|
Name |
Accession |
Description |
Interval |
E-value |
| PLN00012 |
PLN00012 |
chlorophyll synthetase; Provisional |
20-376 |
0e+00 |
|
chlorophyll synthetase; Provisional
Pssm-ID: 215028 Cd Length: 375 Bit Score: 662.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209263382 20 FRPPLLSLRSPPPSSLRLNRRRHFQVVRAAETDK-ETKANAPEKAPA---GGSSFNQLLGIKGAKQENDIWKIRLQLTKP 95
Cdd:PLN00012 15 LRASARSRRPSRPSTLSSPSPRRRLVVRAAETDTdKVKSQAPDKAPEksdGGSAVNQLLGIKGAAQETDIWKIRLQLTKP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209263382 96 VTWPPLVWGVLCGAAASGNFHWTVEDVAKSIVCMIMSGPCLTGYTQTINDWYDRDIDAINEPYRPIPSGAISENEVITQI 175
Cdd:PLN00012 95 VTWPPLVWGVLCGAAASGNFHWTLEDVAKSIVCMLMSGPFLTGYTQTINDWYDREIDAINEPYRPIPSGAISENEVITQI 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209263382 176 WALLLAGLGLGALLDVWAGHDFPIIFYLAVGGSLLSYIYSAPPLKLKQNGWIGNFALGASYIGLPWWAGQALFGTLTPDI 255
Cdd:PLN00012 175 WVLLLGGLGLAYTLDVWAGHDFPIVFYLALGGSLLSYIYSAPPLKLKQNGWIGNYALGASYISLPWWAGQALFGTLTPDV 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209263382 256 VVLTSLYSIAGLGIAIVNDFKSVEGDRALGLQSLPVAFGMETAKWICVGAIDITQLSVAGYLFSSGKPYYALALLGLTIP 335
Cdd:PLN00012 255 VVLTLLYSIAGLGIAIVNDFKSIEGDRALGLQSLPVAFGVETAKWICVGSIDITQLSVAGYLLAIGKPYYALALLGLIIP 334
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 2209263382 336 QVVFQFQYFLKDPVKYDVKYQASAQPFFVLGLLVTALATSH 376
Cdd:PLN00012 335 QIFFQFKYFLPDPVKNDVKYQASAQPFLVFGLLVTALATGH 375
|
|
| ChlG |
TIGR02056 |
chlorophyll synthase, ChlG; This model represents the strictly cyanobacterial and ... |
72-376 |
0e+00 |
|
chlorophyll synthase, ChlG; This model represents the strictly cyanobacterial and plant-specific chlorophyll synthase ChlG. ChlG is the enzyme (esterase) which attaches the side chain moiety onto chlorophyllide a. Both geranylgeranyl and phytyl pyrophosphates are substrates to varying degrees in enzymes from different sources. Thus, ChlG may act as the final or penultimate step in chlorophyll biosynthesis (along with the geranylgeranyl reductase, ChlP). [Biosynthesis of cofactors, prosthetic groups, and carriers, Chlorophyll and bacteriochlorphyll]
Pssm-ID: 131111 Cd Length: 306 Bit Score: 538.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209263382 72 QLLGIKGA-KQENDIWKIRLQLTKPVTWPPLVWGVLCGAAASGNFHWTVEDVAKSIVCMIMSGPCLTGYTQTINDWYDRD 150
Cdd:TIGR02056 1 QLLGIKGAaPGETNIWKIRLQLMKPITWIPLIWGVVCGAAASGNFHWSLEDVAKAALCMLLSGPCLTGYTQTINDFYDRD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209263382 151 IDAINEPYRPIPSGAISENEVITQIWALLLAGLGLGALLDVWAGHDFPIIFYLAVGGSLLSYIYSAPPLKLKQNGWIGNF 230
Cdd:TIGR02056 81 IDAINEPYRPIPSGAISEPEVITQIVLLFIAGIAIAFILDLWAGHEFPNVFVLALFGSFIAFIYSAPPLKLKQNGWLGNF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209263382 231 ALGASYIGLPWWAGQALFGTLTPDIVVLTSLYSIAGLGIAIVNDFKSVEGDRALGLQSLPVAFGMETAKWICVGAIDITQ 310
Cdd:TIGR02056 161 ALGASYIALPWWAGHALFGELNPDIAVLTLIYSIAGLGIAIVNDFKSVEGDRALGLQSLPVAFGIETAAWICVGAIDIFQ 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2209263382 311 LSVAGYLFSSGKPYYALALLGLTIPQVVFQFQYFLKDPVKYDVKYQASAQPFFVLGLLVTALATSH 376
Cdd:TIGR02056 241 GLIAAYLLAIGENLYAAALVALIIPQITFQDKYFLKDPLKNDVKYQASAQPFLVLGIFVAALALGH 306
|
|
| PRK07566 |
PRK07566 |
chlorophyll synthase ChlG; |
60-376 |
5.53e-152 |
|
chlorophyll synthase ChlG;
Pssm-ID: 236052 Cd Length: 314 Bit Score: 430.89 E-value: 5.53e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209263382 60 PEKAPAGGSSFNQLLGIKGAKQENDIWKIRLQLTKPVTWPPLVWGVLCGAAASGNFHWTVEDVAKSIVCMIMSGPCLTGY 139
Cdd:PRK07566 1 ISEALENTSKPRQLLGPKGASPTTSIWKARLQLMKPITWFPPMWAFLCGAVSSGAFGWTLENVLKLLAGMLLAGPLLCGT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209263382 140 TQTINDWYDRDIDAINEPYRPIPSGAISENEVITQIWALLLAGLGLGALLDvwaghdfPIIFYLAVGGSLLSYIYSAPPL 219
Cdd:PRK07566 81 SQTLNDYFDREVDAINEPYRPIPSGAISLRWVLYLIAVLTVLGLAVAYLLG-------PWVFLAALLGLFLAWIYSAPPL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209263382 220 KLKQNGWIGNFALGASYIGLPWWAGQALFGTLTPD--IVVLTSLYSIAGLGIAIVNDFKSVEGDRALGLQSLPVAFGMET 297
Cdd:PRK07566 154 RLKQNGWLGNYAVGLSYEGLPWWAGAAAFGAGLPSwpIVILALLYSLGAHGIMTLNDFKSVEGDRQLGLRSLPVVFGEKN 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2209263382 298 AKWICVGAIDITQLSVAGYLFSSGKPYYALALLGLTIPQVVFQFQYfLKDPVKYDVKYQASAQPFFVLGLLVTALATSH 376
Cdd:PRK07566 234 AARIACVVIDLFQLAVIALLLAWGQPLYAAIVGLLLIPQITLQDRL-LRDPLERDVWYNASAQPFYVLGMLVTALAIRH 311
|
|
| PT_UbiA_chlorophyll |
cd13958 |
Bacteriochlorophyll/chlorophyll synthetase; Chlorophyll synthase catalyzes the last step of ... |
89-371 |
3.75e-150 |
|
Bacteriochlorophyll/chlorophyll synthetase; Chlorophyll synthase catalyzes the last step of chlorophyll (Chl) biosynthesis, the addition of the tetraprenyl (phytyl or geranylgeranyl) side chain. In plant chloroplast, the chlorophyll synthase is located in thylakoid membrane and has been shown to also have a regulatory or channeling function. Prenyltransferases (PTs) catalyze the regioselective transfer of prenyl moieties onto a wide variety of substrates and play an important role in many biosynthetic pathways.
Pssm-ID: 260121 Cd Length: 277 Bit Score: 424.72 E-value: 3.75e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209263382 89 RLQLTKPVTWPPLVWGVLCGAAASGNFHWTVEDVAKSIVCMIMSGPCLTGYTQTINDWYDRDIDAINEPYRPIPSGAISE 168
Cdd:cd13958 1 RLELLKPVTWFPPMWAFLCGAAASGAFQWSNWDVWLLLLGMLLAGPLLTGTSQTINDYYDREVDAINEPYRPIPSGRISE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209263382 169 NEVITQIWALLLAGLGlgalldVWAGHDFPIIFYLAVGGSLLSYIYSAPPLKLKQNGWIGNFALGASYIGLPWWAGQALF 248
Cdd:cd13958 81 REALWNIWVLLLLSLL------VALFLDGPWVFAAAVVGLVLAYIYSAPPLKLKQNGWWGNAAVGLSYEGLPWWAGAAAF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209263382 249 GT-LTPDIVVLTSLYSIAGLGIAIVNDFKSVEGDRALGLQSLPVAFGMETAKWICVGAIDITQLSVAGYLFSSGKPYYAL 327
Cdd:cd13958 155 AGlLTWESLALALLYSIGAHGIMTLNDFKSIEGDRQLGLRSLPVALGVDTAAWIACGVIDVPQLAVAALLLAWGETWYAA 234
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 2209263382 328 ALLGLTIPQVVFQFQYFLKDPVKyDVKYQASAQPFFVLGLLVTA 371
Cdd:cd13958 235 VVGALLLAQIPLQFKLLLDPPAK-AVWYNATAQPFYVLGMMVAA 277
|
|
| chlor_syn_BchG |
TIGR01476 |
bacteriochlorophyll/chlorophyll synthetase; This model describes a subfamily of a large family ... |
87-373 |
6.82e-116 |
|
bacteriochlorophyll/chlorophyll synthetase; This model describes a subfamily of a large family of polyprenyltransferases (pfam01040) that also includes 4-hydroxybenzoate octaprenyltransferase and protoheme IX farnesyltransferase (heme O synthase). Members of this family are found exclusively in photosynthetic organisms, including a single copy in Arabidopsis thaliana. [Biosynthesis of cofactors, prosthetic groups, and carriers, Chlorophyll and bacteriochlorphyll]
Pssm-ID: 130541 Cd Length: 283 Bit Score: 338.29 E-value: 6.82e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209263382 87 KIRLQLTKPVTWPPLVWGVLCGAAASGNFHWTVEDVAKSIVCMIMSGPCLTGYTQTINDWYDRDIDAINEPYRPIPSGAI 166
Cdd:TIGR01476 1 RAHIELMKPVTWIPPIWACFCGALASGYERGFPEHWWLMLLGMLMAGPLGTGFSQSINDYFDRDVDAINEPQRPIPSGII 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209263382 167 SENEVITQIWALLLAGLGLGALLDVWAghdfpiIFYLAVGGSLLSYIYSAPPLKLKQNGWIGNFALGASYIGLPWWAGQA 246
Cdd:TIGR01476 81 SLREVRWNWLVLTVAGLLVALVLGNWL------IVLFTVVGIVLAVIYSMPPIKLKRNGWLGPPAVGLSYEGLPWMAGHA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209263382 247 LFGTLTPDIVVLTSLYSIAGLGIAIVNDFKSVEGDRALGLQSLPVAFGMETAKWICVGAIDITQLSVAGYLFSSGKPYYA 326
Cdd:TIGR01476 155 IFAPLTWQSVVVALIYSLGAHGIMTLNDFKSVEGDRQLGLRSLPVMIGVKRAAIVAVTTINVFQAMVIGLLLIWGQPWVA 234
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 2209263382 327 LALLGLTIPQVVFQFQYFLKDPVKYDVKYQASAQPFFVLGLLVTALA 373
Cdd:TIGR01476 235 TIVFLLLVAQIYNQIKLFLRDPQQNYVRYNATANPFYVLGMLAAGFA 281
|
|
| PRK12392 |
PRK12392 |
bacteriochlorophyll c synthase; Provisional |
87-348 |
4.11e-47 |
|
bacteriochlorophyll c synthase; Provisional
Pssm-ID: 171463 Cd Length: 331 Bit Score: 163.32 E-value: 4.11e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209263382 87 KIR--LQLTKPVTWPPLVWGVLCGAAASGNFHWTVEDVAKSIVCMIMSGPCLTGYTQTINDWYDRDIDAINEPYRPIPSG 164
Cdd:PRK12392 11 KIRahLELLDPVTWISVFPCLAGGVMASGAMQPTLHDYLLLLALFLMYGPLGTGFSQSVNDYFDLELDRVNEPTRPIPSG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209263382 165 AISENEVitqIWALLLAGLGLGALLdVWAGHDFP-----IIFYLAVGGSLLSYIYSAPPLKLKQNGWIGNFALGASYIGL 239
Cdd:PRK12392 91 RLSEKEA---LWNSIIVLLLAIGLG-VWLGLHIGgergmVIISSILAGLFVAYIYSAPPLKLKKNILTSAPAVGFSYGFI 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209263382 240 PWWAGQALFGTLTPDIVVLTSLYSIAGLGIAIVNDFKSVEGDRALGLQSLPVAFGMETAKWICVGAIDITQLSVAGYLFS 319
Cdd:PRK12392 167 TFLSANALFSDIRPEVVWLAGLNFFMAIALIIMNDFKSVEGDKEGGLKSLTVMIGAKNTFLVSFIIIDLVFAVFAWLAWS 246
|
250 260 270
....*....|....*....|....*....|
gi 2209263382 320 SGKPYYA-LALLGLTIpQVVFQFQyFLKDP 348
Cdd:PRK12392 247 WGFTVLMyFILVGLVL-NIVIQIQ-LYRDP 274
|
|
| UbiA |
COG0382 |
4-hydroxybenzoate polyprenyltransferase [Coenzyme transport and metabolism]; 4-hydroxybenzoate ... |
92-373 |
2.53e-46 |
|
4-hydroxybenzoate polyprenyltransferase [Coenzyme transport and metabolism]; 4-hydroxybenzoate polyprenyltransferase is part of the Pathway/BioSystem: Ubiquinone biosynthesis
Pssm-ID: 440151 Cd Length: 280 Bit Score: 159.62 E-value: 2.53e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209263382 92 LTKPVTWPPLVWGVLCGAAASGNFHWTVedvaKSIVCMIMSGPCLTGYTQTINDWYDRDIDAINE--PYRPIPSGAISEN 169
Cdd:COG0382 9 LDRPIGILLLLWPTLWALFLAAGGLPDL----LLLLLAVLGTVLMRSAGYVINDYFDREIDRINErkPNRPLASGRISLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209263382 170 EVITQIWALLLAGLGLGALLDVWAghdfpiiFYLAVGGSLLSYIYsapPLKLKQNGWIGNFALGASYiGLPWWAGQALF- 248
Cdd:COG0382 85 EALLLAIVLLLLALALALLLNPLT-------FLLALAALALAWAY---SLFLKRFTLLGNLVLGLLF-GLGILMGFAAVt 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209263382 249 GTLTPDIVVLTSLYSIAGLGIAIVNDFKSVEGDRALGLQSLPVAFGMETAKWICVGAIDITqLSVAGYLFSSGKPYYALA 328
Cdd:COG0382 154 GSLPLSAWLLALAAFLWTLAYDTIYDLEDREGDRKIGIKTLAILFGVRDALIIAGVLYALA-VLLLLLLGLLAGLGLLYL 232
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 2209263382 329 LLGLTIPQVVFQFQYFLKDPVKYDvkyQASAQPFFVLGLLVTALA 373
Cdd:COG0382 233 LGLLAALLLLYLSQLWLLRPRKKD---PARALKLFKLNMLLGLLL 274
|
|
| PT_UbiA |
cd13956 |
UbiA family of prenyltransferases (PTases); Many characterized members of the UbiA ... |
90-370 |
1.22e-34 |
|
UbiA family of prenyltransferases (PTases); Many characterized members of the UbiA prenyltransferase family are aromatic prenyltransferases and play an important role in the biosynthesis of heme, chlorophyll, vitamin E, and vitamin K. They contain two copies of a motif similar to the active site DxxD motif of trans-prenyltransferases and are potentially related. Prenyltransferases (PTs) catalyze the regioselective transfer of prenyl moieties onto a wide variety of substrates and play an important role in many biosynthetic pathways.
Pssm-ID: 260119 [Multi-domain] Cd Length: 271 Bit Score: 128.62 E-value: 1.22e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209263382 90 LQLTKPVTWPPLVWGVLCGAAASGNFHWtveDVAKSIVCMIMSGPCLTGYTQTINDWYDRDIDAINEPYRPIPSGAISEN 169
Cdd:cd13956 1 LRLMRPYTLLYVLAPALAGAALAGAFAG---PLPALLLLALLAVFLGAGAGYALNDYTDRELDAINKPDRPLPSGRLSPR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209263382 170 EVITQIWALLLAGLGLgalldvwAGHDFPIIFYLAVGGSLLSYIYSAPPLKLKQNGWIGNFALGASYIGLPWWAgqALFG 249
Cdd:cd13956 78 QALAFAAALLLVGLAL-------ALALGPLALLLLLAGLLLGLAYSLGLKRLKLGGWGVLGYATGLALLPGLGA--VAAG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209263382 250 TLTPDIVVLTSLYSIAGLGIAIVNDFKSVEGDRALGLQSLPVAFGMETAKWICVGAIDITQLSVAgyLFSSGKPYYALAL 329
Cdd:cd13956 149 GLVPLALLLALVFLLLGLGINLYNDLPDVEGDRAAGIRTLPVRLGPRRARRLAAGLLLAALILVV--LLAVAGLLGPLAL 226
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 2209263382 330 LGLTIPQVVFQFQYFLKDPVKYDV----KYQASAQPFFVLGLLVT 370
Cdd:cd13956 227 LALLAVALLALRARFARADRLPALprgfLLLAVYRLLLFAALLLA 271
|
|
| UbiA |
pfam01040 |
UbiA prenyltransferase family; |
98-347 |
1.66e-26 |
|
UbiA prenyltransferase family;
Pssm-ID: 460038 [Multi-domain] Cd Length: 250 Bit Score: 106.16 E-value: 1.66e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209263382 98 WPPLVWGVLcgAAASGNFHWTVedvaksIVCMIMSGPCLTGYTQTINDWYDRDIDAINE--PYRPIPSGAISENEVITQI 175
Cdd:pfam01040 2 LIPALAGLA--LAAGGVPDLLL------LLLALLGTVLARAAANALNDYYDRDIDAIMPrtPNRPLPSGRISPREALIFA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209263382 176 WALLLAGLGLGALLDVWAghdfpiiFYLAVGGSLLSYIYSAPplkLKQNGWIGNFALGASYIGLPWWAGQALFGTLTPDI 255
Cdd:pfam01040 74 LVLLALGLLLLLLLNPLT-------ALLGLAALLLYVLYTLR---LKRRTLLGQLVGGLAFGLPPLLGWAAVTGSLSPLA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209263382 256 VVLTSLYSIAGLGIAIVNDFKSVEGDRALGLQSLPVAFGMETAKWICVGAIDITQLSVAGYLFSSGKPYYALALLGLTIP 335
Cdd:pfam01040 144 LLLALALFLWTWAIALANDLRDREDDRKAGIKTLPVVLGRKAARILLALLLAVALLLLLLLLLLLLGGLYLLLALLLAAL 223
|
250
....*....|..
gi 2209263382 336 QVVFQFQYFLKD 347
Cdd:pfam01040 224 ALLYAARLLRLR 235
|
|
| PT_UbiA_DGGGPS |
cd13961 |
Geranylgeranylglycerol-phosphate geranylgeranyltransferase; Digeranylgeranylglyceryl phosphate ... |
126-334 |
8.59e-24 |
|
Geranylgeranylglycerol-phosphate geranylgeranyltransferase; Digeranylgeranylglyceryl phosphate synthase (DGGGPS) transfers a geranylgeranyl group from geranylgeranyl diphosphate to (S)-3-O-geranylgeranylglyceryl phosphate to form (S)-2,3-di-O-geranylgeranylglyceryl phosphate, as part of the isoprenoid ether lipid biosynthesis. Prenyltransferases (PTs) catalyze the regioselective transfer of prenyl moieties onto a wide variety of substrates and play an important role in many biosynthetic pathways.
Pssm-ID: 260124 Cd Length: 270 Bit Score: 99.12 E-value: 8.59e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209263382 126 IVCMIMSGPCLTGYTQTINDWYDRDIDAINEPYRPIPSGAISENEVITQIWALLLAGLGLGALLDvwaghdfPIIFYLAV 205
Cdd:cd13961 37 LLLLFLSVFLIAAAGYIINDYFDVEIDRINKPDRPIPSGRISRREALILSILLNALGLILAFLLS-------PLALLIAL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209263382 206 GGSLLSYIYSApplKLKQNGWIGNFALGASyIGLPWWAGQALFGTLTPDIVVLTSLYSIAGLGIAIVNDFKSVEGDRALG 285
Cdd:cd13961 110 LNSLLLWLYSH---KLKRTPLIGNLLVALL-TGLPFLFGGLAAGNLLLIILLLALFAFLITLGREIVKDIEDVEGDRAEG 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2209263382 286 LQSLPVAFGMETAKWICVGAIDITQLS--VAGYLFSSGKPYYALALLGLTI 334
Cdd:cd13961 186 ARTLPIVYGIKKAKKIAALLLLLAILLspLPYLLGGLGILYLILIIIADLL 236
|
|
| ubiA |
PRK12884 |
prenyltransferase; Reviewed |
136-330 |
4.64e-17 |
|
prenyltransferase; Reviewed
Pssm-ID: 183812 Cd Length: 279 Bit Score: 80.39 E-value: 4.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209263382 136 LTGYTQTINDWYDRDIDAINEPYRPIPSGAISENEVITQIWALLLAGLGLGALLDVWAghdfpiiFYLAVGGSLLSYIYS 215
Cdd:PRK12884 49 ASGSANALNDYFDYEVDRINRPDRPIPSGRISRREALLLAILLFILGLIAAYLISPLA-------FLVVILVSVLGILYN 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209263382 216 ApplKLKQNGWIGNFALgASYIGLPWWAGQALFGTLTPDIVVLTSLYSIAGLGIAIVNDFKSVEGDRALGLQSLPVAFGM 295
Cdd:PRK12884 122 W---KLKEYGLIGNLYV-AFLTGMTFIFGGIAVGELNEAVILLAAMAFLMTLGREIMKDIEDVEGDRLRGARTLAILYGE 197
|
170 180 190
....*....|....*....|....*....|....*.
gi 2209263382 296 ETAKWICVGAIDIT-QLSVAGYLFSSGKPYYALALL 330
Cdd:PRK12884 198 KIAGRIAAALFILAvLLSPLPYLFGIFNILYLAPVL 233
|
|
| ubiA |
PRK12882 |
prenyltransferase; Reviewed |
137-304 |
2.95e-15 |
|
prenyltransferase; Reviewed
Pssm-ID: 183811 Cd Length: 276 Bit Score: 75.01 E-value: 2.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209263382 137 TGYTQTINDWYDRDIDAINEPYRPIPSGAISENEVItqiwalllaglglgalldVWAGHDF-----------PIIFYLAV 205
Cdd:PRK12882 51 TGAGNAINDYFDREIDRINRPDRPIPSGAVSPRGAL------------------AFSILLFaagvalafllpPLCLAIAL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209263382 206 GGSLLSYIYSApplKLKQNGWIGNfALGASYIGLPWWAGQALFGtlTPDIVVLTSLYSIAGLGIA---IVNDFKSVEGDR 282
Cdd:PRK12882 113 FNSLLLVLYAE---TLKGTPGLGN-ASVAYLTGSTFLFGGAAVG--TEGLLALLVLFALAALATLareIIKDVEDIEGDR 186
|
170 180
....*....|....*....|..
gi 2209263382 283 ALGLQSLPVAFGMETAKWICVG 304
Cdd:PRK12882 187 AEGARTLPILIGVRKALYVAAA 208
|
|
| PRK09573 |
PRK09573 |
(S)-2,3-di-O-geranylgeranylglyceryl phosphate synthase; Reviewed |
137-335 |
6.14e-15 |
|
(S)-2,3-di-O-geranylgeranylglyceryl phosphate synthase; Reviewed
Pssm-ID: 181963 Cd Length: 279 Bit Score: 74.23 E-value: 6.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209263382 137 TGYTQTINDWYDRDIDAINEPYRPIPSGAISENEVITQIWALLLAGLGLGALLDVWAghdfpiiFYLAVGGSLLSYIYSa 216
Cdd:PRK09573 50 CAGGNVINDIYDIEIDKINKPERPIPSGRISLKEAKIFSITLFIVGLILSIFINIYA-------FLIALLNSILLYLYA- 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209263382 217 ppLKLKQNGWIGNFaLGASYIGLPWWAGQALFGTLTPdIVVLTSLYSIAGLGIAIVNDFKSVEGDRALGLQSLPVAFGME 296
Cdd:PRK09573 122 --KDLKKTGLIGNL-IVAYLTGLSFIFGGLAVFNVLR-IIILFLCAFFSTWSREIVKDIEDIEGDLKENVITLPIKYGIK 197
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2209263382 297 TAKWICVGAIDITQ-LSVAGYLFSSGKPYYALALLGLTIP 335
Cdd:PRK09573 198 KSWYIAKILLILAIvLSPLPYFLGIFGIYYLIVVIICDIL 237
|
|
| PT_UbiA_HPT1 |
cd13960 |
Tocopherol phytyltransferase; Tocopherol polyprenyltransferase (TPT1), also known as ... |
135-304 |
1.62e-13 |
|
Tocopherol phytyltransferase; Tocopherol polyprenyltransferase (TPT1), also known as homogentisate phytyltransferase 1 (HPT1), tocopherol phytyltransferase, or VTE2, catalyzes the first step in the biosynthesis of the tocopherol forms of vitamin E, which involves the prenylation of homogentisate using phytyl diphosphate (PDP) as the prenyl donor. Prenyltransferases (PTs) catalyze the regioselective transfer of prenyl moieties onto a wide variety of substrates and play an important role in many biosynthetic pathways.
Pssm-ID: 260123 Cd Length: 289 Bit Score: 70.29 E-value: 1.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209263382 135 CLTGYTQTINDWYDRDIDAINEPYRPIPSGAISENEVITQIWALLLAGLGLGALLDVWAghdfpiIFYLAVGGSLLSYIY 214
Cdd:cd13960 49 LGNVYIVGLNQIYDVEIDKINKPYLPLASGELSVRTAWAIVASCGILGLALGALLGSPL------LLTLLLLSLLLGTAY 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209263382 215 SAPPLKLKQngwignFALGASY-----------IGLPWWAGQALFG--TLTPDIVVLTSLYSIAGLGIAIVNDFKSVEGD 281
Cdd:cd13960 123 SVPPPRLKR------FPLLAALciltvrgflvnLGFYLHFQAALGLpfAWPPSLWFLTAFMTVFAIVIALFKDIPDVEGD 196
|
170 180
....*....|....*....|...
gi 2209263382 282 RALGLQSLPVAFGMETAKWICVG 304
Cdd:cd13960 197 RKFGIRTFSVRLGVKRVFWLCVG 219
|
|
| PT_UbiA_UBIAD1 |
cd13962 |
1,4-Dihydroxy-2-naphthoate octaprenyltransferase; Human UBIAD1 is an enzyme involved in the ... |
90-350 |
4.49e-13 |
|
1,4-Dihydroxy-2-naphthoate octaprenyltransferase; Human UBIAD1 is an enzyme involved in the synthesis of MK-4. Menaquinones (MKs, also called bacterial forms) are one of the two forms of natural vitamin K, the other being the plant form, phylloquinone (PK). All forms of vitamin K have a 2-methyl-1,4-naphthoquinone (menadione; K3) ring structure in common. At the 3-position of the ring, PK has a phytyl side chain while MKs have several repeating prenyl units. Prenyltransferases (PTs) catalyze the regioselective transfer of prenyl moieties onto a wide variety of substrates and play an important role in many biosynthetic pathways.
Pssm-ID: 260125 Cd Length: 283 Bit Score: 68.69 E-value: 4.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209263382 90 LQLTKPVTWPPLVWGVLCGAAASgnFHWTVEDVAKSIVCMIMSGPCLTGYTQTINDWYD--RDIDAIN--EPYRPIPSGA 165
Cdd:cd13962 1 LLAARPRTLPASLAPVLLGTALA--YYLGGFFNWLLFLLALLAALLLQIGVNLANDYFDykKGTDTEPrsGPSRVLVSGL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209263382 166 ISENEVITQIWALLLAGLGLGAlldVWAGHDFPIIFYLAVGGSLLSYIYSAPPLKLKQNGWiGNFALGASYIGLPWWAGQ 245
Cdd:cd13962 79 LSPRQVLRAALVLLLLAALLGL---YLVALGGWLLLLLGLLGILAGYFYTGGPFPLSYRGL-GELFVFLFFGLLAVLGTY 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209263382 246 ALF-GTLTPDIVVLTSLYSIAGLGIAIVNDFKSVEGDRALGLQSLPVAFGMETAKWICVGAIDITQLSVAGYLFSSGKPY 324
Cdd:cd13962 155 YVQtGSLSWEVLLAALPLGLLIAAILLANNIRDIEADRAAGKRTLAVRLGRKRARRLYAALLLLAYLLLLLLVLLGLLPL 234
|
250 260
....*....|....*....|....*.
gi 2209263382 325 YALALLgLTIPQVVFQFQYFLKDPVK 350
Cdd:cd13962 235 WSLLAL-LSLPLAIKLLRRLLRKADK 259
|
|
| ubiA |
PRK12883 |
prenyltransferase UbiA-like protein; Reviewed |
142-303 |
2.54e-11 |
|
prenyltransferase UbiA-like protein; Reviewed
Pssm-ID: 171796 Cd Length: 277 Bit Score: 63.59 E-value: 2.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209263382 142 TINDWYDRDIDAINEPYRPIPSGAISENEVITQIWALLLAGLGLGALLDVWAghdfpiiFYLAVGGSLLSYIYSappLKL 221
Cdd:PRK12883 55 TINDYFDYEIDKINRPNRPLPRGAMSRKAALYYSLLLFAVGLALAYLINIEA-------FLFALGAYVLMFLYA---WKL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209263382 222 KQNGWIGNFALGASYIGLPwwagqaLFGTLTPDIVVLTSLYSIAGLGI----AIVNDFKSVEGDRALGLQSLPVAFGMET 297
Cdd:PRK12883 125 KPLPFIGNVVVALLTGATP------IYGAIAVGRIGLAGYLAICAFLVnvarEIMKDIEDIEGDKAKGAKTLPIIIGKKR 198
|
....*.
gi 2209263382 298 AKWICV 303
Cdd:PRK12883 199 AAYIGA 204
|
|
| MenA |
COG1575 |
1,4-dihydroxy-2-naphthoate polyprenyltransferase [Coenzyme transport and metabolism]; 1, ... |
90-371 |
9.04e-11 |
|
1,4-dihydroxy-2-naphthoate polyprenyltransferase [Coenzyme transport and metabolism]; 1,4-dihydroxy-2-naphthoate polyprenyltransferase is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 441183 Cd Length: 290 Bit Score: 62.08 E-value: 9.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209263382 90 LQLTKPVTWPPLVWGVLCGAAAS----GNFHWTVedvakSIVCMImSGPCLTGYTQTINDWYD--RDIDAIN--EPYRPI 161
Cdd:COG1575 3 LEAARPRTLPAAVAPVLLGTALAyyetGSFNWLL-----FLLALL-AALLLQIGVNLANDYFDykKGTDTEErvGPSRVI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209263382 162 PSGAISENEVITQIWALLLAGLGLGALLDVWAGhdfPIIFYLAVGGSLLSYIYSAPPLKLKQNGWiGNFA---------- 231
Cdd:COG1575 77 VSGLLSPKQVLRAALLLLALALLLGLYLVLLSG---WPLLLLGLLGILAAIFYTGGPFPLGYRGL-GELFvflffglvav 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209263382 232 LGASYIglpwwagQAlfGTLTPDIVVLTSLYSIAGLGIAIVNDFKSVEGDRALGLQSLPVAFGMETAKWICVGAIDITQL 311
Cdd:COG1575 153 LGTYYV-------QT--GTLSWAALLASLPVGLLSAAVLLANNLRDIETDRAAGKRTLAVRLGRKRARRLYAALLLLAYL 223
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2209263382 312 SVAGYLFSSGKPYYALALLgLTIPQVVFQFQYFLK--DPVKYDVKYQASAQPFFVLGLLVTA 371
Cdd:COG1575 224 LILLLVLLGLLPPWALLAL-LSLPLALKLVRRVLRgaKPEALIPALKNTALLNLLFGLLLAL 284
|
|
| PT_UbiA_COQ2 |
cd13959 |
4-Hydroxybenzoate polyprenyltransferase; 4-Hydroxybenzoate polyprenyltransferase, also known ... |
98-334 |
1.52e-09 |
|
4-Hydroxybenzoate polyprenyltransferase; 4-Hydroxybenzoate polyprenyltransferase, also known as Coq2, catalyzes the prenylation of p-hydroxybenzoate with an all-trans polyprenyl group, an important step in ubiquinone (CoQ) biosynthesis. Prenyltransferases (PTs) catalyze the regioselective transfer of prenyl moieties onto a wide variety of substrates and play an important role in many biosynthetic pathways.
Pssm-ID: 260122 [Multi-domain] Cd Length: 272 Bit Score: 58.25 E-value: 1.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209263382 98 WPPLVWGVLcgAAASGNFHWTVEDVAKSIVCMIM--SGPCltgytqTINDWYDRDIDAINE--PYRPIPSGAISENEVIT 173
Cdd:cd13959 13 LPPALWGLL--LAAGGLPLPLLKLLLLFLLGAFLmrSAGC------TINDIADRDIDAKVPrtKNRPLASGAISVKEALL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209263382 174 QIWALLLAGLGLGALLDVWAghdfpiiFYLAVGGSLLSYIYS-------APPLklkqngWIGnFALGASYIGlPWWAgqa 246
Cdd:cd13959 85 FLAVQLLLGLALLLQLNPLT-------ILLSPIALLLVLIYPlmkrftyWPQL------VLG-LAFGWGPLM-GWAA--- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209263382 247 lfgtLTPDIVVLTSLYSIAGLGIAIVND----FKSVEGDRALGLQSLPVAFGMETAKWICV-GAIDITQLSVAGYLFSSG 321
Cdd:cd13959 147 ----VTGSLPLPALLLYLAVIFWTAGYDtiyaHQDREDDRKIGVKSTAVLFGDRTKLILALlLHLFVALLLLAGGLAGLG 222
|
250
....*....|...
gi 2209263382 322 KPYYALALLGLTI 334
Cdd:cd13959 223 WPYYLGLGAAAHL 235
|
|
| PT_UbiA_3 |
cd13965 |
UbiA family of prenyltransferases (PTases), Unknown subgroup; Many characterized members of ... |
152-334 |
1.14e-08 |
|
UbiA family of prenyltransferases (PTases), Unknown subgroup; Many characterized members of the UbiA prenyltransferase family are aromatic prenyltransferases and play an important role in the biosynthesis of heme, chlorophyll, vitamin E, and vitamin K. They contain two copies of a motif similar to the active site DxxD motif of trans-prenyltransferases and are potentially related. Prenyltransferases (PTs) catalyze the regioselective transfer of prenyl moieties onto a wide variety of substrates and play an important role in many biosynthetic pathways. The function of this subgroup is unknown.
Pssm-ID: 260128 Cd Length: 273 Bit Score: 55.73 E-value: 1.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209263382 152 DAINEPYRPIPSGAISENEVITQIWALLLAGLGLGALLDVWAghdfPIIFYLAvggslLSYIYSAppLKLKQNGWIGNFA 231
Cdd:cd13965 64 DRINKPWRPIPSGRITPRQARRLRWLLVPLCLALSAYLGVLE----ESLLLIV-----LTWLYNE--LGLADHWLTRNLL 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209263382 232 LGASYIGLPWWAGQ-ALFGTLTPDIVVLTSLYSIAG--LGIAIVNDFKSVEGDRALGLQSLPVAFGMETAKWICVGAIDI 308
Cdd:cd13965 133 NALGYAAFLAGATRiAGGGPHPLDPTAWAWILLSAAiiLTTIHAQDFRDVEGDRARGRRTLPLVFGDAAARWLIAAGVVA 212
|
170 180
....*....|....*....|....*.
gi 2209263382 309 TQLSVAGYLFSSGKPYYALALLGLTI 334
Cdd:cd13965 213 WSVVLPYFWGLPPLLAALLVALGAVV 238
|
|
| ubiA |
PRK12872 |
prenyltransferase; Reviewed |
136-354 |
4.32e-08 |
|
prenyltransferase; Reviewed
Pssm-ID: 237241 Cd Length: 285 Bit Score: 53.79 E-value: 4.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209263382 136 LTGYTqtINDWYDRDIDAINEPYRpipsGAISENEVITQIWALLLAGLGLGALLdVWAGHDFPIIFYLAVGGSLLsYIYS 215
Cdd:PRK12872 50 AAVYI--INYLTDLEEDIINKPER----VVFSETKAYGLFLLLNVLGLYLGAYL-LAVIGGPKFALIFIIPLILG-ILYS 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209263382 216 APPL-KLKQNGWIGNFalgasYIGLPWWAGQALFGTL-----TPDIVVLTSLYSIA-GLGIAIVNDFKSVEGDRALGLQS 288
Cdd:PRK12872 122 VFFKrRLKRIPLFKNL-----VVSLLWALSPLILGVYyyqltIFSLLLLYAVFIFLkSFIREIVFDIKDIEGDRKSGLKT 196
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2209263382 289 LPVAFGMETAKWICVGAIDITQLSVAGYLFSSGKPYYALALLGLTIPqvvfqFQYFLKDPVKYDVK 354
Cdd:PRK12872 197 LPIVLGKERTLKFLLILNLLFLILLILGVYTGLLPLLLLVLLLLLAY-----VLYYIIKLFAADDK 257
|
|
| PT_UbiA_1 |
cd13964 |
UbiA family of prenyltransferases (PTases), Unknown subgroup; Many characterized members of ... |
100-171 |
7.08e-08 |
|
UbiA family of prenyltransferases (PTases), Unknown subgroup; Many characterized members of the UbiA prenyltransferase family are aromatic prenyltransferases and play an important role in the biosynthesis of heme, chlorophyll, vitamin E, and vitamin K. They contain two copies of a motif similar to the active site DxxD motif of trans-prenyltransferases and are potentially related. Prenyltransferases (PTs) catalyze the regioselective transfer of prenyl moieties onto a wide variety of substrates and play an important role in many biosynthetic pathways. The function of this subgroup is unknown.
Pssm-ID: 260127 Cd Length: 282 Bit Score: 53.35 E-value: 7.08e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2209263382 100 PLVWG-VLCGAAASGNFhwtvEDVAKSIVCMIMSGPCLTGYTQTINDWYDRDIDAINEPYRPIPSGAISENEV 171
Cdd:cd13964 11 FTVPAdVLAGAALAGGG----LGPVLRLALLLLASVLLYAAGMVLNDVFDAELDARERPERPIPSGRVSRGAA 79
|
|
| ubiA |
PRK12887 |
tocopherol phytyltransferase; Reviewed |
102-296 |
7.47e-08 |
|
tocopherol phytyltransferase; Reviewed
Pssm-ID: 183813 Cd Length: 308 Bit Score: 53.43 E-value: 7.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209263382 102 VWGVLCGAAASGNFHWTVEDVAKSIVCMImsgPCLTG--YTQTINDWYDRDIDAINEPYRPIPSGAISENEVITQIWALL 179
Cdd:PRK12887 32 VLGLYLIAIAASSNTIALANLGLLLGAWI---ACLCGnvYIVGLNQLTDIEIDRINKPHLPLAAGEFSRRQGQRIVIITG 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209263382 180 LAGLGLGALLDVWAGhdfpiifyLAVGGSLL-SYIYSAPPLKLKQ------------NGWIGNFALGASYIglpWWAGQA 246
Cdd:PRK12887 109 ILALILAALLGPWLL--------ITVGISLLiGTAYSLPPIRLKRfpllaalciftvRGVIVNLGLFLHFQ---WLLGGS 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2209263382 247 lfGTLTPDIVVLTSLYSIAGLGIAIVNDFKSVEGDRALGLQSLPVAFGME 296
Cdd:PRK12887 178 --VLIPPTVWLLTLFVLVFTFAIAIFKDIPDMEGDRQYQITTFTLRLGKQ 225
|
|
| prenyl_rel_EboC |
NF035940 |
UbiA-like protein EboC; |
90-173 |
2.47e-06 |
|
UbiA-like protein EboC;
Pssm-ID: 468273 Cd Length: 292 Bit Score: 48.69 E-value: 2.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209263382 90 LQLTKPVTWPPLVWGVLCGAAASGNFHWTVE--DVAKSIVCMIMSGPCLTGYTQTINDWYDRDIDAINEPYRPIPSGAIS 167
Cdd:NF035940 3 LQLMRPANIVTAWADILAGFAISGFLTLTWSsaPNDISLIWLLLATIGLYGGGVVFNDVFDAELDAVERPERPIPSGRVS 82
|
....*.
gi 2209263382 168 ENEVIT 173
Cdd:NF035940 83 KQAALL 88
|
|
| PT_UbiA_4 |
cd13966 |
UbiA family of prenyltransferases (PTases), Unknown subgroup; Many characterized members of ... |
143-339 |
5.86e-06 |
|
UbiA family of prenyltransferases (PTases), Unknown subgroup; Many characterized members of the UbiA prenyltransferase family are aromatic prenyltransferases and play an important role in the biosynthesis of heme, chlorophyll, vitamin E, and vitamin K. They contain two copies of a motif similar to the active site DxxD motif of trans-prenyltransferases and are potentially related. Prenyltransferases (PTs) catalyze the regioselective transfer of prenyl moieties onto a wide variety of substrates and play an important role in many biosynthetic pathways. The function of this subgroup is unknown.
Pssm-ID: 260129 Cd Length: 272 Bit Score: 47.26 E-value: 5.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209263382 143 INDWYDRDIDAINePYRPIPSGAISENEVITQIWALLLAGLGLGALLDVWAGhDFPIIFYLAVGGsLLSYIYSAPPLKLK 222
Cdd:cd13966 52 VNDVFDYESDARN-PRKGGIEGALLDPAEHRPLLWAVAVSNVPFLLYLVLVG-PPAALLLLALFL-FLVVAYSAPPLRFK 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209263382 223 QNGWIgNFALGASYIGLPWWAGQALFGTLTP-DIVVLTSLYSIAGLGIAIVNDfksVEGDRALGLQSLPVAFGMETAKWI 301
Cdd:cd13966 129 ERPFL-DSLSNGLYFLPPALVGLLASGTLPPwLALAAFFLWGMAMHAFGAIQD---IEADREAGIRTTATVLGARGTLRL 204
|
170 180 190
....*....|....*....|....*....|....*...
gi 2209263382 302 CVGAiditqLSVAGYLFSSGKPYYALALLGLTIPQVVF 339
Cdd:cd13966 205 ALAL-----WLLAAVLVLPLSLPLPLSYLALVYPAISL 237
|
|
| PRK04375 |
PRK04375 |
protoheme IX farnesyltransferase; Provisional |
86-173 |
4.18e-05 |
|
protoheme IX farnesyltransferase; Provisional
Pssm-ID: 235293 Cd Length: 296 Bit Score: 44.75 E-value: 4.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209263382 86 WKIRLQLTKPVTWPPLVWGVLCGA--AASGNFHWTVedvaksIVCMIMSGPCLTGYTQTINDWYDRDIDAI-----Nepy 158
Cdd:PRK04375 10 LKDYLALTKPRVISLNLFTALGGMllAPPGVPPLLL------LLLTLLGIALVAGAAGALNNYIDRDIDAKmertkN--- 80
|
90
....*....|....*
gi 2209263382 159 RPIPSGAISENEVIT 173
Cdd:PRK04375 81 RPLVTGRISPREALI 95
|
|
| PLN02878 |
PLN02878 |
homogentisate phytyltransferase |
135-304 |
5.48e-05 |
|
homogentisate phytyltransferase
Pssm-ID: 178466 Cd Length: 280 Bit Score: 44.31 E-value: 5.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209263382 135 CLTGYTQTINDWYDRDIDAINEPYRPIPSGAISeneVITQIwalllAGLGLGALLDVWAGHDF---PIIFYLAVGgSLLS 211
Cdd:PLN02878 34 LMNIYIVGLNQLYDIEIDKVNKPYLPLASGEFS---VATGV-----AIVTSFAIMSFGMGWIVgswPLFWALFVS-FVLG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209263382 212 YIYSA--PPLKLKQNGWIGNF---ALGASYIGLPWWA--GQALFG---TLTPDIVVLTSLYSIAGLGIAIVNDFKSVEGD 281
Cdd:PLN02878 105 TAYSInlPLLRWKRSAVAAAScilAVRAVVVQLAFFLhmQTHVLGrpaVFTRPLIFATAFMCFFSVVIALFKDIPDVEGD 184
|
170 180
....*....|....*....|...
gi 2209263382 282 RALGLQSLPVAFGMETAKWICVG 304
Cdd:PLN02878 185 RIFGIRSFSVRLGQKRVFWLCVN 207
|
|
| PT_UbiA_Cox10 |
cd13957 |
Protoheme IX farnesyltransferase; Protoheme IX farnesyltransferase (also called heme O ... |
90-173 |
3.41e-04 |
|
Protoheme IX farnesyltransferase; Protoheme IX farnesyltransferase (also called heme O synthase, heme A:farnesyltransferase, cytochrome c oxidase subunit X [Cox10]) converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of the heme B porphyrin ring with a hydroxyethyl farnesyl side group. It is localized at the mitochondrial inner membrane. Eukaryotic Cox10 is important for the maturation of the heme A prosthetic group of cytochrome c oxidase (COX), the terminal component of the mitochondrial respiratory chain, that catalyzes the electron transfer from reduced cytochrome c to oxygen. Prenyltransferases (PTs) catalyze the regioselective transfer of prenyl moieties onto a wide variety of substrates and play an important role in many biosynthetic pathways.
Pssm-ID: 260120 Cd Length: 271 Bit Score: 42.04 E-value: 3.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209263382 90 LQLTKPvtwpPLVWGVL----CGAAASGNFHWTVEDVAKSIVCMIMSgpclTGYTQTINDWYDRDIDAI-----NepyRP 160
Cdd:cd13957 1 LELTKP----RITLLVLltalAGYLLAPGGVPDLLLLLLTLLGTALV----SASANALNQYIERDIDAKmkrtrN---RP 69
|
90
....*....|...
gi 2209263382 161 IPSGAISENEVIT 173
Cdd:cd13957 70 LPSGRISPKHALI 82
|
|
| PLN02809 |
PLN02809 |
4-hydroxybenzoate nonaprenyltransferase |
142-326 |
4.76e-04 |
|
4-hydroxybenzoate nonaprenyltransferase
Pssm-ID: 178405 Cd Length: 289 Bit Score: 41.60 E-value: 4.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209263382 142 TINDWYDRDIDAINE--PYRPIPSGAISEneviTQIWALLLAGLGLGALLDVWAGHdfpiiFYLAVGGSLLSYIYSAPPL 219
Cdd:PLN02809 63 TINDLLDRDIDKKVErtKLRPIASGALTP----FQGVGFLGAQLLLGLGILLQLNN-----YSRILGASSLLLVFTYPLM 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209263382 220 KLKQN---GWIG-NFALGAsyigLPWWAgqALFGTLTPDIVVltSLYsIAGLGIAIVND----FKSVEGDRALGLQSLPV 291
Cdd:PLN02809 134 KRFTFwpqAFLGlTFNWGA----LLGWA--AVKGSLDPAVVL--PLY-ASGVCWTLVYDtiyaHQDKEDDLKVGVKSTAL 204
|
170 180 190
....*....|....*....|....*....|....*.
gi 2209263382 292 AFGMETAKWIC-VGAIDITQLSVAGYLFSSGKPYYA 326
Cdd:PLN02809 205 RFGDDTKLWLTgFGAASIGGLALSGYNAGLGWPYYA 240
|
|
| PLN02922 |
PLN02922 |
prenyltransferase |
209-369 |
5.60e-04 |
|
prenyltransferase
Pssm-ID: 215499 Cd Length: 315 Bit Score: 41.26 E-value: 5.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209263382 209 LLSYIYSAPPLKLKQNGW--------IGNFALGASYIGLPWWAGQALFGT--LTPDIVVLTSLYSIAGLGIAIVNDFKSV 278
Cdd:PLN02922 134 LCGYVYQCPPFRLSYKGLgeplcfaaFGPLATTAFYLALASGAGGSEMAIlpLTPTVLSASVLVGLTTTLILFCSHFHQI 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209263382 279 EGDRALGLQSLPVAFGMETAKWICVGAIDITQLSVAGYLFSSGKPYYALALLGLTIPQVVFQFQYFLK---DPVK----- 350
Cdd:PLN02922 214 DGDRAVGKMSPLVRLGTEKGSRVVRWAVLLLYSLLAALGLLKALPLPCALLCFLTLPLGKLVVDFVEKnhkDNAKifmak 293
|
170 180
....*....|....*....|
gi 2209263382 351 -YDVKYQASAQPFFVLGLLV 369
Cdd:PLN02922 294 yYCVRLHALFGAALALGLVL 313
|
|
| PT_UbiA_5 |
cd13967 |
UbiA family of prenyltransferases (PTases), Unknown subgroup; Many characterized members of ... |
197-301 |
1.29e-03 |
|
UbiA family of prenyltransferases (PTases), Unknown subgroup; Many characterized members of the UbiA prenyltransferase family are aromatic prenyltransferases and play an important role in the biosynthesis of heme, chlorophyll, vitamin E, and vitamin K. They contain two copies of a motif similar to the active site DxxD motif of trans-prenyltransferases and are potentially related. Prenyltransferases (PTs) catalyze the regioselective transfer of prenyl moieties onto a wide variety of substrates and play an important role in many biosynthetic pathways. The function of this subgroup is unknown.
Pssm-ID: 260130 Cd Length: 277 Bit Score: 40.29 E-value: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209263382 197 FPIIFYLaVGGSLLSYIYSAP--PLKLKQNGWIGNFALGASYIGLPWWAGQALFG-----TLTPDIVVLTSLYSIAGLGI 269
Cdd:cd13967 98 LLAFAIL-LLPLLLGLLYSLPikPGKLRLRRRKDIPGSKNLVVALAWAVVIALLPalygqPSTPSVLVVFLFFFLKVFVN 176
|
90 100 110
....*....|....*....|....*....|..
gi 2209263382 270 AIVNDFKSVEGDRALGLQSLPVAFGMETAKWI 301
Cdd:cd13967 177 TAIFDIRDVEGDRIVGIETLPVLLGEERTRLL 208
|
|
| cyoE_ctaB |
TIGR01473 |
protoheme IX farnesyltransferase; This model describes protoheme IX farnesyltransferase, also ... |
87-372 |
1.45e-03 |
|
protoheme IX farnesyltransferase; This model describes protoheme IX farnesyltransferase, also called heme O synthase, an enzyme that creates an intermediate in the biosynthesis of heme A. Prior to the description of its enzymatic function, this protein was often called a cytochrome o ubiquinol oxidase assembly factor. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]
Pssm-ID: 273645 Cd Length: 280 Bit Score: 39.92 E-value: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209263382 87 KIRLQLTKPVTWPPLVWGVLCGAAASGNFHWTVEDVaksIVCMIMSGPCLTGYTQTINDWYDRDIDAINE--PYRPIPSG 164
Cdd:TIGR01473 1 KDYLQLTKPRIISLLLITAFAGMWLAPGGALVNPPL---LLLTLLGTTLAAASANAFNMYIDRDIDKKMKrtRNRPLVTG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209263382 165 AISENEVITqiwalLLAGLGLGALLDVWAGHDFPIIFYLAVGGSLLSYIYSApPLKLK--QNGWIGNFAlGAsyigLPWW 242
Cdd:TIGR01473 78 RISPREALA-----FGLLLGVLGVAILAAFVNPLAALLGLFGIFFYVIVYTI-WLKRRtpQNTVIGGFA-GA----VPPL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209263382 243 AG-QALFGTLTPDIVVLTSLYSI------AGLGIAIVNDFksvegdRALGLQSLPVAFGMETAKW-ICVGAIDITQLSVA 314
Cdd:TIGR01473 147 IGwAAVTGSISLGAWLLFAIIFLwqpphfWALALKYKDDY------RAAGIPMLPVVKGERITKRqIALYTAALLPVSLL 220
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 2209263382 315 GYLFSSGKPYYALALLGLTIPQVVFQFQyFLKDPVKydvkyQASAQPFFVLGLLVTAL 372
Cdd:TIGR01473 221 LAFLGGTGWLYLIVATLLGALFLYLAFK-FYRDPTD-----RKKARKLFKFSLIYLAL 272
|
|
| ubiA |
PRK12875 |
prenyltransferase; Reviewed |
143-304 |
3.90e-03 |
|
prenyltransferase; Reviewed
Pssm-ID: 237243 Cd Length: 282 Bit Score: 38.87 E-value: 3.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209263382 143 INDWYDRDIDAIN----EPYRPIPSG--AISENEVITQIWALLLAGLGLGALLDVWAGHDFpiifylavggslLSYIYSA 216
Cdd:PRK12875 64 VNDVFDADTDELNpkkdREREVRYRGdrRVLVAVALSGALALAFLLVLPPAAWPALLAFLV------------LSVEYSA 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209263382 217 PPLKLKQNGWIgNFALGASYIgLPWWAGQALF-GTLTPDIVVLTSLYSIAGLGI--AIVNdfksVEGDRALGLQSLPVAF 293
Cdd:PRK12875 132 PPLRFKTTPVL-DSLSNGLYI-LPGVAAYALVsGSLPPLLAVAGGWLWAMGMHTfsAIPD----IEPDRAAGIRTTATVL 205
|
170
....*....|.
gi 2209263382 294 GMETAKWICVG 304
Cdd:PRK12875 206 GERRTYAYCAA 216
|
|
| ubiA |
PRK12886 |
prenyltransferase; Reviewed |
144-334 |
4.13e-03 |
|
prenyltransferase; Reviewed
Pssm-ID: 237247 Cd Length: 291 Bit Score: 38.52 E-value: 4.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209263382 144 NDWYDRDIDAINE--PYRPIPSGAISENEVITQIWALLLAGLGLGALLDvwaghdfPIIFYLA--VGGSLLSYIYSappl 219
Cdd:PRK12886 62 NRLIDAEIDARNPrtAGRAIPAGLISKGSAILFIVLSSLLMLFAAWFLN-------PLCLYLSppALFFLLLYSYC---- 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209263382 220 klKQNGWIGNFALGASYIGLPWWAGQALFGTLTPDIVVLT--SLYSIAGLGIAIVndFKSVEGDRALGLQSLPVAFGMET 297
Cdd:PRK12886 131 --KRFTALAHVVLGFCLALAPLGAWIAIRGTIELPAILLGlaVLFWVAGFDILYA--LQDLEFDRKEGLHSIPAKLGVNG 206
|
170 180 190
....*....|....*....|....*....|....*..
gi 2209263382 298 AKWICVGAIDITQLSVAGYLFSSGKPYYALALLGLTI 334
Cdd:PRK12886 207 SLWIARVFHLLMIGFLFALGISAGLGPWFLAGLAVTG 243
|
|
| |
