ID   UBC2_TRIHA              Reviewed;         151 AA.
AC   Q58FS2;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 1.
DT   25-MAY-2022, entry version 74.
DE   RecName: Full=Ubiquitin-conjugating enzyme E2 2;
DE            EC=2.3.2.23;
DE   AltName: Full=E2 ubiquitin-conjugating enzyme 2;
DE   AltName: Full=Ubiquitin carrier protein UBC2;
DE   AltName: Full=Ubiquitin-protein ligase UBC2;
GN   Name=UBC2;
OS   Trichoderma harzianum (Hypocrea lixii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX   NCBI_TaxID=5544;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=HZMA5313;
RA   Yang Q., Liu P., Yang L.;
RT   "Cloning and Sequence Analysis of the Ubiquitin-conjugating enzyme Gene
RT   from Trichoderma harzianum.";
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the covalent attachment of ubiquitin to other
CC       proteins. Plays a role in transcription regulation by catalyzing the
CC       monoubiquitination of histone H2B to form H2BK123ub1. H2BK123ub1 gives
CC       a specific tag for epigenetic transcriptional activation and is also a
CC       prerequisite for H3K4me and H3K79me formation. Also involved in
CC       postreplication repair of UV-damaged DNA, in N-end rule-dependent
CC       protein degradation and in sporulation. {ECO:0000255|PROSITE-
CC       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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q5VVX9}. Nucleus
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; AY955083; AAX55621.1; -; mRNA.
DR   AlphaFoldDB; Q58FS2; -.
DR   SMR; Q58FS2; -.
DR   UniPathway; UPA00143; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
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; -; 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   2: Evidence at transcript level;
KW   ATP-binding; Chromatin regulator; Cytoplasm; DNA damage; DNA repair;
KW   Nucleotide-binding; Nucleus; Sporulation; Transcription;
KW   Transcription regulation; Transferase; Ubl conjugation pathway.
FT   CHAIN           1..151
FT                   /note="Ubiquitin-conjugating enzyme E2 2"
FT                   /id="PRO_0000082537"
FT   DOMAIN          4..150
FT                   /note="UBC core"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT   ACT_SITE        88
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00388,
FT                   ECO:0000255|PROSITE-ProRule:PRU10133"
SQ   SEQUENCE   151 AA;  17295 MW;  E74D192106C9F42B CRC64;
     MSTAARRRLM RDFKRMQTDP PAGVSASPIP DNVMTWNAVI IGPADTPFED GTFRLVMQFE
     EQYPNKPPQV KFISQMFHPN VYANGELCLD ILQNRWSPTY DVAAVLTSIQ SLLNDPNTGS
     PANVEASNLY KDNRREYIKR VRETVERSWE D