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Database: UniProt
Entry: A0A3N4KD16_9PEZI
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ID   A0A3N4KD16_9PEZI        Unreviewed;       166 AA.
AC   A0A3N4KD16;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 14.
DE   RecName: Full=E2 ubiquitin-conjugating enzyme {ECO:0000256|ARBA:ARBA00012486};
DE            EC=2.3.2.23 {ECO:0000256|ARBA:ARBA00012486};
DE   AltName: Full=Ubiquitin carrier protein UBC2 {ECO:0000256|ARBA:ARBA00042190};
DE   AltName: Full=Ubiquitin-protein ligase UBC2 {ECO:0000256|ARBA:ARBA00041569};
GN   ORFNames=P167DRAFT_560528 {ECO:0000313|EMBL:RPB08413.1};
OS   Morchella conica CCBAS932.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Pezizomycetes;
OC   Pezizales; Morchellaceae; Morchella.
OX   NCBI_TaxID=1392247 {ECO:0000313|EMBL:RPB08413.1, ECO:0000313|Proteomes:UP000277580};
RN   [1] {ECO:0000313|EMBL:RPB08413.1, ECO:0000313|Proteomes:UP000277580}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCBAS932 {ECO:0000313|EMBL:RPB08413.1,
RC   ECO:0000313|Proteomes:UP000277580};
RX   PubMed=30420746; DOI=10.1038/s41559-018-0710-4;
RA   Murat C., Payen T., Noel B., Kuo A., Morin E., Chen J., Kohler A.,
RA   Krizsan K., Balestrini R., Da Silva C., Montanini B., Hainaut M.,
RA   Levati E., Barry K.W., Belfiori B., Cichocki N., Clum A., Dockter R.B.,
RA   Fauchery L., Guy J., Iotti M., Le Tacon F., Lindquist E.A., Lipzen A.,
RA   Malagnac F., Mello A., Molinier V., Miyauchi S., Poulain J., Riccioni C.,
RA   Rubini A., Sitrit Y., Splivallo R., Traeger S., Wang M., Zifcakova L.,
RA   Wipf D., Zambonelli A., Paolocci F., Nowrousian M., Ottonello S.,
RA   Baldrian P., Spatafora J.W., Henrissat B., Nagy L.G., Aury J.M.,
RA   Wincker P., Grigoriev I.V., Bonfante P., Martin F.M.;
RT   "Pezizomycetes genomes reveal the molecular basis of ectomycorrhizal
RT   truffle lifestyle.";
RL   Nat. Ecol. Evol. 2:1956-1965(2018).
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:0000256|ARBA:ARBA00000485};
CC   -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC       {ECO:0000256|RuleBase:RU362109}.
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DR   EMBL; ML119163; RPB08413.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3N4KD16; -.
DR   STRING; 1392247.A0A3N4KD16; -.
DR   InParanoid; A0A3N4KD16; -.
DR   Proteomes; UP000277580; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:UniProt.
DR   CDD; cd00195; UBCc; 1.
DR   Gene3D; 3.10.110.10; Ubiquitin Conjugating Enzyme; 1.
DR   InterPro; IPR000608; UBQ-conjugat_E2.
DR   InterPro; IPR023313; UBQ-conjugating_AS.
DR   InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR   PANTHER; PTHR24067; UBIQUITIN-CONJUGATING ENZYME E2; 1.
DR   PANTHER; PTHR24067:SF154; UBIQUITIN-CONJUGATING ENZYME E2 G2; 1.
DR   Pfam; PF00179; UQ_con; 1.
DR   SMART; SM00212; UBCc; 1.
DR   SUPFAM; SSF54495; UBC-like; 1.
DR   PROSITE; PS00183; UBC_1; 1.
DR   PROSITE; PS50127; UBC_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU362109};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU362109};
KW   Reference proteome {ECO:0000313|Proteomes:UP000277580};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW   ECO:0000256|RuleBase:RU362109}.
FT   DOMAIN          5..165
FT                   /note="UBC core"
FT                   /evidence="ECO:0000259|PROSITE:PS50127"
FT   ACT_SITE        90
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10133"
SQ   SEQUENCE   166 AA;  18713 MW;  9523E8A0DB74BB5A CRC64;
     MSFAAANKRL LKEYKALLRE SPEGIVAGPV DESNLFEWEC LIQGPDETPF EGGVFPATLS
     FPKDYPLNPP KMKFTCEMFH PNVYKDGTVC ISILHSPGDD PNQYEDASER WSPIQSVEKI
     LISVMSMLAE PNDESGANID ASKVWRDNKE EYSRRVRQCA RKVLGL
//
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