ID   A0A2K5KMK6_CERAT        Unreviewed;       500 AA.
AC   A0A2K5KMK6;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   RecName: Full=RBR-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012251};
DE            EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
GN   Name=ARIH2 {ECO:0000313|Ensembl:ENSCATP00000001926.1};
OS   Cercocebus atys (Sooty mangabey) (Cercocebus torquatus atys).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Cercocebus.
OX   NCBI_TaxID=9531 {ECO:0000313|Ensembl:ENSCATP00000001926.1, ECO:0000313|Proteomes:UP000233060};
RN   [1] {ECO:0000313|Ensembl:ENSCATP00000001926.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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   RefSeq; XP_011889003.1; XM_012033613.1.
DR   AlphaFoldDB; A0A2K5KMK6; -.
DR   STRING; 9531.ENSCATP00000001926; -.
DR   Ensembl; ENSCATT00000009700.1; ENSCATP00000001926.1; ENSCATG00000008575.1.
DR   GeneID; 105573674; -.
DR   KEGG; caty:105573674; -.
DR   CTD; 10425; -.
DR   GeneTree; ENSGT00940000154875; -.
DR   OMA; ICKVCHT; -.
DR   OrthoDB; 3084186at2759; -.
DR   Proteomes; UP000233060; Unplaced.
DR   Bgee; ENSCATG00000008575; Expressed in skeletal muscle tissue and 12 other cell types or tissues.
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; 2.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000233060};
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          135..344
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51873"
FT   DOMAIN          139..190
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   DOMAIN          300..340
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          1..38
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        15..36
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   500 AA;  58568 MW;  85BD75692A23E83C CRC64;
     MSVDMNSQGS DSNEEDYDPN CEEEEEEEDE DPGDIEDYYV GVASDVEQQG ADAFDPEEYQ
     FTCLTYKESE GALNEHMTSL ASVLKVSHSV AKLILVNFHW QVSEILDRFK SNSAQLLVEA
     RVQPNPSKHV PTSHPPHHCA VCMQFVRKEN LLSLACQHQF CRSCWEQHCS VLIKDGVGVG
     VSCMAQDCPL RTPEDFVFPL LPNEELREKY RRYLFRDYVE SHYQLQLCPG ADCPMVIRVQ
     EPRARRVQCN RCNEVFCFKC RQMYHAPTDC ATIRKWLTKC ADDSETANYI SAHTKDCPKC
     NICIEKNGGC NHMQCSKCKH DFCWMCLGDW KTHGSEYYEC SRYKENPDIV NQSQQAQARE
     ALKKYLFYFE RWENHNKSLQ LEAQTYQRIH EKIQERVMNN LGTWIDWQYL QNAAKLLAKV
     PSLLLQCRYT LQYTYPYAYY MESGPRKKLF EYQQAQLEAE IENLSWKVER ADSYDRGDLE
     NQMHIAEQRR RTLLKDFHDT
//