|
Name |
Accession |
Description |
Interval |
E-value |
| CoaA |
COG1072 |
Panthothenate kinase [Coenzyme transport and metabolism]; Panthothenate kinase is part of the ... |
2-312 |
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: 520.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657199349 2 TTEHNPYLQFTREQWALLRDAVPLTLTEHDLQTLRGINEKVSLREVEEIYLPLSRLLNLYVKAKQRRSRVLEQFLGQSRG 81
Cdd:COG1072 4 TDELSPYVEFSREEWAALRASTPLTLTEEELERLRGLNDPISLDEVEDIYLPLSRLLNLYVAATQRLHRATSAFLGQADK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657199349 82 KGTYIISIAGSVAGGKSTTARILQALLERWPEHPRVELVTTDGFLFPNKELEARGLMRRKGFPESYDIRHLVEFVANIRA 161
Cdd:COG1072 84 KTPFIIGIAGSVAVGKSTTARLLQALLSRWPEHPKVELVTTDGFLYPNAVLERRGLMDRKGFPESYDRRGLLRFLARVKS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657199349 162 GHEKVEAPVYSHLIYDILPDEKKVVEQPDILILEGLNVLQsgmdyPQDPHRVFVSDFVDFSIYVDADAELLRTWYIDRFL 241
Cdd:COG1072 164 GDPEVRAPVYSHLLYDIVPGAIVVVDQPDILIVEGNNVLQ-----DEPNPWLFVSDFFDFSIYVDADEEDLREWYVERFL 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 657199349 242 KFRSGAFSDPDSYFHHYAKLAESEATEIANNIWQDINYLNLQENILPTRERANLILTKGNEHAIEQIKLRK 312
Cdd:COG1072 239 KLRETAFRDPDSYFHRYAGLSEEEARAWAEEIWREINLPNLAENILPTRSRADLILRKGADHSVERVRLRK 309
|
|
| panK_bact |
TIGR00554 |
pantothenate kinase, bacterial type; Shown to be a homodimer in E. coli. This enzyme catalyzes ... |
23-312 |
1.29e-166 |
|
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: 464.47 E-value: 1.29e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657199349 23 VPLTLTEHDLQTLRGINEKVSLREVEEIYLPLSRLLNLYVKAKQRRSRVLEQFLGQSRGKGTYIISIAGSVAGGKSTTAR 102
Cdd:TIGR00554 1 VPLKLSEDDIAPLKGFNEDLSLDEVAEIYLPLSRLINFYIDENLHRQAVLEQFLGRNGAKIPYIISIAGSVAVGKSTSAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657199349 103 ILQALLERWPEHPRVELVTTDGFLFPNKELEARGLMRRKGFPESYDIRHLVEFVANIRAGHEKVEAPVYSHLIYDILPDE 182
Cdd:TIGR00554 81 ILQALLSHWPEERKVDLITTDGFLHPLNKLKEDGLLKKKGFPESYDMHKLIKFLADLKSGKPNVTAPIYSHLIYDIIPDG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657199349 183 KKVVEQPDILILEGLNVLQSGMDYPQDPHRVFVSDFVDFSIYVDADAELLRTWYIDRFLKFRSGAFSDPDSYFHHYAKLA 262
Cdd:TIGR00554 161 DDTVDKPDILILEGLNVLQSGMDKPHDPDHTFVSDFVDFSIYVDAEEDLLKEWYIKRFLKFREGAFNDPDSYFHHYAKLS 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 657199349 263 ESEATEIANNIWQDINYLNLQENILPTRERANLILTKGNEHAIEQIKLRK 312
Cdd:TIGR00554 241 KEEAIATAMKIWDEINGLNLKQNILPTRERANLILKKGANHAVEEIKLRK 290
|
|
| PanK |
cd02025 |
Pantothenate kinase (PanK) catalyzes the phosphorylation of pantothenic acid to form 4 ... |
86-310 |
7.09e-130 |
|
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: 368.56 E-value: 7.09e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657199349 86 IISIAGSVAGGKSTTARILQALLERWPEHPRVELVTTDGFLFPNKELEARGLMRRKGFPESYDIRHLVEFVANIRAGHEK 165
Cdd:cd02025 1 IIGIAGSVAVGKSTTARVLQALLSRWPDHPNVELITTDGFLYPNKELIERGLMDRKGFPESYDMEALLKFLKDIKSGKKN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657199349 166 VEAPVYSHLIYDILPDEKKVVEQPDILILEGLNVLQSGMDYpqdphRVFVSDFVDFSIYVDADAELLRTWYIDRFLKFRS 245
Cdd:cd02025 81 VKIPVYSHLTYDVIPGEKQTVDQPDILIIEGLNVLQTGQNP-----RLFVSDFFDFSIYVDADEDDIEKWYIKRFLKLRE 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 657199349 246 GAFSDPDSYFHHYAKLAESEATEIANNIWQDINYLNLQENILPTRERANLILTKGNEHAIEQIKL 310
Cdd:cd02025 156 TAFSDPDSYFHRYAKMSEEEAIAFAREVWKNINLKNLRENILPTRNRADLILEKGADHSIEEVYL 220
|
|
| PRK09270 |
PRK09270 |
nucleoside triphosphate hydrolase domain-containing protein; Reviewed |
46-243 |
6.81e-26 |
|
nucleoside triphosphate hydrolase domain-containing protein; Reviewed
Pssm-ID: 236442 Cd Length: 229 Bit Score: 102.70 E-value: 6.81e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657199349 46 EVEEIYLPLSRLLNLYVKAKQRRsrvleqflgqsrgkgtYIISIAGSVAGGKSTTARILQALLERWPEHPRVElVTTDGF 125
Cdd:PRK09270 11 EIEAVHKPLLRRLAALQAEPQRR----------------TIVGIAGPPGAGKSTLAEFLEALLQQDGELPAIQ-VPMDGF 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657199349 126 LFPNKELEARGLMRRKGFPESYDIRHLVEFVANIRAGHEKVEAPVYSHLIYDILPDEKKVVEQPDILILEGlNVLQsgmd 205
Cdd:PRK09270 74 HLDNAVLDAHGLRPRKGAPETFDVAGLAALLRRLRAGDDEVYWPVFDRSLEDPVADAIVVPPTARLVIVEG-NYLL---- 148
|
170 180 190
....*....|....*....|....*....|....*...
gi 657199349 206 YPQDPHRVfVSDFVDFSIYVDADAELLRTWYIDRFLKF 243
Cdd:PRK09270 149 LDEEPWRR-LAGLFDFTIFLDAPAEVLRERLVARKLAG 185
|
|
| PRK |
pfam00485 |
Phosphoribulokinase / Uridine kinase family; This family matches three types of P-loop ... |
86-244 |
2.41e-13 |
|
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: 67.42 E-value: 2.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657199349 86 IISIAGSVAGGKSTTARILQALLERWPEHPR----VELVTTDGFLFPNKELE--ARGLMRRKGF-PESYDIRHLVEFVAN 158
Cdd:pfam00485 1 VIGVAGSSGSGKTTVARRIVSIFGREGVPAVgiegDSFHSTDRFYMDLHPEDrkRAGNNGYSFDgPEANDFDLLYEQFKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657199349 159 IRAGhEKVEAPVYSHLIYDILPDEKKvVEQPDILILEGlnvLQSGMDYPqdphrvfVSDFVDFSIYVDADAELLRTWYID 238
Cdd:pfam00485 81 LKEG-GSVDKPIYNHVTHERDPTPEL-IEGADVLVIEG---LHALYDER-------VAQLLDLKIYVDPDIDLELARKIQ 148
|
....*.
gi 657199349 239 RFLKFR 244
Cdd:pfam00485 149 RDMAER 154
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| CoaA |
COG1072 |
Panthothenate kinase [Coenzyme transport and metabolism]; Panthothenate kinase is part of the ... |
2-312 |
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: 520.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657199349 2 TTEHNPYLQFTREQWALLRDAVPLTLTEHDLQTLRGINEKVSLREVEEIYLPLSRLLNLYVKAKQRRSRVLEQFLGQSRG 81
Cdd:COG1072 4 TDELSPYVEFSREEWAALRASTPLTLTEEELERLRGLNDPISLDEVEDIYLPLSRLLNLYVAATQRLHRATSAFLGQADK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657199349 82 KGTYIISIAGSVAGGKSTTARILQALLERWPEHPRVELVTTDGFLFPNKELEARGLMRRKGFPESYDIRHLVEFVANIRA 161
Cdd:COG1072 84 KTPFIIGIAGSVAVGKSTTARLLQALLSRWPEHPKVELVTTDGFLYPNAVLERRGLMDRKGFPESYDRRGLLRFLARVKS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657199349 162 GHEKVEAPVYSHLIYDILPDEKKVVEQPDILILEGLNVLQsgmdyPQDPHRVFVSDFVDFSIYVDADAELLRTWYIDRFL 241
Cdd:COG1072 164 GDPEVRAPVYSHLLYDIVPGAIVVVDQPDILIVEGNNVLQ-----DEPNPWLFVSDFFDFSIYVDADEEDLREWYVERFL 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 657199349 242 KFRSGAFSDPDSYFHHYAKLAESEATEIANNIWQDINYLNLQENILPTRERANLILTKGNEHAIEQIKLRK 312
Cdd:COG1072 239 KLRETAFRDPDSYFHRYAGLSEEEARAWAEEIWREINLPNLAENILPTRSRADLILRKGADHSVERVRLRK 309
|
|
| panK_bact |
TIGR00554 |
pantothenate kinase, bacterial type; Shown to be a homodimer in E. coli. This enzyme catalyzes ... |
23-312 |
1.29e-166 |
|
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: 464.47 E-value: 1.29e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657199349 23 VPLTLTEHDLQTLRGINEKVSLREVEEIYLPLSRLLNLYVKAKQRRSRVLEQFLGQSRGKGTYIISIAGSVAGGKSTTAR 102
Cdd:TIGR00554 1 VPLKLSEDDIAPLKGFNEDLSLDEVAEIYLPLSRLINFYIDENLHRQAVLEQFLGRNGAKIPYIISIAGSVAVGKSTSAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657199349 103 ILQALLERWPEHPRVELVTTDGFLFPNKELEARGLMRRKGFPESYDIRHLVEFVANIRAGHEKVEAPVYSHLIYDILPDE 182
Cdd:TIGR00554 81 ILQALLSHWPEERKVDLITTDGFLHPLNKLKEDGLLKKKGFPESYDMHKLIKFLADLKSGKPNVTAPIYSHLIYDIIPDG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657199349 183 KKVVEQPDILILEGLNVLQSGMDYPQDPHRVFVSDFVDFSIYVDADAELLRTWYIDRFLKFRSGAFSDPDSYFHHYAKLA 262
Cdd:TIGR00554 161 DDTVDKPDILILEGLNVLQSGMDKPHDPDHTFVSDFVDFSIYVDAEEDLLKEWYIKRFLKFREGAFNDPDSYFHHYAKLS 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 657199349 263 ESEATEIANNIWQDINYLNLQENILPTRERANLILTKGNEHAIEQIKLRK 312
Cdd:TIGR00554 241 KEEAIATAMKIWDEINGLNLKQNILPTRERANLILKKGANHAVEEIKLRK 290
|
|
| PanK |
cd02025 |
Pantothenate kinase (PanK) catalyzes the phosphorylation of pantothenic acid to form 4 ... |
86-310 |
7.09e-130 |
|
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: 368.56 E-value: 7.09e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657199349 86 IISIAGSVAGGKSTTARILQALLERWPEHPRVELVTTDGFLFPNKELEARGLMRRKGFPESYDIRHLVEFVANIRAGHEK 165
Cdd:cd02025 1 IIGIAGSVAVGKSTTARVLQALLSRWPDHPNVELITTDGFLYPNKELIERGLMDRKGFPESYDMEALLKFLKDIKSGKKN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657199349 166 VEAPVYSHLIYDILPDEKKVVEQPDILILEGLNVLQSGMDYpqdphRVFVSDFVDFSIYVDADAELLRTWYIDRFLKFRS 245
Cdd:cd02025 81 VKIPVYSHLTYDVIPGEKQTVDQPDILIIEGLNVLQTGQNP-----RLFVSDFFDFSIYVDADEDDIEKWYIKRFLKLRE 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 657199349 246 GAFSDPDSYFHHYAKLAESEATEIANNIWQDINYLNLQENILPTRERANLILTKGNEHAIEQIKL 310
Cdd:cd02025 156 TAFSDPDSYFHRYAKMSEEEAIAFAREVWKNINLKNLRENILPTRNRADLILEKGADHSIEEVYL 220
|
|
| PRK09270 |
PRK09270 |
nucleoside triphosphate hydrolase domain-containing protein; Reviewed |
46-243 |
6.81e-26 |
|
nucleoside triphosphate hydrolase domain-containing protein; Reviewed
Pssm-ID: 236442 Cd Length: 229 Bit Score: 102.70 E-value: 6.81e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657199349 46 EVEEIYLPLSRLLNLYVKAKQRRsrvleqflgqsrgkgtYIISIAGSVAGGKSTTARILQALLERWPEHPRVElVTTDGF 125
Cdd:PRK09270 11 EIEAVHKPLLRRLAALQAEPQRR----------------TIVGIAGPPGAGKSTLAEFLEALLQQDGELPAIQ-VPMDGF 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657199349 126 LFPNKELEARGLMRRKGFPESYDIRHLVEFVANIRAGHEKVEAPVYSHLIYDILPDEKKVVEQPDILILEGlNVLQsgmd 205
Cdd:PRK09270 74 HLDNAVLDAHGLRPRKGAPETFDVAGLAALLRRLRAGDDEVYWPVFDRSLEDPVADAIVVPPTARLVIVEG-NYLL---- 148
|
170 180 190
....*....|....*....|....*....|....*...
gi 657199349 206 YPQDPHRVfVSDFVDFSIYVDADAELLRTWYIDRFLKF 243
Cdd:PRK09270 149 LDEEPWRR-LAGLFDFTIFLDAPAEVLRERLVARKLAG 185
|
|
| Udk |
COG0572 |
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway ... |
79-311 |
1.57e-19 |
|
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: 84.89 E-value: 1.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657199349 79 SRGKGTYIISIAGSVAGGKSTTARilqALLERWPEHpRVELVTTDGFLFPNKEL--EARGlmrRKGF--PESYDIRHLVE 154
Cdd:COG0572 2 ARSGKPRIIGIAGPSGSGKTTFAR---RLAEQLGAD-KVVVISLDDYYKDREHLplDERG---KPNFdhPEAFDLDLLNE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657199349 155 FVANIRAGHEkVEAPVYSHLIYDILPDEKKVvEQPDILILEGLNVLqsgmdypqdpHRVFVSDFVDFSIYVDADAELLRT 234
Cdd:COG0572 75 HLEPLKAGES-VELPVYDFATGTRSGETVKV-EPADVIIVEGIHAL----------NDELLRDLLDLKIYVDADTDVRLI 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657199349 235 WYIDRFLKFRSGAFSDP-DSYFHHYaklaesEATEianniwqdinylnlQENILPTRERANLILTKG---NEHAIEQIKL 310
Cdd:COG0572 143 RRIVRDGEERGRTAESViEQYWATV------RPGH--------------EQYIEPTKEYADIVIPNGgplNPVALDLLVA 202
|
.
gi 657199349 311 R 311
Cdd:COG0572 203 R 203
|
|
| PRK |
pfam00485 |
Phosphoribulokinase / Uridine kinase family; This family matches three types of P-loop ... |
86-244 |
2.41e-13 |
|
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: 67.42 E-value: 2.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657199349 86 IISIAGSVAGGKSTTARILQALLERWPEHPR----VELVTTDGFLFPNKELE--ARGLMRRKGF-PESYDIRHLVEFVAN 158
Cdd:pfam00485 1 VIGVAGSSGSGKTTVARRIVSIFGREGVPAVgiegDSFHSTDRFYMDLHPEDrkRAGNNGYSFDgPEANDFDLLYEQFKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657199349 159 IRAGhEKVEAPVYSHLIYDILPDEKKvVEQPDILILEGlnvLQSGMDYPqdphrvfVSDFVDFSIYVDADAELLRTWYID 238
Cdd:pfam00485 81 LKEG-GSVDKPIYNHVTHERDPTPEL-IEGADVLVIEG---LHALYDER-------VAQLLDLKIYVDPDIDLELARKIQ 148
|
....*.
gi 657199349 239 RFLKFR 244
Cdd:pfam00485 149 RDMAER 154
|
|
| UMPK |
cd02023 |
Uridine monophosphate kinase (UMPK, EC 2.7.1.48), also known as uridine kinase or ... |
86-308 |
1.12e-11 |
|
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: 62.96 E-value: 1.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657199349 86 IISIAGSVAGGKSTTAR-ILQALLERWpehprVELVTTDGFLFPNKELEargLMRRKG----FPESYDIRHLVEFVANIR 160
Cdd:cd02023 1 IIGIAGGSGSGKTTVAEeIIEQLGNPK-----VVIISQDSYYKDLSHEE---LEERKNnnydHPDAFDFDLLISHLQDLK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657199349 161 AGHeKVEAPVYSHLIYDILPdEKKVVEQPDILILEGLNVLqsgmdYPQDphrvfVSDFVDFSIYVDADAELLRTWYIDRF 240
Cdd:cd02023 73 NGK-SVEIPVYDFKTHSRLK-ETVTVYPADVIILEGILAL-----YDKE-----LRDLMDLKIFVDTDADVRLIRRIERD 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657199349 241 LKFRSgafSDPDSYFHHYAKLAESEATEIanniwqdinylnlqenILPTRERANLILTKG--NEHAIEQI 308
Cdd:cd02023 141 IVERG---RDLESVINQYLKFVKPMHEQF----------------IEPTKRYADVIIPRGgdNHVAIDLI 191
|
|
| PLN02348 |
PLN02348 |
phosphoribulokinase |
54-239 |
3.76e-08 |
|
phosphoribulokinase
Pssm-ID: 215198 Cd Length: 395 Bit Score: 54.08 E-value: 3.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657199349 54 LSRLLNLYVKAKQRRSRVLeqflGQSRGKGTYIISIAGSVAGGKSTTARILQALLERWPEHPR------VELV--TTDGF 125
Cdd:PLN02348 23 KSNLGSRRSKSPAASSVVV----ALAADDGTVVIGLAADSGCGKSTFMRRLTSVFGGAAKPPKggnpdsNTLIsdTTTVI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657199349 126 LFPNKELEARGLMRRKGF----PESYDIRHLVEFVANIRAGhEKVEAPVYSHLIYDILPDEKkvVEQPDILILEGLnvlq 201
Cdd:PLN02348 99 CLDDYHSLDRTGRKEKGVtaldPRANNFDLMYEQVKALKEG-KAVEKPIYNHVTGLLDPPEL--IEPPKILVIEGL---- 171
|
170 180 190
....*....|....*....|....*....|....*...
gi 657199349 202 sgmdYPQDPHRVfvSDFVDFSIYVDADAELLRTWYIDR 239
Cdd:PLN02348 172 ----HPMYDERV--RDLLDFSIYLDISDDVKFAWKIQR 203
|
|
| PRK |
cd02026 |
Phosphoribulokinase (PRK) is an enzyme involved in the Benson-Calvin cycle in chloroplasts or ... |
86-244 |
5.64e-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: 5.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657199349 86 IISIAGSVAGGKSTTARILQALLERwpehprvELVT---TDGFLfpnkeLEARGLMRRKGF----PESYDIRHLVEFVAN 158
Cdd:cd02026 1 IIGVAGDSGCGKSTFLRRLTSLFGS-------DLVTvicLDDYH-----SLDRKGRKETGItaldPRANNFDLMYEQLKA 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657199349 159 IRAGhEKVEAPVYSHLIYDILPDEKkvVEQPDILILEGLNVLqsgmdYPQDphrvfVSDFVDFSIYVDADAELLRTWYID 238
Cdd:cd02026 69 LKEG-QAIEKPIYNHVTGLIDPPEL--IKPTKIVVIEGLHPL-----YDER-----VRELLDFSVYLDISDEVKFAWKIQ 135
|
....*.
gi 657199349 239 RFLKFR 244
Cdd:cd02026 136 RDMAER 141
|
|
| PRK05480 |
PRK05480 |
uridine/cytidine kinase; Provisional |
86-231 |
4.27e-07 |
|
uridine/cytidine kinase; Provisional
Pssm-ID: 235492 [Multi-domain] Cd Length: 209 Bit Score: 49.77 E-value: 4.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657199349 86 IISIAGSVAGGKSTTARILQALLerwpEHPRVELVTTDGFLFPNKELEargLMRRKGF----PESYDIRHLVEFVANIRA 161
Cdd:PRK05480 8 IIGIAGGSGSGKTTVASTIYEEL----GDESIAVIPQDSYYKDQSHLS---FEERVKTnydhPDAFDHDLLIEHLKALKA 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657199349 162 GhEKVEAPVYSHLIYDILpDEKKVVEQPDILILEGLNVLqsgmdypQDPHrvfVSDFVDFSIYVDADAEL 231
Cdd:PRK05480 81 G-KAIEIPVYDYTEHTRS-KETIRVEPKDVIILEGILLL-------EDER---LRDLMDIKIFVDTPLDI 138
|
|
| PRK07429 |
PRK07429 |
phosphoribulokinase; Provisional |
86-239 |
2.65e-05 |
|
phosphoribulokinase; Provisional
Pssm-ID: 180975 Cd Length: 327 Bit Score: 45.00 E-value: 2.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657199349 86 IISIAGSVAGGKST-TARILQALLERwpehpRVELVTTDGFlfpnkELEARGLMRRKGF----PESYDIRHLVEFVANIR 160
Cdd:PRK07429 10 LLGVAGDSGCGKTTfLRGLADLLGEE-----LVTVICTDDY-----HSYDRKQRKELGItaldPRANNLDIMYEHLKALK 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 657199349 161 AGhEKVEAPVYSHLIYDILPDEKkvVEQPDILILEGLNVLqsgmdYPQdphrvFVSDFVDFSIYVDADAELLRTWYIDR 239
Cdd:PRK07429 80 TG-QPILKPIYNHETGTFDPPEY--IEPNKIVVVEGLHPL-----YDE-----RVRELYDFKVYLDPPEEVKIAWKIKR 145
|
|
| NRK1 |
cd02024 |
Nicotinamide riboside kinase (NRK) is an enzyme involved in the metabolism of nicotinamide ... |
86-196 |
5.48e-05 |
|
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: 43.08 E-value: 5.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657199349 86 IISIAGSVAGGKSTTARILQALLerwpehPRVELVTTDGFLFPNKELEarglMRRKGF-----PESYDIRHLVEFVANIR 160
Cdd:cd02024 1 IVGISGVTNSGKTTLAKLLQRIL------PNCCVIHQDDFFKPEDEIP----VDENGFkqwdvLEALDMEAMMSTLDYWR 70
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 657199349 161 AG---------HEKVEAPVYSHLIYDILPDEKKVVEQPD---ILILEG 196
Cdd:cd02024 71 ETghfpkflrsHGNENDPEKEFIEDAQIEETKADLLGAEdlhILIVDG 118
|
|
| NK |
cd02019 |
Nucleoside/nucleotide kinase (NK) is a protein superfamily consisting of multiple families of ... |
86-157 |
4.28e-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: 38.09 E-value: 4.28e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 657199349 86 IISIAGSVAGGKSTTARILQALLerwpEHPRVELVTTdGFLfpnkeLEARGLMRRKGFPESYDIRHLVEFVA 157
Cdd:cd02019 1 IIAITGGSGSGKSTVAKKLAEQL----GGRSVVVLDE-IVI-----LEGLYASYKSRDARIRDLADLKIYLD 62
|
|
| |
