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Conserved domains on  [gi|258597304|ref|XP_001347922|]
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endoplasmic reticulum oxidoreductin, putative [Plasmodium falciparum 3D7]

Protein Classification

endoplasmic reticulum oxidoreductin family protein( domain architecture ID 10514194)

endoplasmic reticulum oxidoreductin family protein similar to endoplasmic reticulum oxidoreductin-1 (ERO1) and -2 (ERO2) which are essential oxidoreductases that oxidize proteins in the endoplasmic reticulum to produce disulfide bonds

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ERO1 pfam04137
Endoplasmic Reticulum Oxidoreductin 1 (ERO1); Members of this family are required for the ...
78-417 1.96e-95

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: 291.78  E-value: 1.96e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597304   78 YPILKELKQKDYFRIFKVNLHLSCKVFLKGNEKCKEiKKCSVCECEQDEIPYNFRTNEIEIIENKMTNEDLKKTFIESKL 157
Cdd:pfam04137   3 RPLLQELVQTDFFRYFKVNLYKECPFWSDDNGMCGN-RACAVCTCDESEIPEPWRAEELGKLEGTLAKHDVGESCVVEWD 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597304  158 Y------KDILGIYAPSNEGfISYVDLVYNSPSFTAYEG---RNIWNMIYKENCFQNEKS-----------ECEEMNSFY 217
Cdd:pfam04137  82 DecdaddDDYCVLDDENDSE-GVYVDLLLNPERFTGYSGpsaHRIWRAIYEENCFQPSTEslsedsleldgECLEKRVFY 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597304  218 KIISGMQSNIAV-LSSEYFylkndflfgeiqinNKFNNDYFKNLnydysvTFFKEKIGLYPERIENLYFTFAILLRSMCR 296
Cdd:pfam04137 161 RLISGLHASISThLCNEYL--------------NQETGEWGPNL------ECFMERVGNHPERLENLYFNYALVLRALAK 220
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597304  297 LKSLFKQCKCNSGYEQNDKEAVRLLDDLLENFYHSCS-----SKEFLEPLFPQHGKDILSKFMNITNILDCVPCVKCRLH 371
Cdd:pfam04137 221 LAPYLENYDFCTGDPEEDAETKALIKDILSSLTSIVPpifdeSLLFKDEEAPELKEEFRNRFRNVSRIMDCVGCDKCRLW 300
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 258597304  372 GKLKTTALQIALVEGVSDEH------IGSLERNEITALINALYYFADSILII 417
Cdd:pfam04137 301 GKLQTTGLGTALKILFELDEndeednPLKLRRNELVALFNTFDRLSESIEAI 352
 
Name Accession Description Interval E-value
ERO1 pfam04137
Endoplasmic Reticulum Oxidoreductin 1 (ERO1); Members of this family are required for the ...
78-417 1.96e-95

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: 291.78  E-value: 1.96e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597304   78 YPILKELKQKDYFRIFKVNLHLSCKVFLKGNEKCKEiKKCSVCECEQDEIPYNFRTNEIEIIENKMTNEDLKKTFIESKL 157
Cdd:pfam04137   3 RPLLQELVQTDFFRYFKVNLYKECPFWSDDNGMCGN-RACAVCTCDESEIPEPWRAEELGKLEGTLAKHDVGESCVVEWD 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597304  158 Y------KDILGIYAPSNEGfISYVDLVYNSPSFTAYEG---RNIWNMIYKENCFQNEKS-----------ECEEMNSFY 217
Cdd:pfam04137  82 DecdaddDDYCVLDDENDSE-GVYVDLLLNPERFTGYSGpsaHRIWRAIYEENCFQPSTEslsedsleldgECLEKRVFY 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597304  218 KIISGMQSNIAV-LSSEYFylkndflfgeiqinNKFNNDYFKNLnydysvTFFKEKIGLYPERIENLYFTFAILLRSMCR 296
Cdd:pfam04137 161 RLISGLHASISThLCNEYL--------------NQETGEWGPNL------ECFMERVGNHPERLENLYFNYALVLRALAK 220
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597304  297 LKSLFKQCKCNSGYEQNDKEAVRLLDDLLENFYHSCS-----SKEFLEPLFPQHGKDILSKFMNITNILDCVPCVKCRLH 371
Cdd:pfam04137 221 LAPYLENYDFCTGDPEEDAETKALIKDILSSLTSIVPpifdeSLLFKDEEAPELKEEFRNRFRNVSRIMDCVGCDKCRLW 300
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 258597304  372 GKLKTTALQIALVEGVSDEH------IGSLERNEITALINALYYFADSILII 417
Cdd:pfam04137 301 GKLQTTGLGTALKILFELDEndeednPLKLRRNELVALFNTFDRLSESIEAI 352
ERO1 COG5061
Oxidoreductin, endoplasmic reticulum membrane-associated protein involved in disulfide bond ...
76-425 3.65e-27

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: 113.06  E-value: 3.65e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597304  76 RAYPILKELKQKDYFRIFKVNLHLS-CKVFLKGNEKCKEiKKCSV-CECEQDEIPYNFRtneiEIIENKMTNEDLKKTFI 153
Cdd:COG5061   41 KVRSLLPVLTESDYMFYYRLNLYAKaCTLWPDDNDMCVS-KACNVtVRSEEDLVPKVWK----DKLSLFKPHSKKLDQFC 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597304 154 ESKLYKDILGIYAPSNEGF-ISYVDLVYNSPSFTAYEGRN---IWNMIYKENCFQ-NEKSECEEMNSFYKIISGMQSNIA 228
Cdd:COG5061  116 SESKCPDLSYCYVDNKSIFnDVYISLLENPERFTGYKGNHsaeIWRKIYEQNCFDtLLPPTLLEKRMFYRLVSGFHASIS 195
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597304 229 V-LSSEYFylkndflfgeiqinNKFNNDYFKNLNydysvtFFKEKIGLYPERIENLYFTFAILLRSmcrLKSLFKQCKCN 307
Cdd:COG5061  196 ThLSSFYL--------------NVFFGTWLPNLD------LFRARVGNFPDRIENFYFNYALVRSA---LGKIDVDLSSF 252
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597304 308 SGYEQNDKEAVRLLDDLLENFYHSCS----SKEFLEPLFPQHGKDILSKFMNITNILDCVPCVKCRLHGKLKTTALQIAL 383
Cdd:COG5061  253 TFCPTDKDELSGKLSSLISAIRAQGKtfneIQPFALEKSIQLKDRFREHFRDVSRLMDCVGCEKCRLWGKIQTTGYGTAL 332
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 258597304 384 -VEGVSDEHIGSLERNEITALINALYYFADSILiINKFEDRLK 425
Cdd:COG5061  333 kILFESETQLFDLRSLERVALVNTFDRLSVSVR-EATFENILL 374
 
Name Accession Description Interval E-value
ERO1 pfam04137
Endoplasmic Reticulum Oxidoreductin 1 (ERO1); Members of this family are required for the ...
78-417 1.96e-95

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: 291.78  E-value: 1.96e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597304   78 YPILKELKQKDYFRIFKVNLHLSCKVFLKGNEKCKEiKKCSVCECEQDEIPYNFRTNEIEIIENKMTNEDLKKTFIESKL 157
Cdd:pfam04137   3 RPLLQELVQTDFFRYFKVNLYKECPFWSDDNGMCGN-RACAVCTCDESEIPEPWRAEELGKLEGTLAKHDVGESCVVEWD 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597304  158 Y------KDILGIYAPSNEGfISYVDLVYNSPSFTAYEG---RNIWNMIYKENCFQNEKS-----------ECEEMNSFY 217
Cdd:pfam04137  82 DecdaddDDYCVLDDENDSE-GVYVDLLLNPERFTGYSGpsaHRIWRAIYEENCFQPSTEslsedsleldgECLEKRVFY 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597304  218 KIISGMQSNIAV-LSSEYFylkndflfgeiqinNKFNNDYFKNLnydysvTFFKEKIGLYPERIENLYFTFAILLRSMCR 296
Cdd:pfam04137 161 RLISGLHASISThLCNEYL--------------NQETGEWGPNL------ECFMERVGNHPERLENLYFNYALVLRALAK 220
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597304  297 LKSLFKQCKCNSGYEQNDKEAVRLLDDLLENFYHSCS-----SKEFLEPLFPQHGKDILSKFMNITNILDCVPCVKCRLH 371
Cdd:pfam04137 221 LAPYLENYDFCTGDPEEDAETKALIKDILSSLTSIVPpifdeSLLFKDEEAPELKEEFRNRFRNVSRIMDCVGCDKCRLW 300
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 258597304  372 GKLKTTALQIALVEGVSDEH------IGSLERNEITALINALYYFADSILII 417
Cdd:pfam04137 301 GKLQTTGLGTALKILFELDEndeednPLKLRRNELVALFNTFDRLSESIEAI 352
ERO1 COG5061
Oxidoreductin, endoplasmic reticulum membrane-associated protein involved in disulfide bond ...
76-425 3.65e-27

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: 113.06  E-value: 3.65e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597304  76 RAYPILKELKQKDYFRIFKVNLHLS-CKVFLKGNEKCKEiKKCSV-CECEQDEIPYNFRtneiEIIENKMTNEDLKKTFI 153
Cdd:COG5061   41 KVRSLLPVLTESDYMFYYRLNLYAKaCTLWPDDNDMCVS-KACNVtVRSEEDLVPKVWK----DKLSLFKPHSKKLDQFC 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597304 154 ESKLYKDILGIYAPSNEGF-ISYVDLVYNSPSFTAYEGRN---IWNMIYKENCFQ-NEKSECEEMNSFYKIISGMQSNIA 228
Cdd:COG5061  116 SESKCPDLSYCYVDNKSIFnDVYISLLENPERFTGYKGNHsaeIWRKIYEQNCFDtLLPPTLLEKRMFYRLVSGFHASIS 195
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597304 229 V-LSSEYFylkndflfgeiqinNKFNNDYFKNLNydysvtFFKEKIGLYPERIENLYFTFAILLRSmcrLKSLFKQCKCN 307
Cdd:COG5061  196 ThLSSFYL--------------NVFFGTWLPNLD------LFRARVGNFPDRIENFYFNYALVRSA---LGKIDVDLSSF 252
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597304 308 SGYEQNDKEAVRLLDDLLENFYHSCS----SKEFLEPLFPQHGKDILSKFMNITNILDCVPCVKCRLHGKLKTTALQIAL 383
Cdd:COG5061  253 TFCPTDKDELSGKLSSLISAIRAQGKtfneIQPFALEKSIQLKDRFREHFRDVSRLMDCVGCEKCRLWGKIQTTGYGTAL 332
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 258597304 384 -VEGVSDEHIGSLERNEITALINALYYFADSILiINKFEDRLK 425
Cdd:COG5061  333 kILFESETQLFDLRSLERVALVNTFDRLSVSVR-EATFENILL 374
 
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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