UBC6_DEBHA
ID UBC6_DEBHA Reviewed; 242 AA.
AC Q6BYG4;
DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 25-MAY-2022, entry version 104.
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=DEHA2A09746g;
OS Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX NCBI_TaxID=284592;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
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; CR382133; CAG84716.2; -; Genomic_DNA.
DR RefSeq; XP_456755.2; XM_456755.1.
DR AlphaFoldDB; Q6BYG4; -.
DR SMR; Q6BYG4; -.
DR STRING; 4959.XP_456755.2; -.
DR EnsemblFungi; CAG84716; CAG84716; DEHA2A09746g.
DR GeneID; 2899547; -.
DR KEGG; dha:DEHA2A09746g; -.
DR VEuPathDB; FungiDB:DEHA2A09746g; -.
DR eggNOG; KOG0894; Eukaryota.
DR HOGENOM; CLU_041481_1_0_1; -.
DR InParanoid; Q6BYG4; -.
DR OMA; RPPSIYM; -.
DR OrthoDB; 1230974at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000000599; Chromosome A.
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 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_0000082549"
FT TOPO_DOM 1..220
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 221..240
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 5..156
FT /note="UBC core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT REGION 170..190
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 87
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
SQ SEQUENCE 242 AA; 27282 MW; 881A9D61E0F7F02E CRC64;
MASRQSQKRL TKEYKAITLN PPPYVSAKPN DENILEWHYV ITGPPHTPFE EGQYHGILRF
PSEYPFKPPS ISMITPNGRF ACNTRLCLSM SDYHPDTWNP AWSVATILTG LLSFMTGDES
TTGSITTSDN VKKRLARSSK EWNNAENQRF TKQFPDLVAQ NKVDVAARNA REQAAATTDS
TDPEKPFDVR ENIDSLDPED RARLLVEQDD HSTPSFGVQR FTLVGVVVAA FIAAYFNFFS
RT
