ID A0A0E0KR26_ORYPU Unreviewed; 286 AA.
AC A0A0E0KR26;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
OS Oryza punctata (Red rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=4537 {ECO:0000313|EnsemblPlants:OPUNC04G11720.1};
RN [1] {ECO:0000313|EnsemblPlants:OPUNC04G11720.1}
RP NUCLEOTIDE SEQUENCE.
RA Wing R.;
RT "Oryza genome evolution.";
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:OPUNC04G11720.1}
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; A0A0E0KR26; -.
DR STRING; 4537.A0A0E0KR26; -.
DR EnsemblPlants; OPUNC04G11720.1; OPUNC04G11720.1; OPUNC04G11720.
DR Gramene; OPUNC04G11720.1; OPUNC04G11720.1; OPUNC04G11720.
DR eggNOG; KOG0800; Eukaryota.
DR HOGENOM; CLU_066543_1_1_1; -.
DR OMA; VMHHFLA; -.
DR Proteomes; UP000026962; Chromosome 4.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR46539; E3 UBIQUITIN-PROTEIN LIGASE ATL42; 1.
DR PANTHER; PTHR46539:SF2; RING FINGER PROTEIN 150 ISOFORM X1; 1.
DR Pfam; PF13639; zf-RING_2; 1.
DR SMART; SM00184; RING; 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:UP000026962};
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..53
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 119..161
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 62..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 243..286
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 286 AA; 28679 MW; FEDE684E550E2910 CRC64;
MSALVVGDAD GGAVAPGGGQ ASPTVVVDGD VVLSGVVLIF VALAFVFVMH HFLAAMRRRD
TSDAGSTSSV SSGGGRGVMA GVGTDGAKAG GQGGVDPAVL RALPVTVYRA EEAAVALECA
VCLAEVEDGE AARFLPRCGH GFHAECVDLW LRSHPTCPLC RLAVVDAPPP FTLPPAQPEP
ANYANATTTA LPTNVLFWGS QGAVATTTTI VDSGRHTSAA AASSSGGDEA AAVVLVIEVP
DTTTTATREG RGGAAAAKPQ GDSARVAGSL RRMWSSSRGA PPPPRT
//
