ID   J3S9U9_CROAD            Unreviewed;       489 AA.
AC   J3S9U9;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 1.
DT   27-MAR-2024, entry version 55.
DE   RecName: Full=RBR-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012251};
DE            EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
OS   Crotalus adamanteus (Eastern diamondback rattlesnake).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Crotalus.
OX   NCBI_TaxID=8729 {ECO:0000313|EMBL:AFJ51943.1};
RN   [1] {ECO:0000313|EMBL:AFJ51943.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Venom gland {ECO:0000313|EMBL:AFJ51943.1};
RX   PubMed=23025625; DOI=10.1186/1471-2164-13-312;
RA   Rokyta D.R., Lemmon A.R., Margres M.J., Aronow K.;
RT   "The venom-gland transcriptome of the eastern diamondback rattlesnake
RT   (Crotalus adamanteus).";
RL   BMC Genomics 13:312-312(2012).
RN   [2] {ECO:0000313|EMBL:JAI10709.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Margres M.J., Wray K.P., McGivern J.J., Seavy M., Sanader D., Facente J.,
RA   Rokyta D.R.;
RT   "The extremes of toxin expression variation revealed in two sympatric snake
RT   species.";
RL   Submitted (MAY-2014) 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};
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DR   EMBL; JU176420; AFJ51943.1; -; mRNA.
DR   EMBL; GBEX01003851; JAI10709.1; -; mRNA.
DR   AlphaFoldDB; J3S9U9; -.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
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   Gene3D; 1.20.120.1750; -; 1.
DR   Gene3D; 2.20.25.20; -; 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; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   PANTHER; PTHR11685:SF210; E3 UBIQUITIN-PROTEIN LIGASE ARIH2; 1.
DR   PANTHER; PTHR11685; RBR FAMILY RING FINGER AND IBR DOMAIN-CONTAINING; 1.
DR   Pfam; PF19422; Ariadne; 1.
DR   Pfam; PF01485; IBR; 2.
DR   SMART; SM00647; IBR; 2.
DR   SMART; SM00184; RING; 2.
DR   SUPFAM; SSF57850; RING/U-box; 3.
DR   PROSITE; PS51873; TRIAD; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   2: Evidence at transcript level;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
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, ECO:0000256|PROSITE-
KW   ProRule:PRU00175}.
FT   DOMAIN          131..340
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51873"
FT   DOMAIN          296..336
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          1..39
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        15..33
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   489 AA;  57209 MW;  A460C8C6FD49FFBD CRC64;
     MSVDMNSQGS DSNEEDYDPN CDEEEDEDPG DIEGYYEGVA NDVEQQGADS FDPEEYQFTC
     LTYKESESTL NEHMVRLASA LKVSHAVAKL VLVSFHWQIS EILERNTSNS VQLLVEARVQ
     PASFKHAMVH SSQHCAVCMQ LVRKENLLSL ACQHQFCRSC WEQHCTVLVK DGVGVGVSCM
     AQDCLLRTPE DFVFPLLPSE ELKDKYRRYL FRDYIESHFQ LQLCPGADCP MVIQVQEPKA
     RRVQCNRCNE VFCFKCRQMY HAPTDCATIR KWLTKCADDS ETANYISAHT KDCPKCNICI
     EKNGGCNHMQ CSKCKHDFCW MCLGDWKTHG SEYYECSRYK ENPDIVNQSQ QAQAREALKK
     YLFYFERWEN HNKSLQLEAQ TYQRIQEKIQ ERVMNNLGTW IDWQYLQNAA KLLAKCRYTL
     QYTYPYAYYM ESGPRKKLFE YQQAQLEAEI ENLSWKVERA DSYDRGDLEN QMHIAEQRRR
     TLLKDFHDT
//