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Conserved domains on  [gi|2067579957|emb|CAG7904923|]
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unnamed protein product [Brassica rapa]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PLN02857 PLN02857
octaprenyl-diphosphate synthase
119-536 0e+00

octaprenyl-diphosphate synthase


:

Pssm-ID: 215462  Cd Length: 416  Bit Score: 750.52  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067579957 119 MMTSCRNIDLGTSvldLISCGCGR----RQFLLGNFPKAVCTA--RSYGGRnLVFLRRDVGRsCKAVPTKPkEISLVNGI 192
Cdd:PLN02857    1 MSMSCRNIDLGTS---LVACGCSSnassRRRVVRNGATPVCKScsRSYASS-LVTSRRDIGR-CRVVSPSP-ETSLVNGI 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067579957 193 GEAKTVSFDLRQEtsSKQPISLANLFEVVADDLQTLNDNLLSIVGAENPVLISAAEQIFGAGGKRMRPGLVFLVSRATAE 272
Cdd:PLN02857   75 GQGPTVALDLKAE--SKEPISLSELFEPVADDLQQLNDNLQSIVGAENPVLMSAAEQIFGAGGKRMRPALVFLVSRATAE 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067579957 273 LAGLKELTTEHRRLGEIIEMIHTASLIHDDVLDESDMRRGKETVHELFGTRVAVLAGDFMFAQASWYLANLENLEVIKLI 352
Cdd:PLN02857  153 LAGLKELTTEHRRLAEITEMIHTASLIHDDVLDESDMRRGKETVHQLYGTRVAVLAGDFMFAQSSWYLANLDNLEVIKLI 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067579957 353 SQVIKDFASGEIKQASSLFDCDVTLEDYLLKSYYKTASLVAASTKGAAIFSRVDTDVTEQMYEFGKNLGLSFQVVDDILD 432
Cdd:PLN02857  233 SQVIKDFASGEIKQASSLFDCDVTLDEYLLKSYYKTASLIAASTKSAAIFSGVDSSVKEQMYEYGKNLGLAFQVVDDILD 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067579957 433 FTQSSEQLGKPAGSDLAKGNLTAPVIFALEKEPRLREIIESEFCEEGSLEEGIELVREGGGIRRAQELAREKADEALKNL 512
Cdd:PLN02857  313 FTQSTEQLGKPAGSDLAKGNLTAPVIFALEKEPELREIIESEFCEEGSLEEAIELVNEGGGIERAQELAKEKADLAIQNL 392
                         410       420
                  ....*....|....*....|....
gi 2067579957 513 QCLPQSGFRSALEEMVMFNLERID 536
Cdd:PLN02857  393 ECLPRGAFRSSLEDMVDYNLERIY 416
X8 smart00768
Possibly involved in carbohydrate binding; The X8 domain, which may be involved in ...
31-115 2.25e-33

Possibly involved in carbohydrate binding; The X8 domain, which may be involved in carbohydrate binding, is found in an Olive pollen antigen as well as at the C terminus of family 17 glycosyl hydrolases. It contains 6 conserved cysteine residues which presumably form three disulfide bridges.


:

Pssm-ID: 197867 [Multi-domain]  Cd Length: 85  Bit Score: 121.59  E-value: 2.25e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067579957   31 TWCVAKPSSDQAALLDNINYACSH-VDCRVLSSGCPCYSPGNLINHASVAMNLYYQANGRNYWNCNFKNSGLIVITNPTl 109
Cdd:smart00768   1 LWCVAKPDADEAALQAALDYACGQgADCTAIQPGGSCYSPNTVKAHASYAFNSYYQKQGQSSGACDFSGTATITTTDPS- 79

                   ....*.
gi 2067579957  110 ldSGFC 115
Cdd:smart00768  80 --TGSC 83
 
Name Accession Description Interval E-value
PLN02857 PLN02857
octaprenyl-diphosphate synthase
119-536 0e+00

octaprenyl-diphosphate synthase


Pssm-ID: 215462  Cd Length: 416  Bit Score: 750.52  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067579957 119 MMTSCRNIDLGTSvldLISCGCGR----RQFLLGNFPKAVCTA--RSYGGRnLVFLRRDVGRsCKAVPTKPkEISLVNGI 192
Cdd:PLN02857    1 MSMSCRNIDLGTS---LVACGCSSnassRRRVVRNGATPVCKScsRSYASS-LVTSRRDIGR-CRVVSPSP-ETSLVNGI 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067579957 193 GEAKTVSFDLRQEtsSKQPISLANLFEVVADDLQTLNDNLLSIVGAENPVLISAAEQIFGAGGKRMRPGLVFLVSRATAE 272
Cdd:PLN02857   75 GQGPTVALDLKAE--SKEPISLSELFEPVADDLQQLNDNLQSIVGAENPVLMSAAEQIFGAGGKRMRPALVFLVSRATAE 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067579957 273 LAGLKELTTEHRRLGEIIEMIHTASLIHDDVLDESDMRRGKETVHELFGTRVAVLAGDFMFAQASWYLANLENLEVIKLI 352
Cdd:PLN02857  153 LAGLKELTTEHRRLAEITEMIHTASLIHDDVLDESDMRRGKETVHQLYGTRVAVLAGDFMFAQSSWYLANLDNLEVIKLI 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067579957 353 SQVIKDFASGEIKQASSLFDCDVTLEDYLLKSYYKTASLVAASTKGAAIFSRVDTDVTEQMYEFGKNLGLSFQVVDDILD 432
Cdd:PLN02857  233 SQVIKDFASGEIKQASSLFDCDVTLDEYLLKSYYKTASLIAASTKSAAIFSGVDSSVKEQMYEYGKNLGLAFQVVDDILD 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067579957 433 FTQSSEQLGKPAGSDLAKGNLTAPVIFALEKEPRLREIIESEFCEEGSLEEGIELVREGGGIRRAQELAREKADEALKNL 512
Cdd:PLN02857  313 FTQSTEQLGKPAGSDLAKGNLTAPVIFALEKEPELREIIESEFCEEGSLEEAIELVNEGGGIERAQELAKEKADLAIQNL 392
                         410       420
                  ....*....|....*....|....
gi 2067579957 513 QCLPQSGFRSALEEMVMFNLERID 536
Cdd:PLN02857  393 ECLPRGAFRSSLEDMVDYNLERIY 416
prenyl_cyano TIGR02749
solanesyl diphosphate synthase; Members of this family all are from cyanobacteria or ...
212-536 0e+00

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: 561.29  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067579957 212 ISLANLFEVVADDLQTLNDNLLSIVGAENPVLISAAEQIFGAGGKRMRPGLVFLVSRATAELaglKELTTEHRRLGEIIE 291
Cdd:TIGR02749   1 ASATSLFAPVEDDLYLLTDNLKSLVGARHPILYAAAEHLFSAGGKRLRPAIVLLVSRATAEQ---QELTPRHRRLAEITE 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067579957 292 MIHTASLIHDDVLDESDMRRGKETVHELFGTRVAVLAGDFMFAQASWYLANLENLEVIKLISQVIKDFASGEIKQASSLF 371
Cdd:TIGR02749  78 MIHTASLVHDDVIDESDTRRGIETVHSLFGTRVAVLAGDFLFAQASWYLANLENLEVVKLISKVITDFAEGEIKQGLNQF 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067579957 372 DCDVTLEDYLLKSYYKTASLVAASTKGAAIFSRVDTDVTEQMYEFGKNLGLSFQVVDDILDFTQSSEQLGKPAGSDLAKG 451
Cdd:TIGR02749 158 DSDLSLEDYLEKSFYKTASLVAASSKAAAVLSDVPSQVANDLYEYGKHLGLAFQVVDDILDFTGSTEQLGKPAGSDLMKG 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067579957 452 NLTAPVIFALEKEPRLREIIESEFCEEGSLEEGIELVREGGGIRRAQELAREKADEALKNLQCLPQSGFRSALEEMVMFN 531
Cdd:TIGR02749 238 NLTAPVLFALEEEPKLSELIEREFSQKGDLEQALSLVRKSGGIKKARELAKEQAQLALQSLSFLPPSPPREALKELVHFV 317

                  ....*
gi 2067579957 532 LERID 536
Cdd:TIGR02749 318 LSRLY 322
IspA COG0142
Geranylgeranyl pyrophosphate synthase [Coenzyme transport and metabolism]; Geranylgeranyl ...
213-534 8.01e-111

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: 332.96  E-value: 8.01e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067579957 213 SLANLFEVVADDLQTLNDNLLSIV-GAENPVLISAAEQIFGAGGKRMRPGLVFLvsraTAELAGLKelTTEHRRLGEIIE 291
Cdd:COG0142     2 TLKDLLALLAEDLARVEAALEELLaRSEPPLLAEAMRYLLLAGGKRLRPLLVLL----AARALGGD--PEAALRAAAAVE 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067579957 292 MIHTASLIHDDVLDESDMRRGKETVHELFGTRVAVLAGDFMFAQASWYLANLEN----LEVIKLISQVIKDFASGEIKQA 367
Cdd:COG0142    76 LIHTASLVHDDVMDDDDLRRGKPTVHARFGEATAILAGDALLALAFELLAELGDperrLRALRILARAARGMCEGQALDL 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067579957 368 SSLFDCDVTLEDYLLKSYYKTASLVAASTKGAAIFSRVDTDVTEQMYEFGKNLGLSFQVVDDILDFTQSSEQLGKPAGSD 447
Cdd:COG0142   156 EAEGRLDVTLEEYLRVIRLKTAALFAAALRLGAILAGADEEQVEALRRYGRNLGLAFQIRDDILDVTGDPEVLGKPAGSD 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067579957 448 LAKGNLTAPVIFALEKEP-----RLREIIESEFCEEGSLEEGIELVREGGGIRRAQELAREKADEALKNLQCLPQSGFRS 522
Cdd:COG0142   236 LREGKPTLPLLLALERADpeeraELRELLGKPDLDEEDLAEVRALLRESGALEYARELARELAEEALAALAALPDSEARE 315
                         330
                  ....*....|..
gi 2067579957 523 ALEEMVMFNLER 534
Cdd:COG0142   316 ALRALADYVVER 327
polyprenyl_synt pfam00348
Polyprenyl synthetase;
241-487 1.40e-93

Polyprenyl synthetase;


Pssm-ID: 459773  Cd Length: 251  Bit Score: 285.55  E-value: 1.40e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067579957 241 PVLISAAEQIFGAGGKRMRPGLVFLVSRATaelaGLKELTTEHRRLGEIIEMIHTASLIHDDVLDESDMRRGKETVHELF 320
Cdd:pfam00348   2 KLLYEPLDYLVSAGGKRIRPLLVLLSAEAL----GGPEDLEKAIVLAWAVELLHAASLVHDDIMDNSDLRRGQPTWHRIF 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067579957 321 GTRVAVLAGDFMFAQASWYLANL-ENLEVIKLISQVIKDFASGEIKQASSLF--DCDVTLEDYLLKSYYKTASLVAASTK 397
Cdd:pfam00348  78 GNAIAINDGDYLYALAFQLLAKLfPNPELLELFSEVTLQTAEGQGLDLLWRNddDLSCTEEEYLEIVKYKTAYLFALAVK 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067579957 398 GAAIFSRVDTDVTEQMYEFGKNLGLSFQVVDDILDFTQSSEQLGKPAGSDLAKGNLTAPVIFALEKEP----RLREIIES 473
Cdd:pfam00348 158 LGAILSGADDEVIEALKDYGLNLGLAFQIQDDYLDLFGDPEVLGKPAGTDITEGKCTWPVIHALERTPeqrkILLEIYGK 237
                         250
                  ....*....|....
gi 2067579957 474 EFCEEGSLEEGIEL 487
Cdd:pfam00348 238 RPEDVEKVKEAYEL 251
Trans_IPPS_HT cd00685
Trans-Isoprenyl Diphosphate Synthases, head-to-tail; These trans-Isoprenyl Diphosphate ...
238-534 3.21e-93

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: 285.21  E-value: 3.21e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067579957 238 AENPVLISAAEQIFGAGGKRMRPGLVFLVSRATAElaglkELTTEHRRLGEIIEMIHTASLIHDDVLDESDMRRGKETVH 317
Cdd:cd00685     1 SEVELLREALRYLLLAGGKRLRPLLVLLAARALGG-----PELEAALRLAAAIELLHTASLVHDDVMDNSDLRRGKPTVH 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067579957 318 ELFGTRVAVLAGDFMFAQASWYLANLEN---LEVIKLISQVIKDFASGEIKQASSLFDCDVTLEDYLLKSYYKTASLVAA 394
Cdd:cd00685    76 KVFGNATAILAGDYLLARAFELLARLGNpyyPRALELFSEAILELVEGQLLDLLSEYDTDVTEEEYLRIIRLKTAALFAA 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067579957 395 STKGAAIFSRVDTDVTEQMYEFGKNLGLSFQVVDDILDFTQSSEQLGKPAGSDLAKGNLTAPVIFALEkeprlreiiese 474
Cdd:cd00685   156 APLLGALLAGADEEEAEALKRFGRNLGLAFQIQDDILDLFGDPETLGKPVGSDLREGKCTLPVLLALR------------ 223
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067579957 475 fceegsleegielvregggirraqELAREKADEALKNLQCLPQSGFRSALEEMVMFNLER 534
Cdd:cd00685   224 ------------------------ELAREYEEKALEALKALPESPAREALRALADFILER 259
X8 smart00768
Possibly involved in carbohydrate binding; The X8 domain, which may be involved in ...
31-115 2.25e-33

Possibly involved in carbohydrate binding; The X8 domain, which may be involved in carbohydrate binding, is found in an Olive pollen antigen as well as at the C terminus of family 17 glycosyl hydrolases. It contains 6 conserved cysteine residues which presumably form three disulfide bridges.


Pssm-ID: 197867 [Multi-domain]  Cd Length: 85  Bit Score: 121.59  E-value: 2.25e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067579957   31 TWCVAKPSSDQAALLDNINYACSH-VDCRVLSSGCPCYSPGNLINHASVAMNLYYQANGRNYWNCNFKNSGLIVITNPTl 109
Cdd:smart00768   1 LWCVAKPDADEAALQAALDYACGQgADCTAIQPGGSCYSPNTVKAHASYAFNSYYQKQGQSSGACDFSGTATITTTDPS- 79

                   ....*.
gi 2067579957  110 ldSGFC 115
Cdd:smart00768  80 --TGSC 83
X8 pfam07983
X8 domain; The X8 domain domain contains at least 6 conserved cysteine residues that ...
31-100 1.96e-24

X8 domain; The X8 domain domain contains at least 6 conserved cysteine residues that presumably form three disulphide bridges. The domain is found in an Olive pollen allergen as well as at the C-terminus of several families of glycosyl hydrolases. This domain may be involved in carbohydrate binding. This domain is characteriztic of GPI-anchored domains.


Pssm-ID: 400371  Cd Length: 76  Bit Score: 96.51  E-value: 1.96e-24
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2067579957  31 TWCVAKPSSDQAALLDNINYACSHVDCRVLSSGCP-----CYSPGNLINHASVAMNLYYQANGRNYWNCNFKNSG 100
Cdd:pfam07983   1 LWCVAKDSVDDEDLQDLFDYACGQADCSGIQANGTtgkygCYSPCTVKQHLSYAFNSYYQKQGKASSACDFSGSA 75
 
Name Accession Description Interval E-value
PLN02857 PLN02857
octaprenyl-diphosphate synthase
119-536 0e+00

octaprenyl-diphosphate synthase


Pssm-ID: 215462  Cd Length: 416  Bit Score: 750.52  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067579957 119 MMTSCRNIDLGTSvldLISCGCGR----RQFLLGNFPKAVCTA--RSYGGRnLVFLRRDVGRsCKAVPTKPkEISLVNGI 192
Cdd:PLN02857    1 MSMSCRNIDLGTS---LVACGCSSnassRRRVVRNGATPVCKScsRSYASS-LVTSRRDIGR-CRVVSPSP-ETSLVNGI 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067579957 193 GEAKTVSFDLRQEtsSKQPISLANLFEVVADDLQTLNDNLLSIVGAENPVLISAAEQIFGAGGKRMRPGLVFLVSRATAE 272
Cdd:PLN02857   75 GQGPTVALDLKAE--SKEPISLSELFEPVADDLQQLNDNLQSIVGAENPVLMSAAEQIFGAGGKRMRPALVFLVSRATAE 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067579957 273 LAGLKELTTEHRRLGEIIEMIHTASLIHDDVLDESDMRRGKETVHELFGTRVAVLAGDFMFAQASWYLANLENLEVIKLI 352
Cdd:PLN02857  153 LAGLKELTTEHRRLAEITEMIHTASLIHDDVLDESDMRRGKETVHQLYGTRVAVLAGDFMFAQSSWYLANLDNLEVIKLI 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067579957 353 SQVIKDFASGEIKQASSLFDCDVTLEDYLLKSYYKTASLVAASTKGAAIFSRVDTDVTEQMYEFGKNLGLSFQVVDDILD 432
Cdd:PLN02857  233 SQVIKDFASGEIKQASSLFDCDVTLDEYLLKSYYKTASLIAASTKSAAIFSGVDSSVKEQMYEYGKNLGLAFQVVDDILD 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067579957 433 FTQSSEQLGKPAGSDLAKGNLTAPVIFALEKEPRLREIIESEFCEEGSLEEGIELVREGGGIRRAQELAREKADEALKNL 512
Cdd:PLN02857  313 FTQSTEQLGKPAGSDLAKGNLTAPVIFALEKEPELREIIESEFCEEGSLEEAIELVNEGGGIERAQELAKEKADLAIQNL 392
                         410       420
                  ....*....|....*....|....
gi 2067579957 513 QCLPQSGFRSALEEMVMFNLERID 536
Cdd:PLN02857  393 ECLPRGAFRSSLEDMVDYNLERIY 416
prenyl_cyano TIGR02749
solanesyl diphosphate synthase; Members of this family all are from cyanobacteria or ...
212-536 0e+00

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: 561.29  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067579957 212 ISLANLFEVVADDLQTLNDNLLSIVGAENPVLISAAEQIFGAGGKRMRPGLVFLVSRATAELaglKELTTEHRRLGEIIE 291
Cdd:TIGR02749   1 ASATSLFAPVEDDLYLLTDNLKSLVGARHPILYAAAEHLFSAGGKRLRPAIVLLVSRATAEQ---QELTPRHRRLAEITE 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067579957 292 MIHTASLIHDDVLDESDMRRGKETVHELFGTRVAVLAGDFMFAQASWYLANLENLEVIKLISQVIKDFASGEIKQASSLF 371
Cdd:TIGR02749  78 MIHTASLVHDDVIDESDTRRGIETVHSLFGTRVAVLAGDFLFAQASWYLANLENLEVVKLISKVITDFAEGEIKQGLNQF 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067579957 372 DCDVTLEDYLLKSYYKTASLVAASTKGAAIFSRVDTDVTEQMYEFGKNLGLSFQVVDDILDFTQSSEQLGKPAGSDLAKG 451
Cdd:TIGR02749 158 DSDLSLEDYLEKSFYKTASLVAASSKAAAVLSDVPSQVANDLYEYGKHLGLAFQVVDDILDFTGSTEQLGKPAGSDLMKG 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067579957 452 NLTAPVIFALEKEPRLREIIESEFCEEGSLEEGIELVREGGGIRRAQELAREKADEALKNLQCLPQSGFRSALEEMVMFN 531
Cdd:TIGR02749 238 NLTAPVLFALEEEPKLSELIEREFSQKGDLEQALSLVRKSGGIKKARELAKEQAQLALQSLSFLPPSPPREALKELVHFV 317

                  ....*
gi 2067579957 532 LERID 536
Cdd:TIGR02749 318 LSRLY 322
preA CHL00151
prenyl transferase; Reviewed
216-534 1.23e-135

prenyl transferase; Reviewed


Pssm-ID: 164542  Cd Length: 323  Bit Score: 396.08  E-value: 1.23e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067579957 216 NLFEVVADDLQTLNDNLLSIVGAENPVLISAAEQIFGAGGKRMRPGLVFLVSRATAelaGLKELTTEHRRLGEIIEMIHT 295
Cdd:CHL00151    6 NLLTPIEEELLILEDNLKKLIGSGHPILYAAAKHLFSAGGKRIRPAIVLLVAKATG---GNMEIKTSQQRLAEITEIIHT 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067579957 296 ASLIHDDVLDESDMRRGKETVHELFGTRVAVLAGDFMFAQASWYLANLENLEVIKLISQVIKDFASGEIKQASSLFDCDV 375
Cdd:CHL00151   83 ASLVHDDVIDECSIRRGIPTVHKIFGTKIAVLAGDFLFAQSSWYLANLNNLEVVKLISKVITDFAEGEIRQGLVQFDTTL 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067579957 376 TLEDYLLKSYYKTASLVAASTKGAAIFSRVDTDVTEQMYEFGKNLGLSFQVVDDILDFTQSSEQLGKPAGSDLAKGNLTA 455
Cdd:CHL00151  163 SILNYIEKSFYKTASLIAASCKAAALLSDADEKDHNDFYLYGKHLGLAFQIIDDVLDITSSTESLGKPIGSDLKNGNLTA 242
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2067579957 456 PVIFALEKEPRLREIIESEFCEEGSLEEGIELVREGGGIRRAQELAREKADEALKNLQCLPQSGFRSALEEMVMFNLER 534
Cdd:CHL00151  243 PVLFALTQNSKLAKLIEREFCETKDISQALQIIKETNGIEKAKDLALEHMQAAIQCLKFLPPSSAKDSLIEIANFIINR 321
IspA COG0142
Geranylgeranyl pyrophosphate synthase [Coenzyme transport and metabolism]; Geranylgeranyl ...
213-534 8.01e-111

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: 332.96  E-value: 8.01e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067579957 213 SLANLFEVVADDLQTLNDNLLSIV-GAENPVLISAAEQIFGAGGKRMRPGLVFLvsraTAELAGLKelTTEHRRLGEIIE 291
Cdd:COG0142     2 TLKDLLALLAEDLARVEAALEELLaRSEPPLLAEAMRYLLLAGGKRLRPLLVLL----AARALGGD--PEAALRAAAAVE 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067579957 292 MIHTASLIHDDVLDESDMRRGKETVHELFGTRVAVLAGDFMFAQASWYLANLEN----LEVIKLISQVIKDFASGEIKQA 367
Cdd:COG0142    76 LIHTASLVHDDVMDDDDLRRGKPTVHARFGEATAILAGDALLALAFELLAELGDperrLRALRILARAARGMCEGQALDL 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067579957 368 SSLFDCDVTLEDYLLKSYYKTASLVAASTKGAAIFSRVDTDVTEQMYEFGKNLGLSFQVVDDILDFTQSSEQLGKPAGSD 447
Cdd:COG0142   156 EAEGRLDVTLEEYLRVIRLKTAALFAAALRLGAILAGADEEQVEALRRYGRNLGLAFQIRDDILDVTGDPEVLGKPAGSD 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067579957 448 LAKGNLTAPVIFALEKEP-----RLREIIESEFCEEGSLEEGIELVREGGGIRRAQELAREKADEALKNLQCLPQSGFRS 522
Cdd:COG0142   236 LREGKPTLPLLLALERADpeeraELRELLGKPDLDEEDLAEVRALLRESGALEYARELARELAEEALAALAALPDSEARE 315
                         330
                  ....*....|..
gi 2067579957 523 ALEEMVMFNLER 534
Cdd:COG0142   316 ALRALADYVVER 327
polyprenyl_synt pfam00348
Polyprenyl synthetase;
241-487 1.40e-93

Polyprenyl synthetase;


Pssm-ID: 459773  Cd Length: 251  Bit Score: 285.55  E-value: 1.40e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067579957 241 PVLISAAEQIFGAGGKRMRPGLVFLVSRATaelaGLKELTTEHRRLGEIIEMIHTASLIHDDVLDESDMRRGKETVHELF 320
Cdd:pfam00348   2 KLLYEPLDYLVSAGGKRIRPLLVLLSAEAL----GGPEDLEKAIVLAWAVELLHAASLVHDDIMDNSDLRRGQPTWHRIF 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067579957 321 GTRVAVLAGDFMFAQASWYLANL-ENLEVIKLISQVIKDFASGEIKQASSLF--DCDVTLEDYLLKSYYKTASLVAASTK 397
Cdd:pfam00348  78 GNAIAINDGDYLYALAFQLLAKLfPNPELLELFSEVTLQTAEGQGLDLLWRNddDLSCTEEEYLEIVKYKTAYLFALAVK 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067579957 398 GAAIFSRVDTDVTEQMYEFGKNLGLSFQVVDDILDFTQSSEQLGKPAGSDLAKGNLTAPVIFALEKEP----RLREIIES 473
Cdd:pfam00348 158 LGAILSGADDEVIEALKDYGLNLGLAFQIQDDYLDLFGDPEVLGKPAGTDITEGKCTWPVIHALERTPeqrkILLEIYGK 237
                         250
                  ....*....|....
gi 2067579957 474 EFCEEGSLEEGIEL 487
Cdd:pfam00348 238 RPEDVEKVKEAYEL 251
Trans_IPPS_HT cd00685
Trans-Isoprenyl Diphosphate Synthases, head-to-tail; These trans-Isoprenyl Diphosphate ...
238-534 3.21e-93

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: 285.21  E-value: 3.21e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067579957 238 AENPVLISAAEQIFGAGGKRMRPGLVFLVSRATAElaglkELTTEHRRLGEIIEMIHTASLIHDDVLDESDMRRGKETVH 317
Cdd:cd00685     1 SEVELLREALRYLLLAGGKRLRPLLVLLAARALGG-----PELEAALRLAAAIELLHTASLVHDDVMDNSDLRRGKPTVH 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067579957 318 ELFGTRVAVLAGDFMFAQASWYLANLEN---LEVIKLISQVIKDFASGEIKQASSLFDCDVTLEDYLLKSYYKTASLVAA 394
Cdd:cd00685    76 KVFGNATAILAGDYLLARAFELLARLGNpyyPRALELFSEAILELVEGQLLDLLSEYDTDVTEEEYLRIIRLKTAALFAA 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067579957 395 STKGAAIFSRVDTDVTEQMYEFGKNLGLSFQVVDDILDFTQSSEQLGKPAGSDLAKGNLTAPVIFALEkeprlreiiese 474
Cdd:cd00685   156 APLLGALLAGADEEEAEALKRFGRNLGLAFQIQDDILDLFGDPETLGKPVGSDLREGKCTLPVLLALR------------ 223
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067579957 475 fceegsleegielvregggirraqELAREKADEALKNLQCLPQSGFRSALEEMVMFNLER 534
Cdd:cd00685   224 ------------------------ELAREYEEKALEALKALPESPAREALRALADFILER 259
PLN02890 PLN02890
geranyl diphosphate synthase
199-518 9.16e-83

geranyl diphosphate synthase


Pssm-ID: 178478  Cd Length: 422  Bit Score: 263.71  E-value: 9.16e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067579957 199 SFDLRQETSSKQPISLaNLFEVVADDLQTLNDNLLSIVGAENPVLISAAEQIF--GAGGKRMRPGLVFLVSRA------T 270
Cdd:PLN02890   67 QYQVRHQSSSLVEEQL-DPFSLVADELSLLANKLRSMVVAEVPKLASAAEYFFkvGVEGKRFRPTVLLLMATAlnvplpE 145
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067579957 271 AELAGL-----KELTTEHRRLGEIIEMIHTASLIHDDVLDESDMRRGKETVHELFGTRVAVLAGDFMFAQASWYLANLEN 345
Cdd:PLN02890  146 STEGGVldivaSELRTRQQNIAEITEMIHVASLLHDDVLDDADTRRGVGSLNVVMGNKLSVLAGDFLLSRACVALAALKN 225
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067579957 346 LEVIKLISQVIKDFASGEIKQASSLFDCDVTLEDYLLKSYYKTASLVAASTKGAAIFSRVDTDVTEQMYEFGKNLGLSFQ 425
Cdd:PLN02890  226 TEVVSLLATAVEHLVTGETMQITSSREQRRSMDYYMQKTYYKTASLISNSCKAVAILAGQTAEVAVLAFEYGRNLGLAFQ 305
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067579957 426 VVDDILDFTQSSEQLGKPAGSDLAKGNLTAPVIFALEKEPRLREIIESEFCEEGSLEEGIELVREGGGIRRAQELAREKA 505
Cdd:PLN02890  306 LIDDVLDFTGTSASLGKGSLSDIRHGVITAPILFAMEEFPQLREVVDRGFDNPANVDIALEYLGKSRGIQRTRELAREHA 385
                         330
                  ....*....|...
gi 2067579957 506 DEALKNLQCLPQS 518
Cdd:PLN02890  386 NLAAAAIESLPET 398
PRK10888 PRK10888
octaprenyl diphosphate synthase; Provisional
212-534 6.19e-65

octaprenyl diphosphate synthase; Provisional


Pssm-ID: 182813  Cd Length: 323  Bit Score: 213.94  E-value: 6.19e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067579957 212 ISLANLFEVVADDLQTLNDNLLSIVGAENPVLISAAEQIFGAGGKRMRPGLVFLVSRAtaelagLKELTTEHRRLGEIIE 291
Cdd:PRK10888    1 MNLEKINELTAQDMAGVNAAILEQLNSDVQLINQLGYYIISGGGKRIRPMIAVLAARA------VGYQGNAHVTIAALIE 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067579957 292 MIHTASLIHDDVLDESDMRRGKETVHELFGTRVAVLAGDFMFAQASWYLANLENLEVIKLISQVIKDFASGEIKQASSLF 371
Cdd:PRK10888   75 FIHTATLLHDDVVDESDMRRGKATANAAFGNAASVLVGDFIYTRAFQMMTSLGSLKVLEVMSEAVNVIAEGEVLQLMNVN 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067579957 372 DCDVTLEDYLLKSYYKTASLVAASTKGAAIFSRVDTDVTEQMYEFGKNLGLSFQVVDDILDFTQSSEQLGKPAGSDLAKG 451
Cdd:PRK10888  155 DPDITEENYMRVIYSKTARLFEAAAQCSGILAGCTPEQEKGLQDYGRYLGTAFQLIDDLLDYSADGETLGKNVGDDLNEG 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067579957 452 NLTAPVIFALEK-EPRLREIIESEFcEEGS----LEEGIELVREGGGIRRAQELAREKADEALKNLQCLPQSGFRSALEE 526
Cdd:PRK10888  235 KPTLPLLHAMHHgTPEQAAMIRTAI-EQGNgrhlLEPVLEAMNACGSLEWTRQRAEEEADKAIAALQVLPDTPWREALIG 313

                  ....*...
gi 2067579957 527 MVMFNLER 534
Cdd:PRK10888  314 LAHIAVQR 321
Trans_IPPS cd00867
Trans-Isoprenyl Diphosphate Synthases; Trans-Isoprenyl Diphosphate Synthases (Trans_IPPS) of ...
258-462 2.25e-64

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: 209.51  E-value: 2.25e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067579957 258 MRPGLVFLVSRAtaelagLKELTTEHRRLGEIIEMIHTASLIHDDVLDESDMRRGKETVHEL-FGTRVAVLAGDFMFAQA 336
Cdd:cd00867     1 SRPLLVLLLARA------LGGDLEAALRLAAAVELLHAASLVHDDIVDDSDLRRGKPTAHLRrFGNALAILAGDYLLARA 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067579957 337 SWYLANLENLEVIKLISQVIKDFASGEIKQASSLFDCDVTLEDYLLKSYYKTASLVAASTKGAAIFSRVDTDVTEQMYEF 416
Cdd:cd00867    75 FQLLARLGYPRALELFAEALRELLEGQALDLEFERDTYETLDEYLEYCRYKTAGLVGLLCLLGAGLSGADDEQAEALKDY 154
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2067579957 417 GKNLGLSFQVVDDILDFTQSSEQLGKpAGSDLAKGNLTAPVIFALE 462
Cdd:cd00867   155 GRALGLAFQLTDDLLDVFGDAEELGK-VGSDLREGRITLPVILARE 199
Isoprenoid_Biosyn_C1 cd00385
Isoprenoid Biosynthesis enzymes, Class 1; Superfamily of trans-isoprenyl diphosphate synthases ...
279-518 3.20e-51

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: 175.38  E-value: 3.20e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067579957 279 LTTEHRRLGEIIEMIHTASLIHDDVLDESDMRRGKETVHEL---FGTRVAVLAGDFMFAQASWYLANLENLEVIKLISQV 355
Cdd:cd00385     8 LEPEASRLRAAVEKLHAASLVHDDIVDDSGTRRGLPTAHLAvaiDGLPEAILAGDLLLADAFEELAREGSPEALEILAEA 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067579957 356 IKDFASGEIKQASSLFDCDVTLEDYLLKSYYKTASLVAASTKGAAIFSRVDTDVTEQMYEFGKNLGLSFQVVDDILDFTQ 435
Cdd:cd00385    88 LLDLLEGQLLDLKWRREYVPTLEEYLEYCRYKTAGLVGALCLLGAGLSGGEAELLEALRKLGRALGLAFQLTNDLLDYEG 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067579957 436 SSEQLGkpagsdlakGNLTAPVIFALEKEPRLREIIesefceegsleegieLVREGGGIRRAQELAREKADEALKNLQCL 515
Cdd:cd00385   168 DAERGE---------GKCTLPVLYALEYGVPAEDLL---------------LVEKSGSLEEALEELAKLAEEALKELNEL 223

                  ...
gi 2067579957 516 PQS 518
Cdd:cd00385   224 ILS 226
X8 smart00768
Possibly involved in carbohydrate binding; The X8 domain, which may be involved in ...
31-115 2.25e-33

Possibly involved in carbohydrate binding; The X8 domain, which may be involved in carbohydrate binding, is found in an Olive pollen antigen as well as at the C terminus of family 17 glycosyl hydrolases. It contains 6 conserved cysteine residues which presumably form three disulfide bridges.


Pssm-ID: 197867 [Multi-domain]  Cd Length: 85  Bit Score: 121.59  E-value: 2.25e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067579957   31 TWCVAKPSSDQAALLDNINYACSH-VDCRVLSSGCPCYSPGNLINHASVAMNLYYQANGRNYWNCNFKNSGLIVITNPTl 109
Cdd:smart00768   1 LWCVAKPDADEAALQAALDYACGQgADCTAIQPGGSCYSPNTVKAHASYAFNSYYQKQGQSSGACDFSGTATITTTDPS- 79

                   ....*.
gi 2067579957  110 ldSGFC 115
Cdd:smart00768  80 --TGSC 83
X8 pfam07983
X8 domain; The X8 domain domain contains at least 6 conserved cysteine residues that ...
31-100 1.96e-24

X8 domain; The X8 domain domain contains at least 6 conserved cysteine residues that presumably form three disulphide bridges. The domain is found in an Olive pollen allergen as well as at the C-terminus of several families of glycosyl hydrolases. This domain may be involved in carbohydrate binding. This domain is characteriztic of GPI-anchored domains.


Pssm-ID: 400371  Cd Length: 76  Bit Score: 96.51  E-value: 1.96e-24
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2067579957  31 TWCVAKPSSDQAALLDNINYACSHVDCRVLSSGCP-----CYSPGNLINHASVAMNLYYQANGRNYWNCNFKNSG 100
Cdd:pfam07983   1 LWCVAKDSVDDEDLQDLFDYACGQADCSGIQANGTtgkygCYSPCTVKQHLSYAFNSYYQKQGKASSACDFSGSA 75
PRK10581 PRK10581
(2E,6E)-farnesyl diphosphate synthase;
226-534 2.42e-22

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


Pssm-ID: 182567  Cd Length: 299  Bit Score: 97.53  E-value: 2.42e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067579957 226 QTLNDNLLSIVGA---ENPVLISAAEqiFGA--GGKRMRPGLVFlvsrATAELAGLKELTTEHRrlGEIIEMIHTASLIH 300
Cdd:PRK10581   12 QQANQALSRFIAPlpfQNTPVVEAMQ--YGAllGGKRLRPFLVY----ATGQMFGVSTNTLDAP--AAAVECIHAYSLIH 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067579957 301 DDV--LDESDMRRGKETVHELFGTRVAVLAGDFMFAQASWYLANLENLEV-----IKLISQVIKdfASGEIK----QASS 369
Cdd:PRK10581   84 DDLpaMDDDDLRRGLPTCHVKFGEANAILAGDALQTLAFSILSDAPMPEVsdrdrISMISELAS--ASGIAGmcggQALD 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067579957 370 LF--DCDVTLEDYLLKSYYKTASLVAASTK-GAAIFSRVDTDVTEQMYEFGKNLGLSFQVVDDILDFTQSSEQLGKPAGS 446
Cdd:PRK10581  162 LEaeGKQVPLDALERIHRHKTGALIRAAVRlGALSAGDKGRRALPVLDRYAESIGLAFQVQDDILDVVGDTATLGKRQGA 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067579957 447 DLAKGNLTAPVIFALEKeprlreiiesefceegsleegielvregggirrAQELAREKADEALKNLQCL-PQSGFRSALE 525
Cdd:PRK10581  242 DQQLGKSTYPALLGLEQ---------------------------------ARKKARDLIDDARQSLDQLaAQSLDTSALE 288

                  ....*....
gi 2067579957 526 EMVMFNLER 534
Cdd:PRK10581  289 ALANYIIQR 297
 
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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