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Conserved domains on  [gi|1840394178|ref|NP_001369403|]
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ERO1-like protein alpha isoform 12 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 ...
60-389 1.38e-150

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: 429.68  E-value: 1.38e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840394178  60 IEECE--------QAERLGAVDESLS--EETQKAVLQWTKHDDSSD-NFCEADDIQSPEAEYVDLLLNPERYTGYKGPDA 128
Cdd:pfam04137  43 VCTCDeseipepwRAEELGKLEGTLAkhDVGESCVVEWDDECDADDdDYCVLDDENDSEGVYVDLLLNPERFTGYSGPSA 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840394178 129 WKIWNVIYEENCFKPQTikrplnplasgqgtSEENTFYSWLEGLCVEKRAFYRLISGLHASINVHLSARYLLQETwleKK 208
Cdd:pfam04137 123 HRIWRAIYEENCFQPST--------------ESLSEDSLELDGECLEKRVFYRLISGLHASISTHLCNEYLNQET---GE 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840394178 209 WGHNITEFQQRFdgilteGEGPRRLKNLYFLYLIELRALSKVLPFFERPDFqlFTGNKIQDEENKMLLLEILHEI-KSFP 287
Cdd:pfam04137 186 WGPNLECFMERV------GNHPERLENLYFNYALVLRALAKLAPYLENYDF--CTGDPEEDAETKALIKDILSSLtSIVP 257
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840394178 288 LHFDENSFFAGDkkEAHKLKEDFRLHFRNISRIMDCVGCFKCRLWGKLQTQGLGTALKILFSEKlianmPESGPSYEFHL 367
Cdd:pfam04137 258 PIFDESLLFKDE--EAPELKEEFRNRFRNVSRIMDCVGCDKCRLWGKLQTTGLGTALKILFELD-----ENDEEDNPLKL 330
                         330       340
                  ....*....|....*....|..
gi 1840394178 368 TRQEIVSLFNAFGRISTSVKEL 389
Cdd:pfam04137 331 RRNELVALFNTFDRLSESIEAI 352
 
Name Accession Description Interval E-value
ERO1 pfam04137
Endoplasmic Reticulum Oxidoreductin 1 (ERO1); Members of this family are required for the ...
60-389 1.38e-150

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: 429.68  E-value: 1.38e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840394178  60 IEECE--------QAERLGAVDESLS--EETQKAVLQWTKHDDSSD-NFCEADDIQSPEAEYVDLLLNPERYTGYKGPDA 128
Cdd:pfam04137  43 VCTCDeseipepwRAEELGKLEGTLAkhDVGESCVVEWDDECDADDdDYCVLDDENDSEGVYVDLLLNPERFTGYSGPSA 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840394178 129 WKIWNVIYEENCFKPQTikrplnplasgqgtSEENTFYSWLEGLCVEKRAFYRLISGLHASINVHLSARYLLQETwleKK 208
Cdd:pfam04137 123 HRIWRAIYEENCFQPST--------------ESLSEDSLELDGECLEKRVFYRLISGLHASISTHLCNEYLNQET---GE 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840394178 209 WGHNITEFQQRFdgilteGEGPRRLKNLYFLYLIELRALSKVLPFFERPDFqlFTGNKIQDEENKMLLLEILHEI-KSFP 287
Cdd:pfam04137 186 WGPNLECFMERV------GNHPERLENLYFNYALVLRALAKLAPYLENYDF--CTGDPEEDAETKALIKDILSSLtSIVP 257
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840394178 288 LHFDENSFFAGDkkEAHKLKEDFRLHFRNISRIMDCVGCFKCRLWGKLQTQGLGTALKILFSEKlianmPESGPSYEFHL 367
Cdd:pfam04137 258 PIFDESLLFKDE--EAPELKEEFRNRFRNVSRIMDCVGCDKCRLWGKLQTTGLGTALKILFELD-----ENDEEDNPLKL 330
                         330       340
                  ....*....|....*....|..
gi 1840394178 368 TRQEIVSLFNAFGRISTSVKEL 389
Cdd:pfam04137 331 RRNELVALFNTFDRLSESIEAI 352
ERO1 COG5061
Oxidoreductin, endoplasmic reticulum membrane-associated protein involved in disulfide bond ...
86-399 1.30e-70

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: 227.85  E-value: 1.30e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840394178  86 QWTKHDDssDNFCEADDIQSPEAEYVDLLLNPERYTGYKGPDAWKIWNVIYEENCFKpqtikrplnplasgqgtseentf 165
Cdd:COG5061   116 SESKCPD--LSYCYVDNKSIFNDVYISLLENPERFTGYKGNHSAEIWRKIYEQNCFD----------------------- 170
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840394178 166 ySWLEGLCVEKRAFYRLISGLHASINVHLSARYLLQETwleKKWGHNITEFQQRFdgilteGEGPRRLKNLYFLYLIELR 245
Cdd:COG5061   171 -TLLPPTLLEKRMFYRLVSGFHASISTHLSSFYLNVFF---GTWLPNLDLFRARV------GNFPDRIENFYFNYALVRS 240
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840394178 246 ALSKVlpffeRPDFQLFTGNKIQDEENKMLLLEILHEIKSFPLHFDENSFFAGDKkeAHKLKEDFRLHFRNISRIMDCVG 325
Cdd:COG5061   241 ALGKI-----DVDLSSFTFCPTDKDELSGKLSSLISAIRAQGKTFNEIQPFALEK--SIQLKDRFREHFRDVSRLMDCVG 313
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1840394178 326 CFKCRLWGKLQTQGLGTALKILFSeklianmPESGpsyEFHLTRQEIVSLFNAFGRISTSVKELENFRNLLQNI 399
Cdd:COG5061   314 CEKCRLWGKIQTTGYGTALKILFE-------SETQ---LFDLRSLERVALVNTFDRLSVSVREATFENILLRSY 377
envZ PRK09467
osmolarity sensor protein; Provisional
356-396 8.35e-03

osmolarity sensor protein; Provisional


Pssm-ID: 236531 [Multi-domain]  Cd Length: 435  Bit Score: 37.97  E-value: 8.35e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1840394178 356 MPESGPSyefhltrqEIVSLFNAFGRISTSVKELENFRNLL 396
Cdd:PRK09467  200 LREYGAS--------EVRSVTRAFNQMAAGIKQLEDDRTLL 232
 
Name Accession Description Interval E-value
ERO1 pfam04137
Endoplasmic Reticulum Oxidoreductin 1 (ERO1); Members of this family are required for the ...
60-389 1.38e-150

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: 429.68  E-value: 1.38e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840394178  60 IEECE--------QAERLGAVDESLS--EETQKAVLQWTKHDDSSD-NFCEADDIQSPEAEYVDLLLNPERYTGYKGPDA 128
Cdd:pfam04137  43 VCTCDeseipepwRAEELGKLEGTLAkhDVGESCVVEWDDECDADDdDYCVLDDENDSEGVYVDLLLNPERFTGYSGPSA 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840394178 129 WKIWNVIYEENCFKPQTikrplnplasgqgtSEENTFYSWLEGLCVEKRAFYRLISGLHASINVHLSARYLLQETwleKK 208
Cdd:pfam04137 123 HRIWRAIYEENCFQPST--------------ESLSEDSLELDGECLEKRVFYRLISGLHASISTHLCNEYLNQET---GE 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840394178 209 WGHNITEFQQRFdgilteGEGPRRLKNLYFLYLIELRALSKVLPFFERPDFqlFTGNKIQDEENKMLLLEILHEI-KSFP 287
Cdd:pfam04137 186 WGPNLECFMERV------GNHPERLENLYFNYALVLRALAKLAPYLENYDF--CTGDPEEDAETKALIKDILSSLtSIVP 257
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840394178 288 LHFDENSFFAGDkkEAHKLKEDFRLHFRNISRIMDCVGCFKCRLWGKLQTQGLGTALKILFSEKlianmPESGPSYEFHL 367
Cdd:pfam04137 258 PIFDESLLFKDE--EAPELKEEFRNRFRNVSRIMDCVGCDKCRLWGKLQTTGLGTALKILFELD-----ENDEEDNPLKL 330
                         330       340
                  ....*....|....*....|..
gi 1840394178 368 TRQEIVSLFNAFGRISTSVKEL 389
Cdd:pfam04137 331 RRNELVALFNTFDRLSESIEAI 352
ERO1 COG5061
Oxidoreductin, endoplasmic reticulum membrane-associated protein involved in disulfide bond ...
86-399 1.30e-70

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: 227.85  E-value: 1.30e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840394178  86 QWTKHDDssDNFCEADDIQSPEAEYVDLLLNPERYTGYKGPDAWKIWNVIYEENCFKpqtikrplnplasgqgtseentf 165
Cdd:COG5061   116 SESKCPD--LSYCYVDNKSIFNDVYISLLENPERFTGYKGNHSAEIWRKIYEQNCFD----------------------- 170
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840394178 166 ySWLEGLCVEKRAFYRLISGLHASINVHLSARYLLQETwleKKWGHNITEFQQRFdgilteGEGPRRLKNLYFLYLIELR 245
Cdd:COG5061   171 -TLLPPTLLEKRMFYRLVSGFHASISTHLSSFYLNVFF---GTWLPNLDLFRARV------GNFPDRIENFYFNYALVRS 240
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840394178 246 ALSKVlpffeRPDFQLFTGNKIQDEENKMLLLEILHEIKSFPLHFDENSFFAGDKkeAHKLKEDFRLHFRNISRIMDCVG 325
Cdd:COG5061   241 ALGKI-----DVDLSSFTFCPTDKDELSGKLSSLISAIRAQGKTFNEIQPFALEK--SIQLKDRFREHFRDVSRLMDCVG 313
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1840394178 326 CFKCRLWGKLQTQGLGTALKILFSeklianmPESGpsyEFHLTRQEIVSLFNAFGRISTSVKELENFRNLLQNI 399
Cdd:COG5061   314 CEKCRLWGKIQTTGYGTALKILFE-------SETQ---LFDLRSLERVALVNTFDRLSVSVREATFENILLRSY 377
envZ PRK09467
osmolarity sensor protein; Provisional
356-396 8.35e-03

osmolarity sensor protein; Provisional


Pssm-ID: 236531 [Multi-domain]  Cd Length: 435  Bit Score: 37.97  E-value: 8.35e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1840394178 356 MPESGPSyefhltrqEIVSLFNAFGRISTSVKELENFRNLL 396
Cdd:PRK09467  200 LREYGAS--------EVRSVTRAFNQMAAGIKQLEDDRTLL 232
 
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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