ID   UBC1_PYRO7              Reviewed;         147 AA.
AC   Q9UVR2; A4R868; G4N6D7;
DT   17-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 2.
DT   27-MAR-2024, entry version 122.
DE   RecName: Full=Ubiquitin-conjugating enzyme E2-16 kDa;
DE            EC=2.3.2.23;
DE   AltName: Full=E2 ubiquitin-conjugating enzyme 1;
DE   AltName: Full=Ubiquitin carrier protein;
DE   AltName: Full=Ubiquitin-protein ligase;
GN   Name=UBC1; ORFNames=MGG_06562;
OS   Pyricularia oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast
OS   fungus) (Magnaporthe oryzae).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Magnaporthales; Pyriculariaceae; Pyricularia.
OX   NCBI_TaxID=242507;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Kim Y.-K., Kolattukudy P.E.;
RT   "Identification of a ubiquitin-conjugating enzyme of the rice blast fungus
RT   Magnaporthe grisea.";
RL   Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=70-15 / ATCC MYA-4617 / FGSC 8958;
RX   PubMed=15846337; DOI=10.1038/nature03449;
RA   Dean R.A., Talbot N.J., Ebbole D.J., Farman M.L., Mitchell T.K.,
RA   Orbach M.J., Thon M.R., Kulkarni R., Xu J.-R., Pan H., Read N.D.,
RA   Lee Y.-H., Carbone I., Brown D., Oh Y.Y., Donofrio N., Jeong J.S.,
RA   Soanes D.M., Djonovic S., Kolomiets E., Rehmeyer C., Li W., Harding M.,
RA   Kim S., Lebrun M.-H., Bohnert H., Coughlan S., Butler J., Calvo S.E.,
RA   Ma L.-J., Nicol R., Purcell S., Nusbaum C., Galagan J.E., Birren B.W.;
RT   "The genome sequence of the rice blast fungus Magnaporthe grisea.";
RL   Nature 434:980-986(2005).
CC   -!- FUNCTION: Catalyzes the covalent attachment of ubiquitin to other
CC       proteins. {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, ECO:0000255|PROSITE-
CC         ProRule:PRU10133};
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000255|PROSITE-ProRule:PRU00388}.
CC   -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00388}.
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DR   EMBL; AF161722; AAD55983.1; -; Genomic_DNA.
DR   EMBL; CM001234; EHA50659.1; -; Genomic_DNA.
DR   RefSeq; XP_003716978.1; XM_003716930.1.
DR   AlphaFoldDB; Q9UVR2; -.
DR   SMR; Q9UVR2; -.
DR   STRING; 242507.Q9UVR2; -.
DR   EnsemblFungi; MGG_06562T0; MGG_06562T0; MGG_06562.
DR   GeneID; 2684717; -.
DR   KEGG; mgr:MGG_06562; -.
DR   VEuPathDB; FungiDB:MGG_06562; -.
DR   eggNOG; KOG0417; Eukaryota.
DR   HOGENOM; CLU_030988_13_3_1; -.
DR   InParanoid; Q9UVR2; -.
DR   OMA; VHFTTRI; -.
DR   OrthoDB; 5478564at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000009058; Chromosome 4.
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:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
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; PTHR24068; UBIQUITIN-CONJUGATING ENZYME E2; 1.
DR   PANTHER; PTHR24068:SF74; 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; Nucleotide-binding; Reference proteome; Transferase;
KW   Ubl conjugation pathway.
FT   CHAIN           1..147
FT                   /note="Ubiquitin-conjugating enzyme E2-16 kDa"
FT                   /id="PRO_0000082543"
FT   DOMAIN          1..147
FT                   /note="UBC core"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT   ACT_SITE        107
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00388,
FT                   ECO:0000255|PROSITE-ProRule:PRU10133"
FT   CONFLICT        128
FT                   /note="K -> R (in Ref. 1; AAD55983)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        136
FT                   /note="S -> A (in Ref. 1; AAD55983)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        143
FT                   /note="R -> P (in Ref. 1; AAD55983)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   147 AA;  16438 MW;  C7737C95FB7F61F7 CRC64;
     MALKRINKEL TDLGRDPPSS CSAGPVGEDL FHWQATIMGP SDSPYAGGVF FLAIHFPTDY
     PFKPPKVNFT TRIYHPNINS NGSICLDILR DQWSPALTIS KVLLSICSML TDPNPDDPLV
     PEIAHVYKTA RAQYESTARE WTRKYAI
//