ID   UBE2T_XENLA             Reviewed;         192 AA.
AC   Q7ZY08;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   27-MAR-2024, entry version 97.
DE   RecName: Full=Ubiquitin-conjugating enzyme E2 T;
DE            EC=2.3.2.23;
DE   AltName: Full=E2 ubiquitin-conjugating enzyme T;
DE   AltName: Full=Ubiquitin carrier protein T;
DE   AltName: Full=Ubiquitin-protein ligase T;
GN   Name=ube2t;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Accepts ubiquitin from the E1 complex and catalyzes its
CC       covalent attachment to other proteins. Catalyzes monoubiquitination.
CC       Involved in DNA repair. {ECO:0000250|UniProtKB:Q9NPD8}.
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: Nucleus {ECO:0000250|UniProtKB:Q9NPD8}.
CC       Note=Accumulates to chromatin. {ECO:0000250|UniProtKB:Q9NPD8}.
CC   -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00388}.
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DR   EMBL; BC044029; AAH44029.1; -; mRNA.
DR   RefSeq; NP_001080105.1; NM_001086636.1.
DR   RefSeq; XP_018103516.1; XM_018248027.1.
DR   RefSeq; XP_018103517.1; XM_018248028.1.
DR   AlphaFoldDB; Q7ZY08; -.
DR   SMR; Q7ZY08; -.
DR   MaxQB; Q7ZY08; -.
DR   DNASU; 379797; -.
DR   GeneID; 379797; -.
DR   KEGG; xla:379797; -.
DR   AGR; Xenbase:XB-GENE-6254937; -.
DR   CTD; 379797; -.
DR   Xenbase; XB-GENE-6254937; ube2t.S.
DR   OMA; GVEKKFC; -.
DR   OrthoDB; 52078at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000186698; Chromosome 2S.
DR   Bgee; 379797; Expressed in oocyte and 20 other cell types or tissues.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR   GO; GO:0061631; F:ubiquitin conjugating enzyme activity; IEA:UniProtKB-EC.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; ISS:UniProtKB.
DR   GO; GO:0006974; P:DNA damage response; ISS:UniProtKB.
DR   GO; GO:0006281; P:DNA repair; ISS:UniProtKB.
DR   GO; GO:0051865; P:protein autoubiquitination; ISS:UniProtKB.
DR   GO; GO:0006513; P:protein monoubiquitination; ISS:UniProtKB.
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:SF370; UBIQUITIN-CONJUGATING ENZYME; 1.
DR   PANTHER; PTHR24067; UBIQUITIN-CONJUGATING ENZYME E2; 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   2: Evidence at transcript level;
KW   ATP-binding; DNA damage; DNA repair; Nucleotide-binding; Nucleus;
KW   Reference proteome; Transferase; Ubl conjugation pathway.
FT   CHAIN           1..192
FT                   /note="Ubiquitin-conjugating enzyme E2 T"
FT                   /id="PRO_0000082511"
FT   DOMAIN          2..152
FT                   /note="UBC core"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT   REGION          150..192
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        163..192
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        86
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00388,
FT                   ECO:0000255|PROSITE-ProRule:PRU10133"
SQ   SEQUENCE   192 AA;  21554 MW;  47214E394A77983E CRC64;
     MQRVSRLKRE LQLLNKEPPP GVICWQNESN MDDLRAQIIG GSGSPYEGGI FNLEIIVPER
     YPFEPPKIRF LTPIYHPNID SAGRICLDIL KLPPKGAWRP ALNISTVLTS IQLLMSEPNP
     DDPLMADISS EFKYNRAVFF SNAKKWTEKH ALPAPQGSDK ESQEKSGSSE GTSHKRKSAE
     IAEESKKPCR EP
//