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Conserved domains on  [gi|698401824|ref|XP_009706353|]
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PREDICTED: LOW QUALITY PROTEIN: farnesyl pyrophosphate synthase [Cariama cristata]

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;
1-199 1.06e-68

Polyprenyl synthetase;


:

Pssm-ID: 459773  Cd Length: 251  Bit Score: 211.98  E-value: 1.06e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698401824    1 MDASLTRRGQLCWYKKEGIGLdAINDAFLLASSVY********pyYLHLLELFLQTAYQTELGQMLDLITApvSKVDLNR 80
Cdd:pfam00348  61 MDNSDLRRGQPTWHRIFGNAI-AINDGDYLYALAFQLLAKLFP--NPELLELFSEVTLQTAEGQGLDLLWR--NDDDLSC 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698401824   81 fSEQRYKAIVKYKTAfYSFYLPVAAAMYMTGFDSkEEHDNAKAILLEMGEFFQIQDDYLDCYGDPELTGK-VGTDIQDNK 159
Cdd:pfam00348 136 -TEEEYLEIVKYKTA-YLFALAVKLGAILSGADD-EVIEALKDYGLNLGLAFQIQDDYLDLFGDPEVLGKpAGTDITEGK 212

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 698401824  160 CSWLVVECLRRvTPNQRQILEENYGcKEPEKVIKVKELYD 199
Cdd:pfam00348 213 CTWPVIHALER-TPEQRKILLEIYG-KRPEDVEKVKEAYE 250
 
Name Accession Description Interval E-value
polyprenyl_synt pfam00348
Polyprenyl synthetase;
1-199 1.06e-68

Polyprenyl synthetase;


Pssm-ID: 459773  Cd Length: 251  Bit Score: 211.98  E-value: 1.06e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698401824    1 MDASLTRRGQLCWYKKEGIGLdAINDAFLLASSVY********pyYLHLLELFLQTAYQTELGQMLDLITApvSKVDLNR 80
Cdd:pfam00348  61 MDNSDLRRGQPTWHRIFGNAI-AINDGDYLYALAFQLLAKLFP--NPELLELFSEVTLQTAEGQGLDLLWR--NDDDLSC 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698401824   81 fSEQRYKAIVKYKTAfYSFYLPVAAAMYMTGFDSkEEHDNAKAILLEMGEFFQIQDDYLDCYGDPELTGK-VGTDIQDNK 159
Cdd:pfam00348 136 -TEEEYLEIVKYKTA-YLFALAVKLGAILSGADD-EVIEALKDYGLNLGLAFQIQDDYLDLFGDPEVLGKpAGTDITEGK 212

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 698401824  160 CSWLVVECLRRvTPNQRQILEENYGcKEPEKVIKVKELYD 199
Cdd:pfam00348 213 CTWPVIHALER-TPEQRKILLEIYG-KRPEDVEKVKEAYE 250
Trans_IPPS_HT cd00685
Trans-Isoprenyl Diphosphate Synthases, head-to-tail; These trans-Isoprenyl Diphosphate ...
 1-244 2.29e-54

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: 175.43  E-value: 2.29e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698401824   1 MDASLTRRGQLCWYKKEGIGLdAINDAFLLASSVY********PYYLHLLELFLQTAYQTELGQMLDLITApvskvDLNR 80
Cdd:cd00685   62 MDNSDLRRGKPTVHKVFGNAT-AILAGDYLLARAFELLARLGNPYYPRALELFSEAILELVEGQLLDLLSE-----YDTD 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698401824  81 FSEQRYKAIVKYKTAFYSFYLPVAAAMYMTGfdSKEEHDNAKAILLEMGEFFQIQDDYLDCYGDPELTGK-VGTDIQDNK 159
Cdd:cd00685  136 VTEEEYLRIIRLKTAALFAAAPLLGALLAGA--DEEEAEALKRFGRNLGLAFQIQDDILDLFGDPETLGKpVGSDLREGK 213

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698401824 160 CSWLVVeclrrvtpnqrqileenygckepekvikvkelydsLGMRAAFQEYEESSYQRLQELIQkhanRLPKEIFLGLAR 239
Cdd:cd00685  214 CTLPVL-----------------------------------LALRELAREYEEKALEALKALPE----SPAREALRALAD 254


                 ....*
gi 698401824 240 KIYKR 244
Cdd:cd00685  255 FILER 259
IspA COG0142
Geranylgeranyl pyrophosphate synthase [Coenzyme transport and metabolism]; Geranylgeranyl ...
 1-246 1.03e-25

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: 102.61  E-value: 1.03e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698401824   1 MDASLTRRGQLCWYKKEGIGLdAIN--DaFLLASSVY********PYYLHLLELFLQTAYQTELGQMLDLitAPVSKVDL 78
Cdd:COG0142   88 MDDDDLRRGKPTVHARFGEAT-AILagD-ALLALAFELLAELGDPERRLRALRILARAARGMCEGQALDL--EAEGRLDV 163

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698401824  79 nrfSEQRYKAIVKYKTAFYsfylpVAAAMYM---TGFDSKEEHDNAKAILLEMGEFFQIQDDYLDCYGDPELTGK-VGTD 154
Cdd:COG0142  164 ---TLEEYLRVIRLKTAAL-----FAAALRLgaiLAGADEEQVEALRRYGRNLGLAFQIRDDILDVTGDPEVLGKpAGSD 235

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698401824 155 IQDNKCSWLVVECLRRVTPNQRQILEENYGCKE--PEKVIKVKELYDSLGMRAAfqeyeesSYQRLQELIQK---HANRL 229
Cdd:COG0142  236 LREGKPTLPLLLALERADPEERAELRELLGKPDldEEDLAEVRALLRESGALEY-------ARELARELAEEalaALAAL 308

                        250       260
                 ....*....|....*....|.
gi 698401824 230 P----KEIFLGLARKIYKRQK 246
Cdd:COG0142  309 PdseaREALRALADYVVERDR 329
 
Name Accession Description Interval E-value
polyprenyl_synt pfam00348
Polyprenyl synthetase;
1-199 1.06e-68

Polyprenyl synthetase;


Pssm-ID: 459773  Cd Length: 251  Bit Score: 211.98  E-value: 1.06e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698401824    1 MDASLTRRGQLCWYKKEGIGLdAINDAFLLASSVY********pyYLHLLELFLQTAYQTELGQMLDLITApvSKVDLNR 80
Cdd:pfam00348  61 MDNSDLRRGQPTWHRIFGNAI-AINDGDYLYALAFQLLAKLFP--NPELLELFSEVTLQTAEGQGLDLLWR--NDDDLSC 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698401824   81 fSEQRYKAIVKYKTAfYSFYLPVAAAMYMTGFDSkEEHDNAKAILLEMGEFFQIQDDYLDCYGDPELTGK-VGTDIQDNK 159
Cdd:pfam00348 136 -TEEEYLEIVKYKTA-YLFALAVKLGAILSGADD-EVIEALKDYGLNLGLAFQIQDDYLDLFGDPEVLGKpAGTDITEGK 212

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 698401824  160 CSWLVVECLRRvTPNQRQILEENYGcKEPEKVIKVKELYD 199
Cdd:pfam00348 213 CTWPVIHALER-TPEQRKILLEIYG-KRPEDVEKVKEAYE 250
Trans_IPPS_HT cd00685
Trans-Isoprenyl Diphosphate Synthases, head-to-tail; These trans-Isoprenyl Diphosphate ...
 1-244 2.29e-54

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: 175.43  E-value: 2.29e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698401824   1 MDASLTRRGQLCWYKKEGIGLdAINDAFLLASSVY********PYYLHLLELFLQTAYQTELGQMLDLITApvskvDLNR 80
Cdd:cd00685   62 MDNSDLRRGKPTVHKVFGNAT-AILAGDYLLARAFELLARLGNPYYPRALELFSEAILELVEGQLLDLLSE-----YDTD 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698401824  81 FSEQRYKAIVKYKTAFYSFYLPVAAAMYMTGfdSKEEHDNAKAILLEMGEFFQIQDDYLDCYGDPELTGK-VGTDIQDNK 159
Cdd:cd00685  136 VTEEEYLRIIRLKTAALFAAAPLLGALLAGA--DEEEAEALKRFGRNLGLAFQIQDDILDLFGDPETLGKpVGSDLREGK 213

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698401824 160 CSWLVVeclrrvtpnqrqileenygckepekvikvkelydsLGMRAAFQEYEESSYQRLQELIQkhanRLPKEIFLGLAR 239
Cdd:cd00685  214 CTLPVL-----------------------------------LALRELAREYEEKALEALKALPE----SPAREALRALAD 254


                 ....*
gi 698401824 240 KIYKR 244
Cdd:cd00685  255 FILER 259
Trans_IPPS cd00867
Trans-Isoprenyl Diphosphate Synthases; Trans-Isoprenyl Diphosphate Synthases (Trans_IPPS) of ...
 1-244 1.21e-40

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: 139.40  E-value: 1.21e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698401824   1 MDASLTRRGQLCWYKKEGIGLDAINDAFLLASSVY********pyYLHLLELFLQTAYQTELGQMLDLITApvskvDLNR 80
Cdd:cd00867   41 VDDSDLRRGKPTAHLRRFGNALAILAGDYLLARAFQLLARLG---YPRALELFAEALRELLEGQALDLEFE-----RDTY 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698401824  81 FSEQRYKAIVKYKTAFYSFYLPVAAAMYMTGfdSKEEHDNAKAILLEMGEFFQIQDDYLDCYGDPELTGKVGTDIQDNKC 160
Cdd:cd00867  113 ETLDEYLEYCRYKTAGLVGLLCLLGAGLSGA--DDEQAEALKDYGRALGLAFQLTDDLLDVFGDAEELGKVGSDLREGRI 190

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698401824 161 SWLVVEclrrvtpnqrqileenygckepekvikvkelydslgMRAAFQEYEESSYQRLQELIQkhANRLPKEIFLGLARK 240
Cdd:cd00867  191 TLPVIL------------------------------------ARERAAEYAEEAYAALEALPP--SLPRARRALIALADF 232


                 ....
gi 698401824 241 IYKR 244
Cdd:cd00867  233 LYRR 236
IspA COG0142
Geranylgeranyl pyrophosphate synthase [Coenzyme transport and metabolism]; Geranylgeranyl ...
 1-246 1.03e-25

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: 102.61  E-value: 1.03e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698401824   1 MDASLTRRGQLCWYKKEGIGLdAIN--DaFLLASSVY********PYYLHLLELFLQTAYQTELGQMLDLitAPVSKVDL 78
Cdd:COG0142   88 MDDDDLRRGKPTVHARFGEAT-AILagD-ALLALAFELLAELGDPERRLRALRILARAARGMCEGQALDL--EAEGRLDV 163

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698401824  79 nrfSEQRYKAIVKYKTAFYsfylpVAAAMYM---TGFDSKEEHDNAKAILLEMGEFFQIQDDYLDCYGDPELTGK-VGTD 154
Cdd:COG0142  164 ---TLEEYLRVIRLKTAAL-----FAAALRLgaiLAGADEEQVEALRRYGRNLGLAFQIRDDILDVTGDPEVLGKpAGSD 235

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698401824 155 IQDNKCSWLVVECLRRVTPNQRQILEENYGCKE--PEKVIKVKELYDSLGMRAAfqeyeesSYQRLQELIQK---HANRL 229
Cdd:COG0142  236 LREGKPTLPLLLALERADPEERAELRELLGKPDldEEDLAEVRALLRESGALEY-------ARELARELAEEalaALAAL 308

                        250       260
                 ....*....|....*....|.
gi 698401824 230 P----KEIFLGLARKIYKRQK 246
Cdd:COG0142  309 PdseaREALRALADYVVERDR 329
Isoprenoid_Biosyn_C1 cd00385
Isoprenoid Biosynthesis enzymes, Class 1; Superfamily of trans-isoprenyl diphosphate synthases ...
 1-243 1.61e-24

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: 97.57  E-value: 1.61e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698401824   1 MDASLTRRGQLCWYKKEGIGL--DAINDAFLLASSVY********PYYLHLlelFLQTAYQTELGQMLDLITApvskvDL 78
Cdd:cd00385   33 VDDSGTRRGLPTAHLAVAIDGlpEAILAGDLLLADAFEELAREGSPEALEI---LAEALLDLLEGQLLDLKWR-----RE 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698401824  79 NRFSEQRYKAIVKYKTAFYSFYLPVAAAMYMTGfdSKEEHDNAKAILLEMGEFFQIQDDYLDCYGDPELTgkvgtdiqDN 158
Cdd:cd00385  105 YVPTLEEYLEYCRYKTAGLVGALCLLGAGLSGG--EAELLEALRKLGRALGLAFQLTNDLLDYEGDAERG--------EG 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698401824 159 KCSWLVVECLRRVTPNQRQILEENYGCKEpekvikvkelydslGMRAAFQEYEESSYQRLQELIQKHANRlpKEIFLGLA 238
Cdd:cd00385  175 KCTLPVLYALEYGVPAEDLLLVEKSGSLE--------------EALEELAKLAEEALKELNELILSLPDV--PRALLALA 238


                 ....*
gi 698401824 239 RKIYK 243
Cdd:cd00385  239 LNLYR 243
 
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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