cdd:TIGR00554 161 DDTVDKPDILILEGLNVLQSGMDKPHDPDHTFVSDFVDFSIYVDAEEDLLKEWYIKRFLKFREGAFNDPDSYFHHYAKLS 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 696365843  267 EDEAINTATSLWKEINWLNLKQNILPTRERASLIMTKSANHAVEEVRLRK 316
Cdd:TIGR00554 241 KEEAIATAMKIWDEINGLNLKQNILPTRERANLILKKGANHAVEEIKLRK 290
CoaA COG1072
Panthothenate kinase [Coenzyme transport and metabolism]; Panthothenate kinase is part of the ...
 10-316 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: 531.02  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696365843  10 SPYLQFDRNQWAALRDSVPMTLTEEEIARLKGINEDLSLEEVAEIYLPLSRLLNFYISSNLRRQAVLEQFLGTNGERIPY 89
Cdd:COG1072    8 SPYVEFSREEWAALRASTPLTLTEEELERLRGLNDPISLDEVEDIYLPLSRLLNLYVAATQRLHRATSAFLGQADKKTPF 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696365843  90 IISIAGSVAVGKSTTARVLQALLSRWPEHRKVELITTDGFLHPNQVLKDRGLMKKKGFPQSYDMHRLVKFVSDLKSGVPN 169
Cdd:COG1072   88 IIGIAGSVAVGKSTTARLLQALLSRWPEHPKVELVTTDGFLYPNAVLERRGLMDRKGFPESYDRRGLLRFLARVKSGDPE 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696365843 170 VTAPVYSHLIYDVIPDGDKTVAQPDILILEGLNVLQSGMdyphdPHHVFVSDFVDFSIYVDAPEELLQTWYINRFLKFRE 249
Cdd:COG1072  168 VRAPVYSHLLYDIVPGAIVVVDQPDILIVEGNNVLQDEP-----NPWLFVSDFFDFSIYVDADEEDLREWYVERFLKLRE 242

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 696365843 250 GAFTNPDSYFHNYAKLSEDEAINTATSLWKEINWLNLKQNILPTRERASLIMTKSANHAVEEVRLRK 316
Cdd:COG1072  243 TAFRDPDSYFHRYAGLSEEEARAWAEEIWREINLPNLAENILPTRSRADLILRKGADHSVERVRLRK 309
PanK cd02025
Pantothenate kinase (PanK) catalyzes the phosphorylation of pantothenic acid to form 4 ...
 90-314 1.65e-136

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: 385.51  E-value: 1.65e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696365843  90 IISIAGSVAVGKSTTARVLQALLSRWPEHRKVELITTDGFLHPNQVLKDRGLMKKKGFPQSYDMHRLVKFVSDLKSGVPN 169
Cdd:cd02025    1 IIGIAGSVAVGKSTTARVLQALLSRWPDHPNVELITTDGFLYPNKELIERGLMDRKGFPESYDMEALLKFLKDIKSGKKN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696365843 170 VTAPVYSHLIYDVIPDGDKTVAQPDILILEGLNVLQSGMDYphdphHVFVSDFVDFSIYVDAPEELLQTWYINRFLKFRE 249
Cdd:cd02025   81 VKIPVYSHLTYDVIPGEKQTVDQPDILIIEGLNVLQTGQNP-----RLFVSDFFDFSIYVDADEDDIEKWYIKRFLKLRE 155

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 696365843 250 GAFTNPDSYFHNYAKLSEDEAINTATSLWKEINWLNLKQNILPTRERASLIMTKSANHAVEEVRL 314
Cdd:cd02025  156 TAFSDPDSYFHRYAKMSEEEAIAFAREVWKNINLKNLRENILPTRNRADLILEKGADHSIEEVYL 220
PRK09270 PRK09270
nucleoside triphosphate hydrolase domain-containing protein; Reviewed
 70-251 1.83e-20

nucleoside triphosphate hydrolase domain-containing protein; Reviewed


Pssm-ID: 236442  Cd Length: 229  Bit Score: 88.07  E-value: 1.83e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696365843  70 LRRQAVLEQflgTNGERipYIISIAGSVAVGKSTTARVLQALLSRWPEHRKVELiTTDGFLHPNQVLKDRGLMKKKGFPQ 149
Cdd:PRK09270  20 LRRLAALQA---EPQRR--TIVGIAGPPGAGKSTLAEFLEALLQQDGELPAIQV-PMDGFHLDNAVLDAHGLRPRKGAPE 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696365843 150 SYDMHRLVKFVSDLKSGVPNVTAPVYSHLIYDVIPDGDKTVAQPDILILEGlNVLQSGmDYPHDPhhvfVSDFVDFSIYV 229
Cdd:PRK09270  94 TFDVAGLAALLRRLRAGDDEVYWPVFDRSLEDPVADAIVVPPTARLVIVEG-NYLLLD-EEPWRR----LAGLFDFTIFL 167

                        170       180
                 ....*....|....*....|....*
gi 696365843 230 DAPEELLQTWYINRFLKF---REGA 251
Cdd:PRK09270 168 DAPAEVLRERLVARKLAGglsPEAA 192
PRK pfam00485
Phosphoribulokinase / Uridine kinase family; This family matches three types of P-loop ...
 90-248 1.35e-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: 1.35e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696365843   90 IISIAGSVAVGKSTTARVLQALLSRWPEHRK----VELITTDGFLHPNQVLKDRGlMKKKGF----PQSYDMHRLVKFVS 161
Cdd:pfam00485   1 VIGVAGSSGSGKTTVARRIVSIFGREGVPAVgiegDSFHSTDRFYMDLHPEDRKR-AGNNGYsfdgPEANDFDLLYEQFK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696365843  162 DLKSGVpNVTAPVYSHLIYDVIPDGDKtVAQPDILILEGLnvlqsgmdypHDPHHVFVSDFVDFSIYVDAPEELLQTWYI 241
Cdd:pfam00485  80 ELKEGG-SVDKPIYNHVTHERDPTPEL-IEGADVLVIEGL----------HALYDERVAQLLDLKIYVDPDIDLELARKI 147


                  ....*..
gi 696365843  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: 589.66  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696365843   27 VPMTLTEEEIARLKGINEDLSLEEVAEIYLPLSRLLNFYISSNLRRQAVLEQFLGTNGERIPYIISIAGSVAVGKSTTAR 106
Cdd:TIGR00554   1 VPLKLSEDDIAPLKGFNEDLSLDEVAEIYLPLSRLINFYIDENLHRQAVLEQFLGRNGAKIPYIISIAGSVAVGKSTSAR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696365843  107 VLQALLSRWPEHRKVELITTDGFLHPNQVLKDRGLMKKKGFPQSYDMHRLVKFVSDLKSGVPNVTAPVYSHLIYDVIPDG 186
Cdd:TIGR00554  81 ILQALLSHWPEERKVDLITTDGFLHPLNKLKEDGLLKKKGFPESYDMHKLIKFLADLKSGKPNVTAPIYSHLIYDIIPDG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696365843  187 DKTVAQPDILILEGLNVLQSGMDYPHDPHHVFVSDFVDFSIYVDAPEELLQTWYINRFLKFREGAFTNPDSYFHNYAKLS 266
Cdd:TIGR00554 161 DDTVDKPDILILEGLNVLQSGMDKPHDPDHTFVSDFVDFSIYVDAEEDLLKEWYIKRFLKFREGAFNDPDSYFHHYAKLS 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 696365843  267 EDEAINTATSLWKEINWLNLKQNILPTRERASLIMTKSANHAVEEVRLRK 316
Cdd:TIGR00554 241 KEEAIATAMKIWDEINGLNLKQNILPTRERANLILKKGANHAVEEIKLRK 290
CoaA COG1072
Panthothenate kinase [Coenzyme transport and metabolism]; Panthothenate kinase is part of the ...
 10-316 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: 531.02  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696365843  10 SPYLQFDRNQWAALRDSVPMTLTEEEIARLKGINEDLSLEEVAEIYLPLSRLLNFYISSNLRRQAVLEQFLGTNGERIPY 89
Cdd:COG1072    8 SPYVEFSREEWAALRASTPLTLTEEELERLRGLNDPISLDEVEDIYLPLSRLLNLYVAATQRLHRATSAFLGQADKKTPF 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696365843  90 IISIAGSVAVGKSTTARVLQALLSRWPEHRKVELITTDGFLHPNQVLKDRGLMKKKGFPQSYDMHRLVKFVSDLKSGVPN 169
Cdd:COG1072   88 IIGIAGSVAVGKSTTARLLQALLSRWPEHPKVELVTTDGFLYPNAVLERRGLMDRKGFPESYDRRGLLRFLARVKSGDPE 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696365843 170 VTAPVYSHLIYDVIPDGDKTVAQPDILILEGLNVLQSGMdyphdPHHVFVSDFVDFSIYVDAPEELLQTWYINRFLKFRE 249
Cdd:COG1072  168 VRAPVYSHLLYDIVPGAIVVVDQPDILIVEGNNVLQDEP-----NPWLFVSDFFDFSIYVDADEEDLREWYVERFLKLRE 242

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 696365843 250 GAFTNPDSYFHNYAKLSEDEAINTATSLWKEINWLNLKQNILPTRERASLIMTKSANHAVEEVRLRK 316
Cdd:COG1072  243 TAFRDPDSYFHRYAGLSEEEARAWAEEIWREINLPNLAENILPTRSRADLILRKGADHSVERVRLRK 309
PanK cd02025
Pantothenate kinase (PanK) catalyzes the phosphorylation of pantothenic acid to form 4 ...
 90-314 1.65e-136

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: 385.51  E-value: 1.65e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696365843  90 IISIAGSVAVGKSTTARVLQALLSRWPEHRKVELITTDGFLHPNQVLKDRGLMKKKGFPQSYDMHRLVKFVSDLKSGVPN 169
Cdd:cd02025    1 IIGIAGSVAVGKSTTARVLQALLSRWPDHPNVELITTDGFLYPNKELIERGLMDRKGFPESYDMEALLKFLKDIKSGKKN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696365843 170 VTAPVYSHLIYDVIPDGDKTVAQPDILILEGLNVLQSGMDYphdphHVFVSDFVDFSIYVDAPEELLQTWYINRFLKFRE 249
Cdd:cd02025   81 VKIPVYSHLTYDVIPGEKQTVDQPDILIIEGLNVLQTGQNP-----RLFVSDFFDFSIYVDADEDDIEKWYIKRFLKLRE 155

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 696365843 250 GAFTNPDSYFHNYAKLSEDEAINTATSLWKEINWLNLKQNILPTRERASLIMTKSANHAVEEVRL 314
Cdd:cd02025  156 TAFSDPDSYFHRYAKMSEEEAIAFAREVWKNINLKNLRENILPTRNRADLILEKGADHSIEEVYL 220
PRK09270 PRK09270
nucleoside triphosphate hydrolase domain-containing protein; Reviewed
 70-251 1.83e-20

nucleoside triphosphate hydrolase domain-containing protein; Reviewed


Pssm-ID: 236442  Cd Length: 229  Bit Score: 88.07  E-value: 1.83e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696365843  70 LRRQAVLEQflgTNGERipYIISIAGSVAVGKSTTARVLQALLSRWPEHRKVELiTTDGFLHPNQVLKDRGLMKKKGFPQ 149
Cdd:PRK09270  20 LRRLAALQA---EPQRR--TIVGIAGPPGAGKSTLAEFLEALLQQDGELPAIQV-PMDGFHLDNAVLDAHGLRPRKGAPE 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696365843 150 SYDMHRLVKFVSDLKSGVPNVTAPVYSHLIYDVIPDGDKTVAQPDILILEGlNVLQSGmDYPHDPhhvfVSDFVDFSIYV 229
Cdd:PRK09270  94 TFDVAGLAALLRRLRAGDDEVYWPVFDRSLEDPVADAIVVPPTARLVIVEG-NYLLLD-EEPWRR----LAGLFDFTIFL 167

                        170       180
                 ....*....|....*....|....*
gi 696365843 230 DAPEELLQTWYINRFLKF---REGA 251
Cdd:PRK09270 168 DAPAEVLRERLVARKLAGglsPEAA 192
Udk COG0572
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway ...
 88-300 3.59e-17

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: 78.34  E-value: 3.59e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696365843  88 PYIISIAGSVAVGKSTTARVLQALLSRwpehRKVELITTDGFLHP--NQVLKDRGlmkKKGF--PQSYDMHRLVKFVSDL 163
Cdd:COG0572    7 PRIIGIAGPSGSGKTTFARRLAEQLGA----DKVVVISLDDYYKDreHLPLDERG---KPNFdhPEAFDLDLLNEHLEPL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696365843 164 KSGVPnVTAPVYSHLIYDVIPDgDKTVAQPDILILEGLNVLqsgmdypHDPhhvFVSDFVDFSIYVDAPEELLQTWYINR 243
Cdd:COG0572   80 KAGES-VELPVYDFATGTRSGE-TVKVEPADVIIVEGIHAL-------NDE---LLRDLLDLKIYVDADTDVRLIRRIVR 147

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 696365843 244 flkfregaftnpDSYFHNYaklsedeainTATSLWKEInWLNLK----QNILPTRERASLI 300
Cdd:COG0572  148 ------------DGEERGR----------TAESVIEQY-WATVRpgheQYIEPTKEYADIV 185
PRK pfam00485
Phosphoribulokinase / Uridine kinase family; This family matches three types of P-loop ...
 90-248 1.35e-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: 1.35e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696365843   90 IISIAGSVAVGKSTTARVLQALLSRWPEHRK----VELITTDGFLHPNQVLKDRGlMKKKGF----PQSYDMHRLVKFVS 161
Cdd:pfam00485   1 VIGVAGSSGSGKTTVARRIVSIFGREGVPAVgiegDSFHSTDRFYMDLHPEDRKR-AGNNGYsfdgPEANDFDLLYEQFK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696365843  162 DLKSGVpNVTAPVYSHLIYDVIPDGDKtVAQPDILILEGLnvlqsgmdypHDPHHVFVSDFVDFSIYVDAPEELLQTWYI 241
Cdd:pfam00485  80 ELKEGG-SVDKPIYNHVTHERDPTPEL-IEGADVLVIEGL----------HALYDERVAQLLDLKIYVDPDIDLELARKI 147


                  ....*..
gi 696365843  242 NRFLKFR 248
Cdd:pfam00485 148 QRDMAER 154
PRK cd02026
Phosphoribulokinase (PRK) is an enzyme involved in the Benson-Calvin cycle in chloroplasts or ...
 90-248 5.81e-10

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: 58.89  E-value: 5.81e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696365843  90 IISIAGSVAVGKSTTARVLQALLSrwPEHrkVELITTDGFlHPNqvlkDRGLMKKKGF----PQSYDMHRLVKFVSDLKS 165
Cdd:cd02026    1 IIGVAGDSGCGKSTFLRRLTSLFG--SDL--VTVICLDDY-HSL----DRKGRKETGItaldPRANNFDLMYEQLKALKE 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696365843 166 GVPnVTAPVYSHLIYdvIPDGDKTVAQPDILILEGLNVLqsgmdYPHDphhvfVSDFVDFSIYVDAPEELLQTWYINRFL 245
Cdd:cd02026   72 GQA-IEKPIYNHVTG--LIDPPELIKPTKIVVIEGLHPL-----YDER-----VRELLDFSVYLDISDEVKFAWKIQRDM 138


                 ...
gi 696365843 246 KFR 248
Cdd:cd02026  139 AER 141
UMPK cd02023
Uridine monophosphate kinase (UMPK, EC 2.7.1.48), also known as uridine kinase or ...
 90-235 8.63e-10

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: 57.56  E-value: 8.63e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696365843  90 IISIAGSVAVGKSTTARVLQALLsrwpEHRKVELITTDGFLHPN-QVLKDRGLMKKKGFPQSYDMHRLVKFVSDLKSGVP 168
Cdd:cd02023    1 IIGIAGGSGSGKTTVAEEIIEQL----GNPKVVIISQDSYYKDLsHEELEERKNNNYDHPDAFDFDLLISHLQDLKNGKS 76

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 696365843 169 nVTAPVYSHLIYDVIPDGdKTVAQPDILILEGLNVLqsgmdypHDPHhvfVSDFVDFSIYVDAPEEL 235
Cdd:cd02023   77 -VEIPVYDFKTHSRLKET-VTVYPADVIILEGILAL-------YDKE---LRDLMDLKIFVDTDADV 131
PRK07429 PRK07429
phosphoribulokinase; Provisional
 88-243 4.00e-09

phosphoribulokinase; Provisional


Pssm-ID: 180975  Cd Length: 327  Bit Score: 56.94  E-value: 4.00e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696365843  88 PYIISIAGSVAVGKSTTARVLQALLSrwPEhrKVELITTDGFlHPnqvlKDRGLMKKKGF----PQSYDMHRLVKFVSDL 163
Cdd:PRK07429   8 PVLLGVAGDSGCGKTTFLRGLADLLG--EE--LVTVICTDDY-HS----YDRKQRKELGItaldPRANNLDIMYEHLKAL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696365843 164 KSGVPnVTAPVYSH---LIydvipDGDKTVAQPDILILEGLNVLqsgmdypHDPHhvfVSDFVDFSIYVDAPEELLQTWY 240
Cdd:PRK07429  79 KTGQP-ILKPIYNHetgTF-----DPPEYIEPNKIVVVEGLHPL-------YDER---VRELYDFKVYLDPPEEVKIAWK 142


                 ...
gi 696365843 241 INR 243
Cdd:PRK07429 143 IKR 145
PRK05480 PRK05480
uridine/cytidine kinase; Provisional
 88-235 3.03e-07

uridine/cytidine kinase; Provisional


Pssm-ID: 235492 [Multi-domain]  Cd Length: 209  Bit Score: 50.16  E-value: 3.03e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696365843  88 PYIISIAGSVAVGKSTTARVLQALLsrwPEHrKVELITTDGFlhpnqvLKDRGLM-----KKKGF--PQSYDMHRLVKFV 160
Cdd:PRK05480   6 PIIIGIAGGSGSGKTTVASTIYEEL---GDE-SIAVIPQDSY------YKDQSHLsfeerVKTNYdhPDAFDHDLLIEHL 75

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 696365843 161 SDLKSGVPnVTAPVYSHLIYDVIPDgDKTVAQPDILILEGLNVLqsgmdypHDPHhvfVSDFVDFSIYVDAPEEL 235
Cdd:PRK05480  76 KALKAGKA-IEIPVYDYTEHTRSKE-TIRVEPKDVIILEGILLL-------EDER---LRDLMDIKIFVDTPLDI 138
PLN02348 PLN02348
phosphoribulokinase
 88-243 1.37e-06

phosphoribulokinase


Pssm-ID: 215198  Cd Length: 395  Bit Score: 49.46  E-value: 1.37e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696365843  88 PYIISIAGSVAVGKSTTARVLQALLSRWPEHRK-------------VELITTDGFlHPNqvlkDRGLMKKKGF----PQS 150
Cdd:PLN02348  49 TVVIGLAADSGCGKSTFMRRLTSVFGGAAKPPKggnpdsntlisdtTTVICLDDY-HSL----DRTGRKEKGVtaldPRA 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696365843 151 YDMHRLVKFVSDLKSGVPnVTAPVYSHLiyDVIPDGDKTVAQPDILILEGLnvlqsgmdypHDPHHVFVSDFVDFSIYVD 230
Cdd:PLN02348 124 NNFDLMYEQVKALKEGKA-VEKPIYNHV--TGLLDPPELIEPPKILVIEGL----------HPMYDERVRDLLDFSIYLD 190

                        170
                 ....*....|...
gi 696365843 231 APEELLQTWYINR 243
Cdd:PLN02348 191 ISDDVKFAWKIQR 203
PRK06696 PRK06696
uridine kinase; Validated
 74-234 7.11e-05

uridine kinase; Validated


Pssm-ID: 180660  Cd Length: 223  Bit Score: 43.43  E-value: 7.11e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696365843  74 AVLEQFLGTNGERiPYIISIAGSVAVGKSTTARVLQALLSRWpeHRKVELITTDGFLHPNQVLKDRGLMKKKGF-PQSYD 152
Cdd:PRK06696   9 ELAEHILTLNLTR-PLRVAIDGITASGKTTFADELAEEIKKR--GRPVIRASIDDFHNPRVIRYRRGRESAEGYyEDAYD 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696365843 153 MHRLVKFVsdLKSGVPN-----VTApVYSHlIYDVIPDGDKTVAQPD-ILILEGLnvlqsgmdYPHDPHhvfVSDFVDFS 226
Cdd:PRK06696  86 YTALRRLL--LDPLGPNgdrqyRTA-SHDL-KTDIPVHNPPLLAAPNaVLIVDGT--------FLLRPE---LRDLWDYK 150


                 ....*...
gi 696365843 227 IYVDAPEE 234
Cdd:PRK06696 151 IFLDTDFE 158
NK cd02019
Nucleoside/nucleotide kinase (NK) is a protein superfamily consisting of multiple families of ...
 90-126 1.59e-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: 39.24  E-value: 1.59e-04
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 696365843  90 IISIAGSVAVGKSTTARVLQALLsrwpEHRKVELITT 126
Cdd:cd02019    1 IIAITGGSGSGKSTVAKKLAEQL----GGRSVVVLDE 33
 
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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