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Conserved domains on  [gi|1002235113|ref|XP_015621772|]
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farnesyl pyrophosphate synthase isoform X2 [Oryza sativa Japonica Group]

Protein Classification

FPP/GGPP synthase family protein( domain architecture ID 11092413)

FPP/GGPP synthase family protein such as farnesyl/geranylgeranyl diphosphate synthases, which are key enzymes in isoprenoid biosynthesis, catalyzing the formation of farnesyl diphosphate (FPP) and geranylgeranyl diphosphate (GGPP), respectively

CATH:  1.10.600.10
EC:  2.5.1.-
Gene Ontology:  GO:0004659|GO:0046872|GO:0008299
PubMed:  8003978|11111076
SCOP:  4001453

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
polyprenyl_synt pfam00348
Polyprenyl synthetase;
1-261 5.65e-90

Polyprenyl synthetase;


:

Pssm-ID: 459773  Cd Length: 251  Bit Score: 268.22  E-value: 5.65e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235113   1 MLDYNV-LGGKLNRGLAVVESYKILKaasatepSEEELFLACILGWGIEWLQAYFLVLDDIMDNSQTRRGKPCWFRlpKV 79
Cdd:pfam00348   7 PLDYLVsAGGKRIRPLLVLLSAEALG-------GPEDLEKAIVLAWAVELLHAASLVHDDIMDNSDLRRGQPTWHR--IF 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235113  80 GL-IAINDGLVLRSQISRIFRRYFRgksyYVDLLDLFNEVEIQTTSGQLLDqiTTNEGRKDLNKyNVHVYRRIVEYKTAy 158
Cdd:pfam00348  78 GNaIAINDGDYLYALAFQLLAKLFP----NPELLELFSEVTLQTAEGQGLD--LLWRNDDDLSC-TEEEYLEIVKYKTA- 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235113 159 YSFYLPVACALLLFDESLDNYAQVKHILVEMGVYFQSQDDYLDCFGEPEIIGKI-GSDIEDFKCSWLFVQALERaDEKQK 237
Cdd:pfam00348 150 YLFALAVKLGAILSGADDEVIEALKDYGLNLGLAFQIQDDYLDLFGDPEVLGKPaGTDITEGKCTWPVIHALER-TPEQR 228
                         250       260
                  ....*....|....*....|....
gi 1002235113 238 GVLFENYGKsDPACVAKVKDLYNE 261
Cdd:pfam00348 229 KILLEIYGK-RPEDVEKVKEAYEL 251
 
Name Accession Description Interval E-value
polyprenyl_synt pfam00348
Polyprenyl synthetase;
1-261 5.65e-90

Polyprenyl synthetase;


Pssm-ID: 459773  Cd Length: 251  Bit Score: 268.22  E-value: 5.65e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235113   1 MLDYNV-LGGKLNRGLAVVESYKILKaasatepSEEELFLACILGWGIEWLQAYFLVLDDIMDNSQTRRGKPCWFRlpKV 79
Cdd:pfam00348   7 PLDYLVsAGGKRIRPLLVLLSAEALG-------GPEDLEKAIVLAWAVELLHAASLVHDDIMDNSDLRRGQPTWHR--IF 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235113  80 GL-IAINDGLVLRSQISRIFRRYFRgksyYVDLLDLFNEVEIQTTSGQLLDqiTTNEGRKDLNKyNVHVYRRIVEYKTAy 158
Cdd:pfam00348  78 GNaIAINDGDYLYALAFQLLAKLFP----NPELLELFSEVTLQTAEGQGLD--LLWRNDDDLSC-TEEEYLEIVKYKTA- 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235113 159 YSFYLPVACALLLFDESLDNYAQVKHILVEMGVYFQSQDDYLDCFGEPEIIGKI-GSDIEDFKCSWLFVQALERaDEKQK 237
Cdd:pfam00348 150 YLFALAVKLGAILSGADDEVIEALKDYGLNLGLAFQIQDDYLDLFGDPEVLGKPaGTDITEGKCTWPVIHALER-TPEQR 228
                         250       260
                  ....*....|....*....|....
gi 1002235113 238 GVLFENYGKsDPACVAKVKDLYNE 261
Cdd:pfam00348 229 KILLEIYGK-RPEDVEKVKEAYEL 251
Trans_IPPS_HT cd00685
Trans-Isoprenyl Diphosphate Synthases, head-to-tail; These trans-Isoprenyl Diphosphate ...
1-305 9.00e-69

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: 214.72  E-value: 9.00e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235113   1 MLDYNVL-GGKLNRGLAVVESYKILKAAsatepseeELFLACILGWGIEWLQAYFLVLDDIMDNSQTRRGKPCWFRLPKV 79
Cdd:cd00685     9 ALRYLLLaGGKRLRPLLVLLAARALGGP--------ELEAALRLAAAIELLHTASLVHDDVMDNSDLRRGKPTVHKVFGN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235113  80 GlIAINDGLVLRSQISRIFRRYFRGksYYVDLLDLFNEVEIQTTSGQLLDqiTTNEGRKDlnkYNVHVYRRIVEYKTAYY 159
Cdd:cd00685    81 A-TAILAGDYLLARAFELLARLGNP--YYPRALELFSEAILELVEGQLLD--LLSEYDTD---VTEEEYLRIIRLKTAAL 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235113 160 SFYLPVACALLLfDESLDNYAQVKHILVEMGVYFQSQDDYLDCFGEPEIIGK-IGSDIEDFKCSWLFVQALEradekqkg 238
Cdd:cd00685   153 FAAAPLLGALLA-GADEEEAEALKRFGRNLGLAFQIQDDILDLFGDPETLGKpVGSDLREGKCTLPVLLALR-------- 223
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002235113 239 vlfenygksdpacvakvkdlynelhlqRVFSEYERESYEklisAIEAQPNEAVRAVLKSFLHKIYKR 305
Cdd:cd00685   224 ---------------------------ELAREYEEKALE----ALKALPESPAREALRALADFILER 259
IspA COG0142
Geranylgeranyl pyrophosphate synthase [Coenzyme transport and metabolism]; Geranylgeranyl ...
8-307 1.08e-28

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: 112.24  E-value: 1.08e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235113   8 GGKLNRGLAVvesykiLKAASATEPSEEELF-LACIlgwgIEWLQAYFLVLDDIMDNSQTRRGKP-CWFR-------Lpk 78
Cdd:COG0142    44 GGKRLRPLLV------LLAARALGGDPEAALrAAAA----VELIHTASLVHDDVMDDDDLRRGKPtVHARfgeataiL-- 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235113  79 VG--LIAINDGLVLRSQISRIFRRyfrgksyyvdLLDLFNEVEIQTTSGQLLDqiTTNEGRKDLNkynVHVYRRIVEYKT 156
Cdd:COG0142   112 AGdaLLALAFELLAELGDPERRLR----------ALRILARAARGMCEGQALD--LEAEGRLDVT---LEEYLRVIRLKT 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235113 157 AYYsFYLPVACALLLFD------ESLDNYAqvKHIlvemGVYFQSQDDYLDCFGEPEIIGK-IGSDIEDFKCSWLFVQAL 229
Cdd:COG0142   177 AAL-FAAALRLGAILAGadeeqvEALRRYG--RNL----GLAFQIRDDILDVTGDPEVLGKpAGSDLREGKPTLPLLLAL 249
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235113 230 ERADEKQKGVLFENYGK--SDPACVAKVKDLYNELHLQRVFSEYERESYEKLISAIEAQPNEAVRAVLKSFLHKIYKRSK 307
Cdd:COG0142   250 ERADPEERAELRELLGKpdLDEEDLAEVRALLRESGALEYARELARELAEEALAALAALPDSEAREALRALADYVVERDR 329
 
Name Accession Description Interval E-value
polyprenyl_synt pfam00348
Polyprenyl synthetase;
1-261 5.65e-90

Polyprenyl synthetase;


Pssm-ID: 459773  Cd Length: 251  Bit Score: 268.22  E-value: 5.65e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235113   1 MLDYNV-LGGKLNRGLAVVESYKILKaasatepSEEELFLACILGWGIEWLQAYFLVLDDIMDNSQTRRGKPCWFRlpKV 79
Cdd:pfam00348   7 PLDYLVsAGGKRIRPLLVLLSAEALG-------GPEDLEKAIVLAWAVELLHAASLVHDDIMDNSDLRRGQPTWHR--IF 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235113  80 GL-IAINDGLVLRSQISRIFRRYFRgksyYVDLLDLFNEVEIQTTSGQLLDqiTTNEGRKDLNKyNVHVYRRIVEYKTAy 158
Cdd:pfam00348  78 GNaIAINDGDYLYALAFQLLAKLFP----NPELLELFSEVTLQTAEGQGLD--LLWRNDDDLSC-TEEEYLEIVKYKTA- 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235113 159 YSFYLPVACALLLFDESLDNYAQVKHILVEMGVYFQSQDDYLDCFGEPEIIGKI-GSDIEDFKCSWLFVQALERaDEKQK 237
Cdd:pfam00348 150 YLFALAVKLGAILSGADDEVIEALKDYGLNLGLAFQIQDDYLDLFGDPEVLGKPaGTDITEGKCTWPVIHALER-TPEQR 228
                         250       260
                  ....*....|....*....|....
gi 1002235113 238 GVLFENYGKsDPACVAKVKDLYNE 261
Cdd:pfam00348 229 KILLEIYGK-RPEDVEKVKEAYEL 251
Trans_IPPS_HT cd00685
Trans-Isoprenyl Diphosphate Synthases, head-to-tail; These trans-Isoprenyl Diphosphate ...
1-305 9.00e-69

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: 214.72  E-value: 9.00e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235113   1 MLDYNVL-GGKLNRGLAVVESYKILKAAsatepseeELFLACILGWGIEWLQAYFLVLDDIMDNSQTRRGKPCWFRLPKV 79
Cdd:cd00685     9 ALRYLLLaGGKRLRPLLVLLAARALGGP--------ELEAALRLAAAIELLHTASLVHDDVMDNSDLRRGKPTVHKVFGN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235113  80 GlIAINDGLVLRSQISRIFRRYFRGksYYVDLLDLFNEVEIQTTSGQLLDqiTTNEGRKDlnkYNVHVYRRIVEYKTAYY 159
Cdd:cd00685    81 A-TAILAGDYLLARAFELLARLGNP--YYPRALELFSEAILELVEGQLLD--LLSEYDTD---VTEEEYLRIIRLKTAAL 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235113 160 SFYLPVACALLLfDESLDNYAQVKHILVEMGVYFQSQDDYLDCFGEPEIIGK-IGSDIEDFKCSWLFVQALEradekqkg 238
Cdd:cd00685   153 FAAAPLLGALLA-GADEEEAEALKRFGRNLGLAFQIQDDILDLFGDPETLGKpVGSDLREGKCTLPVLLALR-------- 223
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002235113 239 vlfenygksdpacvakvkdlynelhlqRVFSEYERESYEklisAIEAQPNEAVRAVLKSFLHKIYKR 305
Cdd:cd00685   224 ---------------------------ELAREYEEKALE----ALKALPESPAREALRALADFILER 259
Trans_IPPS cd00867
Trans-Isoprenyl Diphosphate Synthases; Trans-Isoprenyl Diphosphate Synthases (Trans_IPPS) of ...
12-305 1.41e-48

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: 162.13  E-value: 1.41e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235113  12 NRGLAVVESYKILKAAsatepseeeLFLACILGWGIEWLQAYFLVLDDIMDNSQTRRGKPCWFRLPKVGLIAINDGLVLR 91
Cdd:cd00867     1 SRPLLVLLLARALGGD---------LEAALRLAAAVELLHAASLVHDDIVDDSDLRRGKPTAHLRRFGNALAILAGDYLL 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235113  92 SQISRIFRRYFrgksyYVDLLDLFNEVEIQTTSGQLLDQITTNEGRKDLNKynvhvYRRIVEYKTAYYSFYLPVACALLL 171
Cdd:cd00867    72 ARAFQLLARLG-----YPRALELFAEALRELLEGQALDLEFERDTYETLDE-----YLEYCRYKTAGLVGLLCLLGAGLS 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235113 172 fDESLDNYAQVKHILVEMGVYFQSQDDYLDCFGEPEIIGKIGSDIEDFKCSWLFVQALERADekqkgvlfenygksdpac 251
Cdd:cd00867   142 -GADDEQAEALKDYGRALGLAFQLTDDLLDVFGDAEELGKVGSDLREGRITLPVILARERAA------------------ 202
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1002235113 252 vakvkdlynelhlqrvfsEYERESYEKLISAIEAQPneAVRAVLKSFLHKIYKR 305
Cdd:cd00867   203 ------------------EYAEEAYAALEALPPSLP--RARRALIALADFLYRR 236
Isoprenoid_Biosyn_C1 cd00385
Isoprenoid Biosynthesis enzymes, Class 1; Superfamily of trans-isoprenyl diphosphate synthases ...
40-304 1.73e-29

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: 112.59  E-value: 1.73e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235113  40 ACILGWGIEWLQAYFLVLDDIMDNSQTRRGKPCWFRLPKVGL--IAINDGLVLRSQISRIFRRYFRgksyyVDLLDLFNE 117
Cdd:cd00385    12 ASRLRAAVEKLHAASLVHDDIVDDSGTRRGLPTAHLAVAIDGlpEAILAGDLLLADAFEELAREGS-----PEALEILAE 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235113 118 VEIQTTSGQLLDQITTNEGRKDLNKYNvhvyrRIVEYKTAYYSFYLPVACALLLfDESLDNYAQVKHILVEMGVYFQSQD 197
Cdd:cd00385    87 ALLDLLEGQLLDLKWRREYVPTLEEYL-----EYCRYKTAGLVGALCLLGAGLS-GGEAELLEALRKLGRALGLAFQLTN 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235113 198 DYLDCFGEPEIIgkigsdieDFKCSWLFVQALERADEKQKgvlfenygksdpacVAKVKDLYNELHLQRVFSEYERESYE 277
Cdd:cd00385   161 DLLDYEGDAERG--------EGKCTLPVLYALEYGVPAED--------------LLLVEKSGSLEEALEELAKLAEEALK 218
                         250       260
                  ....*....|....*....|....*..
gi 1002235113 278 KLISAIEAQPneAVRAVLKSFLHKIYK 304
Cdd:cd00385   219 ELNELILSLP--DVPRALLALALNLYR 243
IspA COG0142
Geranylgeranyl pyrophosphate synthase [Coenzyme transport and metabolism]; Geranylgeranyl ...
8-307 1.08e-28

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: 112.24  E-value: 1.08e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235113   8 GGKLNRGLAVvesykiLKAASATEPSEEELF-LACIlgwgIEWLQAYFLVLDDIMDNSQTRRGKP-CWFR-------Lpk 78
Cdd:COG0142    44 GGKRLRPLLV------LLAARALGGDPEAALrAAAA----VELIHTASLVHDDVMDDDDLRRGKPtVHARfgeataiL-- 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235113  79 VG--LIAINDGLVLRSQISRIFRRyfrgksyyvdLLDLFNEVEIQTTSGQLLDqiTTNEGRKDLNkynVHVYRRIVEYKT 156
Cdd:COG0142   112 AGdaLLALAFELLAELGDPERRLR----------ALRILARAARGMCEGQALD--LEAEGRLDVT---LEEYLRVIRLKT 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235113 157 AYYsFYLPVACALLLFD------ESLDNYAqvKHIlvemGVYFQSQDDYLDCFGEPEIIGK-IGSDIEDFKCSWLFVQAL 229
Cdd:COG0142   177 AAL-FAAALRLGAILAGadeeqvEALRRYG--RNL----GLAFQIRDDILDVTGDPEVLGKpAGSDLREGKPTLPLLLAL 249
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235113 230 ERADEKQKGVLFENYGK--SDPACVAKVKDLYNELHLQRVFSEYERESYEKLISAIEAQPNEAVRAVLKSFLHKIYKRSK 307
Cdd:COG0142   250 ERADPEERAELRELLGKpdLDEEDLAEVRALLRESGALEYARELARELAEEALAALAALPDSEAREALRALADYVVERDR 329
 
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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