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Conserved domains on  [gi|6319475|ref|NP_009557|]
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trans-hexaprenyltranstransferase [Saccharomyces cerevisiae S288C]

Protein Classification

isoprenoid biosynthesis enzyme family protein( domain architecture ID 89)

isoprenoid biosynthesis enzyme family protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Isoprenoid_Biosyn_C1 super family cl00210
Isoprenoid Biosynthesis enzymes, Class 1; Superfamily of trans-isoprenyl diphosphate synthases ...
48-471 4.23e-90

Isoprenoid Biosynthesis enzymes, Class 1; Superfamily of trans-isoprenyl diphosphate synthases (IPPS) and class I terpene cyclases which either synthesis geranyl/farnesyl diphosphates (GPP/FPP) or longer chained products from isoprene precursors, isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP), or use geranyl (C10)-, farnesyl (C15)-, or geranylgeranyl (C20)-diphosphate as substrate. These enzymes produce a myriad of precursors for such end products as steroids, cholesterol, sesquiterpenes, heme, carotenoids, retinoids, and diterpenes; and are widely distributed among archaea, bacteria, and eukaryota.The enzymes in this superfamily share the same 'isoprenoid synthase fold' and include several subgroups. The head-to-tail (HT) IPPS catalyze the successive 1'-4 condensation of the 5-carbon IPP to the growing isoprene chain to form linear, all-trans, C10-, C15-, C20- C25-, C30-, C35-, C40-, C45-, or C50-isoprenoid diphosphates. Cyclic monoterpenes, diterpenes, and sesquiterpenes, are formed from their respective linear isoprenoid diphosphates by class I terpene cyclases. The head-to-head (HH) IPPS catalyze the successive 1'-1 condensation of 2 farnesyl or 2 geranylgeranyl isoprenoid diphosphates. Cyclization of these 30- and 40-carbon linear forms are catalyzed by class II cyclases. Both the isoprenoid chain elongation reactions and the class I terpene cyclization reactions proceed via electrophilic alkylations in which a new carbon-carbon single bond is generated through interaction between a highly reactive electron-deficient allylic carbocation and an electron-rich carbon-carbon double bond. The catalytic site consists of a large central cavity formed by mostly antiparallel alpha helices with two aspartate-rich regions located on opposite walls. These residues mediate binding of prenyl phosphates via bridging Mg2+ ions, inducing proposed conformational changes that close the active site to solvent, stabilizing reactive carbocation intermediates. Generally, the enzymes in this family exhibit an all-trans reaction pathway, an exception, is the cis-trans terpene cyclase, trichodiene synthase. Mechanistically and structurally distinct, class II terpene cyclases and cis-IPPS are not included in this CD.


The actual alignment was detected with superfamily member TIGR02749:

Pssm-ID: 469660  Cd Length: 322  Bit Score: 277.40  E-value: 4.23e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319475     48 LVSKEMNTLAKNIVALIGSGHPVLNKVTSYYFETEGKKVRPLLVLLLSRALSEipmternhlkidksdvpedpiyskpsq 127
Cdd:TIGR02749   9 PVEDDLYLLTDNLKSLVGARHPILYAAAEHLFSAGGKRLRPAIVLLVSRATAE--------------------------- 61
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319475    128 nqlfqrpassisplhilhgikplnpltkgpeplpeetfdkQRGILPKQRRLAEIVEMIHTASLLHDDVIDHSDTRRGRPS 207
Cdd:TIGR02749  62 ----------------------------------------QQELTPRHRRLAEITEMIHTASLVHDDVIDESDTRRGIET 101
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319475    208 GNAAFTNKMAVLAGDFLLGRATVSISRLHNPEVVELMSNSIANLVEGEFMQLKNtSIDADIDtienghkllpvpskklev 287
Cdd:TIGR02749 102 VHSLFGTRVAVLAGDFLFAQASWYLANLENLEVVKLISKVITDFAEGEIKQGLN-QFDSDLS------------------ 162
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319475    288 kehdfrvpsrqqglqlshdqiietaFEYYIHKTYLKTAALISKSCRCAAILSGASPAVIDECYDFGRNLGICFQLVDDML 367
Cdd:TIGR02749 163 -------------------------LEDYLEKSFYKTASLVAASSKAAAVLSDVPSQVANDLYEYGKHLGLAFQVVDDIL 217
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319475    368 DFTVSGKDLGKPSGADLKLGIATAPVLFAWKEDPSLGPLISRNFSERGDVEKTIDSVRLHNGIAKTKILAEEYRDKALQN 447
Cdd:TIGR02749 218 DFTGSTEQLGKPAGSDLMKGNLTAPVLFALEEEPKLSELIEREFSQKGDLEQALSLVRKSGGIKKARELAKEQAQLALQS 297
                         410       420
                  ....*....|....*....|....
gi 6319475    448 LrDSLPESDARSALEFLTNSILTR 471
Cdd:TIGR02749 298 L-SFLPPSPPREALKELVHFVLSR 320
 
Name Accession Description Interval E-value
prenyl_cyano TIGR02749
solanesyl diphosphate synthase; Members of this family all are from cyanobacteria or ...
48-471 4.23e-90

solanesyl diphosphate synthase; Members of this family all are from cyanobacteria or plastid-containing eukaryotes. A member from Arabidopsis (where both plastoquinone and ubiquinone contain the C(45) prenyl moiety) was characterized by heterologous expression as a solanesyl diphosphate synthase. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]


Pssm-ID: 131796  Cd Length: 322  Bit Score: 277.40  E-value: 4.23e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319475     48 LVSKEMNTLAKNIVALIGSGHPVLNKVTSYYFETEGKKVRPLLVLLLSRALSEipmternhlkidksdvpedpiyskpsq 127
Cdd:TIGR02749   9 PVEDDLYLLTDNLKSLVGARHPILYAAAEHLFSAGGKRLRPAIVLLVSRATAE--------------------------- 61
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319475    128 nqlfqrpassisplhilhgikplnpltkgpeplpeetfdkQRGILPKQRRLAEIVEMIHTASLLHDDVIDHSDTRRGRPS 207
Cdd:TIGR02749  62 ----------------------------------------QQELTPRHRRLAEITEMIHTASLVHDDVIDESDTRRGIET 101
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319475    208 GNAAFTNKMAVLAGDFLLGRATVSISRLHNPEVVELMSNSIANLVEGEFMQLKNtSIDADIDtienghkllpvpskklev 287
Cdd:TIGR02749 102 VHSLFGTRVAVLAGDFLFAQASWYLANLENLEVVKLISKVITDFAEGEIKQGLN-QFDSDLS------------------ 162
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319475    288 kehdfrvpsrqqglqlshdqiietaFEYYIHKTYLKTAALISKSCRCAAILSGASPAVIDECYDFGRNLGICFQLVDDML 367
Cdd:TIGR02749 163 -------------------------LEDYLEKSFYKTASLVAASSKAAAVLSDVPSQVANDLYEYGKHLGLAFQVVDDIL 217
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319475    368 DFTVSGKDLGKPSGADLKLGIATAPVLFAWKEDPSLGPLISRNFSERGDVEKTIDSVRLHNGIAKTKILAEEYRDKALQN 447
Cdd:TIGR02749 218 DFTGSTEQLGKPAGSDLMKGNLTAPVLFALEEEPKLSELIEREFSQKGDLEQALSLVRKSGGIKKARELAKEQAQLALQS 297
                         410       420
                  ....*....|....*....|....
gi 6319475    448 LrDSLPESDARSALEFLTNSILTR 471
Cdd:TIGR02749 298 L-SFLPPSPPREALKELVHFVLSR 320
IspA COG0142
Geranylgeranyl pyrophosphate synthase [Coenzyme transport and metabolism]; Geranylgeranyl ...
177-473 3.86e-81

Geranylgeranyl pyrophosphate synthase [Coenzyme transport and metabolism]; Geranylgeranyl pyrophosphate synthase is part of the Pathway/BioSystem: Isoprenoid biosynthesis


Pssm-ID: 439912 [Multi-domain]  Cd Length: 329  Bit Score: 254.38  E-value: 3.86e-81
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319475  177 RLAEIVEMIHTASLLHDDVIDHSDTRRGRPSGNAAFTNKMAVLAGDFLLGRATVSISRLHNP----EVVELMSNSIANLV 252
Cdd:COG0142  69 RAAAAVELIHTASLVHDDVMDDDDLRRGKPTVHARFGEATAILAGDALLALAFELLAELGDPerrlRALRILARAARGMC 148
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319475  253 EGEFMQLKNtsidadidtienghkllpvpskklevkEHDFRVPsrqqglqlshdqiIETAFEyyIHktYLKTAALISKSC 332
Cdd:COG0142 149 EGQALDLEA---------------------------EGRLDVT-------------LEEYLR--VI--RLKTAALFAAAL 184
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319475  333 RCAAILSGASPAVIDECYDFGRNLGICFQLVDDMLDFTVSGKDLGKPSGADLKLGIATAPVLFAWKEDPS-----LGPLI 407
Cdd:COG0142 185 RLGAILAGADEEQVEALRRYGRNLGLAFQIRDDILDVTGDPEVLGKPAGSDLREGKPTLPLLLALERADPeeraeLRELL 264
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6319475  408 SRNFSERGDVEKTIDSVRLHNGIAKTKILAEEYRDKALQNLrDSLPESDARSALEFLTNSILTRRK 473
Cdd:COG0142 265 GKPDLDEEDLAEVRALLRESGALEYARELARELAEEALAAL-AALPDSEAREALRALADYVVERDR 329
PLN02857 PLN02857
octaprenyl-diphosphate synthase
38-471 1.92e-80

octaprenyl-diphosphate synthase


Pssm-ID: 215462  Cd Length: 416  Bit Score: 255.54  E-value: 1.92e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319475    38 PKILWNNPISLVSKEMNTLAKNIVALIGSGHPVLNKVTSYYFETEGKKVRPLLVLLLSRALSEipmternhlkidksdvp 117
Cdd:PLN02857  90 EPISLSELFEPVADDLQQLNDNLQSIVGAENPVLMSAAEQIFGAGGKRMRPALVFLVSRATAE----------------- 152
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319475   118 edpiyskpsqnqlfqrpassisplhiLHGIKPLNPltkgpeplpeetfdkqrgilpKQRRLAEIVEMIHTASLLHDDVID 197
Cdd:PLN02857 153 --------------------------LAGLKELTT---------------------EHRRLAEITEMIHTASLIHDDVLD 185
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319475   198 HSDTRRGRPSGNAAFTNKMAVLAGDFLLGRATVSISRLHNPEVVELMSNSIANLVEGEFMQLKNTsIDADIdTIENghkl 277
Cdd:PLN02857 186 ESDMRRGKETVHQLYGTRVAVLAGDFMFAQSSWYLANLDNLEVIKLISQVIKDFASGEIKQASSL-FDCDV-TLDE---- 259
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319475   278 lpvpskklevkehdfrvpsrqqglqlshdqiietafeyYIHKTYLKTAALISKSCRCAAILSGASPAVIDECYDFGRNLG 357
Cdd:PLN02857 260 --------------------------------------YLLKSYYKTASLIAASTKSAAIFSGVDSSVKEQMYEYGKNLG 301
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319475   358 ICFQLVDDMLDFTVSGKDLGKPSGADLKLGIATAPVLFAWKEDPSLGPLISRNFSERGDVEKTIDSVRLHNGIAKTKILA 437
Cdd:PLN02857 302 LAFQVVDDILDFTQSTEQLGKPAGSDLAKGNLTAPVIFALEKEPELREIIESEFCEEGSLEEAIELVNEGGGIERAQELA 381
                        410       420       430
                 ....*....|....*....|....*....|....
gi 6319475   438 EEYRDKALQNLRdSLPESDARSALEFLTNSILTR 471
Cdd:PLN02857 382 KEKADLAIQNLE-CLPRGAFRSSLEDMVDYNLER 414
Trans_IPPS_HT cd00685
Trans-Isoprenyl Diphosphate Synthases, head-to-tail; These trans-Isoprenyl Diphosphate ...
172-471 1.70e-78

Trans-Isoprenyl Diphosphate Synthases, head-to-tail; These trans-Isoprenyl Diphosphate Synthases (Trans_IPPS) catalyze head-to-tail (HT) (1'-4) condensation reactions. This CD includes all-trans (E)-isoprenyl diphosphate synthases which synthesize various chain length (C10, C15, C20, C25, C30, C35, C40, C45, and C50) linear isoprenyl diphosphates from precursors, isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP). They catalyze the successive 1'-4 condensation of the 5-carbon IPP to allylic substrates geranyl-, farnesyl-, or geranylgeranyl-diphosphate. Isoprenoid chain elongation reactions proceed via electrophilic alkylations in which a new carbon-carbon single bond is generated through interaction between a highly reactive electron-deficient allylic carbocation and an electron-rich carbon-carbon double bond. The catalytic site consists of a large central cavity formed by mostly antiparallel alpha helices with two aspartate-rich regions (DDXX(XX)D) located on opposite walls. These residues mediate binding of prenyl phosphates via bridging Mg2+ ions, inducing proposed conformational changes that close the active site to solvent, protecting and stabilizing reactive carbocation intermediates. Farnesyl diphosphate synthases produce the precursors of steroids, cholesterol, sesquiterpenes, farnsylated proteins, heme, and vitamin K12; and geranylgeranyl diphosphate and longer chain synthases produce the precursors of carotenoids, retinoids, diterpenes, geranylgeranylated chlorophylls, ubiquinone, and archaeal ether linked lipids. Isoprenyl diphosphate synthases are widely distributed among archaea, bacteria, and eukareya.


Pssm-ID: 173833  Cd Length: 259  Bit Score: 245.15  E-value: 1.70e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319475  172 LPKQRRLAEIVEMIHTASLLHDDVIDHSDTRRGRPSGNAAFTNKMAVLAGDFLLGRATVSISRLHN---PEVVELMSNSI 248
Cdd:cd00685  38 LEAALRLAAAIELLHTASLVHDDVMDNSDLRRGKPTVHKVFGNATAILAGDYLLARAFELLARLGNpyyPRALELFSEAI 117
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319475  249 ANLVEGEFMQLKNTSiDADIDtienghkllpvpskklevkehdfrvpsrqqglqlshdqiietaFEYYIHKTYLKTAALI 328
Cdd:cd00685 118 LELVEGQLLDLLSEY-DTDVT-------------------------------------------EEEYLRIIRLKTAALF 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319475  329 SKSCRCAAILSGASPAVIDECYDFGRNLGICFQLVDDMLDFTVSGKDLGKPSGADLKLGIATAPVLFAWKEdpslgplis 408
Cdd:cd00685 154 AAAPLLGALLAGADEEEAEALKRFGRNLGLAFQIQDDILDLFGDPETLGKPVGSDLREGKCTLPVLLALRE--------- 224
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6319475  409 rnfsergdvektidsvrlhngiaktkiLAEEYRDKALQNLrDSLPESDARSALEFLTNSILTR 471
Cdd:cd00685 225 ---------------------------LAREYEEKALEAL-KALPESPAREALRALADFILER 259
polyprenyl_synt pfam00348
Polyprenyl synthetase;
172-422 1.09e-69

Polyprenyl synthetase;


Pssm-ID: 459773  Cd Length: 251  Bit Score: 222.00  E-value: 1.09e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319475    172 LPKQRRLAEIVEMIHTASLLHDDVIDHSDTRRGRPSGNAAFTNKMAVLAGDFLLGRATVSISRLH-NPEVVELMSNSIAN 250
Cdd:pfam00348  37 LEKAIVLAWAVELLHAASLVHDDIMDNSDLRRGQPTWHRIFGNAIAINDGDYLYALAFQLLAKLFpNPELLELFSEVTLQ 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319475    251 LVEGEFMQLKNTSiDADIDTIEnghkllpvpskklevkehdfrvpsrqqglqlshdqiietafEYYIHKTYLKTAALISK 330
Cdd:pfam00348 117 TAEGQGLDLLWRN-DDDLSCTE-----------------------------------------EEYLEIVKYKTAYLFAL 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319475    331 SCRCAAILSGASPAVIDECYDFGRNLGICFQLVDDMLDFTVSGKDLGKPSGADLKLGIATAPVLFAWKEDPS----LGPL 406
Cdd:pfam00348 155 AVKLGAILSGADDEVIEALKDYGLNLGLAFQIQDDYLDLFGDPEVLGKPAGTDITEGKCTWPVIHALERTPEqrkiLLEI 234
                         250
                  ....*....|....*.
gi 6319475    407 ISRNFSERGDVEKTID 422
Cdd:pfam00348 235 YGKRPEDVEKVKEAYE 250
 
Name Accession Description Interval E-value
prenyl_cyano TIGR02749
solanesyl diphosphate synthase; Members of this family all are from cyanobacteria or ...
48-471 4.23e-90

solanesyl diphosphate synthase; Members of this family all are from cyanobacteria or plastid-containing eukaryotes. A member from Arabidopsis (where both plastoquinone and ubiquinone contain the C(45) prenyl moiety) was characterized by heterologous expression as a solanesyl diphosphate synthase. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]


Pssm-ID: 131796  Cd Length: 322  Bit Score: 277.40  E-value: 4.23e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319475     48 LVSKEMNTLAKNIVALIGSGHPVLNKVTSYYFETEGKKVRPLLVLLLSRALSEipmternhlkidksdvpedpiyskpsq 127
Cdd:TIGR02749   9 PVEDDLYLLTDNLKSLVGARHPILYAAAEHLFSAGGKRLRPAIVLLVSRATAE--------------------------- 61
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319475    128 nqlfqrpassisplhilhgikplnpltkgpeplpeetfdkQRGILPKQRRLAEIVEMIHTASLLHDDVIDHSDTRRGRPS 207
Cdd:TIGR02749  62 ----------------------------------------QQELTPRHRRLAEITEMIHTASLVHDDVIDESDTRRGIET 101
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319475    208 GNAAFTNKMAVLAGDFLLGRATVSISRLHNPEVVELMSNSIANLVEGEFMQLKNtSIDADIDtienghkllpvpskklev 287
Cdd:TIGR02749 102 VHSLFGTRVAVLAGDFLFAQASWYLANLENLEVVKLISKVITDFAEGEIKQGLN-QFDSDLS------------------ 162
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319475    288 kehdfrvpsrqqglqlshdqiietaFEYYIHKTYLKTAALISKSCRCAAILSGASPAVIDECYDFGRNLGICFQLVDDML 367
Cdd:TIGR02749 163 -------------------------LEDYLEKSFYKTASLVAASSKAAAVLSDVPSQVANDLYEYGKHLGLAFQVVDDIL 217
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319475    368 DFTVSGKDLGKPSGADLKLGIATAPVLFAWKEDPSLGPLISRNFSERGDVEKTIDSVRLHNGIAKTKILAEEYRDKALQN 447
Cdd:TIGR02749 218 DFTGSTEQLGKPAGSDLMKGNLTAPVLFALEEEPKLSELIEREFSQKGDLEQALSLVRKSGGIKKARELAKEQAQLALQS 297
                         410       420
                  ....*....|....*....|....
gi 6319475    448 LrDSLPESDARSALEFLTNSILTR 471
Cdd:TIGR02749 298 L-SFLPPSPPREALKELVHFVLSR 320
IspA COG0142
Geranylgeranyl pyrophosphate synthase [Coenzyme transport and metabolism]; Geranylgeranyl ...
177-473 3.86e-81

Geranylgeranyl pyrophosphate synthase [Coenzyme transport and metabolism]; Geranylgeranyl pyrophosphate synthase is part of the Pathway/BioSystem: Isoprenoid biosynthesis


Pssm-ID: 439912 [Multi-domain]  Cd Length: 329  Bit Score: 254.38  E-value: 3.86e-81
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319475  177 RLAEIVEMIHTASLLHDDVIDHSDTRRGRPSGNAAFTNKMAVLAGDFLLGRATVSISRLHNP----EVVELMSNSIANLV 252
Cdd:COG0142  69 RAAAAVELIHTASLVHDDVMDDDDLRRGKPTVHARFGEATAILAGDALLALAFELLAELGDPerrlRALRILARAARGMC 148
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319475  253 EGEFMQLKNtsidadidtienghkllpvpskklevkEHDFRVPsrqqglqlshdqiIETAFEyyIHktYLKTAALISKSC 332
Cdd:COG0142 149 EGQALDLEA---------------------------EGRLDVT-------------LEEYLR--VI--RLKTAALFAAAL 184
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319475  333 RCAAILSGASPAVIDECYDFGRNLGICFQLVDDMLDFTVSGKDLGKPSGADLKLGIATAPVLFAWKEDPS-----LGPLI 407
Cdd:COG0142 185 RLGAILAGADEEQVEALRRYGRNLGLAFQIRDDILDVTGDPEVLGKPAGSDLREGKPTLPLLLALERADPeeraeLRELL 264
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6319475  408 SRNFSERGDVEKTIDSVRLHNGIAKTKILAEEYRDKALQNLrDSLPESDARSALEFLTNSILTRRK 473
Cdd:COG0142 265 GKPDLDEEDLAEVRALLRESGALEYARELARELAEEALAAL-AALPDSEAREALRALADYVVERDR 329
PLN02857 PLN02857
octaprenyl-diphosphate synthase
38-471 1.92e-80

octaprenyl-diphosphate synthase


Pssm-ID: 215462  Cd Length: 416  Bit Score: 255.54  E-value: 1.92e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319475    38 PKILWNNPISLVSKEMNTLAKNIVALIGSGHPVLNKVTSYYFETEGKKVRPLLVLLLSRALSEipmternhlkidksdvp 117
Cdd:PLN02857  90 EPISLSELFEPVADDLQQLNDNLQSIVGAENPVLMSAAEQIFGAGGKRMRPALVFLVSRATAE----------------- 152
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319475   118 edpiyskpsqnqlfqrpassisplhiLHGIKPLNPltkgpeplpeetfdkqrgilpKQRRLAEIVEMIHTASLLHDDVID 197
Cdd:PLN02857 153 --------------------------LAGLKELTT---------------------EHRRLAEITEMIHTASLIHDDVLD 185
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319475   198 HSDTRRGRPSGNAAFTNKMAVLAGDFLLGRATVSISRLHNPEVVELMSNSIANLVEGEFMQLKNTsIDADIdTIENghkl 277
Cdd:PLN02857 186 ESDMRRGKETVHQLYGTRVAVLAGDFMFAQSSWYLANLDNLEVIKLISQVIKDFASGEIKQASSL-FDCDV-TLDE---- 259
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319475   278 lpvpskklevkehdfrvpsrqqglqlshdqiietafeyYIHKTYLKTAALISKSCRCAAILSGASPAVIDECYDFGRNLG 357
Cdd:PLN02857 260 --------------------------------------YLLKSYYKTASLIAASTKSAAIFSGVDSSVKEQMYEYGKNLG 301
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319475   358 ICFQLVDDMLDFTVSGKDLGKPSGADLKLGIATAPVLFAWKEDPSLGPLISRNFSERGDVEKTIDSVRLHNGIAKTKILA 437
Cdd:PLN02857 302 LAFQVVDDILDFTQSTEQLGKPAGSDLAKGNLTAPVIFALEKEPELREIIESEFCEEGSLEEAIELVNEGGGIERAQELA 381
                        410       420       430
                 ....*....|....*....|....*....|....
gi 6319475   438 EEYRDKALQNLRdSLPESDARSALEFLTNSILTR 471
Cdd:PLN02857 382 KEKADLAIQNLE-CLPRGAFRSSLEDMVDYNLER 414
preA CHL00151
prenyl transferase; Reviewed
44-471 3.34e-80

prenyl transferase; Reviewed


Pssm-ID: 164542  Cd Length: 323  Bit Score: 252.02  E-value: 3.34e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319475    44 NPISLVSKEMNTLAKNIVALIGSGHPVLNKVTSYYFETEGKKVRPLLVLLLSRALSEipmternhlkidksdvpedpiys 123
Cdd:CHL00151   6 NLLTPIEEELLILEDNLKKLIGSGHPILYAAAKHLFSAGGKRIRPAIVLLVAKATGG----------------------- 62
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319475   124 kpsqnqlfqrpassisplhilhgikplnpltkgpeplpeetfdkQRGILPKQRRLAEIVEMIHTASLLHDDVIDHSDTRR 203
Cdd:CHL00151  63 --------------------------------------------NMEIKTSQQRLAEITEIIHTASLVHDDVIDECSIRR 98
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319475   204 GRPSGNAAFTNKMAVLAGDFLLGRATVSISRLHNPEVVELMSNSIANLVEGEfMQLKNTSIDADIDTIEnghkllpvpsk 283
Cdd:CHL00151  99 GIPTVHKIFGTKIAVLAGDFLFAQSSWYLANLNNLEVVKLISKVITDFAEGE-IRQGLVQFDTTLSILN----------- 166
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319475   284 klevkehdfrvpsrqqglqlshdqiietafeyYIHKTYLKTAALISKSCRCAAILSGASPAVIDECYDFGRNLGICFQLV 363
Cdd:CHL00151 167 --------------------------------YIEKSFYKTASLIAASCKAAALLSDADEKDHNDFYLYGKHLGLAFQII 214
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319475   364 DDMLDFTVSGKDLGKPSGADLKLGIATAPVLFAWKEDPSLGPLISRNFSERGDVEKTIDSVRLHNGIAKTKILAEEYRDK 443
Cdd:CHL00151 215 DDVLDITSSTESLGKPIGSDLKNGNLTAPVLFALTQNSKLAKLIEREFCETKDISQALQIIKETNGIEKAKDLALEHMQA 294
                        410       420
                 ....*....|....*....|....*...
gi 6319475   444 ALQNLRDsLPESDARSALEFLTNSILTR 471
Cdd:CHL00151 295 AIQCLKF-LPPSSAKDSLIEIANFIINR 321
Trans_IPPS_HT cd00685
Trans-Isoprenyl Diphosphate Synthases, head-to-tail; These trans-Isoprenyl Diphosphate ...
172-471 1.70e-78

Trans-Isoprenyl Diphosphate Synthases, head-to-tail; These trans-Isoprenyl Diphosphate Synthases (Trans_IPPS) catalyze head-to-tail (HT) (1'-4) condensation reactions. This CD includes all-trans (E)-isoprenyl diphosphate synthases which synthesize various chain length (C10, C15, C20, C25, C30, C35, C40, C45, and C50) linear isoprenyl diphosphates from precursors, isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP). They catalyze the successive 1'-4 condensation of the 5-carbon IPP to allylic substrates geranyl-, farnesyl-, or geranylgeranyl-diphosphate. Isoprenoid chain elongation reactions proceed via electrophilic alkylations in which a new carbon-carbon single bond is generated through interaction between a highly reactive electron-deficient allylic carbocation and an electron-rich carbon-carbon double bond. The catalytic site consists of a large central cavity formed by mostly antiparallel alpha helices with two aspartate-rich regions (DDXX(XX)D) located on opposite walls. These residues mediate binding of prenyl phosphates via bridging Mg2+ ions, inducing proposed conformational changes that close the active site to solvent, protecting and stabilizing reactive carbocation intermediates. Farnesyl diphosphate synthases produce the precursors of steroids, cholesterol, sesquiterpenes, farnsylated proteins, heme, and vitamin K12; and geranylgeranyl diphosphate and longer chain synthases produce the precursors of carotenoids, retinoids, diterpenes, geranylgeranylated chlorophylls, ubiquinone, and archaeal ether linked lipids. Isoprenyl diphosphate synthases are widely distributed among archaea, bacteria, and eukareya.


Pssm-ID: 173833  Cd Length: 259  Bit Score: 245.15  E-value: 1.70e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319475  172 LPKQRRLAEIVEMIHTASLLHDDVIDHSDTRRGRPSGNAAFTNKMAVLAGDFLLGRATVSISRLHN---PEVVELMSNSI 248
Cdd:cd00685  38 LEAALRLAAAIELLHTASLVHDDVMDNSDLRRGKPTVHKVFGNATAILAGDYLLARAFELLARLGNpyyPRALELFSEAI 117
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319475  249 ANLVEGEFMQLKNTSiDADIDtienghkllpvpskklevkehdfrvpsrqqglqlshdqiietaFEYYIHKTYLKTAALI 328
Cdd:cd00685 118 LELVEGQLLDLLSEY-DTDVT-------------------------------------------EEEYLRIIRLKTAALF 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319475  329 SKSCRCAAILSGASPAVIDECYDFGRNLGICFQLVDDMLDFTVSGKDLGKPSGADLKLGIATAPVLFAWKEdpslgplis 408
Cdd:cd00685 154 AAAPLLGALLAGADEEEAEALKRFGRNLGLAFQIQDDILDLFGDPETLGKPVGSDLREGKCTLPVLLALRE--------- 224
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6319475  409 rnfsergdvektidsvrlhngiaktkiLAEEYRDKALQNLrDSLPESDARSALEFLTNSILTR 471
Cdd:cd00685 225 ---------------------------LAREYEEKALEAL-KALPESPAREALRALADFILER 259
PLN02890 PLN02890
geranyl diphosphate synthase
44-473 3.13e-74

geranyl diphosphate synthase


Pssm-ID: 178478  Cd Length: 422  Bit Score: 239.83  E-value: 3.13e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319475    44 NPISLVSKEMNTLAKNIVALIGSGHPVLNKVTSYYFE--TEGKKVRPLLVLLLSRALSeipmternhlkidksdvpedpi 121
Cdd:PLN02890  83 DPFSLVADELSLLANKLRSMVVAEVPKLASAAEYFFKvgVEGKRFRPTVLLLMATALN---------------------- 140
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319475   122 yskpsqnqlfqrpassispLHIlhgikplnpltkgPEPLPEETFDKQRGIL-PKQRRLAEIVEMIHTASLLHDDVIDHSD 200
Cdd:PLN02890 141 -------------------VPL-------------PESTEGGVLDIVASELrTRQQNIAEITEMIHVASLLHDDVLDDAD 188
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319475   201 TRRGRPSGNAAFTNKMAVLAGDFLLGRATVSISRLHNPEVVELMSNSIANLVEGEFMQLKNtsidadidtienghkllpv 280
Cdd:PLN02890 189 TRRGVGSLNVVMGNKLSVLAGDFLLSRACVALAALKNTEVVSLLATAVEHLVTGETMQITS------------------- 249
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319475   281 pskklevkehdfrvpSRQQglqlshdqiiETAFEYYIHKTYLKTAALISKSCRCAAILSGASPAVIDECYDFGRNLGICF 360
Cdd:PLN02890 250 ---------------SREQ----------RRSMDYYMQKTYYKTASLISNSCKAVAILAGQTAEVAVLAFEYGRNLGLAF 304
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319475   361 QLVDDMLDFTVSGKDLGKPSGADLKLGIATAPVLFAWKEDPSLGPLISRNFSERGDVEKTIDSVRLHNGIAKTKILAEEY 440
Cdd:PLN02890 305 QLIDDVLDFTGTSASLGKGSLSDIRHGVITAPILFAMEEFPQLREVVDRGFDNPANVDIALEYLGKSRGIQRTRELAREH 384
                        410       420       430
                 ....*....|....*....|....*....|....*....
gi 6319475   441 RDKALQNLrDSLPESD------ARSALEFLTNSILTRRK 473
Cdd:PLN02890 385 ANLAAAAI-ESLPETDdedvltSRRALIDLTERVITRNK 422
polyprenyl_synt pfam00348
Polyprenyl synthetase;
172-422 1.09e-69

Polyprenyl synthetase;


Pssm-ID: 459773  Cd Length: 251  Bit Score: 222.00  E-value: 1.09e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319475    172 LPKQRRLAEIVEMIHTASLLHDDVIDHSDTRRGRPSGNAAFTNKMAVLAGDFLLGRATVSISRLH-NPEVVELMSNSIAN 250
Cdd:pfam00348  37 LEKAIVLAWAVELLHAASLVHDDIMDNSDLRRGQPTWHRIFGNAIAINDGDYLYALAFQLLAKLFpNPELLELFSEVTLQ 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319475    251 LVEGEFMQLKNTSiDADIDTIEnghkllpvpskklevkehdfrvpsrqqglqlshdqiietafEYYIHKTYLKTAALISK 330
Cdd:pfam00348 117 TAEGQGLDLLWRN-DDDLSCTE-----------------------------------------EEYLEIVKYKTAYLFAL 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319475    331 SCRCAAILSGASPAVIDECYDFGRNLGICFQLVDDMLDFTVSGKDLGKPSGADLKLGIATAPVLFAWKEDPS----LGPL 406
Cdd:pfam00348 155 AVKLGAILSGADDEVIEALKDYGLNLGLAFQIQDDYLDLFGDPEVLGKPAGTDITEGKCTWPVIHALERTPEqrkiLLEI 234
                         250
                  ....*....|....*.
gi 6319475    407 ISRNFSERGDVEKTID 422
Cdd:pfam00348 235 YGKRPEDVEKVKEAYE 250
Trans_IPPS cd00867
Trans-Isoprenyl Diphosphate Synthases; Trans-Isoprenyl Diphosphate Synthases (Trans_IPPS) of ...
170-399 9.26e-55

Trans-Isoprenyl Diphosphate Synthases; Trans-Isoprenyl Diphosphate Synthases (Trans_IPPS) of class 1 isoprenoid biosynthesis enzymes which either synthesis geranyl/farnesyl diphosphates (GPP/FPP) or longer chained products from isoprene precursors, isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP), or use geranyl (C10)-, farnesyl (C15)-, or geranylgeranyl (C20)-diphosphate as substrate. These enzymes produce a myriad of precursors for such end products as steroids, cholesterol, sesquiterpenes, heme, carotenoids, retinoids, diterpenes, ubiquinone, and archaeal ether linked lipids; and are widely distributed among archaea, bacteria, and eukareya. The enzymes in this family share the same 'isoprenoid synthase fold' and include the head-to-tail (HT) IPPS which catalyze the successive 1'-4 condensation of the 5-carbon IPP to the growing isoprene chain to form linear, all-trans, C10-, C15-, C20- C25-, C30-, C35-, C40-, C45-, or C50-isoprenoid diphosphates. The head-to-head (HH) IPPS catalyze the successive 1'-1 condensation of 2 farnesyl or 2 geranylgeranyl isoprenoid diphosphates. Isoprenoid chain elongation reactions proceed via electrophilic alkylations in which a new carbon-carbon single bond is generated through interaction between a highly reactive electron-deficient allylic carbocation and an electron-rich carbon-carbon double bond. The catalytic site consists of a large central cavity formed by mostly antiparallel alpha helices with two aspartate-rich regions located on opposite walls. These residues mediate binding of prenyl phosphates via bridging Mg2+ ions, inducing proposed conformational changes that close the active site to solvent, stabilizing reactive carbocation intermediates. Mechanistically and structurally distinct, cis-IPPS are not included in this CD.


Pssm-ID: 173836  Cd Length: 236  Bit Score: 182.93  E-value: 9.26e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319475  170 GILPKQRRLAEIVEMIHTASLLHDDVIDHSDTRRGRPSGNA-AFTNKMAVLAGDFLLGRATVSISRLHNPEVVELMSNSI 248
Cdd:cd00867  15 GDLEAALRLAAAVELLHAASLVHDDIVDDSDLRRGKPTAHLrRFGNALAILAGDYLLARAFQLLARLGYPRALELFAEAL 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319475  249 ANLVEGEFMQLkntsidadidtienghkllpvpskklevkehdfrvpsrqqglqLSHDQIIETaFEYYIHKTYLKTAALI 328
Cdd:cd00867  95 RELLEGQALDL-------------------------------------------EFERDTYET-LDEYLEYCRYKTAGLV 130
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6319475  329 SKSCRCAAILSGASPAVIDECYDFGRNLGICFQLVDDMLDFTVSGKDLGKPsGADLKLGIATAPVLFAWKE 399
Cdd:cd00867 131 GLLCLLGAGLSGADDEQAEALKDYGRALGLAFQLTDDLLDVFGDAEELGKV-GSDLREGRITLPVILARER 200
PRK10888 PRK10888
octaprenyl diphosphate synthase; Provisional
174-472 3.14e-49

octaprenyl diphosphate synthase; Provisional


Pssm-ID: 182813  Cd Length: 323  Bit Score: 171.18  E-value: 3.14e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319475   174 KQRRLAEIVEMIHTASLLHDDVIDHSDTRRGRPSGNAAFTNKMAVLAGDFLLGRATVSISRLHNPEVVELMSNSIANLVE 253
Cdd:PRK10888  65 AHVTIAALIEFIHTATLLHDDVVDESDMRRGKATANAAFGNAASVLVGDFIYTRAFQMMTSLGSLKVLEVMSEAVNVIAE 144
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319475   254 GEFMQLKNTSiDADIdTIENghkllpvpskklevkehdfrvpsrqqglqlshdqiietafeyYIHKTYLKTAALISKSCR 333
Cdd:PRK10888 145 GEVLQLMNVN-DPDI-TEEN------------------------------------------YMRVIYSKTARLFEAAAQ 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319475   334 CAAILSGASPAVIDECYDFGRNLGICFQLVDDMLDFTVSGKDLGKPSGADLKLGIATAPVLFAWKE-DPSLGPLIsRNFS 412
Cdd:PRK10888 181 CSGILAGCTPEQEKGLQDYGRYLGTAFQLIDDLLDYSADGETLGKNVGDDLNEGKPTLPLLHAMHHgTPEQAAMI-RTAI 259
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6319475   413 ERGD----VEKTIDSVRLHNGIAKTKILAEEYRDKALQNLrDSLPESDARSALEFLTNSILTRR 472
Cdd:PRK10888 260 EQGNgrhlLEPVLEAMNACGSLEWTRQRAEEEADKAIAAL-QVLPDTPWREALIGLAHIAVQRD 322
Isoprenoid_Biosyn_C1 cd00385
Isoprenoid Biosynthesis enzymes, Class 1; Superfamily of trans-isoprenyl diphosphate synthases ...
172-460 7.81e-42

Isoprenoid Biosynthesis enzymes, Class 1; Superfamily of trans-isoprenyl diphosphate synthases (IPPS) and class I terpene cyclases which either synthesis geranyl/farnesyl diphosphates (GPP/FPP) or longer chained products from isoprene precursors, isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP), or use geranyl (C10)-, farnesyl (C15)-, or geranylgeranyl (C20)-diphosphate as substrate. These enzymes produce a myriad of precursors for such end products as steroids, cholesterol, sesquiterpenes, heme, carotenoids, retinoids, and diterpenes; and are widely distributed among archaea, bacteria, and eukaryota.The enzymes in this superfamily share the same 'isoprenoid synthase fold' and include several subgroups. The head-to-tail (HT) IPPS catalyze the successive 1'-4 condensation of the 5-carbon IPP to the growing isoprene chain to form linear, all-trans, C10-, C15-, C20- C25-, C30-, C35-, C40-, C45-, or C50-isoprenoid diphosphates. Cyclic monoterpenes, diterpenes, and sesquiterpenes, are formed from their respective linear isoprenoid diphosphates by class I terpene cyclases. The head-to-head (HH) IPPS catalyze the successive 1'-1 condensation of 2 farnesyl or 2 geranylgeranyl isoprenoid diphosphates. Cyclization of these 30- and 40-carbon linear forms are catalyzed by class II cyclases. Both the isoprenoid chain elongation reactions and the class I terpene cyclization reactions proceed via electrophilic alkylations in which a new carbon-carbon single bond is generated through interaction between a highly reactive electron-deficient allylic carbocation and an electron-rich carbon-carbon double bond. The catalytic site consists of a large central cavity formed by mostly antiparallel alpha helices with two aspartate-rich regions located on opposite walls. These residues mediate binding of prenyl phosphates via bridging Mg2+ ions, inducing proposed conformational changes that close the active site to solvent, stabilizing reactive carbocation intermediates. Generally, the enzymes in this family exhibit an all-trans reaction pathway, an exception, is the cis-trans terpene cyclase, trichodiene synthase. Mechanistically and structurally distinct, class II terpene cyclases and cis-IPPS are not included in this CD.


Pssm-ID: 173830 [Multi-domain]  Cd Length: 243  Bit Score: 149.18  E-value: 7.81e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319475  172 LPKQRRLAEIVEMIHTASLLHDDVIDHSDTRRGRPSGNAA---FTNKMAVLAGDFLLGRATVSISRLHNPEVVELMSNSI 248
Cdd:cd00385   9 EPEASRLRAAVEKLHAASLVHDDIVDDSGTRRGLPTAHLAvaiDGLPEAILAGDLLLADAFEELAREGSPEALEILAEAL 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319475  249 ANLVEGEFMQLKNTsidadidtienghkllpvpskklevkehDFRVPSrqqglqlshdqiietaFEYYIHKTYLKTAALI 328
Cdd:cd00385  89 LDLLEGQLLDLKWR----------------------------REYVPT----------------LEEYLEYCRYKTAGLV 124
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319475  329 SKSCRCAAILSGASPAVIDECYDFGRNLGICFQLVDDMLDFTVSgkdlgkpsgADLKLGIATAPVLFAWkedpslgplis 408
Cdd:cd00385 125 GALCLLGAGLSGGEAELLEALRKLGRALGLAFQLTNDLLDYEGD---------AERGEGKCTLPVLYAL----------- 184
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 6319475  409 rnfsERGDVEKTIDSVRLHNGIAKTKILAEEYRDKALQNLRDSLPESDARSA 460
Cdd:cd00385 185 ----EYGVPAEDLLLVEKSGSLEEALEELAKLAEEALKELNELILSLPDVPR 232
PRK10581 PRK10581
(2E,6E)-farnesyl diphosphate synthase;
179-473 9.82e-14

(2E,6E)-farnesyl diphosphate synthase;


Pssm-ID: 182567  Cd Length: 299  Bit Score: 71.73  E-value: 9.82e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319475   179 AEIVEMIHTASLLHDDV--IDHSDTRRGRPSGNAAFTNKMAVLAGDFLLGRATVSISRLHNPEV---------VELMSNS 247
Cdd:PRK10581  70 AAAVECIHAYSLIHDDLpaMDDDDLRRGLPTCHVKFGEANAILAGDALQTLAFSILSDAPMPEVsdrdrismiSELASAS 149
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319475   248 -IANLVEGEFMQLKNTSIDADIDTIENGHKllpvpskklevkeHdfrvpsrqqglqlshdqiietafeyyihktylKTAA 326
Cdd:PRK10581 150 gIAGMCGGQALDLEAEGKQVPLDALERIHR-------------H--------------------------------KTGA 184
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319475   327 LISKSCRCAAILSGASPAVIDECYD-FGRNLGICFQLVDDMLDFTVSGKDLGKPSGADLKLGIATAPVLFawkedpslgp 405
Cdd:PRK10581 185 LIRAAVRLGALSAGDKGRRALPVLDrYAESIGLAFQVQDDILDVVGDTATLGKRQGADQQLGKSTYPALL---------- 254
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6319475   406 lisrnfsergdvektidsvrlhnGIAKTKILAEEYRDKALQNLRDSLPESDARSALEFLTNSILTRRK 473
Cdd:PRK10581 255 -----------------------GLEQARKKARDLIDDARQSLDQLAAQSLDTSALEALANYIIQRDK 299
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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