UBC6_KLULA
ID UBC6_KLULA Reviewed; 251 AA.
AC Q6CMG6;
DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-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=KLLA0E20493g;
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
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; CR382125; CAG99960.1; -; Genomic_DNA.
DR RefSeq; XP_454873.1; XM_454873.1.
DR AlphaFoldDB; Q6CMG6; -.
DR SMR; Q6CMG6; -.
DR STRING; 28985.XP_454873.1; -.
DR EnsemblFungi; CAG99960; CAG99960; KLLA0_E20395g.
DR GeneID; 2894674; -.
DR KEGG; kla:KLLA0_E20395g; -.
DR eggNOG; KOG0894; Eukaryota.
DR HOGENOM; CLU_041481_1_0_1; -.
DR InParanoid; Q6CMG6; -.
DR OMA; RPPSIYM; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000000598; Chromosome E.
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..251
FT /note="Ubiquitin-conjugating enzyme E2 6"
FT /id="PRO_0000082550"
FT TOPO_DOM 1..229
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 230..250
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 5..154
FT /note="UBC core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT REGION 173..200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 173..188
FT /note="Basic and acidic residues"
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 251 AA; 28423 MW; 621A26720595608B CRC64;
MASIQANKRL TKEYKNIVNN PPPFIIAAPH EDNILEWHYV ITGPPSTPYE NGQYHGTLTF
PSDYPFNPPA IRMITPNGRF KENTRLCLSM SDYHPEAWNP AWSVVTILNG LLSFMTGDEQ
TTGSVSTSDK DKRTLAKKSK HFNTYSNFKF KNMFPDLRES NIKDIEREAA LEAESKGAQQ
EENKAQKLAT EKATSLDDIS DPEDRVRIQE LIKAEKDKKD QDKNPGENSN IKSLLCLILA
IAIFFVGLIM K
