|
Name |
Accession |
Description |
Interval |
E-value |
| CoaA |
COG1072 |
Panthothenate kinase [Coenzyme transport and metabolism]; Panthothenate kinase is part of the ... |
1-306 |
1.56e-162 |
|
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: 454.36 E-value: 1.56e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489817673 1 MNDYNHYFHFPREEWRKLEVSKDQILTAEELEEIRGLNDRISLQDISEIYLPLIKLIAIQYHEAIFIHGEKMEYLKKKES 80
Cdd:COG1072 4 TDELSPYVEFSREEWAALRASTPLTLTEEELERLRGLNDPISLDEVEDIYLPLSRLLNLYVAATQRLHRATSAFLGQADK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489817673 81 RAPFIIALAGSVAVGKSTTARVFKLMLDRWFSkTRQVELVTTDGFLYPNKVLEERGIMDKKGFPESYDRDRFAKFLTDLK 160
Cdd:COG1072 84 KTPFIIGIAGSVAVGKSTTARLLQALLSRWPE-HPKVELVTTDGFLYPNAVLERRGLMDRKGFPESYDRRGLLRFLARVK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489817673 161 ANKEDVEIPLYSHFTYDVL-DETRVIHNPDIVIIEGINVLQADQHESLFPSDFFDFSVYMDANEADIKKWYLERFFMLRE 239
Cdd:COG1072 163 SGDPEVRAPVYSHLLYDIVpGAIVVVDQPDILIVEGNNVLQDEPNPWLFVSDFFDFSIYVDADEEDLREWYVERFLKLRE 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489817673 240 TAFQDESSYFHPYTKISKQEAETFALGVWDTINGVNLKENIEKTKYRADLVLQKGTDHLISDIYLRK 306
Cdd:COG1072 243 TAFRDPDSYFHRYAGLSEEEARAWAEEIWREINLPNLAENILPTRSRADLILRKGADHSVERVRLRK 309
|
|
| PanK |
cd02025 |
Pantothenate kinase (PanK) catalyzes the phosphorylation of pantothenic acid to form 4 ... |
85-304 |
8.38e-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: 368.18 E-value: 8.38e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489817673 85 IIALAGSVAVGKSTTARVFKLMLDRWFSKtRQVELVTTDGFLYPNKVLEERGIMDKKGFPESYDRDRFAKFLTDLKANKE 164
Cdd:cd02025 1 IIGIAGSVAVGKSTTARVLQALLSRWPDH-PNVELITTDGFLYPNKELIERGLMDRKGFPESYDMEALLKFLKDIKSGKK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489817673 165 DVEIPLYSHFTYDVLDETR-VIHNPDIVIIEGINVLQADQHESLFPSDFFDFSVYMDANEADIKKWYLERFFMLRETAFQ 243
Cdd:cd02025 80 NVKIPVYSHLTYDVIPGEKqTVDQPDILIIEGLNVLQTGQNPRLFVSDFFDFSIYVDADEDDIEKWYIKRFLKLRETAFS 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489817673 244 DESSYFHPYTKISKQEAETFALGVWDTINGVNLKENIEKTKYRADLVLQKGTDHLISDIYL 304
Cdd:cd02025 160 DPDSYFHRYAKMSEEEAIAFAREVWKNINLKNLRENILPTRNRADLILEKGADHSIEEVYL 220
|
|
| panK_bact |
TIGR00554 |
pantothenate kinase, bacterial type; Shown to be a homodimer in E. coli. This enzyme catalyzes ... |
26-306 |
7.14e-105 |
|
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: 307.70 E-value: 7.14e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489817673 26 LTAEELEEIRGLNDRISLQDISEIYLPLIKLIAIQYHEAIFIHGEKMEYLKKKESRAPFIIALAGSVAVGKSTTARVFKL 105
Cdd:TIGR00554 5 LSEDDIAPLKGFNEDLSLDEVAEIYLPLSRLINFYIDENLHRQAVLEQFLGRNGAKIPYIISIAGSVAVGKSTSARILQA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489817673 106 MLDRWfSKTRQVELVTTDGFLYPNKVLEERGIMDKKGFPESYDRDRFAKFLTDLKANKEDVEIPLYSHFTYDVL-DETRV 184
Cdd:TIGR00554 85 LLSHW-PEERKVDLITTDGFLHPLNKLKEDGLLKKKGFPESYDMHKLIKFLADLKSGKPNVTAPIYSHLIYDIIpDGDDT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489817673 185 IHNPDIVIIEGINVLQA------DQHESlFPSDFFDFSVYMDANEADIKKWYLERFFMLRETAFQDESSYFHPYTKISKQ 258
Cdd:TIGR00554 164 VDKPDILILEGLNVLQSgmdkphDPDHT-FVSDFVDFSIYVDAEEDLLKEWYIKRFLKFREGAFNDPDSYFHHYAKLSKE 242
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 489817673 259 EAETFALGVWDTINGVNLKENIEKTKYRADLVLQKGTDHLISDIYLRK 306
Cdd:TIGR00554 243 EAIATAMKIWDEINGLNLKQNILPTRERANLILKKGANHAVEEIKLRK 290
|
|
| PRK09270 |
PRK09270 |
nucleoside triphosphate hydrolase domain-containing protein; Reviewed |
76-296 |
3.82e-19 |
|
nucleoside triphosphate hydrolase domain-containing protein; Reviewed
Pssm-ID: 236442 Cd Length: 229 Bit Score: 84.21 E-value: 3.82e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489817673 76 KKKESRapFIIALAGSVAVGKSTTArvfklmlDRWFSKTRQVEL-----VTTDGFLYPNKVLEERGIMDKKGFPESYDRD 150
Cdd:PRK09270 28 AEPQRR--TIVGIAGPPGAGKSTLA-------EFLEALLQQDGElpaiqVPMDGFHLDNAVLDAHGLRPRKGAPETFDVA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489817673 151 RFAKFLTDLKANKEDVEIPLYShftydvldetRVIHNP-----------DIVIIEGiNVLQADQheslfPS-----DFFD 214
Cdd:PRK09270 99 GLAALLRRLRAGDDEVYWPVFD----------RSLEDPvadaivvpptaRLVIVEG-NYLLLDE-----EPwrrlaGLFD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489817673 215 FSVYMDANEADikkwyLERFFMLRETAFqdessyfhpytKISKQEAETFALGVwDTINGvnlkENIEKTKYRADLVLQKG 294
Cdd:PRK09270 163 FTIFLDAPAEV-----LRERLVARKLAG-----------GLSPEAAEAFVLRN-DGPNA----RLVLETSRPADLVLEMT 221
|
..
gi 489817673 295 TD 296
Cdd:PRK09270 222 AT 223
|
|
| PRK |
pfam00485 |
Phosphoribulokinase / Uridine kinase family; This family matches three types of P-loop ... |
85-300 |
1.34e-08 |
|
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: 53.94 E-value: 1.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489817673 85 IIALAGSVAVGKSTTARVFKLMLDRWFSKTRQVELV---TTDGFLYPNKVLEERGIMDKkGF----PESYDRDRFAKFLT 157
Cdd:pfam00485 1 VIGVAGSSGSGKTTVARRIVSIFGREGVPAVGIEGDsfhSTDRFYMDLHPEDRKRAGNN-GYsfdgPEANDFDLLYEQFK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489817673 158 DLKANKEdVEIPLYSHFTYDVLDETRVIHNPDIVIIEGINVLQADQHESLfpsdfFDFSVYMDANEaDIK-KWYLERffm 236
Cdd:pfam00485 80 ELKEGGS-VDKPIYNHVTHERDPTPELIEGADVLVIEGLHALYDERVAQL-----LDLKIYVDPDI-DLElARKIQR--- 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489817673 237 lretafqDESSYFHPYTkiskqeaetfalGVWDTINGVnlKEN----IEKTKYRADLVLQKGTDHLIS 300
Cdd:pfam00485 150 -------DMAERGHSLE------------GVTDSILFR--KPDyvnyIDPQFSYADLIIQRVPTNDTA 196
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| CoaA |
COG1072 |
Panthothenate kinase [Coenzyme transport and metabolism]; Panthothenate kinase is part of the ... |
1-306 |
1.56e-162 |
|
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: 454.36 E-value: 1.56e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489817673 1 MNDYNHYFHFPREEWRKLEVSKDQILTAEELEEIRGLNDRISLQDISEIYLPLIKLIAIQYHEAIFIHGEKMEYLKKKES 80
Cdd:COG1072 4 TDELSPYVEFSREEWAALRASTPLTLTEEELERLRGLNDPISLDEVEDIYLPLSRLLNLYVAATQRLHRATSAFLGQADK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489817673 81 RAPFIIALAGSVAVGKSTTARVFKLMLDRWFSkTRQVELVTTDGFLYPNKVLEERGIMDKKGFPESYDRDRFAKFLTDLK 160
Cdd:COG1072 84 KTPFIIGIAGSVAVGKSTTARLLQALLSRWPE-HPKVELVTTDGFLYPNAVLERRGLMDRKGFPESYDRRGLLRFLARVK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489817673 161 ANKEDVEIPLYSHFTYDVL-DETRVIHNPDIVIIEGINVLQADQHESLFPSDFFDFSVYMDANEADIKKWYLERFFMLRE 239
Cdd:COG1072 163 SGDPEVRAPVYSHLLYDIVpGAIVVVDQPDILIVEGNNVLQDEPNPWLFVSDFFDFSIYVDADEEDLREWYVERFLKLRE 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489817673 240 TAFQDESSYFHPYTKISKQEAETFALGVWDTINGVNLKENIEKTKYRADLVLQKGTDHLISDIYLRK 306
Cdd:COG1072 243 TAFRDPDSYFHRYAGLSEEEARAWAEEIWREINLPNLAENILPTRSRADLILRKGADHSVERVRLRK 309
|
|
| PanK |
cd02025 |
Pantothenate kinase (PanK) catalyzes the phosphorylation of pantothenic acid to form 4 ... |
85-304 |
8.38e-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: 368.18 E-value: 8.38e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489817673 85 IIALAGSVAVGKSTTARVFKLMLDRWFSKtRQVELVTTDGFLYPNKVLEERGIMDKKGFPESYDRDRFAKFLTDLKANKE 164
Cdd:cd02025 1 IIGIAGSVAVGKSTTARVLQALLSRWPDH-PNVELITTDGFLYPNKELIERGLMDRKGFPESYDMEALLKFLKDIKSGKK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489817673 165 DVEIPLYSHFTYDVLDETR-VIHNPDIVIIEGINVLQADQHESLFPSDFFDFSVYMDANEADIKKWYLERFFMLRETAFQ 243
Cdd:cd02025 80 NVKIPVYSHLTYDVIPGEKqTVDQPDILIIEGLNVLQTGQNPRLFVSDFFDFSIYVDADEDDIEKWYIKRFLKLRETAFS 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489817673 244 DESSYFHPYTKISKQEAETFALGVWDTINGVNLKENIEKTKYRADLVLQKGTDHLISDIYL 304
Cdd:cd02025 160 DPDSYFHRYAKMSEEEAIAFAREVWKNINLKNLRENILPTRNRADLILEKGADHSIEEVYL 220
|
|
| panK_bact |
TIGR00554 |
pantothenate kinase, bacterial type; Shown to be a homodimer in E. coli. This enzyme catalyzes ... |
26-306 |
7.14e-105 |
|
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: 307.70 E-value: 7.14e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489817673 26 LTAEELEEIRGLNDRISLQDISEIYLPLIKLIAIQYHEAIFIHGEKMEYLKKKESRAPFIIALAGSVAVGKSTTARVFKL 105
Cdd:TIGR00554 5 LSEDDIAPLKGFNEDLSLDEVAEIYLPLSRLINFYIDENLHRQAVLEQFLGRNGAKIPYIISIAGSVAVGKSTSARILQA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489817673 106 MLDRWfSKTRQVELVTTDGFLYPNKVLEERGIMDKKGFPESYDRDRFAKFLTDLKANKEDVEIPLYSHFTYDVL-DETRV 184
Cdd:TIGR00554 85 LLSHW-PEERKVDLITTDGFLHPLNKLKEDGLLKKKGFPESYDMHKLIKFLADLKSGKPNVTAPIYSHLIYDIIpDGDDT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489817673 185 IHNPDIVIIEGINVLQA------DQHESlFPSDFFDFSVYMDANEADIKKWYLERFFMLRETAFQDESSYFHPYTKISKQ 258
Cdd:TIGR00554 164 VDKPDILILEGLNVLQSgmdkphDPDHT-FVSDFVDFSIYVDAEEDLLKEWYIKRFLKFREGAFNDPDSYFHHYAKLSKE 242
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 489817673 259 EAETFALGVWDTINGVNLKENIEKTKYRADLVLQKGTDHLISDIYLRK 306
Cdd:TIGR00554 243 EAIATAMKIWDEINGLNLKQNILPTRERANLILKKGANHAVEEIKLRK 290
|
|
| PRK09270 |
PRK09270 |
nucleoside triphosphate hydrolase domain-containing protein; Reviewed |
76-296 |
3.82e-19 |
|
nucleoside triphosphate hydrolase domain-containing protein; Reviewed
Pssm-ID: 236442 Cd Length: 229 Bit Score: 84.21 E-value: 3.82e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489817673 76 KKKESRapFIIALAGSVAVGKSTTArvfklmlDRWFSKTRQVEL-----VTTDGFLYPNKVLEERGIMDKKGFPESYDRD 150
Cdd:PRK09270 28 AEPQRR--TIVGIAGPPGAGKSTLA-------EFLEALLQQDGElpaiqVPMDGFHLDNAVLDAHGLRPRKGAPETFDVA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489817673 151 RFAKFLTDLKANKEDVEIPLYShftydvldetRVIHNP-----------DIVIIEGiNVLQADQheslfPS-----DFFD 214
Cdd:PRK09270 99 GLAALLRRLRAGDDEVYWPVFD----------RSLEDPvadaivvpptaRLVIVEG-NYLLLDE-----EPwrrlaGLFD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489817673 215 FSVYMDANEADikkwyLERFFMLRETAFqdessyfhpytKISKQEAETFALGVwDTINGvnlkENIEKTKYRADLVLQKG 294
Cdd:PRK09270 163 FTIFLDAPAEV-----LRERLVARKLAG-----------GLSPEAAEAFVLRN-DGPNA----RLVLETSRPADLVLEMT 221
|
..
gi 489817673 295 TD 296
Cdd:PRK09270 222 AT 223
|
|
| Udk |
COG0572 |
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway ... |
77-233 |
8.32e-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: 82.58 E-value: 8.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489817673 77 KKESRAPFIIALAGSVAVGKSTTARVFKLMLdrwfsKTRQVELVTTDGFLYPNKVL--EERGimdKKGF--PESYDRDRF 152
Cdd:COG0572 1 AARSGKPRIIGIAGPSGSGKTTFARRLAEQL-----GADKVVVISLDDYYKDREHLplDERG---KPNFdhPEAFDLDLL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489817673 153 AKFLTDLKANKEdVEIPLYSHFTYDVLDETRVIHNPDIVIIEGINVLqadqHESLFpSDFFDFSVYMDANEADIKKWYLE 232
Cdd:COG0572 73 NEHLEPLKAGES-VELPVYDFATGTRSGETVKVEPADVIIVEGIHAL----NDELL-RDLLDLKIYVDADTDVRLIRRIV 146
|
.
gi 489817673 233 R 233
Cdd:COG0572 147 R 147
|
|
| UMPK |
cd02023 |
Uridine monophosphate kinase (UMPK, EC 2.7.1.48), also known as uridine kinase or ... |
85-296 |
2.65e-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: 61.80 E-value: 2.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489817673 85 IIALAGSVAVGKSTTARVFKLMLdrwfsKTRQVELVTTDGFL--YPNKVLEERgimdKKG---FPESYDRDRFAKFLTDL 159
Cdd:cd02023 1 IIGIAGGSGSGKTTVAEEIIEQL-----GNPKVVIISQDSYYkdLSHEELEER----KNNnydHPDAFDFDLLISHLQDL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489817673 160 KANKeDVEIPLYSHFTYDVLDETRVIHNPDIVIIEGINVLqadQHESLfpSDFFDFSVYMDANeADIKkwYLERffMLRE 239
Cdd:cd02023 72 KNGK-SVEIPVYDFKTHSRLKETVTVYPADVIILEGILAL---YDKEL--RDLMDLKIFVDTD-ADVR--LIRR--IERD 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489817673 240 TAFQ--DESSYFHPYTKISKQEAETFalgvwdtingvnlkenIEKTKYRADLVLQKGTD 296
Cdd:cd02023 141 IVERgrDLESVINQYLKFVKPMHEQF----------------IEPTKRYADVIIPRGGD 183
|
|
| PRK05480 |
PRK05480 |
uridine/cytidine kinase; Provisional |
80-226 |
1.26e-10 |
|
uridine/cytidine kinase; Provisional
Pssm-ID: 235492 [Multi-domain] Cd Length: 209 Bit Score: 59.79 E-value: 1.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489817673 80 SRAPFIIALAGSVAVGKSTTARVFKLMLdrwfsKTRQVELVTTDGFL--YPNKVLEERGimdKKGF--PESYDRDRFAKF 155
Cdd:PRK05480 3 MKKPIIIGIAGGSGSGKTTVASTIYEEL-----GDESIAVIPQDSYYkdQSHLSFEERV---KTNYdhPDAFDHDLLIEH 74
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489817673 156 LTDLKANKeDVEIPLYSHFTYDVLDETRVIHNPDIVIIEGINVLqadQHESLfpSDFFDFSVYMDANeADI 226
Cdd:PRK05480 75 LKALKAGK-AIEIPVYDYTEHTRSKETIRVEPKDVIILEGILLL---EDERL--RDLMDIKIFVDTP-LDI 138
|
|
| PRK |
cd02026 |
Phosphoribulokinase (PRK) is an enzyme involved in the Benson-Calvin cycle in chloroplasts or ... |
85-233 |
6.36e-09 |
|
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: 55.81 E-value: 6.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489817673 85 IIALAGSVAVGKSTTARvfklMLDRWFSKtrqvELVT---TDGFL-YPNKVLEERGIMDKKgfPESYDRDRFAKFLTDLK 160
Cdd:cd02026 1 IIGVAGDSGCGKSTFLR----RLTSLFGS----DLVTvicLDDYHsLDRKGRKETGITALD--PRANNFDLMYEQLKALK 70
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489817673 161 ANKeDVEIPLYSHFTyDVLDETRVIHNPDIVIIEGINvlqadqheSLFPS---DFFDFSVYMDANEADIKKWYLER 233
Cdd:cd02026 71 EGQ-AIEKPIYNHVT-GLIDPPELIKPTKIVVIEGLH--------PLYDErvrELLDFSVYLDISDEVKFAWKIQR 136
|
|
| PRK |
pfam00485 |
Phosphoribulokinase / Uridine kinase family; This family matches three types of P-loop ... |
85-300 |
1.34e-08 |
|
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: 53.94 E-value: 1.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489817673 85 IIALAGSVAVGKSTTARVFKLMLDRWFSKTRQVELV---TTDGFLYPNKVLEERGIMDKkGF----PESYDRDRFAKFLT 157
Cdd:pfam00485 1 VIGVAGSSGSGKTTVARRIVSIFGREGVPAVGIEGDsfhSTDRFYMDLHPEDRKRAGNN-GYsfdgPEANDFDLLYEQFK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489817673 158 DLKANKEdVEIPLYSHFTYDVLDETRVIHNPDIVIIEGINVLQADQHESLfpsdfFDFSVYMDANEaDIK-KWYLERffm 236
Cdd:pfam00485 80 ELKEGGS-VDKPIYNHVTHERDPTPELIEGADVLVIEGLHALYDERVAQL-----LDLKIYVDPDI-DLElARKIQR--- 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489817673 237 lretafqDESSYFHPYTkiskqeaetfalGVWDTINGVnlKEN----IEKTKYRADLVLQKGTDHLIS 300
Cdd:pfam00485 150 -------DMAERGHSLE------------GVTDSILFR--KPDyvnyIDPQFSYADLIIQRVPTNDTA 196
|
|
| PRK07429 |
PRK07429 |
phosphoribulokinase; Provisional |
78-233 |
7.75e-06 |
|
phosphoribulokinase; Provisional
Pssm-ID: 180975 Cd Length: 327 Bit Score: 46.93 E-value: 7.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489817673 78 KESRAPFIIALAGSVAVGKSTTARvfklMLDRWFSKTRqVELVTTDGF-LYPNKVLEERGI--MDkkgfPESYDRDRFAK 154
Cdd:PRK07429 3 SMPDRPVLLGVAGDSGCGKTTFLR----GLADLLGEEL-VTVICTDDYhSYDRKQRKELGItaLD----PRANNLDIMYE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489817673 155 FLTDLKaNKEDVEIPLYSHFTyDVLDETRVIHNPDIVIIEGinvlqadqhesLFP------SDFFDFSVYMDANEADIKK 228
Cdd:PRK07429 74 HLKALK-TGQPILKPIYNHET-GTFDPPEYIEPNKIVVVEG-----------LHPlydervRELYDFKVYLDPPEEVKIA 140
|
....*
gi 489817673 229 WYLER 233
Cdd:PRK07429 141 WKIKR 145
|
|
| PLN02348 |
PLN02348 |
phosphoribulokinase |
159-233 |
1.00e-05 |
|
phosphoribulokinase
Pssm-ID: 215198 Cd Length: 395 Bit Score: 46.76 E-value: 1.00e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489817673 159 LKANKE--DVEIPLYSHFTyDVLDETRVIHNPDIVIIEGINVLqADQHeslfPSDFFDFSVYMDANEaDIK-KWYLER 233
Cdd:PLN02348 133 VKALKEgkAVEKPIYNHVT-GLLDPPELIEPPKILVIEGLHPM-YDER----VRDLLDFSIYLDISD-DVKfAWKIQR 203
|
|
| UMPK_like |
cd02028 |
Uridine monophosphate kinase_like (UMPK_like) is a family of proteins highly similar to the ... |
85-218 |
4.59e-04 |
|
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: 40.37 E-value: 4.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489817673 85 IIALAGSVAVGKSTTArvfKLMLDRWFSKTRQVELVTTDGFLYPNKVleERGIMDKKGFPESYDRDRFAKFLTDLKANKE 164
Cdd:cd02028 1 VVGIAGPSGSGKTTFA---KKLSNQLRVNGIGPVVISLDDYYVPRKT--PRDEDGNYDFESILDLDLLNKNLHDLLNGKE 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 489817673 165 dVEIPLYSHFTYDVLDETRVIHNP-DIVIIEGINVLqadqHESLfpSDFFDFSVY 218
Cdd:cd02028 76 -VELPIYDFRTGKRRGYRKLKLPPsGVVILEGIYAL----NERL--RSLLDIRVA 123
|
|
| PRK06696 |
PRK06696 |
uridine kinase; Validated |
73-224 |
1.50e-03 |
|
uridine kinase; Validated
Pssm-ID: 180660 Cd Length: 223 Bit Score: 39.19 E-value: 1.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489817673 73 EYLKKKESRAPFIIALAGSVAVGKSTTARVFKLMLDRWfskTRQVELVTTDGFLYPNKVLEERGIMDKKGFPE-SYDRDR 151
Cdd:PRK06696 12 EHILTLNLTRPLRVAIDGITASGKTTFADELAEEIKKR---GRPVIRASIDDFHNPRVIRYRRGRESAEGYYEdAYDYTA 88
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489817673 152 FAKFLTDLKANKED--VEIPLYSHFTYDVLDETRVIHNPD-IVIIEGInVLQADQHEslfpsDFFDFSVYMDANEA 224
Cdd:PRK06696 89 LRRLLLDPLGPNGDrqYRTASHDLKTDIPVHNPPLLAAPNaVLIVDGT-FLLRPELR-----DLWDYKIFLDTDFE 158
|
|
| |
