|
Name |
Accession |
Description |
Interval |
E-value |
| ubiA_proteo |
TIGR01474 |
4-hydroxybenzoate polyprenyl transferase, proteobacterial; This model represents a family of ... |
10-288 |
3.68e-118 |
|
4-hydroxybenzoate polyprenyl transferase, proteobacterial; This model represents a family of integral membrane proteins that condenses para-hydroxybenzoate with any of several polyprenyldiphosphates. Heterologous expression studies suggest that for, many but not all members, the activity seen (e.g. octaprenyltransferase in E. coli) reflects available host isoprenyl pools rather than enzyme specificity. A fairly deep split by both clustering (UPGMA) and phylogenetics (NJ tree) separates this group (mostly Proteobacterial and mitochondrial), with several characterized members, from another group (mostly archaeal and Gram-positive bacterial) lacking characterized members. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]
Pssm-ID: 130539 Cd Length: 281 Bit Score: 340.45 E-value: 3.68e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535134085 10 LLAFHRLMRTDKPIGALLLLWPTLWALWVATP--GVPQLWILAVFVAGVWLMRAAGCVVNDYADRKFDGHVKRTANRPLP 87
Cdd:TIGR01474 1 LLPYAKLMRADKPIGTLLLLWPCLWSLLLAAQagGIPPLYLLGLFTVGAILMRGAGCVINDIWDRDFDPQVERTKSRPLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535134085 88 SGAVTEKEARALFVVLVLISFLLVLTLNTMTILLSIAALALAWVYPFMKRYTHLPQVVLGAAFGWSIPMAFAAVSESVPL 167
Cdd:TIGR01474 81 SGAVSVRQAILFLLVQLLVALGVLLQLNPLTILLGVASLALVATYPFMKRITYWPQLVLGLAFGWGALMGWAAVTGDLST 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535134085 168 SCWLMFLANILWAVAYDTQYAMVDRDDDVKIGIKSTAILFGQYDKLIIGILQIGVLALMAIIGELNGLGWGYYWSILVAG 247
Cdd:TIGR01474 161 AAWVLYLANILWTLGYDTIYAMQDKEDDIKIGVKSTALRFGDNTKPWLGGLYALMILLLALAGLIAGLGPVYYLGLAAAA 240
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 535134085 248 ALFVYQQKLIANREREACFKAFMNNNYVGLVLFLGLAMSYW 288
Cdd:TIGR01474 241 LLLIRQIATLDIRDPENCLKLFKANNYVGLLLFAGIALGWL 281
|
|
| PT_UbiA_COQ2 |
cd13959 |
4-Hydroxybenzoate polyprenyltransferase; 4-Hydroxybenzoate polyprenyltransferase, also known ... |
17-286 |
3.00e-109 |
|
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: 317.49 E-value: 3.00e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535134085 17 MRTDKPIGALLLLWPTLWALWVATPGVP--QLWILAVFVAGVWLMRAAGCVVNDYADRKFDGHVKRTANRPLPSGAVTEK 94
Cdd:cd13959 1 MRLDKPIGTLLLLPPALWGLLLAAGGLPlpLLKLLLLFLLGAFLMRSAGCTINDIADRDIDAKVPRTKNRPLASGAISVK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535134085 95 EARALFVVLVLISFLLVLTLNTMTILLSIAALALAWVYPFMKRYTHLPQVVLGAAFGWSIPMAFAAVSESVPLSCWLMFL 174
Cdd:cd13959 81 EALLFLAVQLLLGLALLLQLNPLTILLSPIALLLVLIYPLMKRFTYWPQLVLGLAFGWGPLMGWAAVTGSLPLPALLLYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535134085 175 ANILWAVAYDTQYAMVDRDDDVKIGIKSTAILFGQYDKLIIGILQIGVLALMAIIGELNGLGWGYYWSILVAGALFVYQQ 254
Cdd:cd13959 161 AVIFWTAGYDTIYAHQDREDDRKIGVKSTAVLFGDRTKLILALLLHLFVALLLLAGGLAGLGWPYYLGLGAAAHLLWQEH 240
|
250 260 270
....*....|....*....|....*....|..
gi 535134085 255 KLIANREREACFKAFMNNNYVGLVLFLGLAMS 286
Cdd:cd13959 241 RLDLPDPLRSCLAFFLSNGWVGLLLFAGLLLD 272
|
|
| UbiA |
COG0382 |
4-hydroxybenzoate polyprenyltransferase [Coenzyme transport and metabolism]; 4-hydroxybenzoate ... |
11-285 |
1.23e-89 |
|
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: 267.87 E-value: 1.23e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535134085 11 LAFHRLMRTDKPIGALLLLWPTLWALWVATPGVPQLWILAVFVAGVWLMRAAGCVVNDYADRKFDGHVKRTANRPLPSGA 90
Cdd:COG0382 1 RAYLRLLRLDRPIGILLLLWPTLWALFLAAGGLPDLLLLLLAVLGTVLMRSAGYVINDYFDREIDRINERKPNRPLASGR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535134085 91 VTEKEARALFVVLVLISFLLVLTLNTMTILLSIAALALAWVYP-FMKRYTHLPQVVLGAAFGWSIPMAFAAVSESVPLSC 169
Cdd:COG0382 81 ISLREALLLAIVLLLLALALALLLNPLTFLLALAALALAWAYSlFLKRFTLLGNLVLGLLFGLGILMGFAAVTGSLPLSA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535134085 170 WLMFLANILWAVAYDTQYAMVDRDDDVKIGIKSTAILFGQYDKL-IIGILQIGVLALMAIIGELNGLGWGYYWSILVAG- 247
Cdd:COG0382 161 WLLALAAFLWTLAYDTIYDLEDREGDRKIGIKTLAILFGVRDALiIAGVLYALAVLLLLLLGLLAGLGLLYLLGLLAALl 240
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 535134085 248 ALFVYQQKLIANR--EREACFKAFMNNNYVGLVLFLGLAM 285
Cdd:COG0382 241 LLYLSQLWLLRPRkkDPARALKLFKLNMLLGLLLFLGIAL 280
|
|
| PLN02809 |
PLN02809 |
4-hydroxybenzoate nonaprenyltransferase |
13-283 |
1.56e-59 |
|
4-hydroxybenzoate nonaprenyltransferase
Pssm-ID: 178405 Cd Length: 289 Bit Score: 191.44 E-value: 1.56e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535134085 13 FHRLMRTDKPIGALLLLWPTLWALWVATP--GVPQLWILAVFVAGVWLMRAAGCVVNDYADRKFDGHVKRTANRPLPSGA 90
Cdd:PLN02809 9 YAKLARLDKPIGTWLLAWPCMWSIALAAPpgSLPDLKMLALFGCGALLLRGAGCTINDLLDRDIDKKVERTKLRPIASGA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535134085 91 VTEKEARALFVVLVLISFLLVLTLNTMTILLSIAALALAWVYPFMKRYTHLPQVVLGAAFGWSIPMAFAAVSESV-PLSC 169
Cdd:PLN02809 89 LTPFQGVGFLGAQLLLGLGILLQLNNYSRILGASSLLLVFTYPLMKRFTFWPQAFLGLTFNWGALLGWAAVKGSLdPAVV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535134085 170 WLMFLANILWAVAYDTQYAMVDRDDDVKIGIKSTAILFGQYDKLIIGILQIGVLALMAIIGELNGLGWGYYWSILVAGAL 249
Cdd:PLN02809 169 LPLYASGVCWTLVYDTIYAHQDKEDDLKVGVKSTALRFGDDTKLWLTGFGAASIGGLALSGYNAGLGWPYYAGLAAAAGH 248
|
250 260 270
....*....|....*....|....*....|....
gi 535134085 250 FVYQQKLIANREREACFKAFMNNNYVGLVLFLGL 283
Cdd:PLN02809 249 LAWQIQTVDLSSRADCNRKFVSNKWFGAIVFAGI 282
|
|
| UbiA |
pfam01040 |
UbiA prenyltransferase family; |
28-271 |
5.86e-56 |
|
UbiA prenyltransferase family;
Pssm-ID: 460038 [Multi-domain] Cd Length: 250 Bit Score: 180.89 E-value: 5.86e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535134085 28 LLWPTLWALWVATPGVPQLWILAVFVAGVWLMRAAGCVVNDYADRKFDGHVKRTANRPLPSGAVTEKEARALFVVLVLIS 107
Cdd:pfam01040 1 LLIPALAGLALAAGGVPDLLLLLLALLGTVLARAAANALNDYYDRDIDAIMPRTPNRPLPSGRISPREALIFALVLLALG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535134085 108 FLLVLTLNTMTILLSIAALALAWVYP-FMKRYTHLPQVVLGAAFGWSIPMAFAAVSESVPLSCWLMFLANILWAVAYDTQ 186
Cdd:pfam01040 81 LLLLLLLNPLTALLGLAALLLYVLYTlRLKRRTLLGQLVGGLAFGLPPLLGWAAVTGSLSPLALLLALALFLWTWAIALA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535134085 187 YAMVDRDDDVKIGIKSTAILFGQYDKLIIG-ILQIGVLALMAIIGELNGLGWGYYWSILVAGALFVYQQKLIANREREAC 265
Cdd:pfam01040 161 NDLRDREDDRKAGIKTLPVVLGRKAARILLaLLLAVALLLLLLLLLLLLGGLYLLLALLLAALALLYAARLLRLRDPKKD 240
|
....*.
gi 535134085 266 FKAFMN 271
Cdd:pfam01040 241 AKAFFF 246
|
|
| ubiA |
PRK12873 |
4-hydroxybenzoate polyprenyltransferase; |
7-286 |
1.05e-44 |
|
4-hydroxybenzoate polyprenyltransferase;
Pssm-ID: 171787 [Multi-domain] Cd Length: 294 Bit Score: 153.28 E-value: 1.05e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535134085 7 QNKLLAFHRLMRTDKPIGALLLLWPTLWALWVATPGVPQLWILAVFVAGVWLMRAAGCVVNDYADRKFDGHVKRTANRPL 86
Cdd:PRK12873 4 SIKLSPWFELLRWNKPTGRLILLIPAGWSLWLTPSAPPSLLLLLLIILGGLAVSGAGCIANDLWDRRIDRKVERTKNRPL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535134085 87 PSGAVTEKEARALFVVLVLISFLLVLTLNT----MTILLSIAALALAWVYPFMKRYTHLPQVVLGAAFGWSIPMAFAA-- 160
Cdd:PRK12873 84 ARGKISLKTAYSLLIVLLLLSLFVVLSLPQpsrnLCLSLAFLALPPILIYPSAKRWFAYPQAILALCWGFAVLIPWAAae 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535134085 161 --VSESVPL-SCWlmfLANILWAVAYDTQYAMVDRDDDVKIGIKSTAILFGQYDKLIIGILQIGVLALMAIIGELNGLGW 237
Cdd:PRK12873 164 gsLNGGWPLlFCW---LATLLWTFGFDTVYAMADRRDDAKIGLNSSALSLGSNALKTVQICYFLTSIFLALAAFIAQVGF 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 535134085 238 gYYWsILVAGALFVYQQKLIANREREACFKA----FMNNNYVGLVLFLGLAMS 286
Cdd:PRK12873 241 -IFW-PFWLIASIGMQRDILKLFPEKQSIKTignhFSNQVILGSLLLLGLILA 291
|
|
| ubiA |
PRK13106 |
prenyltransferase; Reviewed |
6-284 |
4.18e-30 |
|
prenyltransferase; Reviewed
Pssm-ID: 237283 Cd Length: 300 Bit Score: 115.21 E-value: 4.18e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535134085 6 TQNKLLAFHRLMRTDKPIGALLLLWptLWALwVATPGVPQLWILAVFVAGVWLMRAAGCVVNDYADRKFDGHVKRTANRP 85
Cdd:PRK13106 11 TRSKFYIILRFLRIEQTFFSLPMAY--LGAF-VAIKGIPPISTLILIFLALFFLRTAGMTNDNLADLEIDAKNPRTKNRP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535134085 86 LPSGAVTEKEARALFVVLVLISFLLVLTLNTMTILLSIAALALAWVYPFMKRYTHLPQVVLG-----AAFGWSIPMA--- 157
Cdd:PRK13106 88 LVTGAIKISEAKALITAGLILFFASAYLVNRWALLLSPIVALIAMSYPYMKRYTAFANYHLAsiqglAVFSGAVAVLgly 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535134085 158 ---FAAVSESVPlscWLMFLANILWAVAYDTQYAMVDRDDDVKIGIKSTAILFGQYDKLIIGILQIGVLALMAIIGELNG 234
Cdd:PRK13106 168 ansLIQVLLRVP---WLFVIGTILWAAGFDLYNHIPDAEFDREMGLHSFAVVLGKWALTFAGLNQLFSVVLDLLGDLYYG 244
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 535134085 235 LGWGYYWSILVAGALFVYQQKLIANREREAcfKAFMNNNYVGLVLFLGLA 284
Cdd:PRK13106 245 LGPIAIAATILHGLIMAYAYYLASKKGDFG--RAFYYNIYSSIVLGLGII 292
|
|
| ubiA |
PRK12888 |
4-hydroxybenzoate octaprenyltransferase; |
33-281 |
1.08e-20 |
|
4-hydroxybenzoate octaprenyltransferase;
Pssm-ID: 183814 Cd Length: 284 Bit Score: 89.39 E-value: 1.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535134085 33 LWALWVATPGVPQLWILAVFVAGVWLmRAAGCVVNDYADRKFDGHVKRTANRPLPSGAVTEKEARALFVVLVLISFLLVL 112
Cdd:PRK12888 26 LTAMFASDGSVHWADLLLVTVAMVGA-RTFAMAANRIIDREIDARNPRTAGRELVTGAVSVRTAWTGALVALAVFLGAAA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535134085 113 TLNTMTILLSIAALALAWVYPFMKRYTHLPQVVLGAAFGWSIPMAFAAVSESVPLSCWLMFLANILWAVAYDTQYAMVDR 192
Cdd:PRK12888 105 LLNPLCLALAPLAVAPLVVYPYAKRFTNFPHAILGLAQAVGPVGAWIAVTGTWSWPAVLLGLAVGLWIGGFDLIYACQDA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535134085 193 DDDVKIGIKSTAILFGQYDKLIIG-ILQIGVLALMAIIGELNGLGWGYYWSILVAGALFVYQQKLIANREREACFKAF-M 270
Cdd:PRK12888 185 EVDRRIGVRSVPARFGVRAALWASrVAHVVTFALFVWFGLAVGFGALWWIGLAITAGAFAYEHAIVSPTDLSRVNRAFfT 264
|
250
....*....|.
gi 535134085 271 NNNYVGLVLFL 281
Cdd:PRK12888 265 ANGFVGIALFG 275
|
|
| PT_UbiA_Cox10 |
cd13957 |
Protoheme IX farnesyltransferase; Protoheme IX farnesyltransferase (also called heme O ... |
21-281 |
8.18e-20 |
|
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: 86.72 E-value: 8.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535134085 21 KPIGALLLLWPTLWALWVATPGVPQLWILAVFVAGVWLMRAAGCVVNDYADRKFDGHVKRTANRPLPSGAVTEKEARALF 100
Cdd:cd13957 5 KPRITLLVLLTALAGYLLAPGGVPDLLLLLLTLLGTALVSASANALNQYIERDIDAKMKRTRNRPLPSGRISPKHALIFG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535134085 101 VVLVLISF-LLVLTLNTMTILLSIAALAL-AWVYPFMKRYTHLPQVVLGAAFGwSIP--MAFAAVSESVPLSCWLMFLAN 176
Cdd:cd13957 85 LVLGILGLaLLALFVNPLTALLGLLGIFLyVFVYTPLKKRTTPLNTVIGGIAG-AIPplIGWAAATGSLDLGAWLLFLIL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535134085 177 ILWavaydtQY------AMVDRDDDVKIGIKSTAILFG-QYDKLIIGILQIGVLALMAIIGELNGLGWGYYWSILVAGAL 249
Cdd:cd13957 164 FLW------QPphfwalAILYRDDYARAGIPMLPVVKGeRRTKRQILLYTLLLVPLSLLLYLLGLTGWIYLVVALLLGLY 237
|
250 260 270
....*....|....*....|....*....|....
gi 535134085 250 FVYQ-QKLIANREREACFKAFMN-NNYVGLVLFL 281
Cdd:cd13957 238 FLYLaIKLYRSPDDKWARKLFFAsLIYLPLLFLL 271
|
|
| ubiA |
PRK12886 |
prenyltransferase; Reviewed |
40-288 |
3.14e-19 |
|
prenyltransferase; Reviewed
Pssm-ID: 237247 Cd Length: 291 Bit Score: 85.51 E-value: 3.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535134085 40 TPGVPQL-WILAVFVAGvwlmRAAGCVVNDYADRKFDGHVKRTANRPLPSGAVTeKEARALFVVLVLISFLLV-LTLNTM 117
Cdd:PRK12886 38 LPGASQLdWILMAMVGA----RTAAMGFNRLIDAEIDARNPRTAGRAIPAGLIS-KGSAILFIVLSSLLMLFAaWFLNPL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535134085 118 TILLSIAALALAWVYPFMKRYTHLPQVVLGAAFGWSIPMAFAAVSESVPLSCWLMFLANILWAVAYDTQYAMVDRDDDVK 197
Cdd:PRK12886 113 CLYLSPPALFFLLLYSYCKRFTALAHVVLGFCLALAPLGAWIAIRGTIELPAILLGLAVLFWVAGFDILYALQDLEFDRK 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535134085 198 IGIKSTAILFGQYDKLIIG-ILQIGVLALMAIIGELNGLGWGYYWSILVAGALFVYQQKLIANREREACFKAFMN-NNYV 275
Cdd:PRK12886 193 EGLHSIPAKLGVNGSLWIArVFHLLMIGFLFALGISAGLGPWFLAGLAVTGILLLYEHWLLRGGDLTRLDAAFFNmNGYI 272
|
250
....*....|...
gi 535134085 276 GLVLFLGLAMSYW 288
Cdd:PRK12886 273 SVTLFAATLFDRL 285
|
|
| PRK04375 |
PRK04375 |
protoheme IX farnesyltransferase; Provisional |
27-288 |
6.65e-19 |
|
protoheme IX farnesyltransferase; Provisional
Pssm-ID: 235293 Cd Length: 296 Bit Score: 84.42 E-value: 6.65e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535134085 27 LLLWPTLWALWVATPGVPQLWILAVFVAGVWLMRAAGCVVNDYADRKFDGHVKRTANRPLPSGAVTEKEARALFVVLVLI 106
Cdd:PRK04375 24 LNLFTALGGMLLAPPGVPPLLLLLLTLLGIALVAGAAGALNNYIDRDIDAKMERTKNRPLVTGRISPREALIFGLVLGVL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535134085 107 SF-LLVLTLNTMTILLSIAALAL-AWVYP-FMKRYThlPQ-VVLGAAFGWSIPM-AFAAVSESVPLSCWLMFLANILWAV 181
Cdd:PRK04375 104 GFlLLGLFVNPLAAWLTLAGIFFyVVVYTlWLKRRT--PQnIVIGGAAGAMPPLiGWAAVTGSLSWEALILFLIIFLWTP 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535134085 182 AYDTQYAMVDRDD--DVKI-------GIKSTAILFgqydkLIIGILQIGVLALMAIIGElngLGWGYYWSILVAGALFVY 252
Cdd:PRK04375 182 PHFWALAIFRKDDyaAAGIpmlpvvkGIRVTKRQI-----LLYTVLLVAVSLLPVLLGM---AGLLYLVVALLLGAWFLY 253
|
250 260 270
....*....|....*....|....*....|....*..
gi 535134085 253 Q-QKLIANREREACFKAFMNNNYVGLVLFLGLAMSYW 288
Cdd:PRK04375 254 YaWRLYRKDDRKWARKLFRYSINYLTLLFVALLVDHL 290
|
|
| PT_UbiA |
cd13956 |
UbiA family of prenyltransferases (PTases); Many characterized members of the UbiA ... |
15-284 |
1.56e-17 |
|
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: 80.47 E-value: 1.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535134085 15 RLMRTdkPIGALLLLWPTLWALWVATPGVPQLWILAVFVAGVWLMRAAGCVVNDYADRKFDGHVKRtaNRPLPSGAVTEK 94
Cdd:cd13956 2 RLMRP--YTLLYVLAPALAGAALAGAFAGPLPALLLLALLAVFLGAGAGYALNDYTDRELDAINKP--DRPLPSGRLSPR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535134085 95 EARALFVVLVLISFLLVLTLNTMTILLSIAALALAWVYPFMKRYTHLPQ-VVLGAAFGWSIPMAFAAVSE-SVPLSCWLM 172
Cdd:cd13956 78 QALAFAAALLLVGLALALALGPLALLLLLAGLLLGLAYSLGLKRLKLGGwGVLGYATGLALLPGLGAVAAgGLVPLALLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535134085 173 FLANILWAVAYDTQYAMVDRDDDVKIGIKSTAILFGQ--YDKLIIGILQIGVLALMAIIGELNGLGWGYYWSILVAGALF 250
Cdd:cd13956 158 ALVFLLLGLGINLYNDLPDVEGDRAAGIRTLPVRLGPrrARRLAAGLLLAALILVVLLAVAGLLGPLALLALLAVALLAL 237
|
250 260 270
....*....|....*....|....*....|....
gi 535134085 251 VYQQKLIANREREAcfKAFMNNNYVGLVLFLGLA 284
Cdd:cd13956 238 RARFARADRLPALP--RGFLLLAVYRLLLFAALL 269
|
|
| cyoE_ctaB |
TIGR01473 |
protoheme IX farnesyltransferase; This model describes protoheme IX farnesyltransferase, also ... |
27-283 |
8.25e-15 |
|
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: 72.66 E-value: 8.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535134085 27 LLLWPTLWALWVAT-PGVPQLWILAVFVAGVWLMRAAGCVVNDYADRKFDGHVKRTANRPLPSGAVTEKEARALFVVLVL 105
Cdd:TIGR01473 14 LLLITAFAGMWLAPgGALVNPPLLLLTLLGTTLAAASANAFNMYIDRDIDKKMKRTRNRPLVTGRISPREALAFGLLLGV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535134085 106 ISF-LLVLTLNTMTILLSIAALAL-AWVY-PFMKRYTHLpQVVLGAAFGwSIP--MAFAAVSESVPLSCWLMFLANILWA 180
Cdd:TIGR01473 94 LGVaILAAFVNPLAALLGLFGIFFyVIVYtIWLKRRTPQ-NTVIGGFAG-AVPplIGWAAVTGSISLGAWLLFAIIFLWQ 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535134085 181 VAYDTQYAMVDRDDDVKIGIKSTAILFG-QYDKLIIGILQIGVLALMAIIGELNGLGWGYYWSILVAGALFVYQ--QKLI 257
Cdd:TIGR01473 172 PPHFWALALKYKDDYRAAGIPMLPVVKGeRITKRQIALYTAALLPVSLLLAFLGGTGWLYLIVATLLGALFLYLafKFYR 251
|
250 260
....*....|....*....|....*..
gi 535134085 258 ANREREACFKAFM-NNNYVGLVLFLGL 283
Cdd:TIGR01473 252 DPTDRKKARKLFKfSLIYLALLFVALL 278
|
|
| ubiA |
PRK12874 |
4-hydroxybenzoate polyprenyltransferase; |
66-288 |
6.85e-12 |
|
4-hydroxybenzoate polyprenyltransferase;
Pssm-ID: 237242 Cd Length: 291 Bit Score: 64.64 E-value: 6.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535134085 66 VNDYADRKFDGHVKRTANRPLPSGAVTEKeARALFVVLVLISFLLVLTL-NTMTILLSIAALALAWVYPFMKRYTHLPQV 144
Cdd:PRK12874 66 FNRLVDRDIDKDNPRTANRPSVDGRISVK-SMVLFIVLNALIFIGVSYFiNPLAFKLSFPFLIVLGGYSYFKRFSSLAHL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535134085 145 VLGAAFGWSiPMAFA-AVSESVPLSCWLMFLANILWAVAYDTQYAMVDRDDDVKIGIKSTAILFGQYDKLIIGIL--QIG 221
Cdd:PRK12874 145 VLGLSLGLA-PIAGVvAVLGEIPLWSVFLALGVMFWVAGFDLLYSLQDMEFDKKRGLHSIPSKFGEKATLFISRLfhLLA 223
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 535134085 222 VLALMAIIGELNGLGWGYYwSILVAGALFVYQQKLIaNREREACFKAFMN-NNYVGLVLFLGLAMSYW 288
Cdd:PRK12874 224 VLFWLLFVWCAHLGLFAYL-GVIVSALILLYEHYLV-RKDFKKIDKAFFTlNGYLGIVFFIFIVLDVL 289
|
|
| ubiA |
PRK12895 |
prenyltransferase; Reviewed |
48-286 |
7.04e-12 |
|
prenyltransferase; Reviewed
Pssm-ID: 237251 Cd Length: 286 Bit Score: 64.45 E-value: 7.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535134085 48 ILAVFVAGVwLMRAAGCVVNDYADRKFDGHVKRTANRPLPSGAVTEKEARALFVVLVLISFLLVLTLNTMTILLSIAALA 127
Cdd:PRK12895 39 ILLILIAAV-SARTSAMSINRIEGLRYDMINPRKKDWALVSGRIKMREAIAFTIIFIAIFEICTFLLNRLVFILSPIVIF 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535134085 128 LAWVYPFMKRYTHLPQVVLGAAFGWSIPMAFAAVSESVP--LSCWLMFLANILWAVAYDTQYAMVDRDDDVKIGIKSTAI 205
Cdd:PRK12895 118 LFIIDPFLKRYTAWRHIYMGSIIGLGVLAGYLAVIPAFPynLLIYIIFISSSLWIAGFDIIYVIPDIEYDKINGLKTIMN 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535134085 206 LFGQYDKLIIGIL-QIGVLALMAIIGELNGLGWgYYWSILVAGALFVYQQKLIANREREACFKAFMN-NNYVGLVLFLGL 283
Cdd:PRK12895 198 TYGIKNGLYISDIfHISSLILFWISGIYIRTLW-YLAALIIIYTLVIYQHLIIDPRNPINKRMSFFNaNSFIGFVFLIGI 276
|
...
gi 535134085 284 AMS 286
Cdd:PRK12895 277 ILS 279
|
|
| ubiA |
PRK12876 |
prenyltransferase; Reviewed |
60-280 |
1.96e-11 |
|
prenyltransferase; Reviewed
Pssm-ID: 237244 Cd Length: 300 Bit Score: 63.23 E-value: 1.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535134085 60 RAAGCVVNDYADRKFDGHVKRTANRPLPSGAVTEKEAralFVVLVLISFLLVLT---LNTMTILLSIAALALAWVYPFMK 136
Cdd:PRK12876 60 RTVGIIVNQIIDCAIDKKNPRTSSRVLPAKLLSINFS---MLLLTLCSFLFLSLcwlLNPLCFSLAVLSTLLMIIYPYTK 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535134085 137 RYTHLPQVVLGAAFGWSIPMAFAAVSESvPLSCWLMFLANiLWAV-------AYDTQYAMVDRDDDVKIGIKSTAILFGQ 209
Cdd:PRK12876 137 RVTFLCHWILGLVYYLAILMNFFAIIET-PLSFSLFCMAS-LWGIsfgmiiaANDIIYAIQDLEFDRKEGLFSIPARFGE 214
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 535134085 210 YDKLII--GILQIGVLALMAIIGELNGLGWGYYWSIL-VAGALFV---YQQKLIANREREACFkaFMNNNYVGLVLF 280
Cdd:PRK12876 215 KKAIRIasANLIASAIAYLLIGYFVSNKKIFYLCSLVpLTVILKTikhYSLIDKKKSTLEQKF--FLGNIYLALSFF 289
|
|
| ubiA |
PRK12884 |
prenyltransferase; Reviewed |
9-268 |
4.43e-11 |
|
prenyltransferase; Reviewed
Pssm-ID: 183812 Cd Length: 279 Bit Score: 61.90 E-value: 4.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535134085 9 KLLAFHRLMRTDKPIGALLLLwptLWALWVATPGVPQLWILAVFVAGVWLMrAAGCVVNDYADRKFDgHVKRTaNRPLPS 88
Cdd:PRK12884 3 KMKAYLELLRPEHGLMAGIAV---VLGAIIALGGLPLDEALLGFLTAFFAS-GSANALNDYFDYEVD-RINRP-DRPIPS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535134085 89 GAVTEKEARALFVVLVLISFLLVLTLNTMTILLSIAALALAWVYPFM-KRYTHLPQVVLgaAFGWSIPMAFAA-VSESVP 166
Cdd:PRK12884 77 GRISRREALLLAILLFILGLIAAYLISPLAFLVVILVSVLGILYNWKlKEYGLIGNLYV--AFLTGMTFIFGGiAVGELN 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535134085 167 LSCWLMFLANILWAVAYDTQYAMVDRDDDVKIGIKSTAILFGQYDKLIIGILQIGVLALMAIIGELNG-LGWGYYWSILV 245
Cdd:PRK12884 155 EAVILLAAMAFLMTLGREIMKDIEDVEGDRLRGARTLAILYGEKIAGRIAAALFILAVLLSPLPYLFGiFNILYLAPVLV 234
|
250 260
....*....|....*....|....
gi 535134085 246 AGALFVYQ-QKLIANREREACFKA 268
Cdd:PRK12884 235 ADLIFLYSaYSLLRSQDRETIRKV 258
|
|
| PT_UbiA_DGGGPS |
cd13961 |
Geranylgeranylglycerol-phosphate geranylgeranyltransferase; Digeranylgeranylglyceryl phosphate ... |
46-264 |
1.78e-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: 60.21 E-value: 1.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535134085 46 LWILAVFVAGVWLMRAAGCVVNDYADRKFDgHVKRTaNRPLPSGAVTEKEARALFVVLVLISFLLVLTLNTMTILLSIAA 125
Cdd:cd13961 34 DLELLLLFLSVFLIAAAGYIINDYFDVEID-RINKP-DRPIPSGRISRREALILSILLNALGLILAFLLSPLALLIALLN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535134085 126 LALAWVYP-FMKRYTHLPQVVLGAAFGWSIPMAFAAVSESVPLScWLMFLANILWAVAYDTQYAMVDRDDDVKIGIKSTA 204
Cdd:cd13961 112 SLLLWLYShKLKRTPLIGNLLVALLTGLPFLFGGLAAGNLLLII-LLLALFAFLITLGREIVKDIEDVEGDRAEGARTLP 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 535134085 205 ILFG-QYDKLIIGILQIGVLALMAIIGELNGLGWGYYWSILVAGALFVYQQKLIANREREA 264
Cdd:cd13961 191 IVYGiKKAKKIAALLLLLAILLSPLPYLLGGLGILYLILIIIADLLFLYSAIRLAKSPKDY 251
|
|
| PRK09573 |
PRK09573 |
(S)-2,3-di-O-geranylgeranylglyceryl phosphate synthase; Reviewed |
48-281 |
2.30e-07 |
|
(S)-2,3-di-O-geranylgeranylglyceryl phosphate synthase; Reviewed
Pssm-ID: 181963 Cd Length: 279 Bit Score: 51.11 E-value: 2.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535134085 48 ILAVFVagVWLMRAAGCVVNDYADRKFDGHVKrtANRPLPSGAVTEKEARALFVVLVLISFLLVLTLNTMTILLSIAALA 127
Cdd:PRK09573 40 ILAALV--VFLVCAGGNVINDIYDIEIDKINK--PERPIPSGRISLKEAKIFSITLFIVGLILSIFINIYAFLIALLNSI 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535134085 128 LAWVYP-FMKRYTHLPQVVLGAAFGWSIpmAFAAVSESVPLSCWLMFLANILWAVAYDTQYAMVDRDDDVKIGIKSTAIL 206
Cdd:PRK09573 116 LLYLYAkDLKKTGLIGNLIVAYLTGLSF--IFGGLAVFNVLRIIILFLCAFFSTWSREIVKDIEDIEGDLKENVITLPIK 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535134085 207 FGQYDKLIIGILQIGVLALMAIIGELNG-LGWGYYWSILVAGALFVYQQ-KLIANREREACFKAFMNNNY---VGLVLFL 281
Cdd:PRK09573 194 YGIKKSWYIAKILLILAIVLSPLPYFLGiFGIYYLIVVIICDILFIIAMlILLKNPSIEGASKASKYLKIimiLGLIAFL 273
|
|
| PT_UbiA_UBIAD1 |
cd13962 |
1,4-Dihydroxy-2-naphthoate octaprenyltransferase; Human UBIAD1 is an enzyme involved in the ... |
42-286 |
1.12e-06 |
|
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: 49.05 E-value: 1.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535134085 42 GVPQLWILAVFVAGVWLMRAAGCVVNDYAD--RKFDGHVKRTANRPLPSGAVTEKEARALFVVLVLISFLLVLTLNTMTI 119
Cdd:cd13962 28 GFFNWLLFLLALLAALLLQIGVNLANDYFDykKGTDTEPRSGPSRVLVSGLLSPRQVLRAALVLLLLAALLGLYLVALGG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535134085 120 LLSIAA----LALAWVY---PFMKRYTHLPQVVLGAAFGWSIPM-AFAAVSESVPLSCWLMFLANILWAVAydTQYA--M 189
Cdd:cd13962 108 WLLLLLgllgILAGYFYtggPFPLSYRGLGELFVFLFFGLLAVLgTYYVQTGSLSWEVLLAALPLGLLIAA--ILLAnnI 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535134085 190 VDRDDDVKIGIKSTAILFG-QYDKLIIGILQIGVLALMAIIGELNGLGWGYYWSILVagALFVYQQKLIANREREACFKA 268
Cdd:cd13962 186 RDIEADRAAGKRTLAVRLGrKRARRLYAALLLLAYLLLLLLVLLGLLPLWSLLALLS--LPLAIKLLRRLLRKADKPLLL 263
|
250
....*....|....*...
gi 535134085 269 FMNNNYVGLVLFLGLAMS 286
Cdd:cd13962 264 IALKLTALLTLLFGLLLA 281
|
|
| ubiA |
PRK12882 |
prenyltransferase; Reviewed |
38-110 |
1.16e-06 |
|
prenyltransferase; Reviewed
Pssm-ID: 183811 Cd Length: 276 Bit Score: 48.82 E-value: 1.16e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 535134085 38 VATPGVPQLWILAVfvagVWLMRAAGCVVNDYADRKFDgHVKRtANRPLPSGAVTEKEARA----LFVVLVLISFLL 110
Cdd:PRK12882 33 ILSSPSLTGLAFAA----VFLATGAGNAINDYFDREID-RINR-PDRPIPSGAVSPRGALAfsilLFAAGVALAFLL 103
|
|
| ubiA |
PRK12883 |
prenyltransferase UbiA-like protein; Reviewed |
38-268 |
6.06e-06 |
|
prenyltransferase UbiA-like protein; Reviewed
Pssm-ID: 171796 Cd Length: 277 Bit Score: 46.65 E-value: 6.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535134085 38 VATPGVPQLWILAVFVAGVWLMRAAGCVVNDYADRKFDgHVKRtANRPLPSGAVTEKEARALFVVLVLISFLLVLTLNTM 117
Cdd:PRK12883 28 VALGGIPPIKTLILIFLVVYLGCSGGNTINDYFDYEID-KINR-PNRPLPRGAMSRKAALYYSLLLFAVGLALAYLINIE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535134085 118 TILLSIAALALAWVYPFMKRYTHLPQVVLGAAFGWSIPMAFAAVSESVPLSCWL---MFLANILWAVAYDTQyamvDRDD 194
Cdd:PRK12883 106 AFLFALGAYVLMFLYAWKLKPLPFIGNVVVALLTGATPIYGAIAVGRIGLAGYLaicAFLVNVAREIMKDIE----DIEG 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 535134085 195 DVKIGIKSTAILFGQYDKLIIGILqIGVLALMAIIGELN-GLGWGYYWSILVAGALFVYQQKLIANREREACFKA 268
Cdd:PRK12883 182 DKAKGAKTLPIIIGKKRAAYIGAI-FGVLTVIASFLPVKaGIGLGYLPIIIVDAIILYAAYLVLRNPDRETAHKG 255
|
|
| PT_UbiA_2 |
cd13963 |
UbiA family of prenyltransferases (PTases), Unknown subgroup; Many characterized members of ... |
65-116 |
7.28e-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: 260126 Cd Length: 278 Bit Score: 43.23 E-value: 7.28e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 535134085 65 VVNDYADRKFDGH--VKRtaNRPLPSGAVTEKEARALFVVLVLISFLLVLTLNT 116
Cdd:cd13963 51 ILNDLLDLEADRLhpTKR--NRPIASGRLSIPAALALAVVLLLAGLALALLLSP 102
|
|
| PT_UbiA_1 |
cd13964 |
UbiA family of prenyltransferases (PTases), Unknown subgroup; Many characterized members of ... |
35-175 |
8.16e-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: 260127 Cd Length: 282 Bit Score: 43.34 E-value: 8.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535134085 35 ALWVATPGVPQLWILAVFVAGVwLMRAAGCVVNDYADRKFDGhVKRtANRPLPSGAVTEKEARALFVVLVLISFLLVLTL 114
Cdd:cd13964 21 AALAGGGLGPVLRLALLLLASV-LLYAAGMVLNDVFDAELDA-RER-PERPIPSGRVSRGAALALGAGLLAAGVALAALV 97
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 535134085 115 NTMTILLSIAALALAWVYP-FMKRYTHLPqVVLGAAFGWSIPMAFAAVSESVPLSCWLMFLA 175
Cdd:cd13964 98 GRLSGLVALLLAAAILLYDaWLKHTPLGP-LLMGLCRGLNLLLGASAAAAGGLGPALLAALA 158
|
|
| PT_UbiA_chlorophyll |
cd13958 |
Bacteriochlorophyll/chlorophyll synthetase; Chlorophyll synthase catalyzes the last step of ... |
44-253 |
1.06e-04 |
|
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: 42.99 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535134085 44 PQLWILAVFVAGVWLMRAAGC----VVNDYADRKFDGhvKRTANRPLPSGAVTEKEARALFVVLVLISFLLVLTLNTMTI 119
Cdd:cd13958 29 WSNWDVWLLLLGMLLAGPLLTgtsqTINDYYDREVDA--INEPYRPIPSGRISEREALWNIWVLLLLSLLVALFLDGPWV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535134085 120 LLSIAA-LALAWVY---PF-MKR------------YTHLPQVVLGAAFGWSIPmafaavSESVPLSCW-------LMFLa 175
Cdd:cd13958 107 FAAAVVgLVLAYIYsapPLkLKQngwwgnaavglsYEGLPWWAGAAAFAGLLT------WESLALALLysigahgIMTL- 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 535134085 176 NILWAVAYDTQYAMvdRDDDVKIGIKSTAILFGqydkLIIGILQIGVLALMAIigelnglgWGYYWSILVAGALFVYQ 253
Cdd:cd13958 180 NDFKSIEGDRQLGL--RSLPVALGVDTAAWIAC----GVIDVPQLAVAALLLA--------WGETWYAAVVGALLLAQ 243
|
|
| PRK12324 |
PRK12324 |
decaprenyl-phosphate phosphoribosyltransferase; |
8-115 |
1.62e-04 |
|
decaprenyl-phosphate phosphoribosyltransferase;
Pssm-ID: 237058 Cd Length: 295 Bit Score: 42.54 E-value: 1.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535134085 8 NKLLAFHRLMRTDKPIGALLLLWPTLWALWVATPGVPQLWILAvFVAgVWLMRAAGCVVNDYADRKFDG-H-VKRtaNRP 85
Cdd:PRK12324 9 NLLAGYLKLLRPKQWIKNLFVFAAPIFAGNLLNPGALLKVLLA-FVL-FCLASSAVYLVNDIRDVEADRlHpTKR--NRP 84
|
90 100 110
....*....|....*....|....*....|
gi 535134085 86 LPSGAVTEKEARALFVVLVLISFLLVLTLN 115
Cdd:PRK12324 85 IASGVVSVSLAYILAVVLLVASLALAYLLS 114
|
|
| PRK07566 |
PRK07566 |
chlorophyll synthase ChlG; |
4-275 |
2.56e-04 |
|
chlorophyll synthase ChlG;
Pssm-ID: 236052 Cd Length: 314 Bit Score: 41.83 E-value: 2.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535134085 4 SLTQNKLLAFHRLMrtdKPIgalllLW-PTLWALW--VATPGVPQLWILAV--FVAGVWL----MRAAGCVVNDYADRKF 74
Cdd:PRK07566 21 SPTTSIWKARLQLM---KPI-----TWfPPMWAFLcgAVSSGAFGWTLENVlkLLAGMLLagplLCGTSQTLNDYFDREV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535134085 75 DghvkrtA----NRPLPSGAVTEKEARALFVVLVLISFLLVLTLNTMTILLSIAALALAWVY---PF-MKRYTHLPQVVL 146
Cdd:PRK07566 93 D------AinepYRPIPSGAISLRWVLYLIAVLTVLGLAVAYLLGPWVFLAALLGLFLAWIYsapPLrLKQNGWLGNYAV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535134085 147 GA---AFGWsipMAFAAVSESVPLSCWLMFLANILWAVAYDTqyaMVDRD-----DDVKIGIKSTAILFGQYDK-----L 213
Cdd:PRK07566 167 GLsyeGLPW---WAGAAAFGAGLPSWPIVILALLYSLGAHGI---MTLNDfksveGDRQLGLRSLPVVFGEKNAariacV 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 535134085 214 IIGILQIGVLALMaiigelngLGWGYYWSILVAGAL----FVYQQKLIAN-REREACFKAFMNNNYV 275
Cdd:PRK07566 241 VIDLFQLAVIALL--------LAWGQPLYAAIVGLLlipqITLQDRLLRDpLERDVWYNASAQPFYV 299
|
|
| ubiA |
PRK12871 |
prenyltransferase; Reviewed |
62-114 |
6.48e-04 |
|
prenyltransferase; Reviewed
Pssm-ID: 106000 Cd Length: 297 Bit Score: 40.57 E-value: 6.48e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 535134085 62 AGCVVNDYADRKFD-----GHVKRT----ANRPLPSGAVTEKEARALFVVLVLISFLLVLTL 114
Cdd:PRK12871 56 AGFVLNDYVDRKRDrldveNTLTRYwrpfKERPIPSGKLSSKNAFALFILLAAVTSALILTL 117
|
|
| PLN02776 |
PLN02776 |
prenyltransferase |
38-201 |
1.80e-03 |
|
prenyltransferase
Pssm-ID: 215415 Cd Length: 341 Bit Score: 39.34 E-value: 1.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535134085 38 VATPGVPQLWILAVFVAGVWLMRAAGCVVNDYADRKFDGHVKRTANRPLPSGAVTEKEArALFVVLVLISFLLVLTL--N 115
Cdd:PLN02776 20 LGSGEAIDLPGLGWTCAGTMLCAASANTLNQVFEVKNDSKMKRTMRRPLPSGRISVPHA-VAWAVVVGAAGVALLAYktN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535134085 116 TMTILLSIA-ALALAWVYPFMKRyTHLPQVVLGAAFGwSIP--MAFAAVSESVPLSCWLMFLANILWAVAYDTQYAMVDR 192
Cdd:PLN02776 99 MLTAGLGAGnILLYAFVYTPLKQ-IHPANTWVGAVVG-AIPplMGWAAASGQLDAGAMVLAAALYFWQMPHFMALAYMCR 176
|
....*....
gi 535134085 193 DDDVKIGIK 201
Cdd:PLN02776 177 DDYAAGGYR 185
|
|
|