|
Name |
Accession |
Description |
Interval |
E-value |
| CoaA |
COG1072 |
Panthothenate kinase [Coenzyme transport and metabolism]; Panthothenate kinase is part of the ... |
18-330 |
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: 516.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310250 18 QSESYSPYHFFSSEQWAKFRADTPLTLTSDEVKRLRSMGDPIDLDEVRRIYLSLSRLLSAHVESSQMLFEQRNRFLSLSD 97
Cdd:COG1072 3 DTDELSPYVEFSREEWAALRASTPLTLTEEELERLRGLNDPISLDEVEDIYLPLSRLLNLYVAATQRLHRATSAFLGQAD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310250 98 vTKTPFVIGIAGSVAVGKSTTARILKELLGRWPSSPKVDLVTTDGFLHPNAVLQREKLMQRKGFPESYDTAAILRFLSAI 177
Cdd:COG1072 83 -KKTPFIIGIAGSVAVGKSTTARLLQALLSRWPEHPKVELVTTDGFLYPNAVLERRGLMDRKGFPESYDRRGLLRFLARV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310250 178 KAGRPDVKAPSYSHLVYDVLPDEYKIVDRPDILIFEGINVLQSRDLPaggriVPMVSDFFDFSIYIDAAEDEIHNWYVTR 257
Cdd:COG1072 162 KSGDPEVRAPVYSHLLYDIVPGAIVVVDQPDILIVEGNNVLQDEPNP-----WLFVSDFFDFSIYVDADEEDLREWYVER 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502310250 258 FMRLRETAFRDPNSYFHRYASISDAEALDIAEDLWANINLKNLRQNILPTRPRADLILKKGKDHLIEQVALRK 330
Cdd:COG1072 237 FLKLRETAFRDPDSYFHRYAGLSEEEARAWAEEIWREINLPNLAENILPTRSRADLILRKGADHSVERVRLRK 309
|
|
| panK_bact |
TIGR00554 |
pantothenate kinase, bacterial type; Shown to be a homodimer in E. coli. This enzyme catalyzes ... |
41-330 |
4.12e-127 |
|
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: 365.09 E-value: 4.12e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310250 41 PLTLTSDEVKRLRSMGDPIDLDEVRRIYLSLSRLLSAHVESSQMLFEQRNRFLSLSDvTKTPFVIGIAGSVAVGKSTTAR 120
Cdd:TIGR00554 2 PLKLSEDDIAPLKGFNEDLSLDEVAEIYLPLSRLINFYIDENLHRQAVLEQFLGRNG-AKIPYIISIAGSVAVGKSTSAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310250 121 ILKELLGRWPSSPKVDLVTTDGFLHPNAVLQREKLMQRKGFPESYDTAAILRFLSAIKAGRPDVKAPSYSHLVYDVLPDE 200
Cdd:TIGR00554 81 ILQALLSHWPEERKVDLITTDGFLHPLNKLKEDGLLKKKGFPESYDMHKLIKFLADLKSGKPNVTAPIYSHLIYDIIPDG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310250 201 YKIVDRPDILIFEGINVLQS-RDLPAGGRIVpMVSDFFDFSIYIDAAEDEIHNWYVTRFMRLRETAFRDPNSYFHRYASI 279
Cdd:TIGR00554 161 DDTVDKPDILILEGLNVLQSgMDKPHDPDHT-FVSDFVDFSIYVDAEEDLLKEWYIKRFLKFREGAFNDPDSYFHHYAKL 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 502310250 280 SDAEALDIAEDLWANINLKNLRQNILPTRPRADLILKKGKDHLIEQVALRK 330
Cdd:TIGR00554 240 SKEEAIATAMKIWDEINGLNLKQNILPTRERANLILKKGANHAVEEIKLRK 290
|
|
| PanK |
cd02025 |
Pantothenate kinase (PanK) catalyzes the phosphorylation of pantothenic acid to form 4 ... |
104-328 |
4.13e-127 |
|
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: 362.40 E-value: 4.13e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310250 104 VIGIAGSVAVGKSTTARILKELLGRWPSSPKVDLVTTDGFLHPNAVLQREKLMQRKGFPESYDTAAILRFLSAIKAGRPD 183
Cdd:cd02025 1 IIGIAGSVAVGKSTTARVLQALLSRWPDHPNVELITTDGFLYPNKELIERGLMDRKGFPESYDMEALLKFLKDIKSGKKN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310250 184 VKAPSYSHLVYDVLPDEYKIVDRPDILIFEGINVLQSrdlpaGGRIVPMVSDFFDFSIYIDAAEDEIHNWYVTRFMRLRE 263
Cdd:cd02025 81 VKIPVYSHLTYDVIPGEKQTVDQPDILIIEGLNVLQT-----GQNPRLFVSDFFDFSIYVDADEDDIEKWYIKRFLKLRE 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502310250 264 TAFRDPNSYFHRYASISDAEALDIAEDLWANINLKNLRQNILPTRPRADLILKKGKDHLIEQVAL 328
Cdd:cd02025 156 TAFSDPDSYFHRYAKMSEEEAIAFAREVWKNINLKNLRENILPTRNRADLILEKGADHSIEEVYL 220
|
|
| PRK09270 |
PRK09270 |
nucleoside triphosphate hydrolase domain-containing protein; Reviewed |
103-315 |
3.19e-21 |
|
nucleoside triphosphate hydrolase domain-containing protein; Reviewed
Pssm-ID: 236442 Cd Length: 229 Bit Score: 90.38 E-value: 3.19e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310250 103 FVIGIAGSVAVGKSTTARILKELLGRWPSSPKVDlVTTDGFLHPNAVLQREKLMQRKGFPESYDTAAILRFLSAIKAGRP 182
Cdd:PRK09270 34 TIVGIAGPPGAGKSTLAEFLEALLQQDGELPAIQ-VPMDGFHLDNAVLDAHGLRPRKGAPETFDVAGLAALLRRLRAGDD 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310250 183 DVKAPSYSHLVYDVLPDEYKIVDRPDILIFEGiNVLQSRDLPAGGrivpmVSDFFDFSIYIDAAEDEihnwyvtRFMRLR 262
Cdd:PRK09270 113 EVYWPVFDRSLEDPVADAIVVPPTARLVIVEG-NYLLLDEEPWRR-----LAGLFDFTIFLDAPAEV-------LRERLV 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 502310250 263 EtafRdpnsyfHRYASISDAEALDIAEDlwanINLKNLRQnILPTRPRADLIL 315
Cdd:PRK09270 180 A---R------KLAGGLSPEAAEAFVLR----NDGPNARL-VLETSRPADLVL 218
|
|
| PRK |
pfam00485 |
Phosphoribulokinase / Uridine kinase family; This family matches three types of P-loop ... |
104-262 |
4.22e-10 |
|
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: 58.56 E-value: 4.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310250 104 VIGIAGSVAVGKSTTARILKELLGRWPSSPK----VDLVTTDGFLHPNAVLQREKlMQRKGF----PESYDTAAILRFLS 175
Cdd:pfam00485 1 VIGVAGSSGSGKTTVARRIVSIFGREGVPAVgiegDSFHSTDRFYMDLHPEDRKR-AGNNGYsfdgPEANDFDLLYEQFK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310250 176 AIKAGRpDVKAPSYSHLVYDVLPDEYKIVDrPDILIFEGINVLQSRDlpaggrivpmVSDFFDFSIYIDAAEDEIHNWYV 255
Cdd:pfam00485 80 ELKEGG-SVDKPIYNHVTHERDPTPELIEG-ADVLVIEGLHALYDER----------VAQLLDLKIYVDPDIDLELARKI 147
|
....*..
gi 502310250 256 TRFMRLR 262
Cdd:pfam00485 148 QRDMAER 154
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| CoaA |
COG1072 |
Panthothenate kinase [Coenzyme transport and metabolism]; Panthothenate kinase is part of the ... |
18-330 |
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: 516.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310250 18 QSESYSPYHFFSSEQWAKFRADTPLTLTSDEVKRLRSMGDPIDLDEVRRIYLSLSRLLSAHVESSQMLFEQRNRFLSLSD 97
Cdd:COG1072 3 DTDELSPYVEFSREEWAALRASTPLTLTEEELERLRGLNDPISLDEVEDIYLPLSRLLNLYVAATQRLHRATSAFLGQAD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310250 98 vTKTPFVIGIAGSVAVGKSTTARILKELLGRWPSSPKVDLVTTDGFLHPNAVLQREKLMQRKGFPESYDTAAILRFLSAI 177
Cdd:COG1072 83 -KKTPFIIGIAGSVAVGKSTTARLLQALLSRWPEHPKVELVTTDGFLYPNAVLERRGLMDRKGFPESYDRRGLLRFLARV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310250 178 KAGRPDVKAPSYSHLVYDVLPDEYKIVDRPDILIFEGINVLQSRDLPaggriVPMVSDFFDFSIYIDAAEDEIHNWYVTR 257
Cdd:COG1072 162 KSGDPEVRAPVYSHLLYDIVPGAIVVVDQPDILIVEGNNVLQDEPNP-----WLFVSDFFDFSIYVDADEEDLREWYVER 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502310250 258 FMRLRETAFRDPNSYFHRYASISDAEALDIAEDLWANINLKNLRQNILPTRPRADLILKKGKDHLIEQVALRK 330
Cdd:COG1072 237 FLKLRETAFRDPDSYFHRYAGLSEEEARAWAEEIWREINLPNLAENILPTRSRADLILRKGADHSVERVRLRK 309
|
|
| panK_bact |
TIGR00554 |
pantothenate kinase, bacterial type; Shown to be a homodimer in E. coli. This enzyme catalyzes ... |
41-330 |
4.12e-127 |
|
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: 365.09 E-value: 4.12e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310250 41 PLTLTSDEVKRLRSMGDPIDLDEVRRIYLSLSRLLSAHVESSQMLFEQRNRFLSLSDvTKTPFVIGIAGSVAVGKSTTAR 120
Cdd:TIGR00554 2 PLKLSEDDIAPLKGFNEDLSLDEVAEIYLPLSRLINFYIDENLHRQAVLEQFLGRNG-AKIPYIISIAGSVAVGKSTSAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310250 121 ILKELLGRWPSSPKVDLVTTDGFLHPNAVLQREKLMQRKGFPESYDTAAILRFLSAIKAGRPDVKAPSYSHLVYDVLPDE 200
Cdd:TIGR00554 81 ILQALLSHWPEERKVDLITTDGFLHPLNKLKEDGLLKKKGFPESYDMHKLIKFLADLKSGKPNVTAPIYSHLIYDIIPDG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310250 201 YKIVDRPDILIFEGINVLQS-RDLPAGGRIVpMVSDFFDFSIYIDAAEDEIHNWYVTRFMRLRETAFRDPNSYFHRYASI 279
Cdd:TIGR00554 161 DDTVDKPDILILEGLNVLQSgMDKPHDPDHT-FVSDFVDFSIYVDAEEDLLKEWYIKRFLKFREGAFNDPDSYFHHYAKL 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 502310250 280 SDAEALDIAEDLWANINLKNLRQNILPTRPRADLILKKGKDHLIEQVALRK 330
Cdd:TIGR00554 240 SKEEAIATAMKIWDEINGLNLKQNILPTRERANLILKKGANHAVEEIKLRK 290
|
|
| PanK |
cd02025 |
Pantothenate kinase (PanK) catalyzes the phosphorylation of pantothenic acid to form 4 ... |
104-328 |
4.13e-127 |
|
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: 362.40 E-value: 4.13e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310250 104 VIGIAGSVAVGKSTTARILKELLGRWPSSPKVDLVTTDGFLHPNAVLQREKLMQRKGFPESYDTAAILRFLSAIKAGRPD 183
Cdd:cd02025 1 IIGIAGSVAVGKSTTARVLQALLSRWPDHPNVELITTDGFLYPNKELIERGLMDRKGFPESYDMEALLKFLKDIKSGKKN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310250 184 VKAPSYSHLVYDVLPDEYKIVDRPDILIFEGINVLQSrdlpaGGRIVPMVSDFFDFSIYIDAAEDEIHNWYVTRFMRLRE 263
Cdd:cd02025 81 VKIPVYSHLTYDVIPGEKQTVDQPDILIIEGLNVLQT-----GQNPRLFVSDFFDFSIYVDADEDDIEKWYIKRFLKLRE 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502310250 264 TAFRDPNSYFHRYASISDAEALDIAEDLWANINLKNLRQNILPTRPRADLILKKGKDHLIEQVAL 328
Cdd:cd02025 156 TAFSDPDSYFHRYAKMSEEEAIAFAREVWKNINLKNLRENILPTRNRADLILEKGADHSIEEVYL 220
|
|
| PRK09270 |
PRK09270 |
nucleoside triphosphate hydrolase domain-containing protein; Reviewed |
103-315 |
3.19e-21 |
|
nucleoside triphosphate hydrolase domain-containing protein; Reviewed
Pssm-ID: 236442 Cd Length: 229 Bit Score: 90.38 E-value: 3.19e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310250 103 FVIGIAGSVAVGKSTTARILKELLGRWPSSPKVDlVTTDGFLHPNAVLQREKLMQRKGFPESYDTAAILRFLSAIKAGRP 182
Cdd:PRK09270 34 TIVGIAGPPGAGKSTLAEFLEALLQQDGELPAIQ-VPMDGFHLDNAVLDAHGLRPRKGAPETFDVAGLAALLRRLRAGDD 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310250 183 DVKAPSYSHLVYDVLPDEYKIVDRPDILIFEGiNVLQSRDLPAGGrivpmVSDFFDFSIYIDAAEDEihnwyvtRFMRLR 262
Cdd:PRK09270 113 EVYWPVFDRSLEDPVADAIVVPPTARLVIVEG-NYLLLDEEPWRR-----LAGLFDFTIFLDAPAEV-------LRERLV 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 502310250 263 EtafRdpnsyfHRYASISDAEALDIAEDlwanINLKNLRQnILPTRPRADLIL 315
Cdd:PRK09270 180 A---R------KLAGGLSPEAAEAFVLR----NDGPNARL-VLETSRPADLVL 218
|
|
| Udk |
COG0572 |
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway ... |
99-331 |
1.00e-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: 85.66 E-value: 1.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310250 99 TKTPFVIGIAGSVAVGKSTTARILKELLGRWpsspKVDLVTTDGFLHPNAVLQREKLMQRkGF--PESYDTAAILRFLSA 176
Cdd:COG0572 4 SGKPRIIGIAGPSGSGKTTFARRLAEQLGAD----KVVVISLDDYYKDREHLPLDERGKP-NFdhPEAFDLDLLNEHLEP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310250 177 IKAGRPdVKAPSYSHLVYDVLPDEYKIvDRPDILIFEGINVLQSRDLpaggrivpmvSDFFDFSIYIDAAEDEihnwyvt 256
Cdd:COG0572 79 LKAGES-VELPVYDFATGTRSGETVKV-EPADVIIVEGIHALNDELL----------RDLLDLKIYVDADTDV------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310250 257 RFMR--LRETAFR--DPNSYFHRY-ASISDAEaldiaedlwaninlknlRQNILPTRPRADLILKKGKDHliEQVALRKL 331
Cdd:COG0572 140 RLIRriVRDGEERgrTAESVIEQYwATVRPGH-----------------EQYIEPTKEYADIVIPNGGPL--NPVALDLL 200
|
|
| UMPK |
cd02023 |
Uridine monophosphate kinase (UMPK, EC 2.7.1.48), also known as uridine kinase or ... |
104-249 |
1.50e-13 |
|
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: 68.35 E-value: 1.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310250 104 VIGIAGSVAVGKSTTARILKELLGrwpsSPKVDLVTTDGFLHPNAVLQREKlmqRKG----FPESYDTAAILRFLSAIKA 179
Cdd:cd02023 1 IIGIAGGSGSGKTTVAEEIIEQLG----NPKVVIISQDSYYKDLSHEELEE---RKNnnydHPDAFDFDLLISHLQDLKN 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310250 180 GRPdVKAPSYSHLVYDVLPDEYKIVDrPDILIFEGINVLQSrdlpaggrivPMVSDFFDFSIYIDAAEDE 249
Cdd:cd02023 74 GKS-VEIPVYDFKTHSRLKETVTVYP-ADVIILEGILALYD----------KELRDLMDLKIFVDTDADV 131
|
|
| PRK05480 |
PRK05480 |
uridine/cytidine kinase; Provisional |
99-260 |
6.03e-12 |
|
uridine/cytidine kinase; Provisional
Pssm-ID: 235492 [Multi-domain] Cd Length: 209 Bit Score: 64.02 E-value: 6.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310250 99 TKTPFVIGIAGSVAVGKSTTARILKELLGrwpsSPKVDLVTTDGFLHPNAVLQREklmQRKGF----PESYDTAAILRFL 174
Cdd:PRK05480 3 MKKPIIIGIAGGSGSGKTTVASTIYEELG----DESIAVIPQDSYYKDQSHLSFE---ERVKTnydhPDAFDHDLLIEHL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310250 175 SAIKAGRPdVKAPSYSHLVYDVLPDEYKIVDRpDILIFEGINVLQSRDLpaggrivpmvSDFFDFSIYIDAAEDEihnwy 254
Cdd:PRK05480 76 KALKAGKA-IEIPVYDYTEHTRSKETIRVEPK-DVIILEGILLLEDERL----------RDLMDIKIFVDTPLDI----- 138
|
....*.
gi 502310250 255 vtRFMR 260
Cdd:PRK05480 139 --RLIR 142
|
|
| PRK |
pfam00485 |
Phosphoribulokinase / Uridine kinase family; This family matches three types of P-loop ... |
104-262 |
4.22e-10 |
|
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: 58.56 E-value: 4.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310250 104 VIGIAGSVAVGKSTTARILKELLGRWPSSPK----VDLVTTDGFLHPNAVLQREKlMQRKGF----PESYDTAAILRFLS 175
Cdd:pfam00485 1 VIGVAGSSGSGKTTVARRIVSIFGREGVPAVgiegDSFHSTDRFYMDLHPEDRKR-AGNNGYsfdgPEANDFDLLYEQFK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310250 176 AIKAGRpDVKAPSYSHLVYDVLPDEYKIVDrPDILIFEGINVLQSRDlpaggrivpmVSDFFDFSIYIDAAEDEIHNWYV 255
Cdd:pfam00485 80 ELKEGG-SVDKPIYNHVTHERDPTPELIEG-ADVLVIEGLHALYDER----------VAQLLDLKIYVDPDIDLELARKI 147
|
....*..
gi 502310250 256 TRFMRLR 262
Cdd:pfam00485 148 QRDMAER 154
|
|
| PLN02348 |
PLN02348 |
phosphoribulokinase |
89-262 |
4.63e-10 |
|
phosphoribulokinase
Pssm-ID: 215198 Cd Length: 395 Bit Score: 60.24 E-value: 4.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310250 89 RNRFLSLSDVTKTPFVIGIAGSVAVGKSTTARILKELLGRWPSSPKVDLVTTDGFLHPNAV---LQREKLMQRKGFPESY 165
Cdd:PLN02348 36 ASSVVVALAADDGTVVIGLAADSGCGKSTFMRRLTSVFGGAAKPPKGGNPDSNTLISDTTTvicLDDYHSLDRTGRKEKG 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310250 166 DTAAILR---F------LSAIKAGRPdVKAPSYSHlVYDVLpDEYKIVDRPDILIFEGINvlqsrdlpaggrivPM---- 232
Cdd:PLN02348 116 VTALDPRannFdlmyeqVKALKEGKA-VEKPIYNH-VTGLL-DPPELIEPPKILVIEGLH--------------PMyder 178
|
170 180 190
....*....|....*....|....*....|
gi 502310250 233 VSDFFDFSIYIDAAEDEIHNWYVTRFMRLR 262
Cdd:PLN02348 179 VRDLLDFSIYLDISDDVKFAWKIQRDMAER 208
|
|
| PRK07429 |
PRK07429 |
phosphoribulokinase; Provisional |
102-262 |
5.33e-09 |
|
phosphoribulokinase; Provisional
Pssm-ID: 180975 Cd Length: 327 Bit Score: 56.56 E-value: 5.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310250 102 PFVIGIAGSVAVGKSTTARILKELLGRwpsspkvDLVT---TDGFlHPnavLQREklmQRK--GF----PESYDTAAILR 172
Cdd:PRK07429 8 PVLLGVAGDSGCGKTTFLRGLADLLGE-------ELVTvicTDDY-HS---YDRK---QRKelGItaldPRANNLDIMYE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310250 173 FLSAIKAGRPDVKaPSYSHLVYDVLPDEYkiVDRPDILIFEGINVLQSRdlpaggrivpMVSDFFDFSIYIDAAEDEIHN 252
Cdd:PRK07429 74 HLKALKTGQPILK-PIYNHETGTFDPPEY--IEPNKIVVVEGLHPLYDE----------RVRELYDFKVYLDPPEEVKIA 140
|
170
....*....|
gi 502310250 253 WYVTRFMRLR 262
Cdd:PRK07429 141 WKIKRDMAKR 150
|
|
| PRK |
cd02026 |
Phosphoribulokinase (PRK) is an enzyme involved in the Benson-Calvin cycle in chloroplasts or ... |
104-331 |
2.49e-08 |
|
Phosphoribulokinase (PRK) is an enzyme involved in the Benson-Calvin cycle in chloroplasts or photosynthetic prokaryotes. This enzyme catalyzes the phosphorylation of D-ribulose 5-phosphate to form D-ribulose 1, 5-biphosphate, using ATP and NADPH produced by the primary reactions of photosynthesis.
Pssm-ID: 238984 [Multi-domain] Cd Length: 273 Bit Score: 54.27 E-value: 2.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310250 104 VIGIAGSVAVGKSTTARILKELLGRwpsspkvDLVT---TDGFLHpnavLQREklmQRK--GF----PESYDTAAILRFL 174
Cdd:cd02026 1 IIGVAGDSGCGKSTFLRRLTSLFGS-------DLVTvicLDDYHS----LDRK---GRKetGItaldPRANNFDLMYEQL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310250 175 SAIKAGRPdVKAPSYSHLVYDVLPDEYkiVDRPDILIFEGINVLQSRDlpaggrivpmVSDFFDFSIYIDAAEDEIHNWY 254
Cdd:cd02026 67 KALKEGQA-IEKPIYNHVTGLIDPPEL--IKPTKIVVIEGLHPLYDER----------VRELLDFSVYLDISDEVKFAWK 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502310250 255 VTRFMRLREtafrdpnsyfHRYasisdaealdiaEDLWANINLK--NLRQNILPTRPRADLILKKGKDHLIEQVALRKL 331
Cdd:cd02026 134 IQRDMAERG----------HSL------------EDVLASIEARkpDFEAYIDPQKQYADVVIQVLPTQLIPDDTEGKV 190
|
|
| NK |
cd02019 |
Nucleoside/nucleotide kinase (NK) is a protein superfamily consisting of multiple families of ... |
104-128 |
2.41e-03 |
|
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: 36.16 E-value: 2.41e-03
10 20
....*....|....*....|....*
gi 502310250 104 VIGIAGSVAVGKSTTARILKELLGR 128
Cdd:cd02019 1 IIAITGGSGSGKSTVAKKLAEQLGG 25
|
|
| PRK07667 |
PRK07667 |
uridine kinase; Provisional |
103-316 |
2.51e-03 |
|
uridine kinase; Provisional
Pssm-ID: 169051 Cd Length: 193 Bit Score: 38.56 E-value: 2.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310250 103 FVIGIAGSVAVGKSTTARILKELLGRWpsSPKVDLVTTDgflhpNAVLQREKLMQrKGFPESYDTAAI------LR--FL 174
Cdd:PRK07667 18 FILGIDGLSRSGKTTFVANLKENMKQE--GIPFHIFHID-----DYIVERNKRYH-TGFEEWYEYYYLqwdiewLRqkFF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310250 175 SAIKAGRpDVKAPSYSHLVyDVLpdEYKIVDRP--DILIFEGInVLQSRDLpaggrivpmvSDFFDFSIYIDAAEDeihn 252
Cdd:PRK07667 90 RKLQNET-KLTLPFYHDET-DTC--EMKKVQIPivGVIVIEGV-FLQRKEW----------RDFFHYMVYLDCPRE---- 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502310250 253 wyvTRFMRLRETAFRDPNSYFHRYASisdaealdiAEDLWAninlknlrQNILPTRpRADLILK 316
Cdd:PRK07667 151 ---TRFLRESEETQKNLSKFKNRYWK---------AEDYYL--------ETESPKD-RADLVIK 193
|
|
| CoaE |
COG0237 |
Dephospho-CoA kinase [Coenzyme transport and metabolism]; Dephospho-CoA kinase is part of the ... |
102-125 |
6.24e-03 |
|
Dephospho-CoA kinase [Coenzyme transport and metabolism]; Dephospho-CoA kinase is part of the Pathway/BioSystem: Pantothenate/CoA biosynthesis
Pssm-ID: 440007 Cd Length: 193 Bit Score: 37.35 E-value: 6.24e-03
10 20
....*....|....*....|....
gi 502310250 102 PFVIGIAGSVAVGKSTTARILKEL 125
Cdd:COG0237 1 MLIIGLTGGIGSGKSTVARMFAEL 24
|
|
| |
