ID   UBC6_ASHGO              Reviewed;         242 AA.
AC   Q74Z34;
DT   24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 114.
DE   RecName: Full=Ubiquitin-conjugating enzyme E2 6;
DE            EC=2.3.2.23;
DE   AltName: Full=E2 ubiquitin-conjugating enzyme 6;
DE   AltName: Full=Ubiquitin carrier protein UBC6;
DE   AltName: Full=Ubiquitin-protein ligase UBC6;
GN   Name=UBC6; OrderedLocusNames=AGR372W;
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
CC   -!- FUNCTION: Catalyzes the covalent attachment of ubiquitin to other
CC       proteins. Functions in degradation of misfolded or regulated proteins
CC       localized in the endoplasmic reticulum (ER) lumen or membrane via the
CC       ubiquitin-proteasome system. Cognate E2 conjugating enzyme for the
CC       DOA10 ubiquitin ligase complex, which is part of the ERAD-C pathway
CC       responsible for the rapid degradation of membrane proteins with
CC       misfolded cytoplasmic domains. {ECO:0000255|PROSITE-ProRule:PRU00388}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine +
CC         [E2 ubiquitin-conjugating enzyme]-L-cysteine = [E1 ubiquitin-
CC         activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-
CC         conjugating enzyme]-L-cysteine.; EC=2.3.2.23;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU00388};
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000255|PROSITE-ProRule:PRU00388}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:Q5VVX9}.
CC   -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00388}.
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DR   EMBL; AE016820; AAS54862.1; -; Genomic_DNA.
DR   RefSeq; NP_987038.1; NM_212100.1.
DR   AlphaFoldDB; Q74Z34; -.
DR   SMR; Q74Z34; -.
DR   STRING; 33169.AAS54862; -.
DR   EnsemblFungi; AAS54862; AAS54862; AGOS_AGR372W.
DR   GeneID; 4623341; -.
DR   KEGG; ago:AGOS_AGR372W; -.
DR   eggNOG; KOG0894; Eukaryota.
DR   HOGENOM; CLU_041481_1_0_1; -.
DR   InParanoid; Q74Z34; -.
DR   OMA; DKMFCEL; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000000591; Chromosome VII.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0061631; F:ubiquitin conjugating enzyme activity; IEA:UniProtKB-EC.
DR   GO; GO:0006513; P:protein monoubiquitination; IEA:EnsemblFungi.
DR   GO; GO:0000209; P:protein polyubiquitination; IEA:EnsemblFungi.
DR   GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IEA:EnsemblFungi.
DR   CDD; cd00195; UBCc; 1.
DR   Gene3D; 3.10.110.10; -; 1.
DR   InterPro; IPR000608; UBQ-conjugat_E2.
DR   InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR   Pfam; PF00179; UQ_con; 1.
DR   SUPFAM; SSF54495; SSF54495; 1.
DR   PROSITE; PS50127; UBC_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Endoplasmic reticulum; Membrane; Nucleotide-binding;
KW   Reference proteome; Transferase; Transmembrane; Transmembrane helix;
KW   Ubl conjugation pathway.
FT   CHAIN           1..242
FT                   /note="Ubiquitin-conjugating enzyme E2 6"
FT                   /id="PRO_0000082547"
FT   TOPO_DOM        1..217
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        218..240
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          5..163
FT                   /note="UBC core"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT   ACT_SITE        87
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
SQ   SEQUENCE   242 AA;  27612 MW;  5F3FC501A5BC21DB CRC64;
     MASRQAYKRL SKEYKMMTEN PPPYIVAAPK EDNILVWHYV ITGPPETPYE DGQYHGTLVF
     PNDYPFNPPA IRMLTPNGRF RENTRLCLSM SDYHPDTWNP SWSVATILTG LLSFMTTDES
     SIGTMESTDS TKRKYAAKSK EHNATRSPIF CQIFPELAEQ NRRDIEEAKK RKDETVVEDE
     HPFKQEQVVS LEEINDPEDR IRAQMLQQPA GNGTTSNSIG RSLLFVLFSL AALLVAVCYT
     RV