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Conserved domains on  [gi|767943180|ref|XP_011534263|]
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all trans-polyprenyl-diphosphate synthase PDSS2 isoform X11 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PLN02890 super family cl27345
geranyl diphosphate synthase
72-243 3.87e-21

geranyl diphosphate synthase


The actual alignment was detected with superfamily member PLN02890:

Pssm-ID: 178478  Cd Length: 422  Bit Score: 92.68  E-value: 3.87e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943180  72 LLSDELSNIAMQVRKLVGTQHPLLTTA------RGLvhdswNSLQLRGLVVLLISKAAG-PSSVNTSCQNYDMV-SGIYS 143
Cdd:PLN02890  87 LVADELSLLANKLRSMVVAEVPKLASAaeyffkVGV-----EGKRFRPTVLLLMATALNvPLPESTEGGVLDIVaSELRT 161
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943180 144 CQRSLAEITELIHIALLVHRGIVNLNELQSSDGPLkDMQFGNKIAILSGDFLLANACNGLALLQNTKVVELLASALMDLV 223
Cdd:PLN02890 162 RQQNIAEITEMIHVASLLHDDVLDDADTRRGVGSL-NVVMGNKLSVLAGDFLLSRACVALAALKNTEVVSLLATAVEHLV 240
                        170       180
                 ....*....|....*....|
gi 767943180 224 QGVYHENSTSKAQEKGrLDY 243
Cdd:PLN02890 241 TGETMQITSSREQRRS-MDY 259
 
Name Accession Description Interval E-value
PLN02890 PLN02890
geranyl diphosphate synthase
72-243 3.87e-21

geranyl diphosphate synthase


Pssm-ID: 178478  Cd Length: 422  Bit Score: 92.68  E-value: 3.87e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943180  72 LLSDELSNIAMQVRKLVGTQHPLLTTA------RGLvhdswNSLQLRGLVVLLISKAAG-PSSVNTSCQNYDMV-SGIYS 143
Cdd:PLN02890  87 LVADELSLLANKLRSMVVAEVPKLASAaeyffkVGV-----EGKRFRPTVLLLMATALNvPLPESTEGGVLDIVaSELRT 161
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943180 144 CQRSLAEITELIHIALLVHRGIVNLNELQSSDGPLkDMQFGNKIAILSGDFLLANACNGLALLQNTKVVELLASALMDLV 223
Cdd:PLN02890 162 RQQNIAEITEMIHVASLLHDDVLDDADTRRGVGSL-NVVMGNKLSVLAGDFLLSRACVALAALKNTEVVSLLATAVEHLV 240
                        170       180
                 ....*....|....*....|
gi 767943180 224 QGVYHENSTSKAQEKGrLDY 243
Cdd:PLN02890 241 TGETMQITSSREQRRS-MDY 259
polyprenyl_synt pfam00348
Polyprenyl synthetase;
110-225 2.58e-12

Polyprenyl synthetase;


Pssm-ID: 459773  Cd Length: 251  Bit Score: 65.22  E-value: 2.58e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943180  110 QLRGLVVLLISKAagpssvntsCQNYDmvsgIYSCQRSLAEITELIHIALLVH----------RGI--VNLnelqssdgp 177
Cdd:pfam00348  18 RIRPLLVLLSAEA---------LGGPE----DLEKAIVLAWAVELLHAASLVHddimdnsdlrRGQptWHR--------- 75
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 767943180  178 lkdmQFGNKIAILSGDFLLANACNGLA-LLQNTKVVELLASALMDLVQG 225
Cdd:pfam00348  76 ----IFGNAIAINDGDYLYALAFQLLAkLFPNPELLELFSEVTLQTAEG 120
Trans_IPPS_HT cd00685
Trans-Isoprenyl Diphosphate Synthases, head-to-tail; These trans-Isoprenyl Diphosphate ...
110-225 2.47e-10

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: 59.87  E-value: 2.47e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943180 110 QLRGLVVLLISKAAGPSSVNTscqnydmvsgiyscQRSLAEITELIHIALLVH----------RGIVNLNElqssdgplk 179
Cdd:cd00685   20 RLRPLLVLLAARALGGPELEA--------------ALRLAAAIELLHTASLVHddvmdnsdlrRGKPTVHK--------- 76
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 767943180 180 dmQFGNKIAILSGDFLLANAC---NGLALLQNTKVVELLASALMDLVQG 225
Cdd:cd00685   77 --VFGNATAILAGDYLLARAFellARLGNPYYPRALELFSEAILELVEG 123
IspA COG0142
Geranylgeranyl pyrophosphate synthase [Coenzyme transport and metabolism]; Geranylgeranyl ...
111-225 2.91e-08

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: 54.07  E-value: 2.91e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943180 111 LRGLVVLLISKAAGPSSVNTscqnydmvsgiyscqRSLAEITELIHIALLVH----------RGIVNLNElqssdgplkd 180
Cdd:COG0142   48 LRPLLVLLAARALGGDPEAA---------------LRAAAAVELIHTASLVHddvmddddlrRGKPTVHA---------- 102
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 767943180 181 mQFGNKIAILSGDFLLANAcngLALL-------QNTKVVELLASALMDLVQG 225
Cdd:COG0142  103 -RFGEATAILAGDALLALA---FELLaelgdpeRRLRALRILARAARGMCEG 150
 
Name Accession Description Interval E-value
PLN02890 PLN02890
geranyl diphosphate synthase
72-243 3.87e-21

geranyl diphosphate synthase


Pssm-ID: 178478  Cd Length: 422  Bit Score: 92.68  E-value: 3.87e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943180  72 LLSDELSNIAMQVRKLVGTQHPLLTTA------RGLvhdswNSLQLRGLVVLLISKAAG-PSSVNTSCQNYDMV-SGIYS 143
Cdd:PLN02890  87 LVADELSLLANKLRSMVVAEVPKLASAaeyffkVGV-----EGKRFRPTVLLLMATALNvPLPESTEGGVLDIVaSELRT 161
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943180 144 CQRSLAEITELIHIALLVHRGIVNLNELQSSDGPLkDMQFGNKIAILSGDFLLANACNGLALLQNTKVVELLASALMDLV 223
Cdd:PLN02890 162 RQQNIAEITEMIHVASLLHDDVLDDADTRRGVGSL-NVVMGNKLSVLAGDFLLSRACVALAALKNTEVVSLLATAVEHLV 240
                        170       180
                 ....*....|....*....|
gi 767943180 224 QGVYHENSTSKAQEKGrLDY 243
Cdd:PLN02890 241 TGETMQITSSREQRRS-MDY 259
preA CHL00151
prenyl transferase; Reviewed
68-232 4.06e-19

prenyl transferase; Reviewed


Pssm-ID: 164542  Cd Length: 323  Bit Score: 85.61  E-value: 4.06e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943180  68 SLRCLLSDELSNIAMQVRKLVGTQHPLLT-TARGLVhdSWNSLQLRGLVVLLISKAAGpssvntscQNYDMVSGiyscQR 146
Cdd:CHL00151   6 NLLTPIEEELLILEDNLKKLIGSGHPILYaAAKHLF--SAGGKRIRPAIVLLVAKATG--------GNMEIKTS----QQ 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943180 147 SLAEITELIHIALLVHRGIVNLNELQSSDgPLKDMQFGNKIAILSGDFLLANACNGLALLQNTKVVELLASALMDLVQGV 226
Cdd:CHL00151  72 RLAEITEIIHTASLVHDDVIDECSIRRGI-PTVHKIFGTKIAVLAGDFLFAQSSWYLANLNNLEVVKLISKVITDFAEGE 150

                 ....*.
gi 767943180 227 YHENST 232
Cdd:CHL00151 151 IRQGLV 156
PLN02857 PLN02857
octaprenyl-diphosphate synthase
63-225 8.88e-15

octaprenyl-diphosphate synthase


Pssm-ID: 215462  Cd Length: 416  Bit Score: 74.11  E-value: 8.88e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943180  63 PTSFMSLRCLLSDELSNIAMQVRKLVGTQHPLLTTARGLVHDSWNSlQLRGLVVLLISKAagpssvntSCQNYDMvSGIY 142
Cdd:PLN02857  91 PISLSELFEPVADDLQQLNDNLQSIVGAENPVLMSAAEQIFGAGGK-RMRPALVFLVSRA--------TAELAGL-KELT 160
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943180 143 SCQRSLAEITELIHIALLVHRGIVNLNELQSSDGPLKDMqFGNKIAILSGDFLLANACNGLALLQNTKVVELLASALMDL 222
Cdd:PLN02857 161 TEHRRLAEITEMIHTASLIHDDVLDESDMRRGKETVHQL-YGTRVAVLAGDFMFAQSSWYLANLDNLEVIKLISQVIKDF 239

                 ...
gi 767943180 223 VQG 225
Cdd:PLN02857 240 ASG 242
polyprenyl_synt pfam00348
Polyprenyl synthetase;
110-225 2.58e-12

Polyprenyl synthetase;


Pssm-ID: 459773  Cd Length: 251  Bit Score: 65.22  E-value: 2.58e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943180  110 QLRGLVVLLISKAagpssvntsCQNYDmvsgIYSCQRSLAEITELIHIALLVH----------RGI--VNLnelqssdgp 177
Cdd:pfam00348  18 RIRPLLVLLSAEA---------LGGPE----DLEKAIVLAWAVELLHAASLVHddimdnsdlrRGQptWHR--------- 75
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 767943180  178 lkdmQFGNKIAILSGDFLLANACNGLA-LLQNTKVVELLASALMDLVQG 225
Cdd:pfam00348  76 ----IFGNAIAINDGDYLYALAFQLLAkLFPNPELLELFSEVTLQTAEG 120
Trans_IPPS_HT cd00685
Trans-Isoprenyl Diphosphate Synthases, head-to-tail; These trans-Isoprenyl Diphosphate ...
110-225 2.47e-10

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: 59.87  E-value: 2.47e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943180 110 QLRGLVVLLISKAAGPSSVNTscqnydmvsgiyscQRSLAEITELIHIALLVH----------RGIVNLNElqssdgplk 179
Cdd:cd00685   20 RLRPLLVLLAARALGGPELEA--------------ALRLAAAIELLHTASLVHddvmdnsdlrRGKPTVHK--------- 76
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 767943180 180 dmQFGNKIAILSGDFLLANAC---NGLALLQNTKVVELLASALMDLVQG 225
Cdd:cd00685   77 --VFGNATAILAGDYLLARAFellARLGNPYYPRALELFSEAILELVEG 123
IspA COG0142
Geranylgeranyl pyrophosphate synthase [Coenzyme transport and metabolism]; Geranylgeranyl ...
111-225 2.91e-08

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: 54.07  E-value: 2.91e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943180 111 LRGLVVLLISKAAGPSSVNTscqnydmvsgiyscqRSLAEITELIHIALLVH----------RGIVNLNElqssdgplkd 180
Cdd:COG0142   48 LRPLLVLLAARALGGDPEAA---------------LRAAAAVELIHTASLVHddvmddddlrRGKPTVHA---------- 102
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 767943180 181 mQFGNKIAILSGDFLLANAcngLALL-------QNTKVVELLASALMDLVQG 225
Cdd:COG0142  103 -RFGEATAILAGDALLALA---FELLaelgdpeRRLRALRILARAARGMCEG 150
Trans_IPPS cd00867
Trans-Isoprenyl Diphosphate Synthases; Trans-Isoprenyl Diphosphate Synthases (Trans_IPPS) of ...
111-225 2.29e-07

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: 50.81  E-value: 2.29e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943180 111 LRGLVVLLISKAAGpssvntscqnydmvsGIYSCQRSLAEITELIHIALLVHRGIVNlNELQSSDGP-LKDMQFGNKIAI 189
Cdd:cd00867    1 SRPLLVLLLARALG---------------GDLEAALRLAAAVELLHAASLVHDDIVD-DSDLRRGKPtAHLRRFGNALAI 64
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 767943180 190 LSGDFLLANACNGLALLQNTKVVELLASALMDLVQG 225
Cdd:cd00867   65 LAGDYLLARAFQLLARLGYPRALELFAEALRELLEG 100
Isoprenoid_Biosyn_C1 cd00385
Isoprenoid Biosynthesis enzymes, Class 1; Superfamily of trans-isoprenyl diphosphate synthases ...
141-225 2.39e-05

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: 44.79  E-value: 2.39e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943180 141 IYSCQRS-LAEITELIHIALLVH----------RGIVNLNELQSsdgplkdmQFGNKIAILSGDFLLANACNGLALLQNT 209
Cdd:cd00385    7 LLEPEASrLRAAVEKLHAASLVHddivddsgtrRGLPTAHLAVA--------IDGLPEAILAGDLLLADAFEELAREGSP 78
                         90
                 ....*....|....*.
gi 767943180 210 KVVELLASALMDLVQG 225
Cdd:cd00385   79 EALEILAEALLDLLEG 94
PRK10888 PRK10888
octaprenyl diphosphate synthase; Provisional
147-225 1.07e-03

octaprenyl diphosphate synthase; Provisional


Pssm-ID: 182813  Cd Length: 323  Bit Score: 40.21  E-value: 1.07e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767943180 147 SLAEITELIHIALLVHRGIVNLNELQSSDGPLKDMqFGNKIAILSGDFLLANACNGLALLQNTKVVELLASALMDLVQG 225
Cdd:PRK10888  68 TIAALIEFIHTATLLHDDVVDESDMRRGKATANAA-FGNAASVLVGDFIYTRAFQMMTSLGSLKVLEVMSEAVNVIAEG 145
 
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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