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Conserved domains on  [gi|1755167372|ref|YP_009702973|]
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BA71V-B318L [African swine fever virus]

Protein Classification

inner membrane-spanning protein YciB( domain architecture ID 1903478)

inner membrane-spanning protein YciB plays a role in cell envelope biogenesis, maintenance of cell envelope integrity and membrane homeostasis

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
IspA super family cl43038
Geranylgeranyl pyrophosphate synthase [Coenzyme transport and metabolism]; Geranylgeranyl ...
 54-261 3.29e-25

Geranylgeranyl pyrophosphate synthase [Coenzyme transport and metabolism]; Geranylgeranyl pyrophosphate synthase is part of the Pathway/BioSystem: Isoprenoid biosynthesis


The actual alignment was detected with superfamily member COG0142:

Pssm-ID: 439912 [Multi-domain]  Cd Length: 329  Bit Score: 102.99  E-value: 3.29e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755167372  54 EEFETILNNAIEDGDFkGQLTEPCSYAL-RGGKYIRPIILMEIVRACQLQhsfGAPIYPAeaALAVEYFHVASLIIDDMp 132
Cdd:COG0142    15 ARVEAALEELLARSEP-PLLAEAMRYLLlAGGKRLRPLLVLLAARALGGD---PEAALRA--AAAVELIHTASLVHDDV- 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755167372 133 sFDNDVKRRNKDTVWARFGVAKAQMSALALTMQGFQNICrqvdwikencpRFPDPNQLGALLCTFVSHSLNSAGsGQLVD 212
Cdd:COG0142    88 -MDDDDLRRGKPTVHARFGEATAILAGDALLALAFELLA-----------ELGDPERRLRALRILARAARGMCE-GQALD 154

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1755167372 213 ---------TPE--------KTIPFFKIAFIMGWVLGTGTIEDIGAIERAAHCFGNAFQLADDIKD 261
Cdd:COG0142   155 leaegrldvTLEeylrvirlKTAALFAAALRLGAILAGADEEQVEALRRYGRNLGLAFQIRDDILD 220
 
Name Accession Description Interval E-value
IspA COG0142
Geranylgeranyl pyrophosphate synthase [Coenzyme transport and metabolism]; Geranylgeranyl ...
 54-261 3.29e-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: 102.99  E-value: 3.29e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755167372  54 EEFETILNNAIEDGDFkGQLTEPCSYAL-RGGKYIRPIILMEIVRACQLQhsfGAPIYPAeaALAVEYFHVASLIIDDMp 132
Cdd:COG0142    15 ARVEAALEELLARSEP-PLLAEAMRYLLlAGGKRLRPLLVLLAARALGGD---PEAALRA--AAAVELIHTASLVHDDV- 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755167372 133 sFDNDVKRRNKDTVWARFGVAKAQMSALALTMQGFQNICrqvdwikencpRFPDPNQLGALLCTFVSHSLNSAGsGQLVD 212
Cdd:COG0142    88 -MDDDDLRRGKPTVHARFGEATAILAGDALLALAFELLA-----------ELGDPERRLRALRILARAARGMCE-GQALD 154

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1755167372 213 ---------TPE--------KTIPFFKIAFIMGWVLGTGTIEDIGAIERAAHCFGNAFQLADDIKD 261
Cdd:COG0142   155 leaegrldvTLEeylrvirlKTAALFAAALRLGAILAGADEEQVEALRRYGRNLGLAFQIRDDILD 220
Trans_IPPS_HT cd00685
Trans-Isoprenyl Diphosphate Synthases, head-to-tail; These trans-Isoprenyl Diphosphate ...
 73-276 1.82e-21

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: 91.46  E-value: 1.82e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755167372  73 LTEPCSYAL-RGGKYIRPIILMEIVRACQLQHSFGApiypAEAALAVEYFHVASLIIDDMpsFDNDVKRRNKDTVWARFG 151
Cdd:cd00685     6 LREALRYLLlAGGKRLRPLLVLLAARALGGPELEAA----LRLAAAIELLHTASLVHDDV--MDNSDLRRGKPTVHKVFG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755167372 152 VAKAQMSALALTMQGFQNICRqvdwikencprfpDPNQLGALLCTFVSHSLNSAGSGQLVD---------TPE------- 215
Cdd:cd00685    80 NATAILAGDYLLARAFELLAR-------------LGNPYYPRALELFSEAILELVEGQLLDllseydtdvTEEeylriir 146

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1755167372 216 -KTIPFFKIAFIMGWVLGTGTIEDIGAIERAAHCFGNAFQLADDIKDHDTDTgrnyaKIHGK 276
Cdd:cd00685   147 lKTAALFAAAPLLGALLAGADEEEAEALKRFGRNLGLAFQIQDDILDLFGDP-----ETLGK 203
polyprenyl_synt pfam00348
Polyprenyl synthetase;
73-261 2.37e-16

Polyprenyl synthetase;


Pssm-ID: 459773  Cd Length: 251  Bit Score: 77.16  E-value: 2.37e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755167372  73 LTEPCSYAL-RGGKYIRPIILMEIVRACQLQHSFGAPIypaEAALAVEYFHVASLIIDDMpsFDNDVKRRNKDTVWARFG 151
Cdd:pfam00348   4 LYEPLDYLVsAGGKRIRPLLVLLSAEALGGPEDLEKAI---VLAWAVELLHAASLVHDDI--MDNSDLRRGQPTWHRIFG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755167372 152 VAKAQMSALALTMQGFQnICRQVdwikencprFPDPNqlgaLLCTFvSHSLNSAGSGQLVD-----------TPE----- 215
Cdd:pfam00348  79 NAIAINDGDYLYALAFQ-LLAKL---------FPNPE----LLELF-SEVTLQTAEGQGLDllwrndddlscTEEeylei 143

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1755167372 216 ---KTIPFFKIAFIMGWVLGTGTIEDIGAIERAAHCFGNAFQLADDIKD 261
Cdd:pfam00348 144 vkyKTAYLFALAVKLGAILSGADDEVIEALKDYGLNLGLAFQIQDDYLD 192
PRK10581 PRK10581
(2E,6E)-farnesyl diphosphate synthase;
80-266 7.60e-08

(2E,6E)-farnesyl diphosphate synthase;


Pssm-ID: 182567  Cd Length: 299  Bit Score: 52.85  E-value: 7.60e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755167372  80 ALRGGKYIRPIILMEIVRAcqlqhsFGAPIYPAEA-ALAVEYFHVASLIIDDMPSFDNDVKRRNKDTVWARFGVAKAQMS 158
Cdd:PRK10581   40 ALLGGKRLRPFLVYATGQM------FGVSTNTLDApAAAVECIHAYSLIHDDLPAMDDDDLRRGLPTCHVKFGEANAILA 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755167372 159 ALALTMQGFQNICrqvdwiKENCPRFPDPNQLG-----------ALLCTfvSHSLNSAGSGQLVDTPE-------KTIPF 220
Cdd:PRK10581  114 GDALQTLAFSILS------DAPMPEVSDRDRISmiselasasgiAGMCG--GQALDLEAEGKQVPLDAlerihrhKTGAL 185

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1755167372 221 FKIAFIMGwVLGTGTI--EDIGAIERAAHCFGNAFQLADDIKDHDTDT 266
Cdd:PRK10581  186 IRAAVRLG-ALSAGDKgrRALPVLDRYAESIGLAFQVQDDILDVVGDT 232
 
Name Accession Description Interval E-value
IspA COG0142
Geranylgeranyl pyrophosphate synthase [Coenzyme transport and metabolism]; Geranylgeranyl ...
 54-261 3.29e-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: 102.99  E-value: 3.29e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755167372  54 EEFETILNNAIEDGDFkGQLTEPCSYAL-RGGKYIRPIILMEIVRACQLQhsfGAPIYPAeaALAVEYFHVASLIIDDMp 132
Cdd:COG0142    15 ARVEAALEELLARSEP-PLLAEAMRYLLlAGGKRLRPLLVLLAARALGGD---PEAALRA--AAAVELIHTASLVHDDV- 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755167372 133 sFDNDVKRRNKDTVWARFGVAKAQMSALALTMQGFQNICrqvdwikencpRFPDPNQLGALLCTFVSHSLNSAGsGQLVD 212
Cdd:COG0142    88 -MDDDDLRRGKPTVHARFGEATAILAGDALLALAFELLA-----------ELGDPERRLRALRILARAARGMCE-GQALD 154

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1755167372 213 ---------TPE--------KTIPFFKIAFIMGWVLGTGTIEDIGAIERAAHCFGNAFQLADDIKD 261
Cdd:COG0142   155 leaegrldvTLEeylrvirlKTAALFAAALRLGAILAGADEEQVEALRRYGRNLGLAFQIRDDILD 220
Trans_IPPS_HT cd00685
Trans-Isoprenyl Diphosphate Synthases, head-to-tail; These trans-Isoprenyl Diphosphate ...
 73-276 1.82e-21

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: 91.46  E-value: 1.82e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755167372  73 LTEPCSYAL-RGGKYIRPIILMEIVRACQLQHSFGApiypAEAALAVEYFHVASLIIDDMpsFDNDVKRRNKDTVWARFG 151
Cdd:cd00685     6 LREALRYLLlAGGKRLRPLLVLLAARALGGPELEAA----LRLAAAIELLHTASLVHDDV--MDNSDLRRGKPTVHKVFG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755167372 152 VAKAQMSALALTMQGFQNICRqvdwikencprfpDPNQLGALLCTFVSHSLNSAGSGQLVD---------TPE------- 215
Cdd:cd00685    80 NATAILAGDYLLARAFELLAR-------------LGNPYYPRALELFSEAILELVEGQLLDllseydtdvTEEeylriir 146

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1755167372 216 -KTIPFFKIAFIMGWVLGTGTIEDIGAIERAAHCFGNAFQLADDIKDHDTDTgrnyaKIHGK 276
Cdd:cd00685   147 lKTAALFAAAPLLGALLAGADEEEAEALKRFGRNLGLAFQIQDDILDLFGDP-----ETLGK 203
polyprenyl_synt pfam00348
Polyprenyl synthetase;
73-261 2.37e-16

Polyprenyl synthetase;


Pssm-ID: 459773  Cd Length: 251  Bit Score: 77.16  E-value: 2.37e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755167372  73 LTEPCSYAL-RGGKYIRPIILMEIVRACQLQHSFGAPIypaEAALAVEYFHVASLIIDDMpsFDNDVKRRNKDTVWARFG 151
Cdd:pfam00348   4 LYEPLDYLVsAGGKRIRPLLVLLSAEALGGPEDLEKAI---VLAWAVELLHAASLVHDDI--MDNSDLRRGQPTWHRIFG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755167372 152 VAKAQMSALALTMQGFQnICRQVdwikencprFPDPNqlgaLLCTFvSHSLNSAGSGQLVD-----------TPE----- 215
Cdd:pfam00348  79 NAIAINDGDYLYALAFQ-LLAKL---------FPNPE----LLELF-SEVTLQTAEGQGLDllwrndddlscTEEeylei 143

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1755167372 216 ---KTIPFFKIAFIMGWVLGTGTIEDIGAIERAAHCFGNAFQLADDIKD 261
Cdd:pfam00348 144 vkyKTAYLFALAVKLGAILSGADDEVIEALKDYGLNLGLAFQIQDDYLD 192
Trans_IPPS cd00867
Trans-Isoprenyl Diphosphate Synthases; Trans-Isoprenyl Diphosphate Synthases (Trans_IPPS) of ...
 87-261 1.73e-09

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: 56.97  E-value: 1.73e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755167372  87 IRPIILMEIVRACQlqhsfGAPIYPAEAALAVEYFHVASLIIDDMpsFDNDVKRRNKDTVWAR-FGVAKAQMSALALTMQ 165
Cdd:cd00867     1 SRPLLVLLLARALG-----GDLEAALRLAAAVELLHAASLVHDDI--VDDSDLRRGKPTAHLRrFGNALAILAGDYLLAR 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755167372 166 GFQNICRQvdwikENCPRFPDPNQLGALLCTfvshslnsagsGQLVD---------TPE--------KTIPFFKIAFIMG 228
Cdd:cd00867    74 AFQLLARL-----GYPRALELFAEALRELLE-----------GQALDleferdtyeTLDeyleycryKTAGLVGLLCLLG 137

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1755167372 229 WVLGTGTIEDIGAIERAAHCFGNAFQLADDIKD 261
Cdd:cd00867   138 AGLSGADDEQAEALKDYGRALGLAFQLTDDLLD 170
Isoprenoid_Biosyn_C1 cd00385
Isoprenoid Biosynthesis enzymes, Class 1; Superfamily of trans-isoprenyl diphosphate synthases ...
 112-274 2.39e-09

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: 56.73  E-value: 2.39e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755167372 112 AEAALAVEYFHVASLIIDDMpsFDNDVKRRNKDTVWARFGVAKAQMSALAltmqGFQNICRQVDWIKENCPRFPDPNQLG 191
Cdd:cd00385    13 SRLRAAVEKLHAASLVHDDI--VDDSGTRRGLPTAHLAVAIDGLPEAILA----GDLLLADAFEELAREGSPEALEILAE 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755167372 192 ALLCTFVSHSLNSAGSGQLVDTPE--------KTIPFFKIAFIMGWVLGTGTIEDIGAIERAAHCFGNAFQLADDIKDHD 263
Cdd:cd00385    87 ALLDLLEGQLLDLKWRREYVPTLEeyleycryKTAGLVGALCLLGAGLSGGEAELLEALRKLGRALGLAFQLTNDLLDYE 166

                         170
                  ....*....|.
gi 1755167372 264 TDTGRNYAKIH 274
Cdd:cd00385   167 GDAERGEGKCT 177
PRK10581 PRK10581
(2E,6E)-farnesyl diphosphate synthase;
80-266 7.60e-08

(2E,6E)-farnesyl diphosphate synthase;


Pssm-ID: 182567  Cd Length: 299  Bit Score: 52.85  E-value: 7.60e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755167372  80 ALRGGKYIRPIILMEIVRAcqlqhsFGAPIYPAEA-ALAVEYFHVASLIIDDMPSFDNDVKRRNKDTVWARFGVAKAQMS 158
Cdd:PRK10581   40 ALLGGKRLRPFLVYATGQM------FGVSTNTLDApAAAVECIHAYSLIHDDLPAMDDDDLRRGLPTCHVKFGEANAILA 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755167372 159 ALALTMQGFQNICrqvdwiKENCPRFPDPNQLG-----------ALLCTfvSHSLNSAGSGQLVDTPE-------KTIPF 220
Cdd:PRK10581  114 GDALQTLAFSILS------DAPMPEVSDRDRISmiselasasgiAGMCG--GQALDLEAEGKQVPLDAlerihrhKTGAL 185

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1755167372 221 FKIAFIMGwVLGTGTI--EDIGAIERAAHCFGNAFQLADDIKDHDTDT 266
Cdd:PRK10581  186 IRAAVRLG-ALSAGDKgrRALPVLDRYAESIGLAFQVQDDILDVVGDT 232
PRK10888 PRK10888
octaprenyl diphosphate synthase; Provisional
 83-269 5.83e-07

octaprenyl diphosphate synthase; Provisional


Pssm-ID: 182813  Cd Length: 323  Bit Score: 50.23  E-value: 5.83e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755167372  83 GGKYIRPIILMEIVRACQLQHSFGAPIypaeAALaVEYFHVASLIIDDMpsFDNDVKRRNKDTVWARFGVAKAQMSALAL 162
Cdd:PRK10888   43 GGKRIRPMIAVLAARAVGYQGNAHVTI----AAL-IEFIHTATLLHDDV--VDESDMRRGKATANAAFGNAASVLVGDFI 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755167372 163 TMQGFQNIcrqvdwikencprfpdpNQLGAL-LCTFVSHSLNSAGSGQLV--------DTPE---------KTIPFFKIA 224
Cdd:PRK10888  116 YTRAFQMM-----------------TSLGSLkVLEVMSEAVNVIAEGEVLqlmnvndpDITEenymrviysKTARLFEAA 178

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1755167372 225 FIMGWVLGTGTIEDIGAIERAAHCFGNAFQLADDIKDHDTDT---GRN 269
Cdd:PRK10888  179 AQCSGILAGCTPEQEKGLQDYGRYLGTAFQLIDDLLDYSADGetlGKN 226
preA CHL00151
prenyl transferase; Reviewed
 83-167 3.83e-05

prenyl transferase; Reviewed


Pssm-ID: 164542  Cd Length: 323  Bit Score: 44.78  E-value: 3.83e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755167372  83 GGKYIRPIILMEIVRAC-QLQHsfgapIYPAEAALA--VEYFHVASLIIDDMpsFDNDVKRRNKDTVWARFGVAKAQMSA 159
Cdd:CHL00151   44 GGKRIRPAIVLLVAKATgGNME-----IKTSQQRLAeiTEIIHTASLVHDDV--IDECSIRRGIPTVHKIFGTKIAVLAG 116


                  ....*...
gi 1755167372 160 LALTMQGF 167
Cdd:CHL00151  117 DFLFAQSS 124
 
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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