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Database: UniProt
Entry: A0A6J2V452_CHACN
LinkDB: A0A6J2V452_CHACN
Original site: A0A6J2V452_CHACN 
ID   A0A6J2V452_CHACN        Unreviewed;       609 AA.
AC   A0A6J2V452;
DT   07-OCT-2020, integrated into UniProtKB/TrEMBL.
DT   07-OCT-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=LOC115809511 {ECO:0000313|RefSeq:XP_030627054.1};
OS   Chanos chanos (Milkfish) (Mugil chanos).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Gonorynchiformes;
OC   Chanidae; Chanos.
OX   NCBI_TaxID=29144 {ECO:0000313|Proteomes:UP000504632, ECO:0000313|RefSeq:XP_030627054.1};
RN   [1] {ECO:0000313|RefSeq:XP_030627054.1}
RP   IDENTIFICATION.
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};
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DR   RefSeq; XP_030627054.1; XM_030771194.1.
DR   AlphaFoldDB; A0A6J2V452; -.
DR   GeneID; 115809511; -.
DR   InParanoid; A0A6J2V452; -.
DR   OrthoDB; 1431934at2759; -.
DR   Proteomes; UP000504632; Chromosome 4.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; cd20338; BRcat_RBR_RNF19; 1.
DR   CDD; cd20355; Rcat_RBR_RNF19; 1.
DR   CDD; cd16776; RING-HC_RBR_RNF19B; 1.
DR   FunFam; 1.20.120.1750:FF:000001; RBR-type E3 ubiquitin transferase; 1.
DR   FunFam; 3.30.40.10:FF:000052; 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; 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; PF01485; IBR; 2.
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   4: Predicted;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000504632};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
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   TRANSMEM        341..373
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        394..427
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          108..331
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51873"
FT   DOMAIN          112..160
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          1..87
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          474..529
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          558..609
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..18
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        21..39
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        59..81
FT                   /note="Gly residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        567..585
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   609 AA;  65929 MW;  EC197B45209A9B80 CRC64;
     MKRPKQQSQP LSFLSFFSRK PKTEARIDLP AETPNHDEVA ITLTPNEQEP AEQEQSPSRG
     GGGCGDNGGN GVDAGVGGGG QQAAECGSSG STGVLSLSSS SQDQLLEHLV ECPLCLLSQP
     RGHFPRLSSC PHRACTDCLR QYLRIEISES RVGIACPQCS ETLAPLDVRA ILDDGTLLER
     FEEYQLRRFL AADPDTRWCP APDCSYAVIA YGCAECPKLS CGREGCDTEF CYLCRQLWHP
     DQTCDQARRQ RARHASGTND PSLLYVFNEE AGGEVEDIKA CPRCGAYIMK TNDGSCNRMN
     CTVCACQFCW LCMQEITDVH YLSPSGCTFW GKKPWSQTRK VLWQVGMLLG APVVISLIAG
     IAIPVIIVGI PIYMGRKVHG RCKKNNISGS KHYLTVASGV MMSVFVSPVI AAITVGVGVP
     LMLTYVYGVV PMSLCRNGWC RTQTESPDTH KIQLEDLASY LVFSHVVSEH WSIQPKPAAS
     EADGQEESGR VQDMATAPST SAVQVEPEGC QDPPDNVQDN DGLPDSQSDD AGVVALSVTQ
     SFASREGTNI EVRVEIEAQP WGERQPSLSS VLSSRSLSAE SLTQSLEPPS ASAQTRDGDP
     LPVTETDSV
//
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