ID   A0A673M7W1_9TELE        Unreviewed;       553 AA.
AC   A0A673M7W1;
DT   17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT   17-JUN-2020, sequence version 1.
DT   18-JUN-2025, entry version 21.
DE   RecName: Full=RBR-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012251};
DE            EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
GN   Name=LOC107738728 {ECO:0000313|Ensembl:ENSSRHP00000084214.1};
OS   Sinocyclocheilus rhinocerous.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Cyprinidae; Cyprininae; Sinocyclocheilus.
OX   NCBI_TaxID=307959 {ECO:0000313|Ensembl:ENSSRHP00000084214.1, ECO:0000313|Proteomes:UP000472270};
RN   [1] {ECO:0000313|Ensembl:ENSSRHP00000084214.1}
RP   IDENTIFICATION.
RG   Ensembl;
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   -!- SIMILARITY: Belongs to the RBR family. Ariadne subfamily.
CC       {ECO:0000256|ARBA:ARBA00005884}.
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DR   AlphaFoldDB; A0A673M7W1; -.
DR   Ensembl; ENSSRHT00000086489.1; ENSSRHP00000084214.1; ENSSRHG00000041657.1.
DR   Proteomes; UP000472270; 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; cd20343; BRcat_RBR_HHARI-like; 1.
DR   CDD; cd20356; Rcat_RBR_HHARI-like; 1.
DR   CDD; cd16626; RING-HC_RBR_HHARI; 1.
DR   FunFam; 1.20.120.1750:FF:000002; RBR-type E3 ubiquitin transferase; 1.
DR   FunFam; 3.30.40.10:FF:000019; 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; IPR048962; ARIH1-like_UBL.
DR   InterPro; IPR031127; E3_UB_ligase_RBR.
DR   InterPro; IPR002867; IBR_dom.
DR   InterPro; IPR044066; TRIAD_supradom.
DR   InterPro; IPR001841; Znf_RING.
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   Pfam; PF21235; UBA_ARI1; 1.
DR   SMART; SM00647; IBR; 2.
DR   SUPFAM; SSF57850; RING/U-box; 3.
DR   PROSITE; PS51873; TRIAD; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000472270};
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          196..407
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51873"
FT   DOMAIN          200..249
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          55..74
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          90..110
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   553 AA;  64338 MW;  5DCBF9F0EF0BF00C CRC64;
     ITYFETAKSS SSKFLFSLCF AVSDKKYTSN LSHLACRYIK LNPVMDSDEG YNYEFDDEEE
     ECSEDSGEEE TADDTLELGE VELVDPVVAG GERDDCGETG GSGLGPGQDE EDYRFEVLTA
     EQILQHMVEC IREVNEVIQN PATITRILLS HFNWDKEKLM ERYFDGNLDK LFSECHVINP
     SKKSRTRLMN TRSSAQDMPC QICYLNYPNS YFTGLECGHK FCMQCWGDYL TTKIIEEGMG
     QTISCPAHSC DILVDDNTVM RLITDSKVKL KYQHLITNSF VECNRLLKWC PAPDCHHVVK
     VQYPDAKPVR CKCGRQFCFN CGENWHDPVK CKWLRKWIKK CDDDSETSNW IAANTKECPK
     CHVTIEKDGG CNHMVCRNQN CKAEFCWVCL GPWEPHGSAW YNCNRYNEDD AKAARDAQER
     SRAALQRYLF YCNRYMNHMQ SLRFEHKLYA QVKQKMEEMQ QHNMSWIEVQ FLKKAVDVLC
     QCRSTLMFTY VFAFYLKKNN QSIIFENNQA DLENATEVLS GYLERDISQD SLQDIKQKVQ
     DKYRQVYTFS LMR
//