NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|61212142|sp|Q9NT62|]
View 

RecName: Full=Ubiquitin-like-conjugating enzyme ATG3; AltName: Full=Autophagy-related protein 3; Short=APG3-like; Short=hApg3; AltName: Full=Protein PC3-96

Protein Classification

ATG3/ATG10 family protein( domain architecture ID 10512533)

ATG3/ATG10 family protein similar to ubiquitin-like-conjugating enzymes ATG3 and ATG10, which are E2 conjugating enzymes required for the cytoplasm to vacuole transport (Cvt), and autophagy

CATH:  3.30.1460.50
Gene Ontology:  GO:0019787|GO:0015031|GO:0006914|GO:0019776
PubMed:  20723759|23142976|23255127
SCOP:  3000727

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
Autophagy_act_C pfam03987
Autophagocytosis associated protein, active-site domain; Autophagocytosis is a ...
 159-308 1.72e-51

Autophagocytosis associated protein, active-site domain; Autophagocytosis is a starvation-induced process responsible for transport of cytoplasmic proteins to the vacuole. The cysteine residue within the HPC motif is the putative active-site residue for recognition of the Apg5 subunit of the autophagosome complex.


:

Pssm-ID: 461120  Cd Length: 151  Bit Score: 166.74  E-value: 1.72e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61212142   159 EYEESGLLETDEATLDTRKIVEACKAKTDAGGEDAILQT-----RTYDLYITYDKYYQTPRLWLFGYDEQRQPLTVEHMY 233
Cdd:pfam03987   1 EFVAAGDALVRKSPRDTWKWPKKRRDYLPKDEEKQYLITrnvpcRTYDYHITYSPSYQVPVLYFRGYDEDGKPLSLDEVY 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 61212142   234 EDISQDHVKKTVTIENHPHLpPPPMCSVHPCRHAEVMKKIIEtvaEGGGELGVHMYLLIFLKFVQAVIPTIEYDY 308
Cdd:pfam03987  81 EDISPDYANKTVTQEEHPHL-GLPWFSIHPCKTAEVMKTLLE---DGGKEIRVDQYLVIWLSFVGSVVPLIEPDY 151
 
Name Accession Description Interval E-value
Autophagy_act_C pfam03987
Autophagocytosis associated protein, active-site domain; Autophagocytosis is a ...
 159-308 1.72e-51

Autophagocytosis associated protein, active-site domain; Autophagocytosis is a starvation-induced process responsible for transport of cytoplasmic proteins to the vacuole. The cysteine residue within the HPC motif is the putative active-site residue for recognition of the Apg5 subunit of the autophagosome complex.


Pssm-ID: 461120  Cd Length: 151  Bit Score: 166.74  E-value: 1.72e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61212142   159 EYEESGLLETDEATLDTRKIVEACKAKTDAGGEDAILQT-----RTYDLYITYDKYYQTPRLWLFGYDEQRQPLTVEHMY 233
Cdd:pfam03987   1 EFVAAGDALVRKSPRDTWKWPKKRRDYLPKDEEKQYLITrnvpcRTYDYHITYSPSYQVPVLYFRGYDEDGKPLSLDEVY 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 61212142   234 EDISQDHVKKTVTIENHPHLpPPPMCSVHPCRHAEVMKKIIEtvaEGGGELGVHMYLLIFLKFVQAVIPTIEYDY 308
Cdd:pfam03987  81 EDISPDYANKTVTQEEHPHL-GLPWFSIHPCKTAEVMKTLLE---DGGKEIRVDQYLVIWLSFVGSVVPLIEPDY 151
 
Name Accession Description Interval E-value
Autophagy_act_C pfam03987
Autophagocytosis associated protein, active-site domain; Autophagocytosis is a ...
 159-308 1.72e-51

Autophagocytosis associated protein, active-site domain; Autophagocytosis is a starvation-induced process responsible for transport of cytoplasmic proteins to the vacuole. The cysteine residue within the HPC motif is the putative active-site residue for recognition of the Apg5 subunit of the autophagosome complex.


Pssm-ID: 461120  Cd Length: 151  Bit Score: 166.74  E-value: 1.72e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61212142   159 EYEESGLLETDEATLDTRKIVEACKAKTDAGGEDAILQT-----RTYDLYITYDKYYQTPRLWLFGYDEQRQPLTVEHMY 233
Cdd:pfam03987   1 EFVAAGDALVRKSPRDTWKWPKKRRDYLPKDEEKQYLITrnvpcRTYDYHITYSPSYQVPVLYFRGYDEDGKPLSLDEVY 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 61212142   234 EDISQDHVKKTVTIENHPHLpPPPMCSVHPCRHAEVMKKIIEtvaEGGGELGVHMYLLIFLKFVQAVIPTIEYDY 308
Cdd:pfam03987  81 EDISPDYANKTVTQEEHPHL-GLPWFSIHPCKTAEVMKTLLE---DGGKEIRVDQYLVIWLSFVGSVVPLIEPDY 151
 
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