|
Name |
Accession |
Description |
Interval |
E-value |
| CoaA |
COG1072 |
Panthothenate kinase [Coenzyme transport and metabolism]; Panthothenate kinase is part of the ... |
2-306 |
1.83e-157 |
|
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: 441.65 E-value: 1.83e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191009 2 ANEFINFEKISRKTWQHLHQESQPPLNENELNSIKSLNDRISIKDVTDIYLPLISLIQIYKKSQENLSFSKSIFLQKNIS 81
Cdd:COG1072 4 TDELSPYVEFSREEWAALRASTPLTLTEEELERLRGLNDPISLDEVEDIYLPLSRLLNLYVAATQRLHRATSAFLGQADK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191009 82 NRPFIIGVSGSVAVGKSTTSRLLQLLLARTFKDSSVELMTTDGFLYPNAVLSSRHMLNKKGFPESYDMERLLDFLDTIKN 161
Cdd:COG1072 84 KTPFIIGIAGSVAVGKSTTARLLQALLSRWPEHPKVELVTTDGFLYPNAVLERRGLMDRKGFPESYDRRGLLRFLARVKS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191009 162 GQS-AEIPVYSHEIYDIVPNKSQIIEVPDFLIIEGINVFQNPQNNRLYMSDFFDFSIYIDADSDYIENWYLERFATLLDL 240
Cdd:COG1072 164 GDPeVRAPVYSHLLYDIVPGAIVVVDQPDILIVEGNNVLQDEPNPWLFVSDFFDFSIYVDADEEDLREWYVERFLKLRET 243
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488191009 241 AKNDKQNYYNRFLKLGEKGALDFARDIWKDINLVNLEKYIEPTRSRAELILHKTKNHKIDEIYLKK 306
Cdd:COG1072 244 AFRDPDSYFHRYAGLSEEEARAWAEEIWREINLPNLAENILPTRSRADLILRKGADHSVERVRLRK 309
|
|
| PanK |
cd02025 |
Pantothenate kinase (PanK) catalyzes the phosphorylation of pantothenic acid to form 4 ... |
86-304 |
1.03e-110 |
|
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: 320.03 E-value: 1.03e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191009 86 IIGVSGSVAVGKSTTSRLLQLLLARTFKDSSVELMTTDGFLYPNAVLSSRHMLNKKGFPESYDMERLLDFLDTIKNG-QS 164
Cdd:cd02025 1 IIGIAGSVAVGKSTTARVLQALLSRWPDHPNVELITTDGFLYPNKELIERGLMDRKGFPESYDMEALLKFLKDIKSGkKN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191009 165 AEIPVYSHEIYDIVPNKSQIIEVPDFLIIEGINVFQNPQNNRLYMSDFFDFSIYIDADSDYIENWYLERFATLLDLAKND 244
Cdd:cd02025 81 VKIPVYSHLTYDVIPGEKQTVDQPDILIIEGLNVLQTGQNPRLFVSDFFDFSIYVDADEDDIEKWYIKRFLKLRETAFSD 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191009 245 KQNYYNRFLKLGEKGALDFARDIWKDINLVNLEKYIEPTRSRAELILHKTKNHKIDEIYL 304
Cdd:cd02025 161 PDSYFHRYAKMSEEEAIAFAREVWKNINLKNLRENILPTRNRADLILEKGADHSIEEVYL 220
|
|
| panK_bact |
TIGR00554 |
pantothenate kinase, bacterial type; Shown to be a homodimer in E. coli. This enzyme catalyzes ... |
27-306 |
4.78e-91 |
|
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: 272.64 E-value: 4.78e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191009 27 LNENELNSIKSLNDRISIKDVTDIYLPLISLIQIYKKSQENLSFSKSIFLQKNISNRPFIIGVSGSVAVGKSTTSRLLQL 106
Cdd:TIGR00554 5 LSEDDIAPLKGFNEDLSLDEVAEIYLPLSRLINFYIDENLHRQAVLEQFLGRNGAKIPYIISIAGSVAVGKSTSARILQA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191009 107 LLARTFKDSSVELMTTDGFLYPNAVLSSRHMLNKKGFPESYDMERLLDFLDTIKNGQS-AEIPVYSHEIYDIVPNKSQII 185
Cdd:TIGR00554 85 LLSHWPEERKVDLITTDGFLHPLNKLKEDGLLKKKGFPESYDMHKLIKFLADLKSGKPnVTAPIYSHLIYDIIPDGDDTV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191009 186 EVPDFLIIEGINVFQNPQN-----NRLYMSDFFDFSIYIDADSDYIENWYLERFATLLDLAKNDKQNYYNRFLKLGEKGA 260
Cdd:TIGR00554 165 DKPDILILEGLNVLQSGMDkphdpDHTFVSDFVDFSIYVDAEEDLLKEWYIKRFLKFREGAFNDPDSYFHHYAKLSKEEA 244
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 488191009 261 LDFARDIWKDINLVNLEKYIEPTRSRAELILHKTKNHKIDEIYLKK 306
Cdd:TIGR00554 245 IATAMKIWDEINGLNLKQNILPTRERANLILKKGANHAVEEIKLRK 290
|
|
| PRK09270 |
PRK09270 |
nucleoside triphosphate hydrolase domain-containing protein; Reviewed |
76-292 |
1.13e-16 |
|
nucleoside triphosphate hydrolase domain-containing protein; Reviewed
Pssm-ID: 236442 Cd Length: 229 Bit Score: 77.28 E-value: 1.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191009 76 LQKNISNRpFIIGVSGSVAVGKSTTSRLLQLLLARTFKDSSVEL-MttDGFLYPNAVLSSRHMLNKKGFPESYDMERLLD 154
Cdd:PRK09270 26 LQAEPQRR-TIVGIAGPPGAGKSTLAEFLEALLQQDGELPAIQVpM--DGFHLDNAVLDAHGLRPRKGAPETFDVAGLAA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191009 155 FLDTIKNG-QSAEIPVYSHEIYDIVPNKSQIIEVPDFLIIEGiN--VFQNPQNNRLYmsDFFDFSIYIDADSDYIEnwyl 231
Cdd:PRK09270 103 LLRRLRAGdDEVYWPVFDRSLEDPVADAIVVPPTARLVIVEG-NylLLDEEPWRRLA--GLFDFTIFLDAPAEVLR---- 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488191009 232 ERfatLLDlakndkqnyynRFLKLG--EKGALDFARDiwKDinLVNLEKyIEPTRSRAELILH 292
Cdd:PRK09270 176 ER---LVA-----------RKLAGGlsPEAAEAFVLR--ND--GPNARL-VLETSRPADLVLE 219
|
|
| PRK |
pfam00485 |
Phosphoribulokinase / Uridine kinase family; This family matches three types of P-loop ... |
86-290 |
6.30e-14 |
|
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: 68.96 E-value: 6.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191009 86 IIGVSGSVAVGKSTTSRLLQLLLARTFKDSSVelMTTDGFLYPNAVLSSRHMLNKKGF---------PESYDMERLLDFL 156
Cdd:pfam00485 1 VIGVAGSSGSGKTTVARRIVSIFGREGVPAVG--IEGDSFHSTDRFYMDLHPEDRKRAgnngysfdgPEANDFDLLYEQF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191009 157 DTIKNGQSAEIPVYSHEIYDIVPNkSQIIEVPDFLIIEGINVFqnpQNNRLymSDFFDFSIYIDADSDYIENWYLERfat 236
Cdd:pfam00485 79 KELKEGGSVDKPIYNHVTHERDPT-PELIEGADVLVIEGLHAL---YDERV--AQLLDLKIYVDPDIDLELARKIQR--- 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488191009 237 llDLAkndkqnyynrflklgEKG-ALDfarDIWKDINLV--NLEKYIEPTRSRAELI 290
Cdd:pfam00485 150 --DMA---------------ERGhSLE---GVTDSILFRkpDYVNYIDPQFSYADLI 186
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| CoaA |
COG1072 |
Panthothenate kinase [Coenzyme transport and metabolism]; Panthothenate kinase is part of the ... |
2-306 |
1.83e-157 |
|
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: 441.65 E-value: 1.83e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191009 2 ANEFINFEKISRKTWQHLHQESQPPLNENELNSIKSLNDRISIKDVTDIYLPLISLIQIYKKSQENLSFSKSIFLQKNIS 81
Cdd:COG1072 4 TDELSPYVEFSREEWAALRASTPLTLTEEELERLRGLNDPISLDEVEDIYLPLSRLLNLYVAATQRLHRATSAFLGQADK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191009 82 NRPFIIGVSGSVAVGKSTTSRLLQLLLARTFKDSSVELMTTDGFLYPNAVLSSRHMLNKKGFPESYDMERLLDFLDTIKN 161
Cdd:COG1072 84 KTPFIIGIAGSVAVGKSTTARLLQALLSRWPEHPKVELVTTDGFLYPNAVLERRGLMDRKGFPESYDRRGLLRFLARVKS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191009 162 GQS-AEIPVYSHEIYDIVPNKSQIIEVPDFLIIEGINVFQNPQNNRLYMSDFFDFSIYIDADSDYIENWYLERFATLLDL 240
Cdd:COG1072 164 GDPeVRAPVYSHLLYDIVPGAIVVVDQPDILIVEGNNVLQDEPNPWLFVSDFFDFSIYVDADEEDLREWYVERFLKLRET 243
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488191009 241 AKNDKQNYYNRFLKLGEKGALDFARDIWKDINLVNLEKYIEPTRSRAELILHKTKNHKIDEIYLKK 306
Cdd:COG1072 244 AFRDPDSYFHRYAGLSEEEARAWAEEIWREINLPNLAENILPTRSRADLILRKGADHSVERVRLRK 309
|
|
| PanK |
cd02025 |
Pantothenate kinase (PanK) catalyzes the phosphorylation of pantothenic acid to form 4 ... |
86-304 |
1.03e-110 |
|
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: 320.03 E-value: 1.03e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191009 86 IIGVSGSVAVGKSTTSRLLQLLLARTFKDSSVELMTTDGFLYPNAVLSSRHMLNKKGFPESYDMERLLDFLDTIKNG-QS 164
Cdd:cd02025 1 IIGIAGSVAVGKSTTARVLQALLSRWPDHPNVELITTDGFLYPNKELIERGLMDRKGFPESYDMEALLKFLKDIKSGkKN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191009 165 AEIPVYSHEIYDIVPNKSQIIEVPDFLIIEGINVFQNPQNNRLYMSDFFDFSIYIDADSDYIENWYLERFATLLDLAKND 244
Cdd:cd02025 81 VKIPVYSHLTYDVIPGEKQTVDQPDILIIEGLNVLQTGQNPRLFVSDFFDFSIYVDADEDDIEKWYIKRFLKLRETAFSD 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191009 245 KQNYYNRFLKLGEKGALDFARDIWKDINLVNLEKYIEPTRSRAELILHKTKNHKIDEIYL 304
Cdd:cd02025 161 PDSYFHRYAKMSEEEAIAFAREVWKNINLKNLRENILPTRNRADLILEKGADHSIEEVYL 220
|
|
| panK_bact |
TIGR00554 |
pantothenate kinase, bacterial type; Shown to be a homodimer in E. coli. This enzyme catalyzes ... |
27-306 |
4.78e-91 |
|
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: 272.64 E-value: 4.78e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191009 27 LNENELNSIKSLNDRISIKDVTDIYLPLISLIQIYKKSQENLSFSKSIFLQKNISNRPFIIGVSGSVAVGKSTTSRLLQL 106
Cdd:TIGR00554 5 LSEDDIAPLKGFNEDLSLDEVAEIYLPLSRLINFYIDENLHRQAVLEQFLGRNGAKIPYIISIAGSVAVGKSTSARILQA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191009 107 LLARTFKDSSVELMTTDGFLYPNAVLSSRHMLNKKGFPESYDMERLLDFLDTIKNGQS-AEIPVYSHEIYDIVPNKSQII 185
Cdd:TIGR00554 85 LLSHWPEERKVDLITTDGFLHPLNKLKEDGLLKKKGFPESYDMHKLIKFLADLKSGKPnVTAPIYSHLIYDIIPDGDDTV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191009 186 EVPDFLIIEGINVFQNPQN-----NRLYMSDFFDFSIYIDADSDYIENWYLERFATLLDLAKNDKQNYYNRFLKLGEKGA 260
Cdd:TIGR00554 165 DKPDILILEGLNVLQSGMDkphdpDHTFVSDFVDFSIYVDAEEDLLKEWYIKRFLKFREGAFNDPDSYFHHYAKLSKEEA 244
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 488191009 261 LDFARDIWKDINLVNLEKYIEPTRSRAELILHKTKNHKIDEIYLKK 306
Cdd:TIGR00554 245 IATAMKIWDEINGLNLKQNILPTRERANLILKKGANHAVEEIKLRK 290
|
|
| Udk |
COG0572 |
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway ... |
78-224 |
4.08e-21 |
|
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: 89.13 E-value: 4.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191009 78 KNISNRPFIIGVSGSVAVGKSTTSRLLqlllARTFKDSSVELMTTDGFLYPNAVLSsRHMLNKKGF--PESYDMERLLDF 155
Cdd:COG0572 1 AARSGKPRIIGIAGPSGSGKTTFARRL----AEQLGADKVVVISLDDYYKDREHLP-LDERGKPNFdhPEAFDLDLLNEH 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488191009 156 LDTIKNGQSAEIPVYSHEIYDIVPnKSQIIEVPDFLIIEGINVFqnpqnNRLYMSDFFDFSIYIDADSD 224
Cdd:COG0572 76 LEPLKAGESVELPVYDFATGTRSG-ETVKVEPADVIIVEGIHAL-----NDELLRDLLDLKIYVDADTD 138
|
|
| PRK09270 |
PRK09270 |
nucleoside triphosphate hydrolase domain-containing protein; Reviewed |
76-292 |
1.13e-16 |
|
nucleoside triphosphate hydrolase domain-containing protein; Reviewed
Pssm-ID: 236442 Cd Length: 229 Bit Score: 77.28 E-value: 1.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191009 76 LQKNISNRpFIIGVSGSVAVGKSTTSRLLQLLLARTFKDSSVEL-MttDGFLYPNAVLSSRHMLNKKGFPESYDMERLLD 154
Cdd:PRK09270 26 LQAEPQRR-TIVGIAGPPGAGKSTLAEFLEALLQQDGELPAIQVpM--DGFHLDNAVLDAHGLRPRKGAPETFDVAGLAA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191009 155 FLDTIKNG-QSAEIPVYSHEIYDIVPNKSQIIEVPDFLIIEGiN--VFQNPQNNRLYmsDFFDFSIYIDADSDYIEnwyl 231
Cdd:PRK09270 103 LLRRLRAGdDEVYWPVFDRSLEDPVADAIVVPPTARLVIVEG-NylLLDEEPWRRLA--GLFDFTIFLDAPAEVLR---- 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488191009 232 ERfatLLDlakndkqnyynRFLKLG--EKGALDFARDiwKDinLVNLEKyIEPTRSRAELILH 292
Cdd:PRK09270 176 ER---LVA-----------RKLAGGlsPEAAEAFVLR--ND--GPNARL-VLETSRPADLVLE 219
|
|
| PRK07429 |
PRK07429 |
phosphoribulokinase; Provisional |
83-297 |
1.47e-14 |
|
phosphoribulokinase; Provisional
Pssm-ID: 180975 Cd Length: 327 Bit Score: 72.73 E-value: 1.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191009 83 RPFIIGVSGSVAVGKST-TSRLLQLLLArtfkdssvELMT---TDGFlypnavlssrHMLNKK-----GF----PESYDM 149
Cdd:PRK07429 7 RPVLLGVAGDSGCGKTTfLRGLADLLGE--------ELVTvicTDDY----------HSYDRKqrkelGItaldPRANNL 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191009 150 ERLLDFLDTIKNGQSAEIPVYSHEIYDIVPnkSQIIEVPDFLIIEGINVFQNPQnnrlyMSDFFDFSIYIDADSDYIENW 229
Cdd:PRK07429 69 DIMYEHLKALKTGQPILKPIYNHETGTFDP--PEYIEPNKIVVVEGLHPLYDER-----VRELYDFKVYLDPPEEVKIAW 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191009 230 YLERfatllDLAkndKQNY-YNRFLKLGEKGALDFARDI-----WKDI-------NLVNLEKyiEPTRSRAELILHKTKN 296
Cdd:PRK07429 142 KIKR-----DMA---KRGHtYEQVLAEIEAREPDFEAYIrpqrqWADVviqflptQLIDNDE--ENKVLRVRLVLRPGIP 211
|
.
gi 488191009 297 H 297
Cdd:PRK07429 212 H 212
|
|
| UMPK |
cd02023 |
Uridine monophosphate kinase (UMPK, EC 2.7.1.48), also known as uridine kinase or ... |
86-292 |
1.63e-14 |
|
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: 70.66 E-value: 1.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191009 86 IIGVSGSVAVGKSTTSRLLQlllaRTFKDSSVELMTTDGFLYPNAVLSS--RHMLNKKgFPESYDMERLLDFLDTIKNGQ 163
Cdd:cd02023 1 IIGIAGGSGSGKTTVAEEII----EQLGNPKVVIISQDSYYKDLSHEELeeRKNNNYD-HPDAFDFDLLISHLQDLKNGK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191009 164 SAEIPVYSHEIYDIVPnKSQIIEVPDFLIIEGINVFQNPQnnrlyMSDFFDFSIYIDADSDyienwylERFATLL--DLA 241
Cdd:cd02023 76 SVEIPVYDFKTHSRLK-ETVTVYPADVIILEGILALYDKE-----LRDLMDLKIFVDTDAD-------VRLIRRIerDIV 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488191009 242 K-----NDKQNYYNRFLKlgekgaldfardiwkdinlVNLEKYIEPTRSRAELILH 292
Cdd:cd02023 143 ErgrdlESVINQYLKFVK-------------------PMHEQFIEPTKRYADVIIP 179
|
|
| PRK |
cd02026 |
Phosphoribulokinase (PRK) is an enzyme involved in the Benson-Calvin cycle in chloroplasts or ... |
86-291 |
2.90e-14 |
|
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: 71.21 E-value: 2.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191009 86 IIGVSGSVAVGKST-TSRLLQLLLArtfkdssvELMT---TDGFlypnavlssrHMLNKKGF---------PESYDMERL 152
Cdd:cd02026 1 IIGVAGDSGCGKSTfLRRLTSLFGS--------DLVTvicLDDY----------HSLDRKGRketgitaldPRANNFDLM 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191009 153 LDFLDTIKNGQSAEIPVYSHEIYDIVPnkSQIIEVPDFLIIEGINVFQNPQnnrlyMSDFFDFSIYIDADSDYIENWYLE 232
Cdd:cd02026 63 YEQLKALKEGQAIEKPIYNHVTGLIDP--PELIKPTKIVVIEGLHPLYDER-----VRELLDFSVYLDISDEVKFAWKIQ 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488191009 233 RfatllDLAKndKQNYYNRFLKLGEKGALDFardiwkdinlvnlEKYIEPTRSRAELIL 291
Cdd:cd02026 136 R-----DMAE--RGHSLEDVLASIEARKPDF-------------EAYIDPQKQYADVVI 174
|
|
| PRK |
pfam00485 |
Phosphoribulokinase / Uridine kinase family; This family matches three types of P-loop ... |
86-290 |
6.30e-14 |
|
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: 68.96 E-value: 6.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191009 86 IIGVSGSVAVGKSTTSRLLQLLLARTFKDSSVelMTTDGFLYPNAVLSSRHMLNKKGF---------PESYDMERLLDFL 156
Cdd:pfam00485 1 VIGVAGSSGSGKTTVARRIVSIFGREGVPAVG--IEGDSFHSTDRFYMDLHPEDRKRAgnngysfdgPEANDFDLLYEQF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191009 157 DTIKNGQSAEIPVYSHEIYDIVPNkSQIIEVPDFLIIEGINVFqnpQNNRLymSDFFDFSIYIDADSDYIENWYLERfat 236
Cdd:pfam00485 79 KELKEGGSVDKPIYNHVTHERDPT-PELIEGADVLVIEGLHAL---YDERV--AQLLDLKIYVDPDIDLELARKIQR--- 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488191009 237 llDLAkndkqnyynrflklgEKG-ALDfarDIWKDINLV--NLEKYIEPTRSRAELI 290
Cdd:pfam00485 150 --DMA---------------ERGhSLE---GVTDSILFRkpDYVNYIDPQFSYADLI 186
|
|
| PRK05480 |
PRK05480 |
uridine/cytidine kinase; Provisional |
81-224 |
2.81e-12 |
|
uridine/cytidine kinase; Provisional
Pssm-ID: 235492 [Multi-domain] Cd Length: 209 Bit Score: 64.79 E-value: 2.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191009 81 SNRPFIIGVSGSVAVGKSTTSRLLqlllARTFKDSSVELMTTDGFLYPNAVLS--SRHMLNkkgF--PESYDMERLLDFL 156
Cdd:PRK05480 3 MKKPIIIGIAGGSGSGKTTVASTI----YEELGDESIAVIPQDSYYKDQSHLSfeERVKTN---YdhPDAFDHDLLIEHL 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488191009 157 DTIKNGQSAEIPVYSHEIYdIVPNKSQIIEVPDFLIIEGINVFQNPqnnRLymSDFFDFSIYIDADSD 224
Cdd:PRK05480 76 KALKAGKAIEIPVYDYTEH-TRSKETIRVEPKDVIILEGILLLEDE---RL--RDLMDIKIFVDTPLD 137
|
|
| PLN02348 |
PLN02348 |
phosphoribulokinase |
81-233 |
6.79e-08 |
|
phosphoribulokinase
Pssm-ID: 215198 Cd Length: 395 Bit Score: 53.31 E-value: 6.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191009 81 SNRPFIIGVSGSVAVGKSTTSRLLQLLLARTFK-------DSSVELMTTDGFLypnaVLSSRHMLNKKGF---------P 144
Cdd:PLN02348 46 DDGTVVIGLAADSGCGKSTFMRRLTSVFGGAAKppkggnpDSNTLISDTTTVI----CLDDYHSLDRTGRkekgvtaldP 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191009 145 ESYDMERLLDFLDTIKNGQSAEIPVYSHEIYDIVPnkSQIIEVPDFLIIEGINVFQNPQnnrlyMSDFFDFSIYIDADSD 224
Cdd:PLN02348 122 RANNFDLMYEQVKALKEGKAVEKPIYNHVTGLLDP--PELIEPPKILVIEGLHPMYDER-----VRDLLDFSIYLDISDD 194
|
....*....
gi 488191009 225 YIENWYLER 233
Cdd:PLN02348 195 VKFAWKIQR 203
|
|
| PRK07667 |
PRK07667 |
uridine kinase; Provisional |
142-254 |
1.53e-03 |
|
uridine kinase; Provisional
Pssm-ID: 169051 Cd Length: 193 Bit Score: 38.94 E-value: 1.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191009 142 GFPESY-------DMERLLD-FLDTIKNGQSAEIPVYSHEIYDIVPNKSQIIEVpDFLIIEGInVFQNPQnnrlyMSDFF 213
Cdd:PRK07667 67 GFEEWYeyyylqwDIEWLRQkFFRKLQNETKLTLPFYHDETDTCEMKKVQIPIV-GVIVIEGV-FLQRKE-----WRDFF 139
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 488191009 214 DFSIYIDADSDyienwylERFATLLDLAKNDKQNYYNRFLK 254
Cdd:PRK07667 140 HYMVYLDCPRE-------TRFLRESEETQKNLSKFKNRYWK 173
|
|
| NRK1 |
cd02024 |
Nicotinamide riboside kinase (NRK) is an enzyme involved in the metabolism of nicotinamide ... |
86-195 |
1.66e-03 |
|
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: 38.85 E-value: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191009 86 IIGVSGSVAVGKSTTSRLLQLLLARTFkdssveLMTTDGFLYPNAVLSsrhmLNKKGF-----PESYDMERLLDFLDTIK 160
Cdd:cd02024 1 IVGISGVTNSGKTTLAKLLQRILPNCC------VIHQDDFFKPEDEIP----VDENGFkqwdvLEALDMEAMMSTLDYWR 70
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 488191009 161 -----------NGQSAEIPVYSHEIYDIVPNKSQIIEVPD--FLIIEG 195
Cdd:cd02024 71 etghfpkflrsHGNENDPEKEFIEDAQIEETKADLLGAEDlhILIVDG 118
|
|
| UMPK_like |
cd02028 |
Uridine monophosphate kinase_like (UMPK_like) is a family of proteins highly similar to the ... |
86-219 |
5.52e-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: 5.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488191009 86 IIGVSGSVAVGKST-TSRLLQLLLARTFKdssVELMTTDGFLYPNavLSSRHMLNKKGFPESYDMERLLDFLDTIKNGQS 164
Cdd:cd02028 1 VVGIAGPSGSGKTTfAKKLSNQLRVNGIG---PVVISLDDYYVPR--KTPRDEDGNYDFESILDLDLLNKNLHDLLNGKE 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 488191009 165 AEIPVYSHEIYDIVPNKSQIIEVPDFLIIEGINVFqnpqNNRLymSDFFDFSIYI 219
Cdd:cd02028 76 VELPIYDFRTGKRRGYRKLKLPPSGVVILEGIYAL----NERL--RSLLDIRVAV 124
|
|
| |
