ID   UBC6_CANGA              Reviewed;         246 AA.
AC   Q6FQK7;
DT   24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 113.
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=CAGL0I05478g;
OS   Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS   Y-65) (Yeast) (Torulopsis glabrata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC   Nakaseomyces/Candida clade.
OX   NCBI_TaxID=284593;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
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; CR380955; CAG60424.1; -; Genomic_DNA.
DR   RefSeq; XP_447487.1; XM_447487.1.
DR   AlphaFoldDB; Q6FQK7; -.
DR   SMR; Q6FQK7; -.
DR   STRING; 5478.XP_447487.1; -.
DR   EnsemblFungi; CAG60424; CAG60424; CAGL0I05478g.
DR   GeneID; 2889269; -.
DR   KEGG; cgr:CAGL0I05478g; -.
DR   CGD; CAL0132568; CAGL0I05478g.
DR   VEuPathDB; FungiDB:CAGL0I05478g; -.
DR   eggNOG; KOG0894; Eukaryota.
DR   HOGENOM; CLU_041481_1_0_1; -.
DR   InParanoid; Q6FQK7; -.
DR   OMA; RPPSIYM; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000002428; Chromosome I.
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..246
FT                   /note="Ubiquitin-conjugating enzyme E2 6"
FT                   /id="PRO_0000082548"
FT   TOPO_DOM        1..224
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        225..245
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          5..154
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   246 AA;  28400 MW;  0A7EC968C091001A CRC64;
     MATKQAQKRL TKEYKMMVEN PPPFIIARPN EENILEWHYV ISGPPDTPYD GGQYHGTLTF
     PSDYPYKPPA IRMITPNGRF KENTRLCLSM SDYHPDTWNP GWSVATILNG LLSFMTGDES
     TTGSITTTQQ EKKILAKKSM YYNTFNSTRF KLVFPEIVEK NITELQRRKQ EEKDMSMFEK
     KEDPLVKAAR EKAIEVKDIV NPEDRIRAEQ ALKELEKQHN DKPNGSSSMF YIGVALFLFL
     VGLFMK