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Database: UniProt
Entry: A8XA84_CAEBR
LinkDB: A8XA84_CAEBR
Original site: A8XA84_CAEBR 
ID   A8XA84_CAEBR            Unreviewed;       164 AA.
AC   A8XA84;
DT   15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT   15-JAN-2008, sequence version 1.
DT   27-MAR-2024, entry version 102.
DE   RecName: Full=E2 ubiquitin-conjugating enzyme {ECO:0000256|ARBA:ARBA00012486};
DE            EC=2.3.2.23 {ECO:0000256|ARBA:ARBA00012486};
GN   Name=ubc-7 {ECO:0000313|WormBase:CBG10037};
GN   Synonyms=Cbr-ubc-7 {ECO:0000313|EMBL:CAP29552.1};
GN   ORFNames=CBG10037 {ECO:0000313|WormBase:CBG10037}, CBG_10037
GN   {ECO:0000313|EMBL:CAP29552.1};
OS   Caenorhabditis briggsae.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6238 {ECO:0000313|EMBL:CAP29552.1, ECO:0000313|Proteomes:UP000008549};
RN   [1] {ECO:0000313|EMBL:CAP29552.1, ECO:0000313|Proteomes:UP000008549}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AF16 {ECO:0000313|EMBL:CAP29552.1,
RC   ECO:0000313|Proteomes:UP000008549};
RX   PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA   Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA   Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA   Fitch D.H., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA   Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA   Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA   Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA   Durbin R., Waterston R.H.;
RT   "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT   genomics.";
RL   PLoS Biol. 1:166-192(2003).
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:0000256|ARBA:ARBA00000485};
CC   -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC       {ECO:0000256|RuleBase:RU362109}.
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DR   EMBL; HE601459; CAP29552.1; -; Genomic_DNA.
DR   RefSeq; XP_002641703.1; XM_002641657.1.
DR   AlphaFoldDB; A8XA84; -.
DR   STRING; 6238.A8XA84; -.
DR   EnsemblMetazoa; CBG10037.1; CBG10037.1; WBGene00031521.
DR   GeneID; 8583697; -.
DR   KEGG; cbr:CBG_10037; -.
DR   CTD; 8583697; -.
DR   WormBase; CBG10037; CBP02442; WBGene00031521; Cbr-ubc-7.
DR   eggNOG; KOG0425; Eukaryota.
DR   HOGENOM; CLU_030988_10_1_1; -.
DR   InParanoid; A8XA84; -.
DR   OMA; RKVTRCV; -.
DR   OrthoDB; 149628at2759; -.
DR   Proteomes; UP000008549; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0061631; F:ubiquitin conjugating enzyme activity; IBA:GO_Central.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR   GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
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:SF3; UBIQUITIN-CONJUGATING ENZYME E2 G1; 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|RuleBase:RU362109};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU362109};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008549};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW   ECO:0000256|RuleBase:RU362109}.
FT   DOMAIN          3..163
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   164 AA;  18939 MW;  09280D9B2F8FD969 CRC64;
     MEQSSLLLKK QLADMRRVPV DGFSAGLVDD NDIYKWEVLV IGPPDTLYEG GFFKAILDFP
     RDYPQKPPKM KFISEIWHPN IDKEGNVCIS ILHDPGDDKW GYERPEERWL PVHTVETILL
     SVISMLTDPN FESPANVDAA KMQRENYADF KKKVAQCVRR TQEE
//
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