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Conserved domains on  [gi|19114211|ref|NP_593299|]
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geranyltranstransferase Fps1 [Schizosaccharomyces pombe]

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;
36-299 2.05e-101

Polyprenyl synthetase;


:

Pssm-ID: 459773  Cd Length: 251  Bit Score: 299.04  E-value: 2.05e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114211    36 EWYKNSLFHNT-LGGKYNRGLSVIDSYEILLGHPLDEaaymKAAVLGWMVELLQSFFLIADDIMDASKTRRGQPCWYLMP 114
Cdd:pfam00348   2 KLLYEPLDYLVsAGGKRIRPLLVLLSAEALGGPEDLE----KAIVLAWAVELLHAASLVHDDIMDNSDLRRGQPTWHRIF 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114211   115 GVgNIAINDAFMVESAIYFLLKKHFRqescYVDLIELFHDVTFQTELGQQLDLLTAPEDSVDLskfSLQKHSFIVIYKTA 194
Cdd:pfam00348  78 GN-AIAINDGDYLYALAFQLLAKLFP----NPELLELFSEVTLQTAEGQGLDLLWRNDDDLSC---TEEEYLEIVKYKTA 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114211   195 fYSFYLPVALAMHLAGvATPENLKCAQDILIILGKYFQVQDDYLDCYGDPTVTGKI-GTDILDNKCSWIINLALAKcTPE 273
Cdd:pfam00348 150 -YLFALAVKLGAILSG-ADDEVIEALKDYGLNLGLAFQIQDDYLDLFGDPEVLGKPaGTDITEGKCTWPVIHALER-TPE 226

                         250       260
                  ....*....|....*....|....*.
gi 19114211   274 QRVILDDNYGrKDSESEKRVKAVFEE 299
Cdd:pfam00348 227 QRKILLEIYG-KRPEDVEKVKEAYEL 251
 
Name Accession Description Interval E-value
polyprenyl_synt pfam00348
Polyprenyl synthetase;
36-299 2.05e-101

Polyprenyl synthetase;


Pssm-ID: 459773  Cd Length: 251  Bit Score: 299.04  E-value: 2.05e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114211    36 EWYKNSLFHNT-LGGKYNRGLSVIDSYEILLGHPLDEaaymKAAVLGWMVELLQSFFLIADDIMDASKTRRGQPCWYLMP 114
Cdd:pfam00348   2 KLLYEPLDYLVsAGGKRIRPLLVLLSAEALGGPEDLE----KAIVLAWAVELLHAASLVHDDIMDNSDLRRGQPTWHRIF 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114211   115 GVgNIAINDAFMVESAIYFLLKKHFRqescYVDLIELFHDVTFQTELGQQLDLLTAPEDSVDLskfSLQKHSFIVIYKTA 194
Cdd:pfam00348  78 GN-AIAINDGDYLYALAFQLLAKLFP----NPELLELFSEVTLQTAEGQGLDLLWRNDDDLSC---TEEEYLEIVKYKTA 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114211   195 fYSFYLPVALAMHLAGvATPENLKCAQDILIILGKYFQVQDDYLDCYGDPTVTGKI-GTDILDNKCSWIINLALAKcTPE 273
Cdd:pfam00348 150 -YLFALAVKLGAILSG-ADDEVIEALKDYGLNLGLAFQIQDDYLDLFGDPEVLGKPaGTDITEGKCTWPVIHALER-TPE 226

                         250       260
                  ....*....|....*....|....*.
gi 19114211   274 QRVILDDNYGrKDSESEKRVKAVFEE 299
Cdd:pfam00348 227 QRKILLEIYG-KRPEDVEKVKEAYEL 251
Trans_IPPS_HT cd00685
Trans-Isoprenyl Diphosphate Synthases, head-to-tail; These trans-Isoprenyl Diphosphate ...
 36-270 8.46e-74

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: 228.97  E-value: 8.46e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114211  36 EWYKNSLFHNTL-GGKYNRGLSVIDSYEILLGHPLDeaaymKAAVLGWMVELLQSFFLIADDIMDASKTRRGQPCWYLMP 114
Cdd:cd00685   4 ELLREALRYLLLaGGKRLRPLLVLLAARALGGPELE-----AALRLAAAIELLHTASLVHDDVMDNSDLRRGKPTVHKVF 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114211 115 GVgNIAINDAFMVESAIYFLLKKHFRqeSCYVDLIELFHDVTFQTELGQQLDLLTAPEdsvdlSKFSLQKHSFIVIYKTA 194
Cdd:cd00685  79 GN-ATAILAGDYLLARAFELLARLGN--PYYPRALELFSEAILELVEGQLLDLLSEYD-----TDVTEEEYLRIIRLKTA 150

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19114211 195 FYSFYLPVALAMHLAgvATPENLKCAQDILIILGKYFQVQDDYLDCYGDPTVTGK-IGTDILDNKCSWIINLALAKC 270
Cdd:cd00685 151 ALFAAAPLLGALLAG--ADEEEAEALKRFGRNLGLAFQIQDDILDLFGDPETLGKpVGSDLREGKCTLPVLLALREL 225
IspA COG0142
Geranylgeranyl pyrophosphate synthase [Coenzyme transport and metabolism]; Geranylgeranyl ...
 1-327 1.24e-31

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: 121.10  E-value: 1.24e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114211   1 MSAVDKRAKFESALPVFVDEIVNYLKtiniPDDVTEWYKNSLFHNTLGGKYNRGLSVIDSYEiLLGHPLDEAayMKAAVL 80
Cdd:COG0142   1 MTLKDLLALLAEDLARVEAALEELLA----RSEPPLLAEAMRYLLLAGGKRLRPLLVLLAAR-ALGGDPEAA--LRAAAA 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114211  81 gwmVELLQSFFLIADDIMDASKTRRGQPC----WylmpgvGN-IAIN--DAFMVESAIYFLlkkHFRQESCYVDLIELFH 153
Cdd:COG0142  74 ---VELIHTASLVHDDVMDDDDLRRGKPTvharF------GEaTAILagDALLALAFELLA---ELGDPERRLRALRILA 141

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114211 154 DVTFQTELGQQLDLLTAPEDSVdlskfSLQKHSFIVIYKTAFYsFYLPVALAMHLAGvATPENLKCAQDILIILGKYFQV 233
Cdd:COG0142 142 RAARGMCEGQALDLEAEGRLDV-----TLEEYLRVIRLKTAAL-FAAALRLGAILAG-ADEEQVEALRRYGRNLGLAFQI 214

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114211 234 QDDYLDCYGDPTVTGK-IGTDILDNKCSWIINLALAKCTPEQRVILDDNYGRKDSESEK--RVKAVFEELNIRGEFENYE 310
Cdd:COG0142 215 RDDILDVTGDPEVLGKpAGSDLREGKPTLPLLLALERADPEERAELRELLGKPDLDEEDlaEVRALLRESGALEYARELA 294

                       330
                ....*....|....*..
gi 19114211 311 ESEVSEIKKLIDGVDES 327
Cdd:COG0142 295 RELAEEALAALAALPDS 311
 
Name Accession Description Interval E-value
polyprenyl_synt pfam00348
Polyprenyl synthetase;
36-299 2.05e-101

Polyprenyl synthetase;


Pssm-ID: 459773  Cd Length: 251  Bit Score: 299.04  E-value: 2.05e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114211    36 EWYKNSLFHNT-LGGKYNRGLSVIDSYEILLGHPLDEaaymKAAVLGWMVELLQSFFLIADDIMDASKTRRGQPCWYLMP 114
Cdd:pfam00348   2 KLLYEPLDYLVsAGGKRIRPLLVLLSAEALGGPEDLE----KAIVLAWAVELLHAASLVHDDIMDNSDLRRGQPTWHRIF 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114211   115 GVgNIAINDAFMVESAIYFLLKKHFRqescYVDLIELFHDVTFQTELGQQLDLLTAPEDSVDLskfSLQKHSFIVIYKTA 194
Cdd:pfam00348  78 GN-AIAINDGDYLYALAFQLLAKLFP----NPELLELFSEVTLQTAEGQGLDLLWRNDDDLSC---TEEEYLEIVKYKTA 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114211   195 fYSFYLPVALAMHLAGvATPENLKCAQDILIILGKYFQVQDDYLDCYGDPTVTGKI-GTDILDNKCSWIINLALAKcTPE 273
Cdd:pfam00348 150 -YLFALAVKLGAILSG-ADDEVIEALKDYGLNLGLAFQIQDDYLDLFGDPEVLGKPaGTDITEGKCTWPVIHALER-TPE 226

                         250       260
                  ....*....|....*....|....*.
gi 19114211   274 QRVILDDNYGrKDSESEKRVKAVFEE 299
Cdd:pfam00348 227 QRKILLEIYG-KRPEDVEKVKEAYEL 251
Trans_IPPS_HT cd00685
Trans-Isoprenyl Diphosphate Synthases, head-to-tail; These trans-Isoprenyl Diphosphate ...
 36-270 8.46e-74

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: 228.97  E-value: 8.46e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114211  36 EWYKNSLFHNTL-GGKYNRGLSVIDSYEILLGHPLDeaaymKAAVLGWMVELLQSFFLIADDIMDASKTRRGQPCWYLMP 114
Cdd:cd00685   4 ELLREALRYLLLaGGKRLRPLLVLLAARALGGPELE-----AALRLAAAIELLHTASLVHDDVMDNSDLRRGKPTVHKVF 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114211 115 GVgNIAINDAFMVESAIYFLLKKHFRqeSCYVDLIELFHDVTFQTELGQQLDLLTAPEdsvdlSKFSLQKHSFIVIYKTA 194
Cdd:cd00685  79 GN-ATAILAGDYLLARAFELLARLGN--PYYPRALELFSEAILELVEGQLLDLLSEYD-----TDVTEEEYLRIIRLKTA 150

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19114211 195 FYSFYLPVALAMHLAgvATPENLKCAQDILIILGKYFQVQDDYLDCYGDPTVTGK-IGTDILDNKCSWIINLALAKC 270
Cdd:cd00685 151 ALFAAAPLLGALLAG--ADEEEAEALKRFGRNLGLAFQIQDDILDLFGDPETLGKpVGSDLREGKCTLPVLLALREL 225
Trans_IPPS cd00867
Trans-Isoprenyl Diphosphate Synthases; Trans-Isoprenyl Diphosphate Synthases (Trans_IPPS) of ...
 52-268 1.88e-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: 175.99  E-value: 1.88e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114211  52 NRGLSVIDSYEILLGHPldeaayMKAAVLGWMVELLQSFFLIADDIMDASKTRRGQPCWYLMPGVGNIAINDAFMVESAI 131
Cdd:cd00867   1 SRPLLVLLLARALGGDL------EAALRLAAAVELLHAASLVHDDIVDDSDLRRGKPTAHLRRFGNALAILAGDYLLARA 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114211 132 YFLLKKHFrqescYVDLIELFHDVTFQTELGQQLDLLTAPEDSvdlskFSLQKHSFIVIYKTAFYSFYLPVALAMHLAgv 211
Cdd:cd00867  75 FQLLARLG-----YPRALELFAEALRELLEGQALDLEFERDTY-----ETLDEYLEYCRYKTAGLVGLLCLLGAGLSG-- 142

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 19114211 212 ATPENLKCAQDILIILGKYFQVQDDYLDCYGDPTVTGKIGTDILDNKCSWIINLALA 268
Cdd:cd00867 143 ADDEQAEALKDYGRALGLAFQLTDDLLDVFGDAEELGKVGSDLREGRITLPVILARE 199
Isoprenoid_Biosyn_C1 cd00385
Isoprenoid Biosynthesis enzymes, Class 1; Superfamily of trans-isoprenyl diphosphate synthases ...
 76-301 4.45e-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: 122.99  E-value: 4.45e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114211  76 KAAVLGWMVELLQSFFLIADDIMDASKTRRGQPCWYL--MPGVGNIAINDAFMVESAIYFLLKKHFRqescyVDLIELFH 153
Cdd:cd00385  11 EASRLRAAVEKLHAASLVHDDIVDDSGTRRGLPTAHLavAIDGLPEAILAGDLLLADAFEELAREGS-----PEALEILA 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114211 154 DVTFQTELGQQLDLLTAPEdsvdlSKFSLQKHSFIVIYKTAFYSFYLPVALAMHlaGVATPENLKCAQDILIILGKYFQV 233
Cdd:cd00385  86 EALLDLLEGQLLDLKWRRE-----YVPTLEEYLEYCRYKTAGLVGALCLLGAGL--SGGEAELLEALRKLGRALGLAFQL 158

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19114211 234 QDDYLDCYGDPtvtgkigtDILDNKCSWIINLALAKCTPEQRVILDDNYGRKD---SESEKRVKAVFEELN 301
Cdd:cd00385 159 TNDLLDYEGDA--------ERGEGKCTLPVLYALEYGVPAEDLLLVEKSGSLEealEELAKLAEEALKELN 221
IspA COG0142
Geranylgeranyl pyrophosphate synthase [Coenzyme transport and metabolism]; Geranylgeranyl ...
 1-327 1.24e-31

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: 121.10  E-value: 1.24e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114211   1 MSAVDKRAKFESALPVFVDEIVNYLKtiniPDDVTEWYKNSLFHNTLGGKYNRGLSVIDSYEiLLGHPLDEAayMKAAVL 80
Cdd:COG0142   1 MTLKDLLALLAEDLARVEAALEELLA----RSEPPLLAEAMRYLLLAGGKRLRPLLVLLAAR-ALGGDPEAA--LRAAAA 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114211  81 gwmVELLQSFFLIADDIMDASKTRRGQPC----WylmpgvGN-IAIN--DAFMVESAIYFLlkkHFRQESCYVDLIELFH 153
Cdd:COG0142  74 ---VELIHTASLVHDDVMDDDDLRRGKPTvharF------GEaTAILagDALLALAFELLA---ELGDPERRLRALRILA 141

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114211 154 DVTFQTELGQQLDLLTAPEDSVdlskfSLQKHSFIVIYKTAFYsFYLPVALAMHLAGvATPENLKCAQDILIILGKYFQV 233
Cdd:COG0142 142 RAARGMCEGQALDLEAEGRLDV-----TLEEYLRVIRLKTAAL-FAAALRLGAILAG-ADEEQVEALRRYGRNLGLAFQI 214

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114211 234 QDDYLDCYGDPTVTGK-IGTDILDNKCSWIINLALAKCTPEQRVILDDNYGRKDSESEK--RVKAVFEELNIRGEFENYE 310
Cdd:COG0142 215 RDDILDVTGDPEVLGKpAGSDLREGKPTLPLLLALERADPEERAELRELLGKPDLDEEDlaEVRALLRESGALEYARELA 294

                       330
                ....*....|....*..
gi 19114211 311 ESEVSEIKKLIDGVDES 327
Cdd:COG0142 295 RELAEEALAALAALPDS 311
 
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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