ID   UBC12_CANGA             Reviewed;         187 AA.
AC   Q6FVQ8;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 101.
DE   RecName: Full=NEDD8-conjugating enzyme UBC12;
DE            EC=2.3.2.34;
DE   AltName: Full=RUB1-conjugating enzyme;
DE   AltName: Full=Ubiquitin carrier protein 12;
GN   Name=UBC12; OrderedLocusNames=CAGL0D06468g;
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: Accepts the ubiquitin-like protein NEDD8/RUB1 from the UBA3-
CC       ULA1 E1 complex and catalyzes its covalent attachment to other
CC       proteins. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[E1 NEDD8-activating enzyme]-S-[NEDD8 protein]-yl-L-cysteine +
CC         [E2 NEDD8-conjugating enzyme]-L-cysteine = [E1 NEDD8-activating
CC         enzyme]-L-cysteine + [E2 NEDD8-conjugating enzyme]-S-[NEDD8-protein]-
CC         yl-L-cysteine.; EC=2.3.2.34;
CC   -!- PATHWAY: Protein modification; protein neddylation.
CC   -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family. UBC12
CC       subfamily. {ECO:0000255|PROSITE-ProRule:PRU00388}.
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DR   EMBL; CR380950; CAG58597.1; -; Genomic_DNA.
DR   RefSeq; XP_445686.1; XM_445686.1.
DR   AlphaFoldDB; Q6FVQ8; -.
DR   SMR; Q6FVQ8; -.
DR   STRING; 5478.XP_445686.1; -.
DR   EnsemblFungi; CAG58597; CAG58597; CAGL0D06468g.
DR   GeneID; 2886969; -.
DR   KEGG; cgr:CAGL0D06468g; -.
DR   CGD; CAL0128479; CAGL0D06468g.
DR   VEuPathDB; FungiDB:CAGL0D06468g; -.
DR   eggNOG; KOG0420; Eukaryota.
DR   HOGENOM; CLU_030988_6_0_1; -.
DR   InParanoid; Q6FVQ8; -.
DR   OMA; KESYFRG; -.
DR   UniPathway; UPA00885; -.
DR   Proteomes; UP000002428; Chromosome D.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0019788; F:NEDD8 transferase activity; IEA:EnsemblFungi.
DR   GO; GO:0045116; P:protein neddylation; IEA:UniProtKB-UniPathway.
DR   CDD; cd00195; UBCc; 1.
DR   Gene3D; 3.10.110.10; -; 1.
DR   InterPro; IPR000608; UBQ-conjugat_E2.
DR   InterPro; IPR023313; UBQ-conjugating_AS.
DR   InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR   Pfam; PF00179; UQ_con; 1.
DR   SUPFAM; SSF54495; SSF54495; 1.
DR   PROSITE; PS00183; UBC_1; 1.
DR   PROSITE; PS50127; UBC_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Nucleotide-binding; Reference proteome; Transferase;
KW   Ubl conjugation pathway.
FT   CHAIN           1..187
FT                   /note="NEDD8-conjugating enzyme UBC12"
FT                   /id="PRO_0000082497"
FT   DOMAIN          32..178
FT                   /note="UBC core"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT   REGION          11..34
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        116
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00388,
FT                   ECO:0000255|PROSITE-ProRule:PRU10133"
SQ   SEQUENCE   187 AA;  21004 MW;  94B94002BFB0AB9C CRC64;
     MLKLRQLQQQ KQQQLAKNAG SSVKANTNST SPAKLRLQKD IEELELPPTV RVNIISLDNH
     KEMSLNIIII PDEGFYKGGK FRFTATFLET YPIDPPKVIC NNKIFHPNID PHGKICLNIL
     REDWSPALDL QCIVLGLLSL FQEPNGNDPL NKEAAEVLNK DKLEFGNLVR LAMSGAMVGS
     TYYECVI