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Conserved domains on  [gi|17539898|ref|NP_502348|]
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Ubiquitin fusion degradation protein 1 homolog [Caenorhabditis elegans]

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

CATH:  3.10.330.10|2.40.40.50
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 ...
 21-196 7.96e-93

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: 460828  Cd Length: 174  Bit Score: 273.98  E-value: 7.96e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539898    21 YDQTFVVYGPVFLPNAtqSKISEINYGGKILLPSSALNLLMQYNIPMPMLFKLTNMAVQRVTHCGVLEFSAPEGQAILPL 100
Cdd:pfam03152   1 FDEYYRCYPVSMLDKG--NEREDLNYGGKIILPPSALDKLTRLNIEYPMLFELSNPNKEKSTHCGVLEFTAEEGRVYLPY 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539898   101 WMMQQLGLDDGDTIRIESATLPKATFAKLKPMSLEFLNITNPKAVLEVELRKYACLTKNDRIPTSYAGQTLEFLVVDLKP 180
Cdd:pfam03152  79 WMMQNLGLQEGDLVQIKSASLPKGTFVKLQPQSTDFLDISNPKAVLENALRNFSTLTKGDIIAINYNDKIYELDVLEVKP 158

                         170
                  ....*....|....*.
gi 17539898   181 ANSVCIIECDVNLDFD 196
Cdd:pfam03152 159 SNAISIIETDLEVDFA 174
 
Name Accession Description Interval E-value
UFD1 pfam03152
Ubiquitin fusion degradation protein UFD1; Post-translational ubiquitin-protein conjugates are ...
 21-196 7.96e-93

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: 460828  Cd Length: 174  Bit Score: 273.98  E-value: 7.96e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539898    21 YDQTFVVYGPVFLPNAtqSKISEINYGGKILLPSSALNLLMQYNIPMPMLFKLTNMAVQRVTHCGVLEFSAPEGQAILPL 100
Cdd:pfam03152   1 FDEYYRCYPVSMLDKG--NEREDLNYGGKIILPPSALDKLTRLNIEYPMLFELSNPNKEKSTHCGVLEFTAEEGRVYLPY 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539898   101 WMMQQLGLDDGDTIRIESATLPKATFAKLKPMSLEFLNITNPKAVLEVELRKYACLTKNDRIPTSYAGQTLEFLVVDLKP 180
Cdd:pfam03152  79 WMMQNLGLQEGDLVQIKSASLPKGTFVKLQPQSTDFLDISNPKAVLENALRNFSTLTKGDIIAINYNDKIYELDVLEVKP 158

                         170
                  ....*....|....*.
gi 17539898   181 ANSVCIIECDVNLDFD 196
Cdd:pfam03152 159 SNAISIIETDLEVDFA 174
UFD1 COG5140
Ubiquitin fusion-degradation protein [Posttranslational modification, protein turnover, ...
 44-207 5.08e-59

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


Pssm-ID: 227469  Cd Length: 331  Bit Score: 193.23  E-value: 5.08e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539898  44 INYGGKILLPSSALNLLMQYNIPMPMLFKLTNMAVQRVTHCGVLEFSAPEGQAILPLWMMQQLGLDDGDTIRIESATLPK 123
Cdd:COG5140  42 ANFGGKVILPPSALVKLSSLNIQYPMLFEISHSDGIYRTHGGVLEFIAEEGRVYLPSWMMQTLSMEPGDLVVLRYTDFPL 121

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539898 124 ATFAKLKPMSLEFLNITNPKAVLEVELRKYACLTKNDRIPTSYAGQTLEFLVVDLKP---ANSVCIIECDVNLDFDPPEG 200
Cdd:COG5140 122 GKFVKLIPQSVDFLDIEDPKAVLENCLRNFSTLTEGDEIEIQYNDEVGSIKFTVVHPepsANAIYVVETDLVVDFLPPIG 201


                ....*..
gi 17539898 201 YVEQPRQ 207
Cdd:COG5140 202 YKEKAQQ 208
PLN03086 PLN03086
PRLI-interacting factor K; Provisional
 47-215 7.65e-26

PRLI-interacting factor K; Provisional


Pssm-ID: 178635 [Multi-domain]  Cd Length: 567  Bit Score: 108.04  E-value: 7.65e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539898   47 GGKILLPSSALNLLMQYNI--PMPMLFKLT-----------NMAVQRVTHCGVLEFSAPEGQAILPLWMMQQL---GLDD 110
Cdd:PLN03086  91 GDKIKLPPSCFTELSDQGAfdKGPLYFRLSvvhqegsgemkDTDSQKTTHSGVLEFTAEEGSVGLPPHVWSNLfpsDPPD 170

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539898  111 GDTIRIESATLPKATFAKLKPMSLEFLNITNPKAVLEVELRKYACLTKNDRIPTSYAGQTLEFLVVDLKPANSVCIIECD 190
Cdd:PLN03086 171 VPLVEVRYIWLPKGTYAKLQPDGVGFSDLPNHKAVLETALRQHATLSEDDVLVVNYGQLTYKLKVLELKPASSVSVLETD 250

                        170       180
                 ....*....|....*....|....*..
gi 17539898  191 VNLDFDPPEGYVEQPRQ--VTPAVTAK 215
Cdd:PLN03086 251 IEVDIVGPDSVSNEENQhvLKPLEFGK 277
 
Name Accession Description Interval E-value
UFD1 pfam03152
Ubiquitin fusion degradation protein UFD1; Post-translational ubiquitin-protein conjugates are ...
 21-196 7.96e-93

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: 460828  Cd Length: 174  Bit Score: 273.98  E-value: 7.96e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539898    21 YDQTFVVYGPVFLPNAtqSKISEINYGGKILLPSSALNLLMQYNIPMPMLFKLTNMAVQRVTHCGVLEFSAPEGQAILPL 100
Cdd:pfam03152   1 FDEYYRCYPVSMLDKG--NEREDLNYGGKIILPPSALDKLTRLNIEYPMLFELSNPNKEKSTHCGVLEFTAEEGRVYLPY 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539898   101 WMMQQLGLDDGDTIRIESATLPKATFAKLKPMSLEFLNITNPKAVLEVELRKYACLTKNDRIPTSYAGQTLEFLVVDLKP 180
Cdd:pfam03152  79 WMMQNLGLQEGDLVQIKSASLPKGTFVKLQPQSTDFLDISNPKAVLENALRNFSTLTKGDIIAINYNDKIYELDVLEVKP 158

                         170
                  ....*....|....*.
gi 17539898   181 ANSVCIIECDVNLDFD 196
Cdd:pfam03152 159 SNAISIIETDLEVDFA 174
UFD1 COG5140
Ubiquitin fusion-degradation protein [Posttranslational modification, protein turnover, ...
 44-207 5.08e-59

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


Pssm-ID: 227469  Cd Length: 331  Bit Score: 193.23  E-value: 5.08e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539898  44 INYGGKILLPSSALNLLMQYNIPMPMLFKLTNMAVQRVTHCGVLEFSAPEGQAILPLWMMQQLGLDDGDTIRIESATLPK 123
Cdd:COG5140  42 ANFGGKVILPPSALVKLSSLNIQYPMLFEISHSDGIYRTHGGVLEFIAEEGRVYLPSWMMQTLSMEPGDLVVLRYTDFPL 121

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539898 124 ATFAKLKPMSLEFLNITNPKAVLEVELRKYACLTKNDRIPTSYAGQTLEFLVVDLKP---ANSVCIIECDVNLDFDPPEG 200
Cdd:COG5140 122 GKFVKLIPQSVDFLDIEDPKAVLENCLRNFSTLTEGDEIEIQYNDEVGSIKFTVVHPepsANAIYVVETDLVVDFLPPIG 201


                ....*..
gi 17539898 201 YVEQPRQ 207
Cdd:COG5140 202 YKEKAQQ 208
PLN03086 PLN03086
PRLI-interacting factor K; Provisional
 47-215 7.65e-26

PRLI-interacting factor K; Provisional


Pssm-ID: 178635 [Multi-domain]  Cd Length: 567  Bit Score: 108.04  E-value: 7.65e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539898   47 GGKILLPSSALNLLMQYNI--PMPMLFKLT-----------NMAVQRVTHCGVLEFSAPEGQAILPLWMMQQL---GLDD 110
Cdd:PLN03086  91 GDKIKLPPSCFTELSDQGAfdKGPLYFRLSvvhqegsgemkDTDSQKTTHSGVLEFTAEEGSVGLPPHVWSNLfpsDPPD 170

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539898  111 GDTIRIESATLPKATFAKLKPMSLEFLNITNPKAVLEVELRKYACLTKNDRIPTSYAGQTLEFLVVDLKPANSVCIIECD 190
Cdd:PLN03086 171 VPLVEVRYIWLPKGTYAKLQPDGVGFSDLPNHKAVLETALRQHATLSEDDVLVVNYGQLTYKLKVLELKPASSVSVLETD 250

                        170       180
                 ....*....|....*....|....*..
gi 17539898  191 VNLDFDPPEGYVEQPRQ--VTPAVTAK 215
Cdd:PLN03086 251 IEVDIVGPDSVSNEENQhvLKPLEFGK 277
 
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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