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Conserved domains on  [gi|1840394227|ref|NP_001369396|]
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ERO1-like protein alpha isoform 5 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

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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 ...
60-448 2.03e-179

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: 505.56  E-value: 2.03e-179
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840394227  60 RLFPRLQKLLESDYFRYYKVNLKRPCPFW-NDISQCGRRDCAVKPCQSDEVPDGIKsasykyseeannlieeceqAERLG 138
Cdd:pfam04137   1 KIRPLLQELVQTDFFRYFKVNLYKECPFWsDDNGMCGNRACAVCTCDESEIPEPWR-------------------AEELG 61
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840394227 139 AVDESLS--EETQKAVLQWTKHDDSSD-NFCEADDIQSPEAEYVDLLLNPERYTGYKGPDAWKIWNVIYEENCFKPQTik 215
Cdd:pfam04137  62 KLEGTLAkhDVGESCVVEWDDECDADDdDYCVLDDENDSEGVYVDLLLNPERFTGYSGPSAHRIWRAIYEENCFQPST-- 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840394227 216 rplNPLASGQGTSEGLCVEKRAFYRLISGLHASINVHLSARYLLQETwleKKWGHNITEFQQRFdgilteGEGPRRLKNL 295
Cdd:pfam04137 140 ---ESLSEDSLELDGECLEKRVFYRLISGLHASISTHLCNEYLNQET---GEWGPNLECFMERV------GNHPERLENL 207
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840394227 296 YFLYLIELRALSKVLPFFERPDFqlFTGNKIQDEENKMLLLEILHEI-KSFPLHFDENSFFAGDkkEAHKLKEDFRLHFR 374
Cdd:pfam04137 208 YFNYALVLRALAKLAPYLENYDF--CTGDPEEDAETKALIKDILSSLtSIVPPIFDESLLFKDE--EAPELKEEFRNRFR 283
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1840394227 375 NISRIMDCVGCFKCRLWGKLQTQGLGTALKILFSEKlianmPESGPSYEFHLTRQEIVSLFNAFGRISTSVKEL 448
Cdd:pfam04137 284 NVSRIMDCVGCDKCRLWGKLQTTGLGTALKILFELD-----ENDEEDNPLKLRRNELVALFNTFDRLSESIEAI 352
 
Name Accession Description Interval E-value
ERO1 pfam04137
Endoplasmic Reticulum Oxidoreductin 1 (ERO1); Members of this family are required for the ...
60-448 2.03e-179

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: 505.56  E-value: 2.03e-179
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840394227  60 RLFPRLQKLLESDYFRYYKVNLKRPCPFW-NDISQCGRRDCAVKPCQSDEVPDGIKsasykyseeannlieeceqAERLG 138
Cdd:pfam04137   1 KIRPLLQELVQTDFFRYFKVNLYKECPFWsDDNGMCGNRACAVCTCDESEIPEPWR-------------------AEELG 61
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840394227 139 AVDESLS--EETQKAVLQWTKHDDSSD-NFCEADDIQSPEAEYVDLLLNPERYTGYKGPDAWKIWNVIYEENCFKPQTik 215
Cdd:pfam04137  62 KLEGTLAkhDVGESCVVEWDDECDADDdDYCVLDDENDSEGVYVDLLLNPERFTGYSGPSAHRIWRAIYEENCFQPST-- 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840394227 216 rplNPLASGQGTSEGLCVEKRAFYRLISGLHASINVHLSARYLLQETwleKKWGHNITEFQQRFdgilteGEGPRRLKNL 295
Cdd:pfam04137 140 ---ESLSEDSLELDGECLEKRVFYRLISGLHASISTHLCNEYLNQET---GEWGPNLECFMERV------GNHPERLENL 207
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840394227 296 YFLYLIELRALSKVLPFFERPDFqlFTGNKIQDEENKMLLLEILHEI-KSFPLHFDENSFFAGDkkEAHKLKEDFRLHFR 374
Cdd:pfam04137 208 YFNYALVLRALAKLAPYLENYDF--CTGDPEEDAETKALIKDILSSLtSIVPPIFDESLLFKDE--EAPELKEEFRNRFR 283
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1840394227 375 NISRIMDCVGCFKCRLWGKLQTQGLGTALKILFSEKlianmPESGPSYEFHLTRQEIVSLFNAFGRISTSVKEL 448
Cdd:pfam04137 284 NVSRIMDCVGCDKCRLWGKLQTTGLGTALKILFELD-----ENDEEDNPLKLRRNELVALFNTFDRLSESIEAI 352
ERO1 COG5061
Oxidoreductin, endoplasmic reticulum membrane-associated protein involved in disulfide bond ...
58-458 1.50e-81

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: 258.28  E-value: 1.50e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840394227  58 NYRLFPRLQKLLESDYFRYYKVNLKRP-CPFW-NDISQCGRRDCAVKPCQS-DEVPDGIKSASYKYSEEANNLIEECeqa 134
Cdd:COG5061    39 NSKVRSLLPVLTESDYMFYYRLNLYAKaCTLWpDDNDMCVSKACNVTVRSEeDLVPKVWKDKLSLFKPHSKKLDQFC--- 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840394227 135 erlgavdeslseetqkavlQWTKHDDssDNFCEADDIQSPEAEYVDLLLNPERYTGYKGPDAWKIWNVIYEENCFkpqTI 214
Cdd:COG5061   116 -------------------SESKCPD--LSYCYVDNKSIFNDVYISLLENPERFTGYKGNHSAEIWRKIYEQNCF---DT 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840394227 215 KRPLNPLasgqgtseglcvEKRAFYRLISGLHASINVHLSARYLLQETwleKKWGHNITEFQQRFdgilteGEGPRRLKN 294
Cdd:COG5061   172 LLPPTLL------------EKRMFYRLVSGFHASISTHLSSFYLNVFF---GTWLPNLDLFRARV------GNFPDRIEN 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840394227 295 LYFLYLIELRALSKVlpffeRPDFQLFTGNKIQDEENKMLLLEILHEIKSFPLHFDENSFFAGDKkeAHKLKEDFRLHFR 374
Cdd:COG5061   231 FYFNYALVRSALGKI-----DVDLSSFTFCPTDKDELSGKLSSLISAIRAQGKTFNEIQPFALEK--SIQLKDRFREHFR 303
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840394227 375 NISRIMDCVGCFKCRLWGKLQTQGLGTALKILFSeklianmPESGpsyEFHLTRQEIVSLFNAFGRISTSVKELENFRNL 454
Cdd:COG5061   304 DVSRLMDCVGCEKCRLWGKIQTTGYGTALKILFE-------SETQ---LFDLRSLERVALVNTFDRLSVSVREATFENIL 373

                  ....
gi 1840394227 455 LQNI 458
Cdd:COG5061   374 LRSY 377
 
Name Accession Description Interval E-value
ERO1 pfam04137
Endoplasmic Reticulum Oxidoreductin 1 (ERO1); Members of this family are required for the ...
60-448 2.03e-179

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: 505.56  E-value: 2.03e-179
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840394227  60 RLFPRLQKLLESDYFRYYKVNLKRPCPFW-NDISQCGRRDCAVKPCQSDEVPDGIKsasykyseeannlieeceqAERLG 138
Cdd:pfam04137   1 KIRPLLQELVQTDFFRYFKVNLYKECPFWsDDNGMCGNRACAVCTCDESEIPEPWR-------------------AEELG 61
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840394227 139 AVDESLS--EETQKAVLQWTKHDDSSD-NFCEADDIQSPEAEYVDLLLNPERYTGYKGPDAWKIWNVIYEENCFKPQTik 215
Cdd:pfam04137  62 KLEGTLAkhDVGESCVVEWDDECDADDdDYCVLDDENDSEGVYVDLLLNPERFTGYSGPSAHRIWRAIYEENCFQPST-- 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840394227 216 rplNPLASGQGTSEGLCVEKRAFYRLISGLHASINVHLSARYLLQETwleKKWGHNITEFQQRFdgilteGEGPRRLKNL 295
Cdd:pfam04137 140 ---ESLSEDSLELDGECLEKRVFYRLISGLHASISTHLCNEYLNQET---GEWGPNLECFMERV------GNHPERLENL 207
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840394227 296 YFLYLIELRALSKVLPFFERPDFqlFTGNKIQDEENKMLLLEILHEI-KSFPLHFDENSFFAGDkkEAHKLKEDFRLHFR 374
Cdd:pfam04137 208 YFNYALVLRALAKLAPYLENYDF--CTGDPEEDAETKALIKDILSSLtSIVPPIFDESLLFKDE--EAPELKEEFRNRFR 283
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1840394227 375 NISRIMDCVGCFKCRLWGKLQTQGLGTALKILFSEKlianmPESGPSYEFHLTRQEIVSLFNAFGRISTSVKEL 448
Cdd:pfam04137 284 NVSRIMDCVGCDKCRLWGKLQTTGLGTALKILFELD-----ENDEEDNPLKLRRNELVALFNTFDRLSESIEAI 352
ERO1 COG5061
Oxidoreductin, endoplasmic reticulum membrane-associated protein involved in disulfide bond ...
58-458 1.50e-81

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: 258.28  E-value: 1.50e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840394227  58 NYRLFPRLQKLLESDYFRYYKVNLKRP-CPFW-NDISQCGRRDCAVKPCQS-DEVPDGIKSASYKYSEEANNLIEECeqa 134
Cdd:COG5061    39 NSKVRSLLPVLTESDYMFYYRLNLYAKaCTLWpDDNDMCVSKACNVTVRSEeDLVPKVWKDKLSLFKPHSKKLDQFC--- 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840394227 135 erlgavdeslseetqkavlQWTKHDDssDNFCEADDIQSPEAEYVDLLLNPERYTGYKGPDAWKIWNVIYEENCFkpqTI 214
Cdd:COG5061   116 -------------------SESKCPD--LSYCYVDNKSIFNDVYISLLENPERFTGYKGNHSAEIWRKIYEQNCF---DT 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840394227 215 KRPLNPLasgqgtseglcvEKRAFYRLISGLHASINVHLSARYLLQETwleKKWGHNITEFQQRFdgilteGEGPRRLKN 294
Cdd:COG5061   172 LLPPTLL------------EKRMFYRLVSGFHASISTHLSSFYLNVFF---GTWLPNLDLFRARV------GNFPDRIEN 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840394227 295 LYFLYLIELRALSKVlpffeRPDFQLFTGNKIQDEENKMLLLEILHEIKSFPLHFDENSFFAGDKkeAHKLKEDFRLHFR 374
Cdd:COG5061   231 FYFNYALVRSALGKI-----DVDLSSFTFCPTDKDELSGKLSSLISAIRAQGKTFNEIQPFALEK--SIQLKDRFREHFR 303
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840394227 375 NISRIMDCVGCFKCRLWGKLQTQGLGTALKILFSeklianmPESGpsyEFHLTRQEIVSLFNAFGRISTSVKELENFRNL 454
Cdd:COG5061   304 DVSRLMDCVGCEKCRLWGKIQTTGYGTALKILFE-------SETQ---LFDLRSLERVALVNTFDRLSVSVREATFENIL 373

                  ....
gi 1840394227 455 LQNI 458
Cdd:COG5061   374 LRSY 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.
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