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Conserved domains on  [gi|568995071|ref|XP_006522070|]
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ubiquitin recognition factor in ER-associated degradation protein 1 isoform X3 [Mus musculus]

Protein Classification

ubiquitin fusion degradation UFD1 family protein( domain architecture ID 10504432)

ubiquitin fusion degradation UFD1 family protein similar to human ubiquitin recognition factor in ER-associated degradation protein 1 (UFD1), an essential component of the ubiquitin-dependent proteolytic pathway which degrades ubiquitin fusion proteins

Gene Ontology:  GO:0006511

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
UFD1 pfam03152
Ubiquitin fusion degradation protein UFD1; Post-translational ubiquitin-protein conjugates are ...
3-149 1.06e-107

Ubiquitin fusion degradation protein UFD1; Post-translational ubiquitin-protein conjugates are recognized for degradation by the ubiquitin fusion degradation (UFD) pathway. Several proteins involved in this pathway have been identified. This family includes UFD1, a 40kD protein that is essential for vegetative cell viability. The human UFD1 gene is expressed at high levels during embryogenesis, especially in the eyes and in the inner ear primordia and is thought to be important in the determination of ectoderm-derived structures, including neural crest cells. In addition, this gene is deleted in the CATCH-22 (cardiac defects, abnormal facies, thymic hypoplasia, cleft palate and hypocalcaemia with deletions on chromosome 22) syndrome. This clinical syndrome is associated with a variety of developmental defects, all characterized by microdeletions on 22q11.2. Two such developmental defects are the DiGeorge syndrome OMIM:188400, and the velo-cardio- facial syndrome OMIM:145410. Several of the abnormalities associated with these conditions are thought to be due to defective neural crest cell differentiation.


:

Pssm-ID: 427169  Cd Length: 174  Bit Score: 308.65  E-value: 1.06e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995071    3 VIMPPSALDQLSRLNITYPMLFKLTNKNSDRMTHCGVLEFVADEGICYLPHWMMQNLLLEEGGLVQVESVNLQVATYSKF 82
Cdd:pfam03152  28 IILPPSALDKLTRLNIEYPMLFELSNPNKEKSTHCGVLEFTAEEGRVYLPYWMMQNLGLQEGDLVQIKSASLPKGTFVKL 107
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568995071   83 QPQSPDFLDITNPKAVLENALRNFACLTTGDVIAINYNEKIYELRVMETKPDKAVSIIECDMNVDFD 149
Cdd:pfam03152 108 QPQSTDFLDISNPKAVLENALRNFSTLTKGDIIAINYNDKIYELDVLEVKPSNAISIIETDLEVDFA 174
 
Name Accession Description Interval E-value
UFD1 pfam03152
Ubiquitin fusion degradation protein UFD1; Post-translational ubiquitin-protein conjugates are ...
3-149 1.06e-107

Ubiquitin fusion degradation protein UFD1; Post-translational ubiquitin-protein conjugates are recognized for degradation by the ubiquitin fusion degradation (UFD) pathway. Several proteins involved in this pathway have been identified. This family includes UFD1, a 40kD protein that is essential for vegetative cell viability. The human UFD1 gene is expressed at high levels during embryogenesis, especially in the eyes and in the inner ear primordia and is thought to be important in the determination of ectoderm-derived structures, including neural crest cells. In addition, this gene is deleted in the CATCH-22 (cardiac defects, abnormal facies, thymic hypoplasia, cleft palate and hypocalcaemia with deletions on chromosome 22) syndrome. This clinical syndrome is associated with a variety of developmental defects, all characterized by microdeletions on 22q11.2. Two such developmental defects are the DiGeorge syndrome OMIM:188400, and the velo-cardio- facial syndrome OMIM:145410. Several of the abnormalities associated with these conditions are thought to be due to defective neural crest cell differentiation.


Pssm-ID: 427169  Cd Length: 174  Bit Score: 308.65  E-value: 1.06e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995071    3 VIMPPSALDQLSRLNITYPMLFKLTNKNSDRMTHCGVLEFVADEGICYLPHWMMQNLLLEEGGLVQVESVNLQVATYSKF 82
Cdd:pfam03152  28 IILPPSALDKLTRLNIEYPMLFELSNPNKEKSTHCGVLEFTAEEGRVYLPYWMMQNLGLQEGDLVQIKSASLPKGTFVKL 107
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568995071   83 QPQSPDFLDITNPKAVLENALRNFACLTTGDVIAINYNEKIYELRVMETKPDKAVSIIECDMNVDFD 149
Cdd:pfam03152 108 QPQSTDFLDISNPKAVLENALRNFSTLTKGDIIAINYNDKIYELDVLEVKPSNAISIIETDLEVDFA 174
UFD1 COG5140
Ubiquitin fusion-degradation protein [Posttranslational modification, protein turnover, ...
3-259 6.95e-70

Ubiquitin fusion-degradation protein [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227469  Cd Length: 331  Bit Score: 218.27  E-value: 6.95e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995071   3 VIMPPSALDQLSRLNITYPMLFKLTNKNSDRMTHCGVLEFVADEGICYLPHWMMQNLLLEEGGLVQVESVNLQVATYSKF 82
Cdd:COG5140   48 VILPPSALVKLSSLNIQYPMLFEISHSDGIYRTHGGVLEFIAEEGRVYLPSWMMQTLSMEPGDLVVLRYTDFPLGKFVKL 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995071  83 QPQSPDFLDITNPKAVLENALRNFACLTTGDVIAINYNEKIYELRVMETKPD---KAVSIIECDMNVDFDAPLGYKEPER 159
Cdd:COG5140  128 IPQSVDFLDIEDPKAVLENCLRNFSTLTEGDEIEIQYNDEVGSIKFTVVHPEpsaNAIYVVETDLVVDFLPPIGYKEKAQ 207
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995071 160 PVQHEESIEGEA------DHSGYAGEVGFRAFSGSGNRLDGKKKGVEPSPSpIKPGDIKRGIPNYEFKLGKITFirnSRP 233
Cdd:COG5140  208 QDKERNSFGVQGtmatyiEYIDSSHDVKPILMKGLGLYLYGKVDKAEPKQD-IKDMKIDGEPAKLDLPEGQLFF---GFP 283
                        250       260
                 ....*....|....*....|....*...
gi 568995071 234 LV--KKVEEDEAGGRFIAFSGEGQSLRK 259
Cdd:COG5140  284 MVlpKEDEESAAKSSEQNFQGQGISLRK 311
PLN03086 PLN03086
PRLI-interacting factor K; Provisional
5-151 4.14e-31

PRLI-interacting factor K; Provisional


Pssm-ID: 178635 [Multi-domain]  Cd Length: 567  Bit Score: 120.75  E-value: 4.14e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995071   5 MPPSALDQLSRLNI--TYPMLFKLT-----------NKNSDRMTHCGVLEFVADEGICYLPHWMMQNLLLE---EGGLVQ 68
Cdd:PLN03086  96 LPPSCFTELSDQGAfdKGPLYFRLSvvhqegsgemkDTDSQKTTHSGVLEFTAEEGSVGLPPHVWSNLFPSdppDVPLVE 175
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995071  69 VESVNLQVATYSKFQPQSPDFLDITNPKAVLENALRNFACLTTGDVIAINYNEKIYELRVMETKPDKAVSIIECDMNVDF 148
Cdd:PLN03086 176 VRYIWLPKGTYAKLQPDGVGFSDLPNHKAVLETALRQHATLSEDDVLVVNYGQLTYKLKVLELKPASSVSVLETDIEVDI 255

                 ...
gi 568995071 149 DAP 151
Cdd:PLN03086 256 VGP 258
 
Name Accession Description Interval E-value
UFD1 pfam03152
Ubiquitin fusion degradation protein UFD1; Post-translational ubiquitin-protein conjugates are ...
3-149 1.06e-107

Ubiquitin fusion degradation protein UFD1; Post-translational ubiquitin-protein conjugates are recognized for degradation by the ubiquitin fusion degradation (UFD) pathway. Several proteins involved in this pathway have been identified. This family includes UFD1, a 40kD protein that is essential for vegetative cell viability. The human UFD1 gene is expressed at high levels during embryogenesis, especially in the eyes and in the inner ear primordia and is thought to be important in the determination of ectoderm-derived structures, including neural crest cells. In addition, this gene is deleted in the CATCH-22 (cardiac defects, abnormal facies, thymic hypoplasia, cleft palate and hypocalcaemia with deletions on chromosome 22) syndrome. This clinical syndrome is associated with a variety of developmental defects, all characterized by microdeletions on 22q11.2. Two such developmental defects are the DiGeorge syndrome OMIM:188400, and the velo-cardio- facial syndrome OMIM:145410. Several of the abnormalities associated with these conditions are thought to be due to defective neural crest cell differentiation.


Pssm-ID: 427169  Cd Length: 174  Bit Score: 308.65  E-value: 1.06e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995071    3 VIMPPSALDQLSRLNITYPMLFKLTNKNSDRMTHCGVLEFVADEGICYLPHWMMQNLLLEEGGLVQVESVNLQVATYSKF 82
Cdd:pfam03152  28 IILPPSALDKLTRLNIEYPMLFELSNPNKEKSTHCGVLEFTAEEGRVYLPYWMMQNLGLQEGDLVQIKSASLPKGTFVKL 107
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568995071   83 QPQSPDFLDITNPKAVLENALRNFACLTTGDVIAINYNEKIYELRVMETKPDKAVSIIECDMNVDFD 149
Cdd:pfam03152 108 QPQSTDFLDISNPKAVLENALRNFSTLTKGDIIAINYNDKIYELDVLEVKPSNAISIIETDLEVDFA 174
UFD1 COG5140
Ubiquitin fusion-degradation protein [Posttranslational modification, protein turnover, ...
3-259 6.95e-70

Ubiquitin fusion-degradation protein [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227469  Cd Length: 331  Bit Score: 218.27  E-value: 6.95e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995071   3 VIMPPSALDQLSRLNITYPMLFKLTNKNSDRMTHCGVLEFVADEGICYLPHWMMQNLLLEEGGLVQVESVNLQVATYSKF 82
Cdd:COG5140   48 VILPPSALVKLSSLNIQYPMLFEISHSDGIYRTHGGVLEFIAEEGRVYLPSWMMQTLSMEPGDLVVLRYTDFPLGKFVKL 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995071  83 QPQSPDFLDITNPKAVLENALRNFACLTTGDVIAINYNEKIYELRVMETKPD---KAVSIIECDMNVDFDAPLGYKEPER 159
Cdd:COG5140  128 IPQSVDFLDIEDPKAVLENCLRNFSTLTEGDEIEIQYNDEVGSIKFTVVHPEpsaNAIYVVETDLVVDFLPPIGYKEKAQ 207
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995071 160 PVQHEESIEGEA------DHSGYAGEVGFRAFSGSGNRLDGKKKGVEPSPSpIKPGDIKRGIPNYEFKLGKITFirnSRP 233
Cdd:COG5140  208 QDKERNSFGVQGtmatyiEYIDSSHDVKPILMKGLGLYLYGKVDKAEPKQD-IKDMKIDGEPAKLDLPEGQLFF---GFP 283
                        250       260
                 ....*....|....*....|....*...
gi 568995071 234 LV--KKVEEDEAGGRFIAFSGEGQSLRK 259
Cdd:COG5140  284 MVlpKEDEESAAKSSEQNFQGQGISLRK 311
PLN03086 PLN03086
PRLI-interacting factor K; Provisional
5-151 4.14e-31

PRLI-interacting factor K; Provisional


Pssm-ID: 178635 [Multi-domain]  Cd Length: 567  Bit Score: 120.75  E-value: 4.14e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995071   5 MPPSALDQLSRLNI--TYPMLFKLT-----------NKNSDRMTHCGVLEFVADEGICYLPHWMMQNLLLE---EGGLVQ 68
Cdd:PLN03086  96 LPPSCFTELSDQGAfdKGPLYFRLSvvhqegsgemkDTDSQKTTHSGVLEFTAEEGSVGLPPHVWSNLFPSdppDVPLVE 175
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995071  69 VESVNLQVATYSKFQPQSPDFLDITNPKAVLENALRNFACLTTGDVIAINYNEKIYELRVMETKPDKAVSIIECDMNVDF 148
Cdd:PLN03086 176 VRYIWLPKGTYAKLQPDGVGFSDLPNHKAVLETALRQHATLSEDDVLVVNYGQLTYKLKVLELKPASSVSVLETDIEVDI 255

                 ...
gi 568995071 149 DAP 151
Cdd:PLN03086 256 VGP 258
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
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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