|
Name |
Accession |
Description |
Interval |
E-value |
| UbiA |
COG0382 |
4-hydroxybenzoate polyprenyltransferase [Coenzyme transport and metabolism]; 4-hydroxybenzoate ... |
2-201 |
4.24e-16 |
|
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: 77.19 E-value: 4.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008838442 2 KLYLKLIR---PYGMLFIGFTPFFGAI--ANGEYRLLPLTILVIIGMLAHIFTFVQNDYYDTEIDKKSKYVSNRPLVTDG 76
Cdd:COG0382 1 RAYLRLLRldrPIGILLLLWPTLWALFlaAGGLPDLLLLLLAVLGTVLMRSAGYVINDYFDREIDRINERKPNRPLASGR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008838442 77 ISIKTAIVIFLSSFIFSIILnmIFLFSIYSFLMLLFSFLCMTLYNKYSKRFFGMEYVLAIGVFSYGIF-GTLTVSNSISN 155
Cdd:COG0382 81 ISLREALLLAIVLLLLALAL--ALLLNPLTFLLALAALALAWAYSLFLKRFTLLGNLVLGLLFGLGILmGFAAVTGSLPL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1008838442 156 LAIIISSIGFMhWLFSVGVSANLKDVEFDTKLGIRTTPAVFGVYAK 201
Cdd:COG0382 159 SAWLLALAAFL-WTLAYDTIYDLEDREGDRKIGIKTLAILFGVRDA 203
|
|
| UbiA |
pfam01040 |
UbiA prenyltransferase family; |
14-239 |
5.45e-16 |
|
UbiA prenyltransferase family;
Pssm-ID: 460038 [Multi-domain] Cd Length: 250 Bit Score: 76.11 E-value: 5.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008838442 14 LFIGFTPFFGAIANGEYRLLPLTILVIIGMLAHIFTFVQNDYYDTEIDKKSKYVSNRPLVTDGISIKTAIVIFLSSFIFS 93
Cdd:pfam01040 1 LLIPALAGLALAAGGVPDLLLLLLALLGTVLARAAANALNDYYDRDIDAIMPRTPNRPLPSGRISPREALIFALVLLALG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008838442 94 IILnmIFLFSIYSFLMLLFSFLCMTLYNKYSKRFFGM-EYVLAIGVFSYGIFGTLTVSNSISNLAIIISSIGFMhWLFSV 172
Cdd:pfam01040 81 LLL--LLLLNPLTALLGLAALLLYVLYTLRLKRRTLLgQLVGGLAFGLPPLLGWAAVTGSLSPLALLLALALFL-WTWAI 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1008838442 173 GVSANLKDVEFDTKLGIRTTPAVFGVYAkdkRLVIPISFQIYAYFIKIIHIFIATLPFIFGYTSILV 239
Cdd:pfam01040 158 ALANDLRDREDDRKAGIKTLPVVLGRKA---ARILLALLLAVALLLLLLLLLLLLGGLYLLLALLLA 221
|
|
| PT_UbiA |
cd13956 |
UbiA family of prenyltransferases (PTases); Many characterized members of the UbiA ... |
5-198 |
7.04e-15 |
|
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: 73.54 E-value: 7.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008838442 5 LKLIRPYGMLFIGFTPFFGAIANGEYRLLPLTILVIIGM---LAHIFTFVQNDYYDTEIDKKSKyvSNRPLVTDGISIKT 81
Cdd:cd13956 1 LRLMRPYTLLYVLAPALAGAALAGAFAGPLPALLLLALLavfLGAGAGYALNDYTDRELDAINK--PDRPLPSGRLSPRQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008838442 82 AIVIFLSSFIFSIILnmIFLFSIYSFLMLLFSFLCMTLYNKYSKRF-FGMEYVLAIGVFSYGIFGTLTVSNSISNLAIII 160
Cdd:cd13956 79 ALAFAAALLLVGLAL--ALALGPLALLLLLAGLLLGLAYSLGLKRLkLGGWGVLGYATGLALLPGLGAVAAGGLVPLALL 156
|
170 180 190
....*....|....*....|....*....|....*...
gi 1008838442 161 SSIGFMHWLFSVGVSANLKDVEFDTKLGIRTTPAVFGV 198
Cdd:cd13956 157 LALVFLLLGLGINLYNDLPDVEGDRAAGIRTLPVRLGP 194
|
|
| ubiA |
PRK12884 |
prenyltransferase; Reviewed |
1-244 |
8.88e-12 |
|
prenyltransferase; Reviewed
Pssm-ID: 183812 Cd Length: 279 Bit Score: 64.59 E-value: 8.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008838442 1 MKLYLKLIRPYGMLFIGFTPFFGAIANGEYrlLPLTIlVIIGMLAHIF----TFVQNDYYDTEIDKKSKyvSNRPLVTDG 76
Cdd:PRK12884 4 MKAYLELLRPEHGLMAGIAVVLGAIIALGG--LPLDE-ALLGFLTAFFasgsANALNDYFDYEVDRINR--PDRPIPSGR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008838442 77 ISIKTAIVIFLSSFIFSIILNmiFLFSIYSFLMLLFSFLCMTLYNKYSKR--FFGMEYVLAIGVFSYgIFGTLTVSNsiS 154
Cdd:PRK12884 79 ISRREALLLAILLFILGLIAA--YLISPLAFLVVILVSVLGILYNWKLKEygLIGNLYVAFLTGMTF-IFGGIAVGE--L 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008838442 155 NLAIIIssIGFMHWLFSVG--VSANLKDVEFDTKLGIRTTPAVFGvyaKDKRLVIPISFQIYAyfikiihIFIATLPFIF 232
Cdd:PRK12884 154 NEAVIL--LAAMAFLMTLGreIMKDIEDVEGDRLRGARTLAILYG---EKIAGRIAAALFILA-------VLLSPLPYLF 221
|
250
....*....|..
gi 1008838442 233 GYTSILvYDFPI 244
Cdd:PRK12884 222 GIFNIL-YLAPV 232
|
|
| PT_UbiA_DGGGPS |
cd13961 |
Geranylgeranylglycerol-phosphate geranylgeranyltransferase; Digeranylgeranylglyceryl phosphate ... |
4-243 |
3.00e-10 |
|
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: 59.82 E-value: 3.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008838442 4 YLKLIRPYGMLFIGFTPFFGAIA----NGEYRLLPLTILVIIGMLAHIFTFVQNDYYDTEIDKKSKyvSNRPLVTDGISI 79
Cdd:cd13961 2 YLELIRPPNLLMAALAQYLGALFalgpLLSLNDLELLLLFLSVFLIAAAGYIINDYFDVEIDRINK--PDRPIPSGRISR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008838442 80 KTAIVIFLSSFIFSIILNmiFLFSIYSFLMLLFSFLCMTLYNKYSKR--FFGMEYVLAIGVFSYgIFGTLTVSNSIsnla 157
Cdd:cd13961 80 REALILSILLNALGLILA--FLLSPLALLIALLNSLLLWLYSHKLKRtpLIGNLLVALLTGLPF-LFGGLAAGNLL---- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008838442 158 IIISSIGFMHWLFSVG--VSANLKDVEFDTKLGIRTTPAVFGVyAKDKRL-----VIPISFQIYAYFIKIIHI----FIA 226
Cdd:cd13961 153 LIILLLALFAFLITLGreIVKDIEDVEGDRAEGARTLPIVYGI-KKAKKIaalllLLAILLSPLPYLLGGLGIlyliLII 231
|
250
....*....|....*..
gi 1008838442 227 TLPFIFGYTSILVYDFP 243
Cdd:cd13961 232 IADLLFLYSAIRLAKSP 248
|
|
| PRK09573 |
PRK09573 |
(S)-2,3-di-O-geranylgeranylglyceryl phosphate synthase; Reviewed |
1-238 |
1.70e-09 |
|
(S)-2,3-di-O-geranylgeranylglyceryl phosphate synthase; Reviewed
Pssm-ID: 181963 Cd Length: 279 Bit Score: 57.66 E-value: 1.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008838442 1 MKLYLKLIRPYGMLFIGFTPFFGAIANGEYRL--LPLTILVIIGMLAHIFTFVQNDYYDTEIDKKSKyvSNRPLVTDGIS 78
Cdd:PRK09573 3 IKAYFELIRPKNCIGASIGAIIGYLIASNFKIdlKGIILAALVVFLVCAGGNVINDIYDIEIDKINK--PERPIPSGRIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008838442 79 IKTAIVIFLSSFIFSIILNmiFLFSIYSFLMLLFSFLCMTLYNKYSKRffgmeyvlaigvfsYGIFGTLTVSNSISNL-- 156
Cdd:PRK09573 81 LKEAKIFSITLFIVGLILS--IFINIYAFLIALLNSILLYLYAKDLKK--------------TGLIGNLIVAYLTGLSfi 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008838442 157 --AIIISSIGFMHWLFSVGVSANL--------KDVEFDTKLGIRTTPAVFGVyakDKRLVIpisfqiyAYFIKIIHIFIA 226
Cdd:PRK09573 145 fgGLAVFNVLRIIILFLCAFFSTWsreivkdiEDIEGDLKENVITLPIKYGI---KKSWYI-------AKILLILAIVLS 214
|
250
....*....|..
gi 1008838442 227 TLPFIFGYTSIL 238
Cdd:PRK09573 215 PLPYFLGIFGIY 226
|
|
| PT_UbiA_COQ2 |
cd13959 |
4-Hydroxybenzoate polyprenyltransferase; 4-Hydroxybenzoate polyprenyltransferase, also known ... |
5-201 |
3.38e-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: 56.71 E-value: 3.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008838442 5 LKLIRPYGMLFIGFTPFFG---AIANGEYRLLPLTILVIIGM-LAHIFTFVQNDYYDTEIDKKSKYVSNRPLVTDGISIK 80
Cdd:cd13959 1 MRLDKPIGTLLLLPPALWGlllAAGGLPLPLLKLLLLFLLGAfLMRSAGCTINDIADRDIDAKVPRTKNRPLASGAISVK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008838442 81 TAIVIFLSSFIFSIILnmIFLFSIYSFLMLLFSFLCMTLYnKYSKRFFGM-EYVLAIgVFSYGIFGT-LTVSNSISNLAI 158
Cdd:cd13959 81 EALLFLAVQLLLGLAL--LLQLNPLTILLSPIALLLVLIY-PLMKRFTYWpQLVLGL-AFGWGPLMGwAAVTGSLPLPAL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1008838442 159 IISsIGFMHWLFSVGVSANLKDVEFDTKLGIRTTPAVFGVYAK 201
Cdd:cd13959 157 LLY-LAVIFWTAGYDTIYAHQDREDDRKIGVKSTAVLFGDRTK 198
|
|
| PT_UbiA_UBIAD1 |
cd13962 |
1,4-Dihydroxy-2-naphthoate octaprenyltransferase; Human UBIAD1 is an enzyme involved in the ... |
5-197 |
2.35e-05 |
|
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: 45.20 E-value: 2.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008838442 5 LKLIRPYgMLFIGFTPF----FGAIANGEYRLLPLTILVIIGMLA-HIFTFVQNDYYDTE--IDKKSKYVSNRPLVTDGI 77
Cdd:cd13962 1 LLAARPR-TLPASLAPVllgtALAYYLGGFFNWLLFLLALLAALLlQIGVNLANDYFDYKkgTDTEPRSGPSRVLVSGLL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008838442 78 SIKTAIVIFLSSFIFSIILnMIFLFSIYSFLMLLFSFLCMTL---Y----NKYSKRFFGMeyvLAIGVFsYGIFGTLT-- 148
Cdd:cd13962 80 SPRQVLRAALVLLLLAALL-GLYLVALGGWLLLLLGLLGILAgyfYtggpFPLSYRGLGE---LFVFLF-FGLLAVLGty 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1008838442 149 -VSNSISNLAIIISSIGFMHWLFSVGVSANLKDVEFDTKLGIRTTPAVFG 197
Cdd:cd13962 155 yVQTGSLSWEVLLAALPLGLLIAAILLANNIRDIEADRAAGKRTLAVRLG 204
|
|
| ubiA |
PRK12874 |
4-hydroxybenzoate polyprenyltransferase; |
38-239 |
2.75e-05 |
|
4-hydroxybenzoate polyprenyltransferase;
Pssm-ID: 237242 Cd Length: 291 Bit Score: 45.00 E-value: 2.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008838442 38 LVIIGMLAHI----FTFVQNDYYDTEIDKKSKYVSNRPLVTDGISIKtaiviflSSFIFSIILNMIFLFSIYSFLMLLF- 112
Cdd:PRK12874 48 LLILGILAAVsarnFAMAFNRLVDRDIDKDNPRTANRPSVDGRISVK-------SMVLFIVLNALIFIGVSYFINPLAFk 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008838442 113 -SFLCMTLYNKYS--KRFFGM-EYVLAIGVFSYGIFGTLTVSNSISnLAIIISSIGFMHWLFSVGVSANLKDVEFDTKLG 188
Cdd:PRK12874 121 lSFPFLIVLGGYSyfKRFSSLaHLVLGLSLGLAPIAGVVAVLGEIP-LWSVFLALGVMFWVAGFDLLYSLQDMEFDKKRG 199
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1008838442 189 IRTTPAVFGVyakDKRLVIPISFQIYAYFIKIIHIFIATLPFiFGYTSILV 239
Cdd:PRK12874 200 LHSIPSKFGE---KATLFISRLFHLLAVLFWLLFVWCAHLGL-FAYLGVIV 246
|
|
| PT_UbiA_3 |
cd13965 |
UbiA family of prenyltransferases (PTases), Unknown subgroup; Many characterized members of ... |
32-197 |
9.07e-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: 260128 Cd Length: 273 Bit Score: 43.40 E-value: 9.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008838442 32 LLPLTILVIIGMLaHIFTF-VQNDYYDTEIDKKSKyvSNRPLVTDGISIKTAIVIFLSSFIFSIILNmiFLFSIysFLML 110
Cdd:cd13965 35 ALPLLLGFLWIWL-HLYQFdNQNQPESVEEDRINK--PWRPIPSGRITPRQARRLRWLLVPLCLALS--AYLGV--LEES 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008838442 111 LFSFLCMTLYN--KYSKRFFGMEYVLAIGVFSYGIFGTLTVSNSISNLA-IIISSIGFMHWLFSVGVSA-NLKDVEFDTK 186
Cdd:cd13965 108 LLLIVLTWLYNelGLADHWLTRNLLNALGYAAFLAGATRIAGGGPHPLDpTAWAWILLSAAIILTTIHAqDFRDVEGDRA 187
|
170
....*....|.
gi 1008838442 187 LGIRTTPAVFG 197
Cdd:cd13965 188 RGRRTLPLVFG 198
|
|
| PT_UbiA_2 |
cd13963 |
UbiA family of prenyltransferases (PTases), Unknown subgroup; Many characterized members of ... |
4-126 |
1.43e-04 |
|
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: 42.85 E-value: 1.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008838442 4 YLKLIRPYGM---LFIgftpFFGAIANGEYRLLPLTILVIIGMLAHIF----TFVQNDYYDTEIDKKSKYVSNRPLVTDG 76
Cdd:cd13963 1 LLKLLRPHQWvknLLV----FAPLLFAGQLFDPDLLLAALLAFVAFCLaasaVYILNDLLDLEADRLHPTKRNRPIASGR 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1008838442 77 ISIKTAIVIFLSSFIFSIILNmiFLFSIYSFLMLLFSFLCMTLYNKYSKR 126
Cdd:cd13963 77 LSIPAALALAVVLLLAGLALA--LLLSPAFLLVLLAYLVLNLAYSLKLKR 124
|
|
| ubiA |
PRK12883 |
prenyltransferase UbiA-like protein; Reviewed |
1-197 |
2.53e-04 |
|
prenyltransferase UbiA-like protein; Reviewed
Pssm-ID: 171796 Cd Length: 277 Bit Score: 42.02 E-value: 2.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008838442 1 MKLYLKLIRPYGMLFIGFTPFFGAIANGEYrLLPLTILVIIGMLAHIFTF---VQNDYYDTEIDKKSKyvSNRPLVTDGI 77
Cdd:PRK12883 3 LKAFIEITRPHNCILAGIVGILGSLVALGG-IPPIKTLILIFLVVYLGCSggnTINDYFDYEIDKINR--PNRPLPRGAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008838442 78 SIKTAIVIFLSSFIFSIILnmIFLFSIYSFLMLLFSFLCMTLYNKYSKrffGMEYVLAIGVfsygifGTLTVSNSISNlA 157
Cdd:PRK12883 80 SRKAALYYSLLLFAVGLAL--AYLINIEAFLFALGAYVLMFLYAWKLK---PLPFIGNVVV------ALLTGATPIYG-A 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1008838442 158 IIISSIGFMHWL----FSVGVS----ANLKDVEFDTKLGIRTTPAVFG 197
Cdd:PRK12883 148 IAVGRIGLAGYLaicaFLVNVAreimKDIEDIEGDKAKGAKTLPIIIG 195
|
|
| ubiA |
PRK12888 |
4-hydroxybenzoate octaprenyltransferase; |
38-200 |
3.35e-04 |
|
4-hydroxybenzoate octaprenyltransferase;
Pssm-ID: 183814 Cd Length: 284 Bit Score: 41.63 E-value: 3.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008838442 38 LVIIGML-AHIFTFVQNDYYDTEIDKKSKYVSNRPLVTDGISIKTAIVIFLSSFIfsiilnmIFLFS--IYSFLMLLFSF 114
Cdd:PRK12888 43 LVTVAMVgARTFAMAANRIIDREIDARNPRTAGRELVTGAVSVRTAWTGALVALA-------VFLGAaaLLNPLCLALAP 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008838442 115 LC---MTLYnKYSKRFFGMEY-VLAIGVFSYGIFGTLTVSNSISNLAIIIS-SIGFmhWLFSVGVSANLKDVEFDTKLGI 189
Cdd:PRK12888 116 LAvapLVVY-PYAKRFTNFPHaILGLAQAVGPVGAWIAVTGTWSWPAVLLGlAVGL--WIGGFDLIYACQDAEVDRRIGV 192
|
170
....*....|.
gi 1008838442 190 RTTPAVFGVYA 200
Cdd:PRK12888 193 RSVPARFGVRA 203
|
|
| ubiA |
PRK12882 |
prenyltransferase; Reviewed |
1-198 |
3.42e-04 |
|
prenyltransferase; Reviewed
Pssm-ID: 183811 Cd Length: 276 Bit Score: 41.50 E-value: 3.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008838442 1 MKLYLKLIRPYGMLFIGFTPFFGA-IANGEYRLLPLT-ILVIIGMLAHIFTFVQNDYYDTEIDKKSKyvSNRPLVTDGIS 78
Cdd:PRK12882 4 VRGYLELTRPVNAVVAGVAAFIGAfIAGGILSSPSLTgLAFAAVFLATGAGNAINDYFDREIDRINR--PDRPIPSGAVS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008838442 79 IKTAIVIFLSSFIFSIILNmiFLFSIYSFLMLLFSFLCMTLYNKYSKR--FFGMEYV--LAIGVFSYG--IFGT-----L 147
Cdd:PRK12882 82 PRGALAFSILLFAAGVALA--FLLPPLCLAIALFNSLLLVLYAETLKGtpGLGNASVayLTGSTFLFGgaAVGTegllaL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1008838442 148 TVSNSISNLAIIISSIgfmhwlfsvgvsanLKDVE---FDTKLGIRTTPAVFGV 198
Cdd:PRK12882 160 LVLFALAALATLAREI--------------IKDVEdieGDRAEGARTLPILIGV 199
|
|
| ubiA |
PRK13106 |
prenyltransferase; Reviewed |
4-238 |
6.24e-04 |
|
prenyltransferase; Reviewed
Pssm-ID: 237283 Cd Length: 300 Bit Score: 40.87 E-value: 6.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008838442 4 YLKLIRPYGMLFIGFTPFFGAIANGEYRLLPLTILVIIGMLAHIFT--FVQNDYYDTEIDKKSKYVSNRPLVTDGISIKT 81
Cdd:PRK13106 18 ILRFLRIEQTFFSLPMAYLGAFVAIKGIPPISTLILIFLALFFLRTagMTNDNLADLEIDAKNPRTKNRPLVTGAIKISE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008838442 82 A-IVIFLSSFIFSIilnMIFLFSIYSFLMLLFSFLCMTLYnKYSKRF-----FGMEYVLAIGVFSygifGTLTVSNSISN 155
Cdd:PRK13106 98 AkALITAGLILFFA---SAYLVNRWALLLSPIVALIAMSY-PYMKRYtafanYHLASIQGLAVFS----GAVAVLGLYAN 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008838442 156 LAIIIssIGFMHWLFSVGVS---------ANLKDVEFDTKLGIRTTPAVFGvyakDKRLVIPISFQIYAYFIKIIHIFIA 226
Cdd:PRK13106 170 SLIQV--LLRVPWLFVIGTIlwaagfdlyNHIPDAEFDREMGLHSFAVVLG----KWALTFAGLNQLFSVVLDLLGDLYY 243
|
250
....*....|..
gi 1008838442 227 TLPFIFGYTSIL 238
Cdd:PRK13106 244 GLGPIAIAATIL 255
|
|
| ubiA |
PRK12873 |
4-hydroxybenzoate polyprenyltransferase; |
51-232 |
9.51e-04 |
|
4-hydroxybenzoate polyprenyltransferase;
Pssm-ID: 171787 [Multi-domain] Cd Length: 294 Bit Score: 40.42 E-value: 9.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008838442 51 VQNDYYDTEIDKKSKYVSNRPLVTDGISIKTA--IVIFLSSFIFSIILNMIFLFSIYSFLMLLFSFLCMTLYNKySKRFF 128
Cdd:PRK12873 62 IANDLWDRRIDRKVERTKNRPLARGKISLKTAysLLIVLLLLSLFVVLSLPQPSRNLCLSLAFLALPPILIYPS-AKRWF 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008838442 129 gmEYVLAIGVFSYGIFGTLTVSNSISNLAIIISSIG----FMHWLFSVGVSANLKDVEFDTKLGIRTTPAVFGVYAKdkr 204
Cdd:PRK12873 141 --AYPQAILALCWGFAVLIPWAAAEGSLNGGWPLLFcwlaTLLWTFGFDTVYAMADRRDDAKIGLNSSALSLGSNAL--- 215
|
170 180
....*....|....*....|....*...
gi 1008838442 205 LVIPISFQIYAYFIKIIhIFIATLPFIF 232
Cdd:PRK12873 216 KTVQICYFLTSIFLALA-AFIAQVGFIF 242
|
|
| ubiA |
PRK12886 |
prenyltransferase; Reviewed |
53-232 |
1.08e-03 |
|
prenyltransferase; Reviewed
Pssm-ID: 237247 Cd Length: 291 Bit Score: 40.06 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008838442 53 NDYYDTEIDKKSKYVSNRPLVTDGISIKTAIV-IFLSSFIFSIILNMIFLFSIY-SFLMLLFSFLcmtlyNKYSKRFFGM 130
Cdd:PRK12886 62 NRLIDAEIDARNPRTAGRAIPAGLISKGSAILfIVLSSLLMLFAAWFLNPLCLYlSPPALFFLLL-----YSYCKRFTAL 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008838442 131 -EYVLAIGVFSYGIFGTLTVSNSISNLAIIISsIGFMHWLFSVGVSANLKDVEFDTKLGIRTTPAVFGVyakDKRLVIPI 209
Cdd:PRK12886 137 aHVVLGFCLALAPLGAWIAIRGTIELPAILLG-LAVLFWVAGFDILYALQDLEFDRKEGLHSIPAKLGV---NGSLWIAR 212
|
170 180
....*....|....*....|...
gi 1008838442 210 SFQIYAYFIKIIHIFIATLPFIF 232
Cdd:PRK12886 213 VFHLLMIGFLFALGISAGLGPWF 235
|
|
| PT_UbiA_Cox10 |
cd13957 |
Protoheme IX farnesyltransferase; Protoheme IX farnesyltransferase (also called heme O ... |
5-115 |
1.95e-03 |
|
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: 39.34 E-value: 1.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008838442 5 LKLIRPYGMLFIGFTPFFG-AIANGEYRLLPLTILVIIGML-----AHIFtfvqNDYYDTEIDKKSKYVSNRPLVTDGIS 78
Cdd:cd13957 1 LELTKPRITLLVLLTALAGyLLAPGGVPDLLLLLLTLLGTAlvsasANAL----NQYIERDIDAKMKRTRNRPLPSGRIS 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 1008838442 79 IKTAIVIFLSSFIFSIILnMIFLFSIYSFLMLLFSFL 115
Cdd:cd13957 77 PKHALIFGLVLGILGLAL-LALFVNPLTALLGLLGIF 112
|
|
| |
