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Database: UniProt
Entry: A0A8S1F9U8_9PELO
LinkDB: A0A8S1F9U8_9PELO
Original site: A0A8S1F9U8_9PELO 
ID   A0A8S1F9U8_9PELO        Unreviewed;       646 AA.
AC   A0A8S1F9U8;
DT   12-OCT-2022, integrated into UniProtKB/TrEMBL.
DT   12-OCT-2022, sequence version 1.
DT   18-JUN-2025, entry version 12.
DE   RecName: Full=RBR-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012251};
DE            EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
GN   ORFNames=CBOVIS_LOCUS10745 {ECO:0000313|EMBL:CAB3409047.1};
OS   Caenorhabditis bovis.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=2654633 {ECO:0000313|EMBL:CAB3409047.1, ECO:0000313|Proteomes:UP000494206};
RN   [1] {ECO:0000313|EMBL:CAB3409047.1, ECO:0000313|Proteomes:UP000494206}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Laetsch R D., Stevens L., Kumar S., Blaxter L. M.;
RL   Submitted (APR-2020) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine +
CC         [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC         cysteine + [acceptor protein]-N(6)-ubiquitinyl-L-lysine.;
CC         EC=2.3.2.31; Evidence={ECO:0000256|ARBA:ARBA00001798};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the RBR family. Ariadne subfamily.
CC       {ECO:0000256|ARBA:ARBA00005884}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:CAB3409047.1}.
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DR   EMBL; CADEPM010000008; CAB3409047.1; -; Genomic_DNA.
DR   OrthoDB; 10009520at2759; -.
DR   Proteomes; UP000494206; Unassembled WGS sequence.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:InterPro.
DR   CDD; cd20344; BRcat_RBR_TRIAD1; 1.
DR   CDD; cd20360; Rcat_RBR_TRIAD1; 1.
DR   CDD; cd16773; RING-HC_RBR_TRIAD1; 1.
DR   FunFam; 1.20.120.1750:FF:000004; RBR-type E3 ubiquitin transferase; 1.
DR   Gene3D; 1.20.120.1750; -; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR045840; Ariadne.
DR   InterPro; IPR047555; BRcat_RBR_TRIAD1.
DR   InterPro; IPR031127; E3_UB_ligase_RBR.
DR   InterPro; IPR002867; IBR_dom.
DR   InterPro; IPR047556; Rcat_RBR_TRIAD1.
DR   InterPro; IPR044066; TRIAD_supradom.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR11685; RBR FAMILY RING FINGER AND IBR DOMAIN-CONTAINING; 1.
DR   Pfam; PF19422; Ariadne; 1.
DR   Pfam; PF01485; IBR; 1.
DR   Pfam; PF22191; IBR_1; 1.
DR   SMART; SM00647; IBR; 2.
DR   SUPFAM; SSF57850; RING/U-box; 3.
DR   PROSITE; PS51873; TRIAD; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000494206};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT   DOMAIN          290..498
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51873"
SQ   SEQUENCE   646 AA;  74663 MW;  0F75E1D65C6724E3 CRC64;
     MFDVRFVETD EDIDFSQIPF DVTVPHILRF PVSSNISENG TGQSDVGTFL FYPLGFLYVK
     SPLEKASSSA KKKYENIMKQ MEIVKGMIVV VVIRLDISLY KQDKMFESST LPSFKIVPNS
     SGVKIKDMSI VLQNSEESED MVIKLDYFPA ITTPGITCYK ITNNEDFDSG NMDDEDMSCT
     SGDDDYDCCD DDYYNDCDLD ATDEVAVTST HSEDAKFECL EVSQVERLMA DSVKIVTNFL
     SINENISRML LHANSWDIDL VINMWRKNKS ELFRQSHMAA KPDSKYERPM NGYCAVCAVD
     GYPALLFLAC GHCFCEQCWK CHIESRLTEG VASRIECMES DCGVYCPPEF VHQLLDKGPL
     RARYDRFLFR DLVQSHPELK FCVGKDCQIV IRSKEEKPKR VTCEKCHTSF CVTCGVDYHA
     PTSCDTIKQW LTKCADDSET ANYISAHTKD CPRCHSCIEK AGGCNHIQCT RCRHHFCWMC
     FGDWKTHGSE YYECSRYKEN PSIAAEANHV KARRALEKYL HYFERFENHS KSLKMEEQLR
     EKIKKKIDDK VNEHNGTWID WQYLHTAVSQ LTKCRYTLQY TYPFAYYMQS GPRKQLFEYQ
     QAQLEKEVEE LAWAVERADA TARGALEAHM HRAEHKRQTL LHDFFF
//
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