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Database: UniProt
Entry: A0A811Q9A3_9POAL
LinkDB: A0A811Q9A3_9POAL
Original site: A0A811Q9A3_9POAL 
ID   A0A811Q9A3_9POAL        Unreviewed;       537 AA.
AC   A0A811Q9A3;
DT   29-SEP-2021, integrated into UniProtKB/TrEMBL.
DT   29-SEP-2021, sequence version 1.
DT   18-JUN-2025, entry version 17.
DE   RecName: Full=RBR-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012251};
DE            EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
GN   ORFNames=NCGR_LOCUS39362 {ECO:0000313|EMBL:CAD6255832.1};
OS   Miscanthus lutarioriparius.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Saccharinae; Miscanthus.
OX   NCBI_TaxID=422564 {ECO:0000313|EMBL:CAD6255832.1, ECO:0000313|Proteomes:UP000604825};
RN   [1] {ECO:0000313|EMBL:CAD6255832.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Han B., Lu T., Zhao Q., Huang X., Zhao Y.;
RL   Submitted (OCT-2020) 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:CAD6255832.1}.
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DR   EMBL; CAJGYO010000010; CAD6255832.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A811Q9A3; -.
DR   OrthoDB; 10009520at2759; -.
DR   Proteomes; UP000604825; 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; cd20346; BRcat_RBR_ANKIB1; 1.
DR   FunFam; 1.20.120.1750:FF:000027; 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; IPR048962; ARIH1-like_UBL.
DR   InterPro; IPR031127; E3_UB_ligase_RBR.
DR   InterPro; IPR002867; IBR_dom.
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; 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; PS00518; ZF_RING_1; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000604825};
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          131..353
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51873"
FT   REGION          1..30
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          350..371
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        7..30
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        355..364
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   537 AA;  59706 MW;  3D6F8F97A3B6DE2C CRC64;
     MRTGHEYDED MAGDDDGYGE DDDYTFDDDS CDYDEVETTE VNAADDGEEA EQRYVVLNED
     AVRARQEGET AKVAEILSIP RGFAAVLLRH FKWSAGRIQE EWFSDDARVR AAIGMPADDG
     GVPVPTAVSR AEMSCAICFV NYPAGETRSA GCAHYYCGEC WRAYIRAAVD DGARCLALRC
     PDPSCPAAVV QELVDIAADK ADRERYARFA LRSFVEEGGG GGAGSVPMRW CPGAGCTRAV
     EFLGGGTGDA HAADVFCACR HGFCWSCGEE AHRPVSCDTV RAWLDKNASY TETSNWMLAN
     TKHCPRCRLP IEKNQGCMHM TCPPPCGHEF CWVCLDPWDN HTGCAGFPAA ADGDGNGRQE
     ERTKRQQSRS QAAMDMDRYV YHYERWAANY SSLENVFKDM AQLESAEIER IAAVVGQPAA
     SFAFLSKAYE QIAHGRRVLK WAHAYGYYLD PVRDAAKRGL FEDLLDQANS QLERLHAAAE
     LERRELFCSD AEPAVVRDLL KYYKDKVESY TAVTRTFLRN LVTAFETTDL PEFKSLK
//
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