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Database: UniProt
Entry: A0A0E0BYZ6_9ORYZ
LinkDB: A0A0E0BYZ6_9ORYZ
Original site: A0A0E0BYZ6_9ORYZ 
ID   A0A0E0BYZ6_9ORYZ        Unreviewed;       231 AA.
AC   A0A0E0BYZ6;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE            EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
OS   Oryza meridionalis.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX   NCBI_TaxID=40149 {ECO:0000313|EnsemblPlants:OMERI01G07190.1};
RN   [1] {ECO:0000313|EnsemblPlants:OMERI01G07190.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=OR44 {ECO:0000313|EnsemblPlants:OMERI01G07190.1};
RA   Wing R.A., Panaud O., Henry R.;
RL   Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblPlants:OMERI01G07190.1}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (APR-2015) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC         [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC         cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC         EC=2.3.2.27; Evidence={ECO:0000256|ARBA:ARBA00000900};
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000256|ARBA:ARBA00004906}.
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DR   AlphaFoldDB; A0A0E0BYZ6; -.
DR   STRING; 40149.A0A0E0BYZ6; -.
DR   EnsemblPlants; OMERI01G07190.1; OMERI01G07190.1; OMERI01G07190.
DR   Gramene; OMERI01G07190.1; OMERI01G07190.1; OMERI01G07190.
DR   eggNOG; KOG0800; Eukaryota.
DR   HOGENOM; CLU_013137_12_0_1; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000008021; Chromosome 1.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   CDD; cd16461; RING-H2_EL5-like; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR011016; Znf_RING-CH.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR46539; E3 UBIQUITIN-PROTEIN LIGASE ATL42; 1.
DR   PANTHER; PTHR46539:SF29; RING-TYPE E3 UBIQUITIN TRANSFERASE; 1.
DR   Pfam; PF13639; zf-RING_2; 1.
DR   SMART; SM01197; FANCL_C; 1.
DR   SMART; SM00184; RING; 1.
DR   SMART; SM00744; RINGv; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00175};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008021};
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|PROSITE-ProRule:PRU00175};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00175}.
FT   TRANSMEM        31..58
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          127..169
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          182..231
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        205..231
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   231 AA;  23415 MW;  A98C3FF9DBE6CD72 CRC64;
     MSDTALSGAP PAARSEDSWS QQQSYNFSGR VLLTAVVILF VIAVVFAVTR VLLYYLVVRP
     GGGGGGRRRG GLAGGILRSL NSLGVSGRRG LDASALAALP VTAYRKNGGG GGEGSNRGGP
     GATAADCAVC LSELADGEKV RELPNCRHVF HVECVDAWLR SRTTCPLCRA EAEVPKARAS
     AAAQSSSSLG DGGITVVVTI NGGSDEAGGR STALTGQPGS SNSPSCEPAR N
//
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