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Conserved domains on  [gi|149027598|gb|EDL83161|]
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similar to endoplasmic oxidoreductase 1 beta (predicted), isoform CRA_b [Rattus norvegicus]

Protein Classification

endoplasmic reticulum oxidoreductin family protein( domain architecture ID 141571)

endoplasmic reticulum oxidoreductin family protein similar to endoplasmic reticulum oxidoreductin-1 (ERO1) and -2 which are essential oxidoreductases that oxidize proteins in the endoplasmic reticulum to produce disulfide bonds

EC:  1.-.-.-
Gene Ontology:  GO:0016491|GO:0071949
PubMed:  9659914

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ERO1 super family cl19883
Endoplasmic Reticulum Oxidoreductin 1 (ERO1); Members of this family are required for the ...
56-170 1.48e-29

Endoplasmic Reticulum Oxidoreductin 1 (ERO1); Members of this family are required for the formation of disulphide bonds in the ER.


The actual alignment was detected with superfamily member pfam04137:

Pssm-ID: 473246  Cd Length: 352  Bit Score: 110.73  E-value: 1.48e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149027598   56 KIFPKIKKLQERDYFRYYKVNLKRPCPFWAED-GHCSIKDCHVEPCPESKIPVGIKagrsnkysqaanntkelddceqAN 134
Cdd:pfam04137   1 KIRPLLQELVQTDFFRYFKVNLYKECPFWSDDnGMCGNRACAVCTCDESEIPEPWR----------------------AE 58
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 149027598  135 KLGAINSTLS--NESKEAFIDWARYDD-SQDHFCELDDF 170
Cdd:pfam04137  59 ELGKLEGTLAkhDVGESCVVEWDDECDaDDDDYCVLDDE 97
 
Name Accession Description Interval E-value
ERO1 pfam04137
Endoplasmic Reticulum Oxidoreductin 1 (ERO1); Members of this family are required for the ...
56-170 1.48e-29

Endoplasmic Reticulum Oxidoreductin 1 (ERO1); Members of this family are required for the formation of disulphide bonds in the ER.


Pssm-ID: 461191  Cd Length: 352  Bit Score: 110.73  E-value: 1.48e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149027598   56 KIFPKIKKLQERDYFRYYKVNLKRPCPFWAED-GHCSIKDCHVEPCPESKIPVGIKagrsnkysqaanntkelddceqAN 134
Cdd:pfam04137   1 KIRPLLQELVQTDFFRYFKVNLYKECPFWSDDnGMCGNRACAVCTCDESEIPEPWR----------------------AE 58
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 149027598  135 KLGAINSTLS--NESKEAFIDWARYDD-SQDHFCELDDF 170
Cdd:pfam04137  59 ELGKLEGTLAkhDVGESCVVEWDDECDaDDDDYCVLDDE 97
ERO1 COG5061
Oxidoreductin, endoplasmic reticulum membrane-associated protein involved in disulfide bond ...
48-172 1.07e-04

Oxidoreductin, endoplasmic reticulum membrane-associated protein involved in disulfide bond formation [Posttranslational modification, protein turnover, chaperones / Intracellular trafficking and secretion];


Pssm-ID: 227393  Cd Length: 425  Bit Score: 41.41  E-value: 1.07e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149027598  48 SIDNFNTyKIFPKIKKLQERDYFRYYKVNLKRP-CPFW-AEDGHCSIKDCHVEPCPESKIpvgIKAGRSNKYSQAANNTK 125
Cdd:COG5061   34 GIYQMNS-KVRSLLPVLTESDYMFYYRLNLYAKaCTLWpDDNDMCVSKACNVTVRSEEDL---VPKVWKDKLSLFKPHSK 109
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 149027598 126 ELDDceqanklgainstLSNESKEAFIDWARYDDSQDHFCELDDFLQ 172
Cdd:COG5061  110 KLDQ-------------FCSESKCPDLSYCYVDNKSIFNDVYISLLE 143
 
Name Accession Description Interval E-value
ERO1 pfam04137
Endoplasmic Reticulum Oxidoreductin 1 (ERO1); Members of this family are required for the ...
56-170 1.48e-29

Endoplasmic Reticulum Oxidoreductin 1 (ERO1); Members of this family are required for the formation of disulphide bonds in the ER.


Pssm-ID: 461191  Cd Length: 352  Bit Score: 110.73  E-value: 1.48e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149027598   56 KIFPKIKKLQERDYFRYYKVNLKRPCPFWAED-GHCSIKDCHVEPCPESKIPVGIKagrsnkysqaanntkelddceqAN 134
Cdd:pfam04137   1 KIRPLLQELVQTDFFRYFKVNLYKECPFWSDDnGMCGNRACAVCTCDESEIPEPWR----------------------AE 58
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 149027598  135 KLGAINSTLS--NESKEAFIDWARYDD-SQDHFCELDDF 170
Cdd:pfam04137  59 ELGKLEGTLAkhDVGESCVVEWDDECDaDDDDYCVLDDE 97
ERO1 COG5061
Oxidoreductin, endoplasmic reticulum membrane-associated protein involved in disulfide bond ...
48-172 1.07e-04

Oxidoreductin, endoplasmic reticulum membrane-associated protein involved in disulfide bond formation [Posttranslational modification, protein turnover, chaperones / Intracellular trafficking and secretion];


Pssm-ID: 227393  Cd Length: 425  Bit Score: 41.41  E-value: 1.07e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149027598  48 SIDNFNTyKIFPKIKKLQERDYFRYYKVNLKRP-CPFW-AEDGHCSIKDCHVEPCPESKIpvgIKAGRSNKYSQAANNTK 125
Cdd:COG5061   34 GIYQMNS-KVRSLLPVLTESDYMFYYRLNLYAKaCTLWpDDNDMCVSKACNVTVRSEEDL---VPKVWKDKLSLFKPHSK 109
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 149027598 126 ELDDceqanklgainstLSNESKEAFIDWARYDDSQDHFCELDDFLQ 172
Cdd:COG5061  110 KLDQ-------------FCSESKCPDLSYCYVDNKSIFNDVYISLLE 143
 
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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