ID J3MQM5_ORYBR Unreviewed; 494 AA.
AC J3MQM5;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=E3 ubiquitin-protein ligase RMA {ECO:0000256|RuleBase:RU369090};
DE EC=2.3.2.27 {ECO:0000256|RuleBase:RU369090};
DE AltName: Full=Protein RING membrane-anchor {ECO:0000256|RuleBase:RU369090};
DE AltName: Full=RING-type E3 ubiquitin transferase RMA {ECO:0000256|RuleBase:RU369090};
GN Name=102722883 {ECO:0000313|EnsemblPlants:OB08G14040.1};
OS Oryza brachyantha (malo sina).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=4533 {ECO:0000313|EnsemblPlants:OB08G14040.1};
RN [1] {ECO:0000313|EnsemblPlants:OB08G14040.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IRGC 101232 {ECO:0000313|EnsemblPlants:OB08G14040.1};
RX PubMed=23481403;
RA Chen J., Huang Q., Gao D., Wang J., Lang Y., Liu T., Li B., Bai Z.,
RA Luis Goicoechea J., Liang C., Chen C., Zhang W., Sun S., Liao Y., Zhang X.,
RA Yang L., Song C., Wang M., Shi J., Liu G., Liu J., Zhou H., Zhou W., Yu Q.,
RA An N., Chen Y., Cai Q., Wang B., Liu B., Min J., Huang Y., Wu H., Li Z.,
RA Zhang Y., Yin Y., Song W., Jiang J., Jackson S.A., Wing R.A., Wang J.,
RA Chen M.;
RT "Whole-genome sequencing of Oryza brachyantha reveals mechanisms underlying
RT Oryza genome evolution.";
RL Nat. Commun. 4:1595-1595(2013).
RN [2] {ECO:0000313|EnsemblPlants:OB08G14040.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (APR-2013) to UniProtKB.
CC -!- FUNCTION: E3 ubiquitin-protein ligase. {ECO:0000256|RuleBase:RU369090}.
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 ECO:0000256|RuleBase:RU369090};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906, ECO:0000256|RuleBase:RU369090}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|RuleBase:RU369090}; Single-pass type IV membrane protein
CC {ECO:0000256|RuleBase:RU369090}.
CC -!- DOMAIN: The RING-type zinc finger domain is responsible for E3 ligase
CC activity. {ECO:0000256|RuleBase:RU369090}.
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DR RefSeq; XP_015696052.1; XM_015840566.1.
DR AlphaFoldDB; J3MQM5; -.
DR STRING; 4533.J3MQM5; -.
DR EnsemblPlants; OB08G14040.1; OB08G14040.1; OB08G14040.
DR GeneID; 102722883; -.
DR Gramene; OB08G14040.1; OB08G14040.1; OB08G14040.
DR KEGG; obr:102722883; -.
DR eggNOG; KOG0823; Eukaryota.
DR HOGENOM; CLU_574093_0_0_1; -.
DR OMA; GTRRRMD; -.
DR OrthoDB; 901818at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000006038; Chromosome 8.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd16745; RING-HC_AtRMA-like; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR045103; RNF5/RNF185-like.
DR InterPro; IPR018957; Znf_C3HC4_RING-type.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR12313; E3 UBIQUITIN-PROTEIN LIGASE RNF5-RELATED; 1.
DR PANTHER; PTHR12313:SF95; RING-TYPE E3 UBIQUITIN TRANSFERASE; 1.
DR Pfam; PF00097; zf-C3HC4; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Endoplasmic reticulum {ECO:0000256|RuleBase:RU369090};
KW Membrane {ECO:0000256|RuleBase:RU369090};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU369090};
KW Reference proteome {ECO:0000313|Proteomes:UP000006038};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU369090};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|RuleBase:RU369090};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU369090};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 268..309
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 192..259
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 329..351
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 377..494
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..23
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 35..49
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 218..232
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 233..259
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 403..425
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 445..466
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 494 AA; 52433 MW; 5A20FA44D3B67355 CRC64;
MDLNLYLGLP PLPQPPGRLD VAADYPPPPN SGGSAVVVAN EQRSSSEPQE VAVAPPAATP
PLPVVVPTPP AGAAYSPSNA LSTPEQVLVD PVAAWLVDPV DQRAVPLETP SNMAMASSAP
AQFARYDAEF VQALEAAGER RRPQTWLVQS GRAIPTALIR GAEIAAARRE SAQASPAATE
RMTPENRLRR LIQVSDQHRI GRGGPGQVSR GHHENSPEAD SLAQSINRSH NSLEASRRQK
LDGDGKVGKT DAAKKDDSCG GCHGSFECNI CLESAKDPVV TPCGHLFCWP CIYQWLHRHS
EYSDCPVCKS ELFEVNVTPI YGRGSAEQNS PINGIKIPPR PSAQRTESLR QQLQMPDRGI
ANMVRRLIQN QDIVAGQAAS SAGVERTGAS APRPRARGRR QARQDQNATA PVPATQQQVG
NADTGGGNQA PLPPPDANDA APAVAVAPQQ SSSVEQASTS STVGVAVGGP AQGRRSRNSE
STPTTTRRTR RRQQ
//
