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Conserved domains on  [gi|1002235111|ref|XP_015621771|]
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farnesyl pyrophosphate synthase isoform X3 [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

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
polyprenyl_synt pfam00348
Polyprenyl synthetase;
3-215 2.75e-74

Polyprenyl synthetase;


:

Pssm-ID: 459773  Cd Length: 251  Bit Score: 226.62  E-value: 2.75e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235111   3 LLQAYFLVLDDIMDNSQTRRGKPCWFRlpKVGL-IAINDGLVLRSQISRIFRRYFRgksyYVDLLDLFNEVEIQTTSGQL 81
Cdd:pfam00348  49 LLHAASLVHDDIMDNSDLRRGQPTWHR--IFGNaIAINDGDYLYALAFQLLAKLFP----NPELLELFSEVTLQTAEGQG 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235111  82 LDqiTTNEGRKDLNKyNVHVYRRIVEYKTAYySFYLPVACALLLFDESLDNYAQVKHILVEMGVYFQSQDDYLDCFGEPE 161
Cdd:pfam00348 123 LD--LLWRNDDDLSC-TEEEYLEIVKYKTAY-LFALAVKLGAILSGADDEVIEALKDYGLNLGLAFQIQDDYLDLFGDPE 198

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1002235111 162 IIGKI-GSDIEDFKCSWLFVQALERaDEKQKGVLFENYGKsDPACVAKVKDLYNE 215
Cdd:pfam00348 199 VLGKPaGTDITEGKCTWPVIHALER-TPEQRKILLEIYGK-RPEDVEKVKEAYEL 251
 
Name Accession Description Interval E-value
polyprenyl_synt pfam00348
Polyprenyl synthetase;
3-215 2.75e-74

Polyprenyl synthetase;


Pssm-ID: 459773  Cd Length: 251  Bit Score: 226.62  E-value: 2.75e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235111   3 LLQAYFLVLDDIMDNSQTRRGKPCWFRlpKVGL-IAINDGLVLRSQISRIFRRYFRgksyYVDLLDLFNEVEIQTTSGQL 81
Cdd:pfam00348  49 LLHAASLVHDDIMDNSDLRRGQPTWHR--IFGNaIAINDGDYLYALAFQLLAKLFP----NPELLELFSEVTLQTAEGQG 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235111  82 LDqiTTNEGRKDLNKyNVHVYRRIVEYKTAYySFYLPVACALLLFDESLDNYAQVKHILVEMGVYFQSQDDYLDCFGEPE 161
Cdd:pfam00348 123 LD--LLWRNDDDLSC-TEEEYLEIVKYKTAY-LFALAVKLGAILSGADDEVIEALKDYGLNLGLAFQIQDDYLDLFGDPE 198

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1002235111 162 IIGKI-GSDIEDFKCSWLFVQALERaDEKQKGVLFENYGKsDPACVAKVKDLYNE 215
Cdd:pfam00348 199 VLGKPaGTDITEGKCTWPVIHALER-TPEQRKILLEIYGK-RPEDVEKVKEAYEL 251
Trans_IPPS_HT cd00685
Trans-Isoprenyl Diphosphate Synthases, head-to-tail; These trans-Isoprenyl Diphosphate ...
 3-259 5.53e-58

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: 185.45  E-value: 5.53e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235111   3 LLQAYFLVLDDIMDNSQTRRGKPCWFRLPKVGlIAINDGLVLRSQISRIFRRYFRGksYYVDLLDLFNEVEIQTTSGQLL 82
Cdd:cd00685    50 LLHTASLVHDDVMDNSDLRRGKPTVHKVFGNA-TAILAGDYLLARAFELLARLGNP--YYPRALELFSEAILELVEGQLL 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235111  83 DqiTTNEGRKDlnkYNVHVYRRIVEYKTAYYSFYLPVACALLLfDESLDNYAQVKHILVEMGVYFQSQDDYLDCFGEPEI 162
Cdd:cd00685   127 D--LLSEYDTD---VTEEEYLRIIRLKTAALFAAAPLLGALLA-GADEEEAEALKRFGRNLGLAFQIQDDILDLFGDPET 200

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235111 163 IGK-IGSDIEDFKCSWLFVQALEradekqkgvlfenygksdpacvakvkdlynelhlqRVFSEYERESYEklisAIEAQP 241
Cdd:cd00685   201 LGKpVGSDLREGKCTLPVLLALR-----------------------------------ELAREYEEKALE----ALKALP 241

                         250
                  ....*....|....*...
gi 1002235111 242 NEAVRAVLKSFLHKIYKR 259
Cdd:cd00685   242 ESPAREALRALADFILER 259
IspA COG0142
Geranylgeranyl pyrophosphate synthase [Coenzyme transport and metabolism]; Geranylgeranyl ...
 3-261 3.91e-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: 109.54  E-value: 3.91e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235111   3 LLQAYFLVLDDIMDNSQTRRGKP-CWFR-------LpkVG--LIAINDGLVLRSQISRIFRRyfrgksyyvdLLDLFNEV 72
Cdd:COG0142    76 LIHTASLVHDDVMDDDDLRRGKPtVHARfgeataiL--AGdaLLALAFELLAELGDPERRLR----------ALRILARA 143

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235111  73 EIQTTSGQLLDqiTTNEGRKDLNkynVHVYRRIVEYKTAYYsFYLPVACALLLFD------ESLDNYAqvKHIlvemGVY 146
Cdd:COG0142   144 ARGMCEGQALD--LEAEGRLDVT---LEEYLRVIRLKTAAL-FAAALRLGAILAGadeeqvEALRRYG--RNL----GLA 211

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235111 147 FQSQDDYLDCFGEPEIIGK-IGSDIEDFKCSWLFVQALERADEKQKGVLFENYGK--SDPACVAKVKDLYNELHLQRVFS 223
Cdd:COG0142   212 FQIRDDILDVTGDPEVLGKpAGSDLREGKPTLPLLLALERADPEERAELRELLGKpdLDEEDLAEVRALLRESGALEYAR 291

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1002235111 224 EYERESYEKLISAIEAQPNEAVRAVLKSFLHKIYKRSK 261
Cdd:COG0142   292 ELARELAEEALAALAALPDSEAREALRALADYVVERDR 329
 
Name Accession Description Interval E-value
polyprenyl_synt pfam00348
Polyprenyl synthetase;
3-215 2.75e-74

Polyprenyl synthetase;


Pssm-ID: 459773  Cd Length: 251  Bit Score: 226.62  E-value: 2.75e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235111   3 LLQAYFLVLDDIMDNSQTRRGKPCWFRlpKVGL-IAINDGLVLRSQISRIFRRYFRgksyYVDLLDLFNEVEIQTTSGQL 81
Cdd:pfam00348  49 LLHAASLVHDDIMDNSDLRRGQPTWHR--IFGNaIAINDGDYLYALAFQLLAKLFP----NPELLELFSEVTLQTAEGQG 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235111  82 LDqiTTNEGRKDLNKyNVHVYRRIVEYKTAYySFYLPVACALLLFDESLDNYAQVKHILVEMGVYFQSQDDYLDCFGEPE 161
Cdd:pfam00348 123 LD--LLWRNDDDLSC-TEEEYLEIVKYKTAY-LFALAVKLGAILSGADDEVIEALKDYGLNLGLAFQIQDDYLDLFGDPE 198

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1002235111 162 IIGKI-GSDIEDFKCSWLFVQALERaDEKQKGVLFENYGKsDPACVAKVKDLYNE 215
Cdd:pfam00348 199 VLGKPaGTDITEGKCTWPVIHALER-TPEQRKILLEIYGK-RPEDVEKVKEAYEL 251
Trans_IPPS_HT cd00685
Trans-Isoprenyl Diphosphate Synthases, head-to-tail; These trans-Isoprenyl Diphosphate ...
 3-259 5.53e-58

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: 185.45  E-value: 5.53e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235111   3 LLQAYFLVLDDIMDNSQTRRGKPCWFRLPKVGlIAINDGLVLRSQISRIFRRYFRGksYYVDLLDLFNEVEIQTTSGQLL 82
Cdd:cd00685    50 LLHTASLVHDDVMDNSDLRRGKPTVHKVFGNA-TAILAGDYLLARAFELLARLGNP--YYPRALELFSEAILELVEGQLL 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235111  83 DqiTTNEGRKDlnkYNVHVYRRIVEYKTAYYSFYLPVACALLLfDESLDNYAQVKHILVEMGVYFQSQDDYLDCFGEPEI 162
Cdd:cd00685   127 D--LLSEYDTD---VTEEEYLRIIRLKTAALFAAAPLLGALLA-GADEEEAEALKRFGRNLGLAFQIQDDILDLFGDPET 200

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235111 163 IGK-IGSDIEDFKCSWLFVQALEradekqkgvlfenygksdpacvakvkdlynelhlqRVFSEYERESYEklisAIEAQP 241
Cdd:cd00685   201 LGKpVGSDLREGKCTLPVLLALR-----------------------------------ELAREYEEKALE----ALKALP 241

                         250
                  ....*....|....*...
gi 1002235111 242 NEAVRAVLKSFLHKIYKR 259
Cdd:cd00685   242 ESPAREALRALADFILER 259
Trans_IPPS cd00867
Trans-Isoprenyl Diphosphate Synthases; Trans-Isoprenyl Diphosphate Synthases (Trans_IPPS) of ...
 3-259 3.33e-44

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: 149.03  E-value: 3.33e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235111   3 LLQAYFLVLDDIMDNSQTRRGKPCWFRLPKVGLIAINDGLVLRSQISRIFRRYFrgksyYVDLLDLFNEVEIQTTSGQLL 82
Cdd:cd00867    29 LLHAASLVHDDIVDDSDLRRGKPTAHLRRFGNALAILAGDYLLARAFQLLARLG-----YPRALELFAEALRELLEGQAL 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235111  83 DQITTNEGRKDLNKYnvhvyRRIVEYKTAYYSFYLPVACALLLfDESLDNYAQVKHILVEMGVYFQSQDDYLDCFGEPEI 162
Cdd:cd00867   104 DLEFERDTYETLDEY-----LEYCRYKTAGLVGLLCLLGAGLS-GADDEQAEALKDYGRALGLAFQLTDDLLDVFGDAEE 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235111 163 IGKIGSDIEDFKCSWLFVQALERADekqkgvlfenygksdpacvakvkdlynelhlqrvfsEYERESYEKLISAIEAQPn 242
Cdd:cd00867   178 LGKVGSDLREGRITLPVILARERAA------------------------------------EYAEEAYAALEALPPSLP- 220

                         250
                  ....*....|....*..
gi 1002235111 243 eAVRAVLKSFLHKIYKR 259
Cdd:cd00867   221 -RARRALIALADFLYRR 236
Isoprenoid_Biosyn_C1 cd00385
Isoprenoid Biosynthesis enzymes, Class 1; Superfamily of trans-isoprenyl diphosphate synthases ...
 3-258 2.89e-28

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: 107.97  E-value: 2.89e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235111   3 LLQAYFLVLDDIMDNSQTRRGKPCWFRLPKVGL--IAINDGLVLRSQISRIFRRYFRgksyyVDLLDLFNEVEIQTTSGQ 80
Cdd:cd00385    21 KLHAASLVHDDIVDDSGTRRGLPTAHLAVAIDGlpEAILAGDLLLADAFEELAREGS-----PEALEILAEALLDLLEGQ 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235111  81 LLDQITTNEGRKDLNKYNvhvyrRIVEYKTAYYSFYLPVACALLLfDESLDNYAQVKHILVEMGVYFQSQDDYLDCFGEP 160
Cdd:cd00385    96 LLDLKWRREYVPTLEEYL-----EYCRYKTAGLVGALCLLGAGLS-GGEAELLEALRKLGRALGLAFQLTNDLLDYEGDA 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235111 161 EIIgkigsdieDFKCSWLFVQALERADEKQKgvlfenygksdpacVAKVKDLYNELHLQRVFSEYERESYEKLISAIEAQ 240
Cdd:cd00385   170 ERG--------EGKCTLPVLYALEYGVPAED--------------LLLVEKSGSLEEALEELAKLAEEALKELNELILSL 227

                         250
                  ....*....|....*...
gi 1002235111 241 PneAVRAVLKSFLHKIYK 258
Cdd:cd00385   228 P--DVPRALLALALNLYR 243
IspA COG0142
Geranylgeranyl pyrophosphate synthase [Coenzyme transport and metabolism]; Geranylgeranyl ...
 3-261 3.91e-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: 109.54  E-value: 3.91e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235111   3 LLQAYFLVLDDIMDNSQTRRGKP-CWFR-------LpkVG--LIAINDGLVLRSQISRIFRRyfrgksyyvdLLDLFNEV 72
Cdd:COG0142    76 LIHTASLVHDDVMDDDDLRRGKPtVHARfgeataiL--AGdaLLALAFELLAELGDPERRLR----------ALRILARA 143

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235111  73 EIQTTSGQLLDqiTTNEGRKDLNkynVHVYRRIVEYKTAYYsFYLPVACALLLFD------ESLDNYAqvKHIlvemGVY 146
Cdd:COG0142   144 ARGMCEGQALD--LEAEGRLDVT---LEEYLRVIRLKTAAL-FAAALRLGAILAGadeeqvEALRRYG--RNL----GLA 211

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235111 147 FQSQDDYLDCFGEPEIIGK-IGSDIEDFKCSWLFVQALERADEKQKGVLFENYGK--SDPACVAKVKDLYNELHLQRVFS 223
Cdd:COG0142   212 FQIRDDILDVTGDPEVLGKpAGSDLREGKPTLPLLLALERADPEERAELRELLGKpdLDEEDLAEVRALLRESGALEYAR 291

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1002235111 224 EYERESYEKLISAIEAQPNEAVRAVLKSFLHKIYKRSK 261
Cdd:COG0142   292 ELARELAEEALAALAALPDSEAREALRALADYVVERDR 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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