|
Name |
Accession |
Description |
Interval |
E-value |
| ubiA |
PRK12887 |
tocopherol phytyltransferase; Reviewed |
1-300 |
2.88e-163 |
|
tocopherol phytyltransferase; Reviewed
Pssm-ID: 183813 Cd Length: 308 Bit Score: 456.35 E-value: 2.88e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402797847 1 MATIQAFWRFSRPHTIIGTTLSVWAVYLLTILGDGNSVNSpASLDLVFGAWLACLLGNVYIVGLNQLWDVDIDRINKPNL 80
Cdd:PRK12887 10 TSWLYALWKFSRPHTIIGTSLSVLGLYLIAIAASSNTIAL-ANLGLLLGAWIACLCGNVYIVGLNQLTDIEIDRINKPHL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402797847 81 PLANGDFSIAQGRWIVGLCGVASLAIAWGLGLWLGLTVGISLIIGTAYSVPPVRLKRFSLLAALCILTVRGIVVNLGLFL 160
Cdd:PRK12887 89 PLAAGEFSRRQGQRIVIITGILALILAALLGPWLLITVGISLLIGTAYSLPPIRLKRFPLLAALCIFTVRGVIVNLGLFL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402797847 161 FFRIGLGYPPTLITPIWVLTLFILVFTVAIAIFKDVPDMEGDRQFKIQTLTLQIGKQNVFRGTLILLTGCYLAMAIWGLW 240
Cdd:PRK12887 169 HFQWLLGGSVLIPPTVWLLTLFVLVFTFAIAIFKDIPDMEGDRQYQITTFTLRLGKQAVFKLSCWVLTACYLGMIAVGLL 248
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 402797847 241 AAMPLNTAFLIVSHLCLLALLWWRSRDVHLESKTEIASFYQFIWKLFFLEYLLYPLALWL 300
Cdd:PRK12887 249 SLPTVNPAFLIVSHLILLALLWWRSQRVDLQDKQAIAQFYQFIWKLFFLEYLLFPIACLL 308
|
|
| PT_UbiA_HPT1 |
cd13960 |
Tocopherol phytyltransferase; Tocopherol polyprenyltransferase (TPT1), also known as ... |
7-295 |
1.73e-133 |
|
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: 380.37 E-value: 1.73e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402797847 7 FWRFSRPHTIIGTTLSVWAVYLLTILGDGNSVNSpASLDLVFGAWLACLLGNVYIVGLNQLWDVDIDRINKPNLPLANGD 86
Cdd:cd13960 1 FWKFSRPHTIIGTILSVTSLSLLALESNSDLLLL-FLLPGALQALVALLLGNVYIVGLNQIYDVEIDKINKPYLPLASGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402797847 87 FSIAQGRWIVGLCGVASLAIAWGLGLWLGLTVGI-SLIIGTAYSVPPVRLKRFSLLAALCILTVRGIVVNLGLFLFFRIG 165
Cdd:cd13960 80 LSVRTAWAIVASCGILGLALGALLGSPLLLTLLLlSLLLGTAYSVPPPRLKRFPLLAALCILTVRGFLVNLGFYLHFQAA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402797847 166 LGYPPTLITPIWVLTLFILVFTVAIAIFKDVPDMEGDRQFKIQTLTLQIGKQNVFRGTLILLTGCYLAMAIWGLWAAMPL 245
Cdd:cd13960 160 LGLPFAWPPSLWFLTAFMTVFAIVIALFKDIPDVEGDRKFGIRTFSVRLGVKRVFWLCVGLLLMNYAGAILVGLTSPALF 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 402797847 246 NTAFLIVSHLCLLALLWWRSRDVHLESKTEIASFYQFIWKLFFLEYLLYP 295
Cdd:cd13960 240 SKIFMVVGHAVLAAVLWYRSKRVDLESKESIYSFYMFIWKLFYAEYLLLP 289
|
|
| PLN02878 |
PLN02878 |
homogentisate phytyltransferase |
21-296 |
2.42e-70 |
|
homogentisate phytyltransferase
Pssm-ID: 178466 Cd Length: 280 Bit Score: 219.57 E-value: 2.42e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402797847 21 LSVWAVYLLTIlgDGNSVNSPASLDLVFGAWLACLLGNVYIVGLNQLWDVDIDRINKPNLPLANGDFSIAQGRWIVGLCG 100
Cdd:PLN02878 1 LGITSVSLLAV--ESLSDFSPLFFTGLLEALVPALLMNIYIVGLNQLYDIEIDKVNKPYLPLASGEFSVATGVAIVTSFA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402797847 101 VASLAIAWGLGLW-LGLTVGISLIIGTAYSV--PPVRLKRFSLLAALCILTVRGIVVNLGLFLFFRIG-LGYPPTLITPI 176
Cdd:PLN02878 79 IMSFGMGWIVGSWpLFWALFVSFVLGTAYSInlPLLRWKRSAVAAASCILAVRAVVVQLAFFLHMQTHvLGRPAVFTRPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402797847 177 WVLTLFILVFTVAIAIFKDVPDMEGDRQFKIQTLTLQIGKQNVFRGTLILLTGCYLAMAIWGLWAAMPLNTAFLIVSHLC 256
Cdd:PLN02878 159 IFATAFMCFFSVVIALFKDIPDVEGDRIFGIRSFSVRLGQKRVFWLCVNLLEMAYAAAILVGASSSFLWSKIITVLGHGI 238
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 402797847 257 LLALLWWRSRDVHLESKTEIASFYQFIWKLFFLEYLLYPL 296
Cdd:PLN02878 239 LASILWQRAQSVDLSSKAAITSFYMFIWKLFYAEYFLIPL 278
|
|
| UbiA |
COG0382 |
4-hydroxybenzoate polyprenyltransferase [Coenzyme transport and metabolism]; 4-hydroxybenzoate ... |
5-266 |
1.00e-33 |
|
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: 124.57 E-value: 1.00e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402797847 5 QAFWRFSRPHTIIGTTLSVWAVYLLTILgdgnSVNSPASLDLVFGAWLACLLGNVYIVGLNQLWDVDIDRIN--KPNLPL 82
Cdd:COG0382 1 RAYLRLLRLDRPIGILLLLWPTLWALFL----AAGGLPDLLLLLLAVLGTVLMRSAGYVINDYFDREIDRINerKPNRPL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402797847 83 ANGDFSIAQGRWIVGLCGVASLAIAWGLGLWLGLTVGISLIIGTAYsvpPVRLKRFSLLAALCILTVRGIVVNLGLFLFF 162
Cdd:COG0382 77 ASGRISLREALLLAIVLLLLALALALLLNPLTFLLALAALALAWAY---SLFLKRFTLLGNLVLGLLFGLGILMGFAAVT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402797847 163 RiglgyppTLITPIWVLTLFILVFTVAIAIFKDVPDMEGDRQFKIQTLTLQIGKQNVFRGTLILLTGCYLAMAIWGLWAa 242
Cdd:COG0382 154 G-------SLPLSAWLLALAAFLWTLAYDTIYDLEDREGDRKIGIKTLAILFGVRDALIIAGVLYALAVLLLLLLGLLA- 225
|
250 260
....*....|....*....|....
gi 402797847 243 mPLNTAFLIVshLCLLALLWWRSR 266
Cdd:COG0382 226 -GLGLLYLLG--LLAALLLLYLSQ 246
|
|
| UbiA |
pfam01040 |
UbiA prenyltransferase family; |
37-286 |
6.90e-30 |
|
UbiA prenyltransferase family;
Pssm-ID: 460038 [Multi-domain] Cd Length: 250 Bit Score: 113.48 E-value: 6.90e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402797847 37 SVNSPASLDLVFGAWLACLLGNVYIVGLNQLWDVDIDRI--NKPNLPLANGDFSIAQGRWIVGLCGVASLAIAWGLGLWL 114
Cdd:pfam01040 12 AAGGVPDLLLLLLALLGTVLARAAANALNDYYDRDIDAImpRTPNRPLPSGRISPREALIFALVLLALGLLLLLLLNPLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402797847 115 GLTVGISLIIGTAYSVppvRLKRFSLLAALCILTVRGIVVNLGLFLFFriglgypPTLITPIWVLTLFILVFTVAIAIFK 194
Cdd:pfam01040 92 ALLGLAALLLYVLYTL---RLKRRTLLGQLVGGLAFGLPPLLGWAAVT-------GSLSPLALLLALALFLWTWAIALAN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402797847 195 DVPDMEGDRQFKIQTLTLQIGKQNVFRGTLILLTGCYLAMAIWGLWAAMPLntaFLIVSHLCLLALLWWRSRDVHLESKT 274
Cdd:pfam01040 162 DLRDREDDRKAGIKTLPVVLGRKAARILLALLLAVALLLLLLLLLLLLGGL---YLLLALLLAALALLYAARLLRLRDPK 238
|
250
....*....|..
gi 402797847 275 EIASFYQFIWKL 286
Cdd:pfam01040 239 KDAKAFFFLSSL 250
|
|
| PT_UbiA |
cd13956 |
UbiA family of prenyltransferases (PTases); Many characterized members of the UbiA ... |
8-270 |
9.14e-21 |
|
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: 89.71 E-value: 9.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402797847 8 WRFSRPHTIIGTTLSVWAVYLLTILGDgnsvnsPASLDLVFGAWLACLLGNVYIVGLNQLWDVDIDRINKPNLPLANGDF 87
Cdd:cd13956 1 LRLMRPYTLLYVLAPALAGAALAGAFA------GPLPALLLLALLAVFLGAGAGYALNDYTDRELDAINKPDRPLPSGRL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402797847 88 SIAQGRWIVGLCGVASLAIAWGLGLWLGLTVGISLIIGTAYSVPPVRLKRFSLLaalciltVRGIVVnlGLFLFFRIGLG 167
Cdd:cd13956 75 SPRQALAFAAALLLVGLALALALGPLALLLLLAGLLLGLAYSLGLKRLKLGGWG-------VLGYAT--GLALLPGLGAV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402797847 168 YPPTLITPIWVLTLFILVFTVAIAIFKDVPDMEGDRQFKIQTLTLQIGKqnvfRGTLILLTGCYLAMAIWGLWAAMPLNT 247
Cdd:cd13956 146 AAGGLVPLALLLALVFLLLGLGINLYNDLPDVEGDRAAGIRTLPVRLGP----RRARRLAAGLLLAALILVVLLAVAGLL 221
|
250 260
....*....|....*....|...
gi 402797847 248 AFLIVSHLCLLALLWWRSRDVHL 270
Cdd:cd13956 222 GPLALLALLAVALLALRARFARA 244
|
|
| PT_UbiA_DGGGPS |
cd13961 |
Geranylgeranylglycerol-phosphate geranylgeranyltransferase; Digeranylgeranylglyceryl phosphate ... |
6-286 |
2.12e-17 |
|
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: 80.24 E-value: 2.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402797847 6 AFWRFSRPHTIIGTTLSVWAVYLLtILGDGNSVNSPASLDLVFGAWLACLLGNVyivgLNQLWDVDIDRINKPNLPLANG 85
Cdd:cd13961 1 AYLELIRPPNLLMAALAQYLGALF-ALGPLLSLNDLELLLLFLSVFLIAAAGYI----INDYFDVEIDRINKPDRPIPSG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402797847 86 DFSIAQGRWIVGLCGVASLAIAWGLGLWLGLTVGISLIIGTAYSvppVRLKRFSLLAALciltvrgIVVNLGLFLFFRIG 165
Cdd:cd13961 76 RISRREALILSILLNALGLILAFLLSPLALLIALLNSLLLWLYS---HKLKRTPLIGNL-------LVALLTGLPFLFGG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402797847 166 LGYPPTLITpIWVLTLFILVFTVAIAIFKDVPDMEGDRQFKIQTLTLQIGKQNvfrgTLILLTGCYLAMAIWGLWAAM-- 243
Cdd:cd13961 146 LAAGNLLLI-ILLLALFAFLITLGREIVKDIEDVEGDRAEGARTLPIVYGIKK----AKKIAALLLLLAILLSPLPYLlg 220
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 402797847 244 PLNTAFLIVSHLCLLALLWWRSRdvhLESKTEIASFYQFIWKL 286
Cdd:cd13961 221 GLGILYLILIIIADLLFLYSAIR---LAKSPKDYSKLSKLLKL 260
|
|
| PT_UbiA_chlorophyll |
cd13958 |
Bacteriochlorophyll/chlorophyll synthetase; Chlorophyll synthase catalyzes the last step of ... |
23-250 |
2.32e-15 |
|
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: 74.57 E-value: 2.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402797847 23 VWAVyLLTILGDGNSV-NSPASLDLVFGAWLACLLGNVYIVGLNQLWDVDIDRINKPNLPLANGDFSIAQGRWIVGLCGV 101
Cdd:cd13958 14 MWAF-LCGAAASGAFQwSNWDVWLLLLGMLLAGPLLTGTSQTINDYYDREVDAINEPYRPIPSGRISEREALWNIWVLLL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402797847 102 ASLAIAWGL-GLWLGLTVGISLIIGTAYSVPPVRLKRFSLL-AALCILTVRGIVVNLGLFLFfriglgyPPTLITPIWVL 179
Cdd:cd13958 93 LSLLVALFLdGPWVFAAAVVGLVLAYIYSAPPLKLKQNGWWgNAAVGLSYEGLPWWAGAAAF-------AGLLTWESLAL 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 402797847 180 TLFILVFTVAIAIFKDVPDMEGDRQFKIQTLTLQIGKQNVFRGTLILLTGCYLAMAIWGLWAAMPLNTAFL 250
Cdd:cd13958 166 ALLYSIGAHGIMTLNDFKSIEGDRQLGLRSLPVALGVDTAAWIACGVIDVPQLAVAALLLAWGETWYAAVV 236
|
|
| ubiA |
PRK12882 |
prenyltransferase; Reviewed |
1-240 |
5.32e-15 |
|
prenyltransferase; Reviewed
Pssm-ID: 183811 Cd Length: 276 Bit Score: 73.47 E-value: 5.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402797847 1 MATIQAFWRFSRPHTIIgttlsvwAVYLLTILG---DGNSVNSPASLDLVFGA-WLACLLGNVyivgLNQLWDVDIDRIN 76
Cdd:PRK12882 1 GMTVRGYLELTRPVNAV-------VAGVAAFIGafiAGGILSSPSLTGLAFAAvFLATGAGNA----INDYFDREIDRIN 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402797847 77 KPNLPLANGDFSIAQGRWIVGLCGVASLAIAWGLGLWLGLTVGISLIIGTAYSvppVRLKRFSLLAALCILTVRGIVvnl 156
Cdd:PRK12882 70 RPDRPIPSGAVSPRGALAFSILLFAAGVALAFLLPPLCLAIALFNSLLLVLYA---ETLKGTPGLGNASVAYLTGST--- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402797847 157 glFLFFRIGLGypptLITPIWVLTLFILVF--TVAIAIFKDVPDMEGDRQFKIQTLTLQIGKQNVFRGTLILLTGCYLA- 233
Cdd:PRK12882 144 --FLFGGAAVG----TEGLLALLVLFALAAlaTLAREIIKDVEDIEGDRAEGARTLPILIGVRKALYVAAAFLLVAVAAs 217
|
250
....*....|..
gi 402797847 234 -----MAIWGLW 240
Cdd:PRK12882 218 plpylLSTFGLW 229
|
|
| PRK07566 |
PRK07566 |
chlorophyll synthase ChlG; |
64-252 |
1.52e-14 |
|
chlorophyll synthase ChlG;
Pssm-ID: 236052 Cd Length: 314 Bit Score: 72.65 E-value: 1.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402797847 64 LNQLWDVDIDRINKPNLPLANGDFSIAQGRWIVGLCGVASLAIAWGLGLWLGLTVGISLIIGTAYSVPPVRLKRFSLLA- 142
Cdd:PRK07566 84 LNDYFDREVDAINEPYRPIPSGAISLRWVLYLIAVLTVLGLAVAYLLGPWVFLAALLGLFLAWIYSAPPLRLKQNGWLGn 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402797847 143 ALCILTVRGIVVNLGLFLFfriglgYPPTLITPIWVLTLFILVFTVAIAIFKDVPDMEGDRQFKIQTLTLQIGKQNVFRG 222
Cdd:PRK07566 164 YAVGLSYEGLPWWAGAAAF------GAGLPSWPIVILALLYSLGAHGIMTLNDFKSVEGDRQLGLRSLPVVFGEKNAARI 237
|
170 180 190
....*....|....*....|....*....|
gi 402797847 223 TLILLTGCYLAMAIWGLWAAMPLNTAFLIV 252
Cdd:PRK07566 238 ACVVIDLFQLAVIALLLAWGQPLYAAIVGL 267
|
|
| ubiA |
PRK12884 |
prenyltransferase; Reviewed |
1-217 |
4.26e-14 |
|
prenyltransferase; Reviewed
Pssm-ID: 183812 Cd Length: 279 Bit Score: 71.14 E-value: 4.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402797847 1 MATIQAFWRFSRP-HTIIgttlSVWAVYLLTILGDGNSVNSPASLDLVfGAWLACLLGNVyivgLNQLWDVDIDRINKPN 79
Cdd:PRK12884 1 RTKMKAYLELLRPeHGLM----AGIAVVLGAIIALGGLPLDEALLGFL-TAFFASGSANA----LNDYFDYEVDRINRPD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402797847 80 LPLANGDFSIAQGRWIVGLCGVASLAIAWGLGLWLGLTVGISLIIGTAYSvppVRLKRFSLLAALCILTVRGIVvnlglF 159
Cdd:PRK12884 72 RPIPSGRISRREALLLAILLFILGLIAAYLISPLAFLVVILVSVLGILYN---WKLKEYGLIGNLYVAFLTGMT-----F 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 402797847 160 LFFRIGLGYPPTLitpIWVLTLFILVFTVAIAIFKDVPDMEGDRQFKIQTLTLQIGKQ 217
Cdd:PRK12884 144 IFGGIAVGELNEA---VILLAAMAFLMTLGREIMKDIEDVEGDRLRGARTLAILYGEK 198
|
|
| PRK12392 |
PRK12392 |
bacteriochlorophyll c synthase; Provisional |
56-252 |
1.43e-09 |
|
bacteriochlorophyll c synthase; Provisional
Pssm-ID: 171463 Cd Length: 331 Bit Score: 58.16 E-value: 1.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402797847 56 LGNVYIVGLNQLWDVDIDRINKPNLPLANGDFSIAQGRW---IVGLcgvaslaIAWGLGLWLGLTVG------------I 120
Cdd:PRK12392 61 LGTGFSQSVNDYFDLELDRVNEPTRPIPSGRLSEKEALWnsiIVLL-------LAIGLGVWLGLHIGgergmviissilA 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402797847 121 SLIIGTAYSVPPVRLKRFSLLAAlciltvRGIVVNLGLFLFFRIGLGYPPTLITPIWVLTLFILVfTVAIAIFKDVPDME 200
Cdd:PRK12392 134 GLFVAYIYSAPPLKLKKNILTSA------PAVGFSYGFITFLSANALFSDIRPEVVWLAGLNFFM-AIALIIMNDFKSVE 206
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 402797847 201 GDRQFKIQTLTLQIGKQNVFRGTLILLTGCYLAMAI----WGLWAAMPLNTAFLIV 252
Cdd:PRK12392 207 GDKEGGLKSLTVMIGAKNTFLVSFIIIDLVFAVFAWlawsWGFTVLMYFILVGLVL 262
|
|
| PT_UbiA_4 |
cd13966 |
UbiA family of prenyltransferases (PTases), Unknown subgroup; Many characterized members of ... |
8-299 |
4.62e-09 |
|
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: 56.12 E-value: 4.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402797847 8 WRFSRPHTIIGTTLSVWAVYLLTilGDGNSVNSPAsldLVFGAWLaCLLGNVYIVGLNQLWDVDIDRINK-------PNL 80
Cdd:cd13966 2 LKVSRPRFWINTAGPFAVGYLLA--GSGFDDLLRL---ILGLLYF-LFPANLLIYGVNDVFDYESDARNPrkggiegALL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402797847 81 PLANGDFSIaqgRWIVGLCGVASLAIAWGLGLWLGLTVGISLIIGTAYSVPPVRLKRFSLLAALciltvrgivvNLGLFL 160
Cdd:cd13966 76 DPAEHRPLL---WAVAVSNVPFLLYLVLVGPPAALLLLALFLFLVVAYSAPPLRFKERPFLDSL----------SNGLYF 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402797847 161 FFRIGLGYPPTLITPIWVLTLFILVFTVAIAIFKDVPDMEGDRQFKIQTLTLQIGKqnvfRGTLILLTGCYLAMAIWGLW 240
Cdd:cd13966 143 LPPALVGLLASGTLPPWLALAAFFLWGMAMHAFGAIQDIEADREAGIRTTATVLGA----RGTLRLALALWLLAAVLVLP 218
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 402797847 241 AAMPLNTAFLivshlcLLALLWWRSRDVHLESKTEIASFYqFIWKLFFLEYLLYPLALW 299
Cdd:cd13966 219 LSLPLPLSYL------ALVYPAISLADALAGRTNPRGYWR-FPWINTVVGFVLTVLLIW 270
|
|
| PLN00012 |
PLN00012 |
chlorophyll synthetase; Provisional |
54-215 |
1.46e-08 |
|
chlorophyll synthetase; Provisional
Pssm-ID: 215028 Cd Length: 375 Bit Score: 55.26 E-value: 1.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402797847 54 CLLGnvYIVGLNQLWDVDIDRINKPNLPLANGDFS----IAQgRWIVGLCGvasLAIAWGLGLWLG--------LTVGIS 121
Cdd:PLN00012 134 FLTG--YTQTINDWYDREIDAINEPYRPIPSGAISenevITQ-IWVLLLGG---LGLAYTLDVWAGhdfpivfyLALGGS 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402797847 122 LiIGTAYSVPPVRLKRfsllaalciltvRGIVVNLGL-----FLFFRIGLGYPPTLITPIWVLTLFILVFTVAIAIFKDV 196
Cdd:PLN00012 208 L-LSYIYSAPPLKLKQ------------NGWIGNYALgasyiSLPWWAGQALFGTLTPDVVVLTLLYSIAGLGIAIVNDF 274
|
170
....*....|....*....
gi 402797847 197 PDMEGDRQFKIQTLTLQIG 215
Cdd:PLN00012 275 KSIEGDRALGLQSLPVAFG 293
|
|
| PT_UbiA_2 |
cd13963 |
UbiA family of prenyltransferases (PTases), Unknown subgroup; Many characterized members of ... |
59-146 |
1.67e-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: 260126 Cd Length: 278 Bit Score: 54.40 E-value: 1.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402797847 59 VYIvgLNQLWDVDIDRIN--KPNLPLANGDFSIAQGRWIVGLCGVASLAIAWGLGLWLGLTVGISLIIGTAYSvppVRLK 136
Cdd:cd13963 49 VYI--LNDLLDLEADRLHptKRNRPIASGRLSIPAALALAVVLLLAGLALALLLSPAFLLVLLAYLVLNLAYS---LKLK 123
|
90
....*....|
gi 402797847 137 RFSLLAALCI 146
Cdd:cd13963 124 RIPLLDVFVI 133
|
|
| PRK09573 |
PRK09573 |
(S)-2,3-di-O-geranylgeranylglyceryl phosphate synthase; Reviewed |
4-227 |
1.85e-08 |
|
(S)-2,3-di-O-geranylgeranylglyceryl phosphate synthase; Reviewed
Pssm-ID: 181963 Cd Length: 279 Bit Score: 54.58 E-value: 1.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402797847 4 IQAFWRFSRPHTIIGTTLSVWAVYLLTIlgdGNSVNSPASLDLVFGAWLACLLGNVyivgLNQLWDVDIDRINKPNLPLA 83
Cdd:PRK09573 3 IKAYFELIRPKNCIGASIGAIIGYLIAS---NFKIDLKGIILAALVVFLVCAGGNV----INDIYDIEIDKINKPERPIP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402797847 84 NGDFSIAQGRWIvglcGVASLAIAWGLGLWLGL-TVGISLIIGTAYSVPPVRLKRFSLLAALCILTVRGIVVNLGLFLFF 162
Cdd:PRK09573 76 SGRISLKEAKIF----SITLFIVGLILSIFINIyAFLIALLNSILLYLYAKDLKKTGLIGNLIVAYLTGLSFIFGGLAVF 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 402797847 163 RIGlgypptlitPIWVLTLFILVFTVAIAIFKDVPDMEGDRQFKIQTLTLQIGKQNVFRGTLILL 227
Cdd:PRK09573 152 NVL---------RIIILFLCAFFSTWSREIVKDIEDIEGDLKENVITLPIKYGIKKSWYIAKILL 207
|
|
| ubiA |
PRK12883 |
prenyltransferase UbiA-like protein; Reviewed |
4-217 |
2.63e-08 |
|
prenyltransferase UbiA-like protein; Reviewed
Pssm-ID: 171796 Cd Length: 277 Bit Score: 53.96 E-value: 2.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402797847 4 IQAFWRFSRPHTIIGTTLsvwaVYLLTILGDGNSVNSPASLDLVF-GAWLACLLGNVyivgLNQLWDVDIDRINKPNLPL 82
Cdd:PRK12883 3 LKAFIEITRPHNCILAGI----VGILGSLVALGGIPPIKTLILIFlVVYLGCSGGNT----INDYFDYEIDKINRPNRPL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402797847 83 ANGDFSIAQGRWIVGLCGVASLAIAWGLGLWLGLTVGISLIIGTAYSvppVRLKRFSLLAALCILTVRGIVVNLGLFLFF 162
Cdd:PRK12883 75 PRGAMSRKAALYYSLLLFAVGLALAYLINIEAFLFALGAYVLMFLYA---WKLKPLPFIGNVVVALLTGATPIYGAIAVG 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 402797847 163 RIGL-GYpptlitpiwvLTLFILVFTVAIAIFKDVPDMEGDRQFKIQTLTLQIGKQ 217
Cdd:PRK12883 152 RIGLaGY----------LAICAFLVNVAREIMKDIEDIEGDKAKGAKTLPIIIGKK 197
|
|
| PT_UbiA_UBIAD1 |
cd13962 |
1,4-Dihydroxy-2-naphthoate octaprenyltransferase; Human UBIAD1 is an enzyme involved in the ... |
8-288 |
4.92e-08 |
|
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: 53.29 E-value: 4.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402797847 8 WRFSRPHTIIGTTLSVWAVYLLTILGDGNSVNSPASLdlvfgAWLACLLGNVYIVGLNQLWD----VDIDRINKPNLPLA 83
Cdd:cd13962 1 LLAARPRTLPASLAPVLLGTALAYYLGGFFNWLLFLL-----ALLAALLLQIGVNLANDYFDykkgTDTEPRSGPSRVLV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402797847 84 NGDFSIAQGRWIVGLCGVAS----LAIAWGLGLWLGLTVGISLIIGTAYSVPPVRLKRFSLLAALCILTVRGIVVNLGLF 159
Cdd:cd13962 76 SGLLSPRQVLRAALVLLLLAallgLYLVALGGWLLLLLGLLGILAGYFYTGGPFPLSYRGLGELFVFLFFGLLAVLGTYY 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402797847 160 LffriglgYPPTLITPIWVLTLFILVFTVAIAIFKDVPDMEGDRQFKIQTLTLQIGKQNVFRGTLILLTGCYLAMAIWGL 239
Cdd:cd13962 156 V-------QTGSLSWEVLLAALPLGLLIAAILLANNIRDIEADRAAGKRTLAVRLGRKRARRLYAALLLLAYLLLLLLVL 228
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 402797847 240 WAAMPLNTAFLIVShLCLLALLWWRSRDVHLESKTEIASFYQFIWKLFF 288
Cdd:cd13962 229 LGLLPLWSLLALLS-LPLAIKLLRRLLRKADKPLLLIALKLTALLTLLF 276
|
|
| ubiA |
PRK12875 |
prenyltransferase; Reviewed |
57-251 |
7.37e-08 |
|
prenyltransferase; Reviewed
Pssm-ID: 237243 Cd Length: 282 Bit Score: 52.73 E-value: 7.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402797847 57 GNVYIVGLNQLWDVDIDRINKPNlplANGDFSIAQGRW----IVGLCGVASLAIAWGLGLWLGLTVGISLIIGTAYSVPP 132
Cdd:PRK12875 57 ANVFLYGVNDVFDADTDELNPKK---DREREVRYRGDRrvlvAVALSGALALAFLLVLPPAAWPALLAFLVLSVEYSAPP 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402797847 133 VRLKRFSLLAALCiltvRGIVVNLGLFLFFRIGLGYPPTLITPIWVLtlfilvFTVAIAIFKDVPDMEGDRQFKIQTLTL 212
Cdd:PRK12875 134 LRFKTTPVLDSLS----NGLYILPGVAAYALVSGSLPPLLAVAGGWL------WAMGMHTFSAIPDIEPDRAAGIRTTAT 203
|
170 180 190
....*....|....*....|....*....|....*....
gi 402797847 213 QIGKqnvfRGTLILLTGCYLAMAIWGLWAAMPLNTAFLI 251
Cdd:PRK12875 204 VLGE----RRTYAYCAACWLLAAAAFAAVDLRLGALLLV 238
|
|
| PRK08238 |
PRK08238 |
UbiA family prenyltransferase; |
49-146 |
9.81e-07 |
|
UbiA family prenyltransferase;
Pssm-ID: 236195 [Multi-domain] Cd Length: 479 Bit Score: 49.87 E-value: 9.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402797847 49 GAWLACLLG---------NVYIvgLNQLWDVDIDRIN--KPNLPLANGDFSIAQGRWIVGLCGVASLAIAWGLGLWLGLT 117
Cdd:PRK08238 223 QALLAALLAflafslcasAVYI--LNDLLDLEADRAHprKRRRPFASGALPIPFGLAAAPLLLLAGLALALALGPAFLLV 300
|
90 100
....*....|....*....|....*....
gi 402797847 118 VGISLIIGTAYSvppVRLKRFSLLAALCI 146
Cdd:PRK08238 301 LLAYLALTLAYS---LRLKRKVLVDVLTL 326
|
|
| ubiA |
PRK12872 |
prenyltransferase; Reviewed |
1-261 |
1.25e-06 |
|
prenyltransferase; Reviewed
Pssm-ID: 237241 Cd Length: 285 Bit Score: 48.79 E-value: 1.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402797847 1 MATIQAFWRFSR--PHTIIGTTLSVwaVYLLTILgdgnsVNSPASLDLVFGAWLACLLGNVYivglNQLWDVDIDRINKP 78
Cdd:PRK12872 1 RKLLFAFLKLFRygNLLIAALGQSL--VYMASLL-----LGLPISWLLLLITFLIAAAVYII----NYLTDLEEDIINKP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402797847 79 -----NLPLANGDFSIAqgrwIVGLCGVASLAIAWGLGLWLGLTVGISLIIGTAYSVPPV-RLKRFSLLAALCILTVRGI 152
Cdd:PRK12872 70 ervvfSETKAYGLFLLL----NVLGLYLGAYLLAVIGGPKFALIFIIPLILGILYSVFFKrRLKRIPLFKNLVVSLLWAL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402797847 153 VVnlgLFLFFrigLGYPPTLITPIWVLTLFILVFTVAIAIFKDVPDMEGDRQFKIQTLTLQIGKQNvfrgTLILLTGCYL 232
Cdd:PRK12872 146 SP---LILGV---YYYQLTIFSLLLLYAVFIFLKSFIREIVFDIKDIEGDRKSGLKTLPIVLGKER----TLKFLLILNL 215
|
250 260
....*....|....*....|....*....
gi 402797847 233 AMAIWglwaaMPLNTAFLIVSHLCLLALL 261
Cdd:PRK12872 216 LFLIL-----LILGVYTGLLPLLLLVLLL 239
|
|
| PT_UbiA_3 |
cd13965 |
UbiA family of prenyltransferases (PTases), Unknown subgroup; Many characterized members of ... |
65-265 |
7.23e-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: 260128 Cd Length: 273 Bit Score: 46.48 E-value: 7.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402797847 65 NQLWDVDIDRINKPNLPLANGDFSIAQGRWIVglcgVASLAIAWGLGLWLG-LTVGISLIIGTAYsvppvrlkrFSLLAA 143
Cdd:cd13965 56 NQPESVEEDRINKPWRPIPSGRITPRQARRLR----WLLVPLCLALSAYLGvLEESLLLIVLTWL---------YNELGL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402797847 144 LCILTVRGIVVNLGLFLFFR------IGLGYPPTLITPIWVLTLFILVFTVAIAifKDVPDMEGDRQFKIQTLTLQIGkq 217
Cdd:cd13965 123 ADHWLTRNLLNALGYAAFLAgatriaGGGPHPLDPTAWAWILLSAAIILTTIHA--QDFRDVEGDRARGRRTLPLVFG-- 198
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 402797847 218 NVFRGTLILLTGCYLAMAIWGLWAAMPLNTA-FLIVSHLCLLALLWWRS 265
Cdd:cd13965 199 DAAARWLIAAGVVAWSVVLPYFWGLPPLLAAlLVALGAVVAVRFLLLRS 247
|
|
| PT_UbiA_5 |
cd13967 |
UbiA family of prenyltransferases (PTases), Unknown subgroup; Many characterized members of ... |
51-273 |
3.84e-05 |
|
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: 44.52 E-value: 3.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402797847 51 WLACLLGNVYIV---GLNQLWDVDIDRINKPN---LPLANGDFSIAqgrwiVGLC-GVASLAIAWGLGLWLGLTVGISLI 123
Cdd:cd13967 35 LPALLIAGLVVYsvyTLNRLTDSEEDAYNDPEraaFYEKYKKLLLA-----LAIAaGLLALALAFILGLLAFAILLLPLL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402797847 124 IGTAYSVPpVRLKRFSLLAALCILTVRGIVVNL--GLFLFFRIGLGYPPTLITPIWVLTLFILVFTVAIAIFkDVPDMEG 201
Cdd:cd13967 110 LGLLYSLP-IKPGKLRLRRRKDIPGSKNLVVALawAVVIALLPALYGQPSTPSVLVVFLFFFLKVFVNTAIF-DIRDVEG 187
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 402797847 202 DRQFKIQTLTLQIGKQNVFRGTLILLTGCYLAMAIWGLWAAMPLNTAFLIVSHLCLLALLWWRSRDVHLESK 273
Cdd:cd13967 188 DRIVGIETLPVLLGEERTRLLLLVLNILLALLLVAGVLLGLLASEFLVLLLSLIYGLIYIIFFSRDENEEGL 259
|
|
| MenA |
COG1575 |
1,4-dihydroxy-2-naphthoate polyprenyltransferase [Coenzyme transport and metabolism]; 1, ... |
82-253 |
3.07e-04 |
|
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: 41.67 E-value: 3.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402797847 82 LANGDFSIAQGRWIVGLCGVASLAIAWGL----GLWLGLTVGISLIIGTAYSVPPVRLKRFSLLAALCILTVRGIVVNLG 157
Cdd:COG1575 76 IVSGLLSPKQVLRAALLLLALALLLGLYLvllsGWPLLLLGLLGILAAIFYTGGPFPLGYRGLGELFVFLFFGLVAVLGT 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402797847 158 LFLffriglgYPPTLITPIWVLTLFILVFTVAIAIFKDVPDMEGDRQFKIQTLTLQIGKQNVFRGTLILLTGCYLAMAIW 237
Cdd:COG1575 156 YYV-------QTGTLSWAALLASLPVGLLSAAVLLANNLRDIETDRAAGKRTLAVRLGRKRARRLYAALLLLAYLLILLL 228
|
170
....*....|....*.
gi 402797847 238 GLWAAMPLNTAFLIVS 253
Cdd:COG1575 229 VLLGLLPPWALLALLS 244
|
|
| ubiA |
PRK13595 |
prenyltransferase; Provisional |
58-266 |
8.12e-04 |
|
prenyltransferase; Provisional
Pssm-ID: 172161 Cd Length: 292 Bit Score: 40.61 E-value: 8.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402797847 58 NVYIVGLNQLWDVDIDRINKPNLPLANGDFSIAQGRWIVGLCGVASLAIAWGLGLWL----GLTVGISLIIGTAYSVPPV 133
Cdd:PRK13595 60 NLLIYGLNDLADRETDAASPRKGGWQGARLSPGEVRPLLRAVLLLNAPFLLYLALLLppaaTLLLLLYAALFVGYSLPPL 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402797847 134 RLKRFSLLAALCILTvrgivvnlglflfFRIGLGYPPTLI--TPIWVLTLFILVFTVAIAIFKDVPDMEGDRQFKIQTLT 211
Cdd:PRK13595 140 RFKARPFLDGLSNAA-------------YALPLALPALALgaPVPWPPLLALMAWSVGKHAFDAAQDIPADRAAGTRTVA 206
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 402797847 212 LQIGkqnvFRGTlILLTGCYLAMAIWGLWAAMPLNTAFLIVSHLCLLALLWWRSR 266
Cdd:PRK13595 207 TTLG----VRGT-ALYALAWFLLAGALLWPVSRLTALALWLICGGMALALWRRPT 256
|
|
| PT_UbiA_COQ2 |
cd13959 |
4-Hydroxybenzoate polyprenyltransferase; 4-Hydroxybenzoate polyprenyltransferase, also known ... |
11-284 |
1.88e-03 |
|
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: 39.37 E-value: 1.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402797847 11 SRPHTIIGTTLSVWAVYLLTILGDGNSVNSPASLDLVF--GAWLACLLGNVYivglNQLWDVDIDRINK--PNLPLANGD 86
Cdd:cd13959 1 MRLDKPIGTLLLLPPALWGLLLAAGGLPLPLLKLLLLFllGAFLMRSAGCTI----NDIADRDIDAKVPrtKNRPLASGA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402797847 87 FSIAQGRWIVGLCGVASLAIAWGLG---LWLGLtvgISLIIGTAYSVppvrLKRFSLLAALciltVRGIVVNLGLFLFFR 163
Cdd:cd13959 77 ISVKEALLFLAVQLLLGLALLLQLNpltILLSP---IALLLVLIYPL----MKRFTYWPQL----VLGLAFGWGPLMGWA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402797847 164 IGLGyppTLITPIWVLTLFILVFTVAIAIFKDVPDMEGDRQFKIQTLTLQIGKQnvfrgTLILLTGCYLAMAIWGLWAA- 242
Cdd:cd13959 146 AVTG---SLPLPALLLYLAVIFWTAGYDTIYAHQDREDDRKIGVKSTAVLFGDR-----TKLILALLLHLFVALLLLAGg 217
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 402797847 243 -MPLNTAFLIVSHLCLLALLWWRSRDVHLESKTEIASFYQFIW 284
Cdd:cd13959 218 lAGLGWPYYLGLGAAAHLLWQEHRLDLPDPLRSCLAFFLSNGW 260
|
|
|