ID   A0A8U1C9U1_SALNM        Unreviewed;       517 AA.
AC   A0A8U1C9U1;
DT   14-DEC-2022, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2022, sequence version 1.
DT   18-JUN-2025, entry version 15.
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|RefSeq:XP_038864425.1};
OS   Salvelinus namaycush (Lake trout) (Salmo namaycush).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC   Salmonidae; Salmoninae; Salvelinus.
OX   NCBI_TaxID=8040 {ECO:0000313|Proteomes:UP000808372, ECO:0000313|RefSeq:XP_038864425.1};
RN   [1] {ECO:0000313|RefSeq:XP_038864425.1}
RP   IDENTIFICATION.
RC   TISSUE=White muscle {ECO:0000313|RefSeq:XP_038864425.1};
RG   RefSeq;
RL   Submitted (MAR-2025) 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};
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000256|ARBA:ARBA00004906}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the RBR family. Ariadne subfamily.
CC       {ECO:0000256|ARBA:ARBA00005884}.
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DR   RefSeq; XP_038864425.1; XM_039008497.1.
DR   GeneID; 120059447; -.
DR   KEGG; snh:120059447; -.
DR   OrthoDB; 10009520at2759; -.
DR   Proteomes; UP000808372; Chromosome 14.
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   FunFam; 3.30.40.10:FF:000098; RBR-type E3 ubiquitin transferase; 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; IPR054694; Parkin-like_IBR.
DR   InterPro; IPR047556; Rcat_RBR_TRIAD1.
DR   InterPro; IPR044066; TRIAD_supradom.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   PANTHER; PTHR11685; RBR FAMILY RING FINGER AND IBR DOMAIN-CONTAINING; 1.
DR   Pfam; PF19422; Ariadne; 1.
DR   Pfam; PF01485; IBR; 1.
DR   Pfam; PF22605; IBR_2; 1.
DR   SMART; SM00647; IBR; 2.
DR   SUPFAM; SSF57850; RING/U-box; 3.
DR   PROSITE; PS51873; TRIAD; 1.
DR   PROSITE; PS00518; ZF_RING_1; 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:UP000808372};
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          135..357
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51873"
FT   REGION          1..39
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..11
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        12..34
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   517 AA;  59697 MW;  734B44CA71403190 CRC64;
     MSVDMNSQAY DSNEDDLGVN SEDDDGGDDD DQGDIADYYD GVAGDMEQQG ADSFDPEEYQ
     FTCLTYRESQ KVLCDEVNSI AAILKVLPAV AKLVLVHFHW QVSQILDRYK SSSSQLLSDA
     QVQPSSTCRS VPAPQSLQCG VCLQLVRRDT LLALPCQHSF CKGCWEQHCT VLVKDGVGVG
     ISCMAQDCSL QMPEDFVLPL LPGEELKDKY RRYLFRDYVE SHFQLQLCPG ADCPIVIQVQ
     EPRARRVQCS RCNEVFCFKC RAMYHAPTDC PTVRRWLTKC ADDSETANYI SAHTKDCPKC
     NICIEKNGGC NHMVLFKSDI AFPLFQLCSK CKHDFCWMCL GDWKTHGSEY YECSRYKENP
     DIVNQSQQAQ AREALKKYLF YFERWENHNK SLQLEAQTYQ RIQEKIQERV MNNLGTWIDW
     QYMQNAAKLL AKCRYTLQYT YPYAYYMESG PRKKLFEYQQ AQLEAEIENL SWKVERADSY
     ESVSEGELNA NDRGDLENQM HIAEQRRRTL LKDFHDT
//