ID B6TF06_MAIZE Unreviewed; 236 AA.
AC B6TF06;
DT 16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT 16-DEC-2008, sequence version 1.
DT 27-MAR-2024, entry version 57.
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};
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577 {ECO:0000313|EMBL:ACG35689.1};
RN [1] {ECO:0000313|EMBL:ACG35689.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=18937034; DOI=10.1007/s11103-008-9415-4;
RA Alexandrov N.N., Brover V.V., Freidin S., Troukhan M.E., Tatarinova T.V.,
RA Zhang H., Swaller T.J., Lu Y.P., Bouck J., Flavell R.B., Feldmann K.A.;
RT "Insights into corn genes derived from large-scale cDNA sequencing.";
RL Plant Mol. Biol. 69:179-194(2009).
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 EMBL; EU963571; ACG35689.1; -; mRNA.
DR AlphaFoldDB; B6TF06; -.
DR UniPathway; UPA00143; -.
DR ExpressionAtlas; B6TF06; baseline and differential.
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; 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:SF7; RING-TYPE E3 UBIQUITIN TRANSFERASE; 1.
DR Pfam; PF13639; zf-RING_2; 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 2: Evidence at transcript level;
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 Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU369090};
KW Transmembrane {ECO:0000256|RuleBase:RU369090};
KW Transmembrane helix {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 TRANSMEM 216..235
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU369090"
FT DOMAIN 24..65
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 79..110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 79..94
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 236 AA; 25502 MW; B1C02EB4B5F17439 CRC64;
MSANVGESTS GVSSSDAAGG SFECNICFEL PQEPIVTLCG HLFCWPCLYR WLHIHAHSPE
CPVCKALVEE DKLVPLYGRG KDRVDPRSKN MPEGEIPHRP TGQRPATAPR AHANSNFANA
NANANPWFPG AGVPLANARW GNYAFSAAFG GLFPMLSFQV HGFPDAAAYA QPAGFHYEYG
HGHGHGFHHG GHMGQAQAHG VHRQAPLGQQ QQQADIYLKA LLFMIVILVL ASLLAF
//
