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Database: UniProt
Entry: A0A6A2Z7W6_HIBSY
LinkDB: A0A6A2Z7W6_HIBSY
Original site: A0A6A2Z7W6_HIBSY 
ID   A0A6A2Z7W6_HIBSY        Unreviewed;       564 AA.
AC   A0A6A2Z7W6;
DT   17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT   17-JUN-2020, sequence version 1.
DT   02-APR-2025, entry version 16.
DE   RecName: Full=RBR-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012251};
DE            EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
GN   ORFNames=F3Y22_tig00111022pilonHSYRG00260
GN   {ECO:0000313|EMBL:KAE8687205.1};
OS   Hibiscus syriacus (Rose of Sharon).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Malvales; Malvaceae; Malvoideae; Hibiscus.
OX   NCBI_TaxID=106335 {ECO:0000313|EMBL:KAE8687205.1, ECO:0000313|Proteomes:UP000436088};
RN   [1] {ECO:0000313|EMBL:KAE8687205.1, ECO:0000313|Proteomes:UP000436088}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Baekdansim {ECO:0000313|Proteomes:UP000436088};
RC   TISSUE=Leaf {ECO:0000313|EMBL:KAE8687205.1};
RA   Kim Y.-M.;
RT   "Draft genome information of white flower Hibiscus syriacus.";
RL   Submitted (SEP-2019) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Might act as an E3 ubiquitin-protein ligase, or as part of E3
CC       complex, which accepts ubiquitin from specific E2 ubiquitin-conjugating
CC       enzymes and then transfers it to substrates.
CC       {ECO:0000256|ARBA:ARBA00003976}.
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   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KAE8687205.1}.
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DR   EMBL; VEPZ02001205; KAE8687205.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A6A2Z7W6; -.
DR   OrthoDB; 9977870at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000436088; Unassembled WGS sequence.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0004523; F:RNA-DNA hybrid ribonuclease activity; IEA:InterPro.
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:UniProtKB-UniPathway.
DR   CDD; cd22582; BRcat_RBR_unk; 1.
DR   CDD; cd22584; Rcat_RBR_unk; 1.
DR   FunFam; 1.20.120.1750:FF:000019; RBR-type E3 ubiquitin transferase; 1.
DR   FunFam; 3.30.40.10:FF:000230; RBR-type E3 ubiquitin transferase; 1.
DR   FunFam; 3.30.420.10:FF:000076; RBR-type E3 ubiquitin transferase; 1.
DR   Gene3D; 1.20.120.1750; -; 1.
DR   Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 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; IPR012337; RNaseH-like_sf.
DR   InterPro; IPR002156; RNaseH_domain.
DR   InterPro; IPR036397; RNaseH_sf.
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; RBR FAMILY RING FINGER AND IBR DOMAIN-CONTAINING; 1.
DR   Pfam; PF01485; IBR; 2.
DR   Pfam; PF13456; RVT_3; 1.
DR   SMART; SM00647; IBR; 2.
DR   SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR   SUPFAM; SSF57850; RING/U-box; 2.
DR   PROSITE; PS51873; TRIAD; 1.
DR   PROSITE; PS00518; ZF_RING_1; 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:UP000436088};
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          318..536
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51873"
FT   DOMAIN          322..366
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          543..564
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        546..564
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   564 AA;  64395 MW;  2DDBB96A566638E8 CRC64;
     MAATANTDGG DDNLNPLFSL QHNELMAAHS LDSDLDFAFH LQLQEALSAS LSLDTSQPPP
     HLPPQPSIQS DSVFSLTSQE LSKFQQESID HKCFLLETQK LKEDLKRRVH DEKFARRIAG
     IPEEDWADWG DCFERPFGEG CSKDQRLDGT DSELEFVDDV SDDDACEFRI YFKGLISEEK
     VRDKASNCAG IGVAICDFRD NLILEITKPL IGVGLSKQAA ELKALIEGLN AALSLELDRV
     EFCCDYYPIY QYVTRRWQPK QRKISMLVNQ VLLLQRKFTC CSPTLVARND IKYAFKLSRE
     AIVSQVSRPV EKNESKTVKE TCIICLEDVD SGSMFSVDGC MHRYCFSCMK QHVEVKLLHG
     MVPKCPHEGC KSELIVDSCR KFMTPKMMET LKQRMKEASI PVTEKVYCPY PRCSTLMSRI
     EISEYAKDAL VGIERSGARK CLKCHGLFCI NCKVPWHSSM TCEDYKIKNP LPAAEDLKLK
     SLARMNLWRQ CVKCNHMIEL SEGCYHMTCR CGNEFCYNCG AEWKNKKATC SCPLWEEDLI
     WHDNRDSDEE EEEEYSDEED GDWS
//
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