ID A8X547_CAEBR Unreviewed; 531 AA.
AC A8X547;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 1.
DT 27-MAR-2024, entry version 83.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN ORFNames=CBG07248 {ECO:0000313|EMBL:CAP27758.1,
GN ECO:0000313|WormBase:CBG07248}, CBG_07248
GN {ECO:0000313|EMBL:CAP27758.1};
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:CAP27758.1, ECO:0000313|Proteomes:UP000008549};
RN [1] {ECO:0000313|EMBL:CAP27758.1, ECO:0000313|Proteomes:UP000008549}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16 {ECO:0000313|EMBL:CAP27758.1,
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-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27; Evidence={ECO:0000256|ARBA:ARBA00000900};
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DR EMBL; HE601041; CAP27758.1; -; Genomic_DNA.
DR RefSeq; XP_002645633.1; XM_002645587.1.
DR AlphaFoldDB; A8X547; -.
DR STRING; 6238.A8X547; -.
DR EnsemblMetazoa; CBG07248.1; CBG07248.1; WBGene00029362.
DR GeneID; 8587632; -.
DR KEGG; cbr:CBG_07248; -.
DR CTD; 8587632; -.
DR WormBase; CBG07248; CBP15882; WBGene00029362; -.
DR eggNOG; KOG4265; Eukaryota.
DR HOGENOM; CLU_016631_3_2_1; -.
DR InParanoid; A8X547; -.
DR OMA; HERGNSH; -.
DR OrthoDB; 383715at2759; -.
DR Proteomes; UP000008549; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:EnsemblMetazoa.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0040027; P:negative regulation of vulval development; IEA:EnsemblMetazoa.
DR GO; GO:1903361; P:protein localization to basolateral plasma membrane; IEA:EnsemblMetazoa.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR045194; MGRN1/RNF157-like.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR22996; MAHOGUNIN; 1.
DR PANTHER; PTHR22996:SF0; RING-TYPE E3 UBIQUITIN TRANSFERASE; 1.
DR Pfam; PF13920; zf-C3HC4_3; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}; Reference proteome {ECO:0000313|Proteomes:UP000008549};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 269..308
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 350..374
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 415..531
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 427..446
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 461..486
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 497..511
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 531 AA; 59951 MW; F33D98239F40F1AB CRC64;
MGQIASVFRG RNTHVRGNSH DEEDPEAQMT FSNAAGTYFG SHFLMCGCKF EMARPEAYLF
GENSDLDQLG SRALSFPYPP GPLGNDEIRP LNLLVNIRKE SVKFQRVKKD NGEYDPNLYQ
LTFVFDCDVA CVIQVHFHAK EVYHDGEIQF AYRNRRAQNS ETFHFEMGAD QNFGGYVFDA
TLWDSSDLSY SAGLYYPFVI SITTSGVEST QMQTTMCTIE TGNDSSKALV LKPLRQKIAC
DGVTYLLQEI FGIENKGNES MDDDNGLECI ICLSDIRDTV ILPCRHLCVC SNCADSLRYK
HNNCPICRSP FRALIRLRAH RQTRNQIYET VSLVEGLNGS FSSMPTVIDP VSTINSSTRR
KRHSSSRSGG KAMHQVLTMD QLGDNSRVQE CIEMTYIAND EEDAKRVIEE IIQQAEEKEK
TRSQVDSEEG SSGSSGSSSQ PLKKHRTNSS ELSESEEEEF EPPLPEKKIP DDLESDKNKN
EEEEKSSPGA SEDDEDEHEE TIRRNSEKRR SFQSGSRNSS SQLLEDQHRK N
//
