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Database: UniProt
Entry: A0A1Y2W6P4_9PEZI
LinkDB: A0A1Y2W6P4_9PEZI
Original site: A0A1Y2W6P4_9PEZI 
ID   A0A1Y2W6P4_9PEZI        Unreviewed;       151 AA.
AC   A0A1Y2W6P4;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=Ubiquitin-conjugating enzyme E2 2 {ECO:0000256|ARBA:ARBA00039884};
DE            EC=2.3.2.23 {ECO:0000256|ARBA:ARBA00012486};
DE   AltName: Full=E2 ubiquitin-conjugating enzyme 2 {ECO:0000256|ARBA:ARBA00042179};
DE   AltName: Full=Ubiquitin carrier protein UBC2 {ECO:0000256|ARBA:ARBA00042190};
DE   AltName: Full=Ubiquitin-protein ligase UBC2 {ECO:0000256|ARBA:ARBA00041569};
GN   ORFNames=M426DRAFT_319729 {ECO:0000313|EMBL:OTB05465.1};
OS   Hypoxylon sp. CI-4A.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Xylariomycetidae; Xylariales; Hypoxylaceae; Hypoxylon.
OX   NCBI_TaxID=1001833 {ECO:0000313|EMBL:OTB05465.1, ECO:0000313|Proteomes:UP000242955};
RN   [1] {ECO:0000313|EMBL:OTB05465.1, ECO:0000313|Proteomes:UP000242955}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CI-4A {ECO:0000313|EMBL:OTB05465.1,
RC   ECO:0000313|Proteomes:UP000242955};
RX   PubMed=28078400; DOI=10.1007/s00253-017-8091-1;
RA   Wu W., Davis R.W., Tran-Gyamfi M.B., Kuo A., LaButti K., Mihaltcheva S.,
RA   Hundley H., Chovatia M., Lindquist E., Barry K., Grigoriev I.V.,
RA   Henrissat B., Gladden J.M.;
RT   "Characterization of four endophytic fungi as potential consolidated
RT   bioprocessing hosts for conversion of lignocellulose into advanced
RT   biofuels.";
RL   Appl. Microbiol. Biotechnol. 101:2603-2618(2017).
CC   -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC       {ECO:0000256|RuleBase:RU362109}.
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DR   EMBL; KZ111542; OTB05465.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y2W6P4; -.
DR   STRING; 1001833.A0A1Y2W6P4; -.
DR   InParanoid; A0A1Y2W6P4; -.
DR   OrthoDB; 5478564at2759; -.
DR   Proteomes; UP000242955; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:UniProt.
DR   GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
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:SF254; UBIQUITIN-CONJUGATING ENZYME E2-17 KDA; 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:UP000242955};
KW   Sporulation {ECO:0000256|ARBA:ARBA00022969};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW   ECO:0000256|RuleBase:RU362109}.
FT   DOMAIN          4..150
FT                   /note="UBC core"
FT                   /evidence="ECO:0000259|PROSITE:PS50127"
FT   ACT_SITE        88
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10133"
SQ   SEQUENCE   151 AA;  17151 MW;  A70EDF5A7C06EB71 CRC64;
     MSTAARRRLM RDFKRMQTDP PAGVSASPVP DNVMTWNAVI IGPADTPFED GTFRLVMHFE
     EQYPNKPPAV KFISQMFHPN VYATGELCLD ILQNRWSPTY DVAAVLTSIQ SLLNDPNTGS
     PANVEASNLY KDNRKEYTKR VRETVEKSWE D
//
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