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Conserved domains on  [gi|338797808|ref|NP_001229753|]
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farnesyl pyrophosphate synthase isoform b [Homo sapiens]

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;
42-307 6.14e-100

Polyprenyl synthetase;


:

Pssm-ID: 459773  Cd Length: 251  Bit Score: 295.57  E-value: 6.14e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338797808   42 IARLKEVLEYNA-IGGKYNRGLTVVVAFRELVEPrkqdaDSLQRAWTVGWCVELLQAFFLVADDIMDSSLTRRGQICWYQ 120
Cdd:pfam00348   1 EKLLYEPLDYLVsAGGKRIRPLLVLLSAEALGGP-----EDLEKAIVLAWAVELLHAASLVHDDIMDNSDLRRGQPTWHR 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338797808  121 KPGVGLdAINDANLLEACIYRLLKLYCReqpyYLNLIELFLQSSYQTEIGQTLDLLTAPQGNVDLvrfTEKRYKSIVKYK 200
Cdd:pfam00348  76 IFGNAI-AINDGDYLYALAFQLLAKLFP----NPELLELFSEVTLQTAEGQGLDLLWRNDDDLSC---TEEEYLEIVKYK 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338797808  201 TAfYSFYLPIAAAMYMAGIDgEKEHANAKKILLEMGEFFQIQDDYLDLFGDPSVTGKI-GTDIQDNKCSWLVVQCLQRaT 279
Cdd:pfam00348 148 TA-YLFALAVKLGAILSGAD-DEVIEALKDYGLNLGLAFQIQDDYLDLFGDPEVLGKPaGTDITEGKCTWPVIHALER-T 224
                         250       260
                  ....*....|....*....|....*...
gi 338797808  280 PEQYQILKENYGQKeAEKVARVKALYEE 307
Cdd:pfam00348 225 PEQRKILLEIYGKR-PEDVEKVKEAYEL 251
 
Name Accession Description Interval E-value
polyprenyl_synt pfam00348
Polyprenyl synthetase;
42-307 6.14e-100

Polyprenyl synthetase;


Pssm-ID: 459773  Cd Length: 251  Bit Score: 295.57  E-value: 6.14e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338797808   42 IARLKEVLEYNA-IGGKYNRGLTVVVAFRELVEPrkqdaDSLQRAWTVGWCVELLQAFFLVADDIMDSSLTRRGQICWYQ 120
Cdd:pfam00348   1 EKLLYEPLDYLVsAGGKRIRPLLVLLSAEALGGP-----EDLEKAIVLAWAVELLHAASLVHDDIMDNSDLRRGQPTWHR 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338797808  121 KPGVGLdAINDANLLEACIYRLLKLYCReqpyYLNLIELFLQSSYQTEIGQTLDLLTAPQGNVDLvrfTEKRYKSIVKYK 200
Cdd:pfam00348  76 IFGNAI-AINDGDYLYALAFQLLAKLFP----NPELLELFSEVTLQTAEGQGLDLLWRNDDDLSC---TEEEYLEIVKYK 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338797808  201 TAfYSFYLPIAAAMYMAGIDgEKEHANAKKILLEMGEFFQIQDDYLDLFGDPSVTGKI-GTDIQDNKCSWLVVQCLQRaT 279
Cdd:pfam00348 148 TA-YLFALAVKLGAILSGAD-DEVIEALKDYGLNLGLAFQIQDDYLDLFGDPEVLGKPaGTDITEGKCTWPVIHALER-T 224
                         250       260
                  ....*....|....*....|....*...
gi 338797808  280 PEQYQILKENYGQKeAEKVARVKALYEE 307
Cdd:pfam00348 225 PEQRKILLEIYGKR-PEDVEKVKEAYEL 251
Trans_IPPS_HT cd00685
Trans-Isoprenyl Diphosphate Synthases, head-to-tail; These trans-Isoprenyl Diphosphate ...
40-351 4.81e-76

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: 234.75  E-value: 4.81e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338797808  40 DAIARLKEVLEYN-AIGGKYNRGLTVVVAFRELVEPRkqdadsLQRAWTVGWCVELLQAFFLVADDIMDSSLTRRGQICW 118
Cdd:cd00685    1 SEVELLREALRYLlLAGGKRLRPLLVLLAARALGGPE------LEAALRLAAAIELLHTASLVHDDVMDNSDLRRGKPTV 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338797808 119 YQKPGVGLdAINDANLLEACIYRLLKLYCReqPYYLNLIELFLQSSYQTEIGQTLDLLTAPQGNvdlvrFTEKRYKSIVK 198
Cdd:cd00685   75 HKVFGNAT-AILAGDYLLARAFELLARLGN--PYYPRALELFSEAILELVEGQLLDLLSEYDTD-----VTEEEYLRIIR 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338797808 199 YKTAFYSFYLPIAAAMYMAGidGEKEHANAKKILLEMGEFFQIQDDYLDLFGDPSVTGK-IGTDIQDNKCSWLVVQCLQr 277
Cdd:cd00685  147 LKTAALFAAAPLLGALLAGA--DEEEAEALKRFGRNLGLAFQIQDDILDLFGDPETLGKpVGSDLREGKCTLPVLLALR- 223
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 338797808 278 atpeqyqilkenygqkeaekvarvkalyeeldlpAVFLQYEEDSYSHIMALIEQYAAPLppavFLGLARKIYKR 351
Cdd:cd00685  224 ----------------------------------ELAREYEEKALEALKALPESPAREA----LRALADFILER 259
IspA COG0142
Geranylgeranyl pyrophosphate synthase [Coenzyme transport and metabolism]; Geranylgeranyl ...
40-353 1.08e-29

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: 116.09  E-value: 1.08e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338797808  40 DAIARLKEVLEY--NAiGGKYNRGLTVVVAFRELveprkqdADSLQRAWTVGWCVELLQAFFLVADDIMDSSLTRRGqic 117
Cdd:COG0142   28 SEPPLLAEAMRYllLA-GGKRLRPLLVLLAARAL-------GGDPEAALRAAAAVELIHTASLVHDDVMDDDDLRRG--- 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338797808 118 wyqKP------GVGLdAINDANLLEACIYRLLkLYCREQPYYLNLIELFLQSSYQTEIGQTLDLLTAPQGNVdlvrfTEK 191
Cdd:COG0142   97 ---KPtvharfGEAT-AILAGDALLALAFELL-AELGDPERRLRALRILARAARGMCEGQALDLEAEGRLDV-----TLE 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338797808 192 RYKSIVKYKTAFYsfylpIAAAMYMAGI--DGEKEHANAkkilleMGEF-------FQIQDDYLDLFGDPSVTGK-IGTD 261
Cdd:COG0142  167 EYLRVIRLKTAAL-----FAAALRLGAIlaGADEEQVEA------LRRYgrnlglaFQIRDDILDVTGDPEVLGKpAGSD 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338797808 262 IQDNKCSWLVVQCLQRATPEQYQILKENYGQKE--AEKVARVKALYEELdlpavflqyeeDSYSHIMALIEQYA------ 333
Cdd:COG0142  236 LREGKPTLPLLLALERADPEERAELRELLGKPDldEEDLAEVRALLRES-----------GALEYARELARELAeealaa 304
                        330       340
                 ....*....|....*....|....*
gi 338797808 334 -APLPP----AVFLGLARKIYKRRK 353
Cdd:COG0142  305 lAALPDsearEALRALADYVVERDR 329
 
Name Accession Description Interval E-value
polyprenyl_synt pfam00348
Polyprenyl synthetase;
42-307 6.14e-100

Polyprenyl synthetase;


Pssm-ID: 459773  Cd Length: 251  Bit Score: 295.57  E-value: 6.14e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338797808   42 IARLKEVLEYNA-IGGKYNRGLTVVVAFRELVEPrkqdaDSLQRAWTVGWCVELLQAFFLVADDIMDSSLTRRGQICWYQ 120
Cdd:pfam00348   1 EKLLYEPLDYLVsAGGKRIRPLLVLLSAEALGGP-----EDLEKAIVLAWAVELLHAASLVHDDIMDNSDLRRGQPTWHR 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338797808  121 KPGVGLdAINDANLLEACIYRLLKLYCReqpyYLNLIELFLQSSYQTEIGQTLDLLTAPQGNVDLvrfTEKRYKSIVKYK 200
Cdd:pfam00348  76 IFGNAI-AINDGDYLYALAFQLLAKLFP----NPELLELFSEVTLQTAEGQGLDLLWRNDDDLSC---TEEEYLEIVKYK 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338797808  201 TAfYSFYLPIAAAMYMAGIDgEKEHANAKKILLEMGEFFQIQDDYLDLFGDPSVTGKI-GTDIQDNKCSWLVVQCLQRaT 279
Cdd:pfam00348 148 TA-YLFALAVKLGAILSGAD-DEVIEALKDYGLNLGLAFQIQDDYLDLFGDPEVLGKPaGTDITEGKCTWPVIHALER-T 224
                         250       260
                  ....*....|....*....|....*...
gi 338797808  280 PEQYQILKENYGQKeAEKVARVKALYEE 307
Cdd:pfam00348 225 PEQRKILLEIYGKR-PEDVEKVKEAYEL 251
Trans_IPPS_HT cd00685
Trans-Isoprenyl Diphosphate Synthases, head-to-tail; These trans-Isoprenyl Diphosphate ...
40-351 4.81e-76

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: 234.75  E-value: 4.81e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338797808  40 DAIARLKEVLEYN-AIGGKYNRGLTVVVAFRELVEPRkqdadsLQRAWTVGWCVELLQAFFLVADDIMDSSLTRRGQICW 118
Cdd:cd00685    1 SEVELLREALRYLlLAGGKRLRPLLVLLAARALGGPE------LEAALRLAAAIELLHTASLVHDDVMDNSDLRRGKPTV 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338797808 119 YQKPGVGLdAINDANLLEACIYRLLKLYCReqPYYLNLIELFLQSSYQTEIGQTLDLLTAPQGNvdlvrFTEKRYKSIVK 198
Cdd:cd00685   75 HKVFGNAT-AILAGDYLLARAFELLARLGN--PYYPRALELFSEAILELVEGQLLDLLSEYDTD-----VTEEEYLRIIR 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338797808 199 YKTAFYSFYLPIAAAMYMAGidGEKEHANAKKILLEMGEFFQIQDDYLDLFGDPSVTGK-IGTDIQDNKCSWLVVQCLQr 277
Cdd:cd00685  147 LKTAALFAAAPLLGALLAGA--DEEEAEALKRFGRNLGLAFQIQDDILDLFGDPETLGKpVGSDLREGKCTLPVLLALR- 223
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 338797808 278 atpeqyqilkenygqkeaekvarvkalyeeldlpAVFLQYEEDSYSHIMALIEQYAAPLppavFLGLARKIYKR 351
Cdd:cd00685  224 ----------------------------------ELAREYEEKALEALKALPESPAREA----LRALADFILER 259
Trans_IPPS cd00867
Trans-Isoprenyl Diphosphate Synthases; Trans-Isoprenyl Diphosphate Synthases (Trans_IPPS) of ...
59-351 1.26e-53

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: 176.38  E-value: 1.26e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338797808  59 NRGLTVVVAFRELVEPrkqdadsLQRAWTVGWCVELLQAFFLVADDIMDSSLTRRGQICWYQKPGVGLDAINDANLLEAC 138
Cdd:cd00867    1 SRPLLVLLLARALGGD-------LEAALRLAAAVELLHAASLVHDDIVDDSDLRRGKPTAHLRRFGNALAILAGDYLLAR 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338797808 139 IYRLLKLYCreqpyYLNLIELFLQSSYQTEIGQTLDLLTAPQGNvdlvrFTEKRYKSIVKYKTAFYSFYLPIAAAMYMAG 218
Cdd:cd00867   74 AFQLLARLG-----YPRALELFAEALRELLEGQALDLEFERDTY-----ETLDEYLEYCRYKTAGLVGLLCLLGAGLSGA 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338797808 219 IDgeKEHANAKKILLEMGEFFQIQDDYLDLFGDPSVTGKIGTDIQDNKCSWLVVQCLQRAtpeqyqilkenygqkeaekv 298
Cdd:cd00867  144 DD--EQAEALKDYGRALGLAFQLTDDLLDVFGDAEELGKVGSDLREGRITLPVILARERA-------------------- 201
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 338797808 299 arvkalyeeldlpavfLQYEEDSYSHIMALIEQyaAPLPPAVFLGLARKIYKR 351
Cdd:cd00867  202 ----------------AEYAEEAYAALEALPPS--LPRARRALIALADFLYRR 236
Isoprenoid_Biosyn_C1 cd00385
Isoprenoid Biosynthesis enzymes, Class 1; Superfamily of trans-isoprenyl diphosphate synthases ...
84-350 1.63e-33

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: 124.14  E-value: 1.63e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338797808  84 RAWTVGWCVELLQAFFLVADDIMDSSLTRRGQICWYQK--PGVGLDAINDANLLEACIYRLLklycrEQPYYLNLIELFL 161
Cdd:cd00385   11 EASRLRAAVEKLHAASLVHDDIVDDSGTRRGLPTAHLAvaIDGLPEAILAGDLLLADAFEEL-----AREGSPEALEILA 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338797808 162 QSSYQTEIGQTLDLLTAPQGNvdlvrFTEKRYKSIVKYKTAFYSFYLPIAAAMYMAGidGEKEHANAKKILLEMGEFFQI 241
Cdd:cd00385   86 EALLDLLEGQLLDLKWRREYV-----PTLEEYLEYCRYKTAGLVGALCLLGAGLSGG--EAELLEALRKLGRALGLAFQL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338797808 242 QDDYLDLFGDPSVTgkigtdiqDNKCSWLVVQCLQRATPEQYQILkenygqkeaekvarVKALYEELDLPAVFLQYEEDS 321
Cdd:cd00385  159 TNDLLDYEGDAERG--------EGKCTLPVLYALEYGVPAEDLLL--------------VEKSGSLEEALEELAKLAEEA 216
                        250       260
                 ....*....|....*....|....*....
gi 338797808 322 YSHIMALIEQyaAPLPPAVFLGLARKIYK 350
Cdd:cd00385  217 LKELNELILS--LPDVPRALLALALNLYR 243
IspA COG0142
Geranylgeranyl pyrophosphate synthase [Coenzyme transport and metabolism]; Geranylgeranyl ...
40-353 1.08e-29

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: 116.09  E-value: 1.08e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338797808  40 DAIARLKEVLEY--NAiGGKYNRGLTVVVAFRELveprkqdADSLQRAWTVGWCVELLQAFFLVADDIMDSSLTRRGqic 117
Cdd:COG0142   28 SEPPLLAEAMRYllLA-GGKRLRPLLVLLAARAL-------GGDPEAALRAAAAVELIHTASLVHDDVMDDDDLRRG--- 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338797808 118 wyqKP------GVGLdAINDANLLEACIYRLLkLYCREQPYYLNLIELFLQSSYQTEIGQTLDLLTAPQGNVdlvrfTEK 191
Cdd:COG0142   97 ---KPtvharfGEAT-AILAGDALLALAFELL-AELGDPERRLRALRILARAARGMCEGQALDLEAEGRLDV-----TLE 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338797808 192 RYKSIVKYKTAFYsfylpIAAAMYMAGI--DGEKEHANAkkilleMGEF-------FQIQDDYLDLFGDPSVTGK-IGTD 261
Cdd:COG0142  167 EYLRVIRLKTAAL-----FAAALRLGAIlaGADEEQVEA------LRRYgrnlglaFQIRDDILDVTGDPEVLGKpAGSD 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338797808 262 IQDNKCSWLVVQCLQRATPEQYQILKENYGQKE--AEKVARVKALYEELdlpavflqyeeDSYSHIMALIEQYA------ 333
Cdd:COG0142  236 LREGKPTLPLLLALERADPEERAELRELLGKPDldEEDLAEVRALLRES-----------GALEYARELARELAeealaa 304
                        330       340
                 ....*....|....*....|....*
gi 338797808 334 -APLPP----AVFLGLARKIYKRRK 353
Cdd:COG0142  305 lAALPDsearEALRALADYVVERDR 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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