NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1840394174|ref|NP_001369397|]
View 

ERO1-like protein alpha isoform 6 precursor [Homo sapiens]

Protein Classification

ERO1 family protein( domain architecture ID 10514194)

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

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
60-444 1.23e-178

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: 503.25  E-value: 1.23e-178
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840394174  60 RLFPRLQKLLESDYFRYYKVNLKRPCPFW-NDISQCGRRDCAVKPCQSDEVPDGIKsasykyseeannlieeceqAERLG 138
Cdd:pfam04137   1 KIRPLLQELVQTDFFRYFKVNLYKECPFWsDDNGMCGNRACAVCTCDESEIPEPWR-------------------AEELG 61
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840394174 139 AVDESLS--EETQKAVLQWTKHDDSSD-NFCEADDIQSPEAEYVDLLLNPERYTGYKGPDAWKIWNVIYEENCFKPQTiK 215
Cdd:pfam04137  62 KLEGTLAkhDVGESCVVEWDDECDADDdDYCVLDDENDSEGVYVDLLLNPERFTGYSGPSAHRIWRAIYEENCFQPST-E 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840394174 216 RPLNPLASGQGLCVEKRAFYRLISGLHASINVHLSARYLLQETwleKKWGHNITEFQQRFdgilteGEGPRRLKNLYFLY 295
Cdd:pfam04137 141 SLSEDSLELDGECLEKRVFYRLISGLHASISTHLCNEYLNQET---GEWGPNLECFMERV------GNHPERLENLYFNY 211
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840394174 296 LIELRALSKVLPFFERPDFqlFTGNKIQDEENKMLLLEILHEI-KSFPLHFDENSFFAGDkkEAHKLKEDFRLHFRNISR 374
Cdd:pfam04137 212 ALVLRALAKLAPYLENYDF--CTGDPEEDAETKALIKDILSSLtSIVPPIFDESLLFKDE--EAPELKEEFRNRFRNVSR 287
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840394174 375 IMDCVGCFKCRLWGKLQTQGLGTALKILFSEKlianmPESGPSYEFHLTRQEIVSLFNAFGRISTSVKEL 444
Cdd:pfam04137 288 IMDCVGCDKCRLWGKLQTTGLGTALKILFELD-----ENDEEDNPLKLRRNELVALFNTFDRLSESIEAI 352
 
Name Accession Description Interval E-value
ERO1 pfam04137
Endoplasmic Reticulum Oxidoreductin 1 (ERO1); Members of this family are required for the ...
60-444 1.23e-178

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: 503.25  E-value: 1.23e-178
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840394174  60 RLFPRLQKLLESDYFRYYKVNLKRPCPFW-NDISQCGRRDCAVKPCQSDEVPDGIKsasykyseeannlieeceqAERLG 138
Cdd:pfam04137   1 KIRPLLQELVQTDFFRYFKVNLYKECPFWsDDNGMCGNRACAVCTCDESEIPEPWR-------------------AEELG 61
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840394174 139 AVDESLS--EETQKAVLQWTKHDDSSD-NFCEADDIQSPEAEYVDLLLNPERYTGYKGPDAWKIWNVIYEENCFKPQTiK 215
Cdd:pfam04137  62 KLEGTLAkhDVGESCVVEWDDECDADDdDYCVLDDENDSEGVYVDLLLNPERFTGYSGPSAHRIWRAIYEENCFQPST-E 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840394174 216 RPLNPLASGQGLCVEKRAFYRLISGLHASINVHLSARYLLQETwleKKWGHNITEFQQRFdgilteGEGPRRLKNLYFLY 295
Cdd:pfam04137 141 SLSEDSLELDGECLEKRVFYRLISGLHASISTHLCNEYLNQET---GEWGPNLECFMERV------GNHPERLENLYFNY 211
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840394174 296 LIELRALSKVLPFFERPDFqlFTGNKIQDEENKMLLLEILHEI-KSFPLHFDENSFFAGDkkEAHKLKEDFRLHFRNISR 374
Cdd:pfam04137 212 ALVLRALAKLAPYLENYDF--CTGDPEEDAETKALIKDILSSLtSIVPPIFDESLLFKDE--EAPELKEEFRNRFRNVSR 287
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840394174 375 IMDCVGCFKCRLWGKLQTQGLGTALKILFSEKlianmPESGPSYEFHLTRQEIVSLFNAFGRISTSVKEL 444
Cdd:pfam04137 288 IMDCVGCDKCRLWGKLQTTGLGTALKILFELD-----ENDEEDNPLKLRRNELVALFNTFDRLSESIEAI 352
ERO1 COG5061
Oxidoreductin, endoplasmic reticulum membrane-associated protein involved in disulfide bond ...
58-454 5.03e-82

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: 259.43  E-value: 5.03e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840394174  58 NYRLFPRLQKLLESDYFRYYKVNLKRP-CPFW-NDISQCGRRDCAVKPCQS-DEVPDGIKSASYKYSEEANNLIEECeqa 134
Cdd:COG5061    39 NSKVRSLLPVLTESDYMFYYRLNLYAKaCTLWpDDNDMCVSKACNVTVRSEeDLVPKVWKDKLSLFKPHSKKLDQFC--- 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840394174 135 erlgavdeslseetqkavlQWTKHDDssDNFCEADDIQSPEAEYVDLLLNPERYTGYKGPDAWKIWNVIYEENCFkpqTI 214
Cdd:COG5061   116 -------------------SESKCPD--LSYCYVDNKSIFNDVYISLLENPERFTGYKGNHSAEIWRKIYEQNCF---DT 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840394174 215 KRPLNPLasgqglcvEKRAFYRLISGLHASINVHLSARYLLQETwleKKWGHNITEFQQRFdgilteGEGPRRLKNLYFL 294
Cdd:COG5061   172 LLPPTLL--------EKRMFYRLVSGFHASISTHLSSFYLNVFF---GTWLPNLDLFRARV------GNFPDRIENFYFN 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840394174 295 YLIELRALSKVlpffeRPDFQLFTGNKIQDEENKMLLLEILHEIKSFPLHFDENSFFAGDKkeAHKLKEDFRLHFRNISR 374
Cdd:COG5061   235 YALVRSALGKI-----DVDLSSFTFCPTDKDELSGKLSSLISAIRAQGKTFNEIQPFALEK--SIQLKDRFREHFRDVSR 307
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840394174 375 IMDCVGCFKCRLWGKLQTQGLGTALKILFSeklianmPESGpsyEFHLTRQEIVSLFNAFGRISTSVKELENFRNLLQNI 454
Cdd:COG5061   308 LMDCVGCEKCRLWGKIQTTGYGTALKILFE-------SETQ---LFDLRSLERVALVNTFDRLSVSVREATFENILLRSY 377
 
Name Accession Description Interval E-value
ERO1 pfam04137
Endoplasmic Reticulum Oxidoreductin 1 (ERO1); Members of this family are required for the ...
60-444 1.23e-178

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: 503.25  E-value: 1.23e-178
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840394174  60 RLFPRLQKLLESDYFRYYKVNLKRPCPFW-NDISQCGRRDCAVKPCQSDEVPDGIKsasykyseeannlieeceqAERLG 138
Cdd:pfam04137   1 KIRPLLQELVQTDFFRYFKVNLYKECPFWsDDNGMCGNRACAVCTCDESEIPEPWR-------------------AEELG 61
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840394174 139 AVDESLS--EETQKAVLQWTKHDDSSD-NFCEADDIQSPEAEYVDLLLNPERYTGYKGPDAWKIWNVIYEENCFKPQTiK 215
Cdd:pfam04137  62 KLEGTLAkhDVGESCVVEWDDECDADDdDYCVLDDENDSEGVYVDLLLNPERFTGYSGPSAHRIWRAIYEENCFQPST-E 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840394174 216 RPLNPLASGQGLCVEKRAFYRLISGLHASINVHLSARYLLQETwleKKWGHNITEFQQRFdgilteGEGPRRLKNLYFLY 295
Cdd:pfam04137 141 SLSEDSLELDGECLEKRVFYRLISGLHASISTHLCNEYLNQET---GEWGPNLECFMERV------GNHPERLENLYFNY 211
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840394174 296 LIELRALSKVLPFFERPDFqlFTGNKIQDEENKMLLLEILHEI-KSFPLHFDENSFFAGDkkEAHKLKEDFRLHFRNISR 374
Cdd:pfam04137 212 ALVLRALAKLAPYLENYDF--CTGDPEEDAETKALIKDILSSLtSIVPPIFDESLLFKDE--EAPELKEEFRNRFRNVSR 287
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840394174 375 IMDCVGCFKCRLWGKLQTQGLGTALKILFSEKlianmPESGPSYEFHLTRQEIVSLFNAFGRISTSVKEL 444
Cdd:pfam04137 288 IMDCVGCDKCRLWGKLQTTGLGTALKILFELD-----ENDEEDNPLKLRRNELVALFNTFDRLSESIEAI 352
ERO1 COG5061
Oxidoreductin, endoplasmic reticulum membrane-associated protein involved in disulfide bond ...
58-454 5.03e-82

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: 259.43  E-value: 5.03e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840394174  58 NYRLFPRLQKLLESDYFRYYKVNLKRP-CPFW-NDISQCGRRDCAVKPCQS-DEVPDGIKSASYKYSEEANNLIEECeqa 134
Cdd:COG5061    39 NSKVRSLLPVLTESDYMFYYRLNLYAKaCTLWpDDNDMCVSKACNVTVRSEeDLVPKVWKDKLSLFKPHSKKLDQFC--- 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840394174 135 erlgavdeslseetqkavlQWTKHDDssDNFCEADDIQSPEAEYVDLLLNPERYTGYKGPDAWKIWNVIYEENCFkpqTI 214
Cdd:COG5061   116 -------------------SESKCPD--LSYCYVDNKSIFNDVYISLLENPERFTGYKGNHSAEIWRKIYEQNCF---DT 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840394174 215 KRPLNPLasgqglcvEKRAFYRLISGLHASINVHLSARYLLQETwleKKWGHNITEFQQRFdgilteGEGPRRLKNLYFL 294
Cdd:COG5061   172 LLPPTLL--------EKRMFYRLVSGFHASISTHLSSFYLNVFF---GTWLPNLDLFRARV------GNFPDRIENFYFN 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840394174 295 YLIELRALSKVlpffeRPDFQLFTGNKIQDEENKMLLLEILHEIKSFPLHFDENSFFAGDKkeAHKLKEDFRLHFRNISR 374
Cdd:COG5061   235 YALVRSALGKI-----DVDLSSFTFCPTDKDELSGKLSSLISAIRAQGKTFNEIQPFALEK--SIQLKDRFREHFRDVSR 307
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840394174 375 IMDCVGCFKCRLWGKLQTQGLGTALKILFSeklianmPESGpsyEFHLTRQEIVSLFNAFGRISTSVKELENFRNLLQNI 454
Cdd:COG5061   308 LMDCVGCEKCRLWGKIQTTGYGTALKILFE-------SETQ---LFDLRSLERVALVNTFDRLSVSVREATFENILLRSY 377
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH