ID   UBE2W_XENTR             Reviewed;         151 AA.
AC   Q28FC1;
DT   18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT   04-APR-2006, sequence version 1.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=Ubiquitin-conjugating enzyme E2 W;
DE            EC=2.3.2.23;
DE   AltName: Full=E2 ubiquitin-conjugating enzyme W;
DE   AltName: Full=N-terminal E2 ubiquitin-conjugating enzyme;
DE            EC=2.3.2.25;
DE   AltName: Full=Ubiquitin carrier protein W;
DE   AltName: Full=Ubiquitin-protein ligase W;
GN   Name=ube2w; ORFNames=TEgg096e02.1;
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Egg;
RG   Sanger Xenopus tropicalis EST/cDNA project;
RL   Submitted (OCT-2006) 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 degradation of misfolded chaperone substrate and DNA
CC       repair. {ECO:0000250|UniProtKB:Q96B02}.
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:0000250|UniProtKB:Q96B02, ECO:0000255|PROSITE-
CC         ProRule:PRU00388};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine +
CC         [acceptor protein]-N-terminal-amino acid = [E1 ubiquitin-activating
CC         enzyme]-L-cysteine + N-terminal-ubiquitinyl-[acceptor protein].;
CC         EC=2.3.2.25; Evidence={ECO:0000250|UniProtKB:Q96B02};
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000255|PROSITE-ProRule:PRU00388}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q96B02}.
CC   -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00388}.
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DR   EMBL; CR762043; CAJ83690.1; -; mRNA.
DR   RefSeq; NP_001016132.1; NM_001016132.2.
DR   AlphaFoldDB; Q28FC1; -.
DR   SMR; Q28FC1; -.
DR   GeneID; 548886; -.
DR   KEGG; xtr:548886; -.
DR   CTD; 55284; -.
DR   Xenbase; XB-GENE-954746; ube2w.
DR   InParanoid; Q28FC1; -.
DR   OrthoDB; 1522577at2759; -.
DR   Reactome; R-XTR-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000008143; Chromosome 6.
DR   Proteomes; UP000790000; Unplaced.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0061631; F:ubiquitin conjugating enzyme activity; IBA:GO_Central.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; ISS:UniProtKB.
DR   GO; GO:0071218; P:cellular response to misfolded protein; ISS:UniProtKB.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR   GO; GO:0006513; P:protein monoubiquitination; ISS:UniProtKB.
DR   GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR   GO; GO:0006515; P:protein quality control for misfolded or incompletely synthesized proteins; ISS:UniProtKB.
DR   CDD; cd00195; UBCc; 1.
DR   Gene3D; 3.10.110.10; -; 1.
DR   InterPro; IPR000608; UBQ-conjugat_E2.
DR   InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR   Pfam; PF00179; UQ_con; 1.
DR   SUPFAM; SSF54495; SSF54495; 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..151
FT                   /note="Ubiquitin-conjugating enzyme E2 W"
FT                   /id="PRO_0000416882"
FT   DOMAIN          3..151
FT                   /note="UBC core"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT   ACT_SITE        91
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
SQ   SEQUENCE   151 AA;  17331 MW;  B91B585BBD091F34 CRC64;
     MASMQKRLQK ELLALQNEPP PGMTLNEKSV QNSITQWIVD MEGAPGTLYE GEKFQLLFKF
     SSRYPFDSPQ VMFTGDNIPV HPHVYSNGHI CLSILTEDWS PALSVQSVCL SIISMLSSCK
     EKRRPPDNSF YVRTCNKNPK KTKWWYHDDT C