ID A0A0D3HEY4_9ORYZ Unreviewed; 414 AA.
AC A0A0D3HEY4;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
OS Oryza barthii.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=65489 {ECO:0000313|EnsemblPlants:OBART10G13910.1};
RN [1] {ECO:0000313|EnsemblPlants:OBART10G13910.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IRGC 105608 {ECO:0000313|EnsemblPlants:OBART10G13910.1};
RX DOI=10.1007/s12284-009-9025-z;
RA Rounsley S., Marri P.R., Yu Y., He R., Sisneros N., Goicoechea J.L.,
RA Lee S.J., Angelova A., Kudrna D., Luo M., Affourtit J., Desany B.,
RA Knight J., Niazi F., Egholm M., Wing R.A.;
RT "De novo next generation sequencing of plant genomes.";
RL Rice 2:35-43(2009).
RN [2] {ECO:0000313|EnsemblPlants:OBART10G13910.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (MAR-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};
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DR AlphaFoldDB; A0A0D3HEY4; -.
DR STRING; 65489.A0A0D3HEY4; -.
DR PaxDb; 65489-OBART10G13910-1; -.
DR EnsemblPlants; OBART10G13910.1; OBART10G13910.1; OBART10G13910.
DR Gramene; OBART10G13910.1; OBART10G13910.1; OBART10G13910.
DR eggNOG; KOG0800; Eukaryota.
DR HOGENOM; CLU_034892_3_1_1; -.
DR Proteomes; UP000026960; Chromosome 10.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR CDD; cd16667; RING-H2_RNF126-like; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR039525; RNF126-like_zinc-ribbon.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR15710; E3 UBIQUITIN-PROTEIN LIGASE PRAJA; 1.
DR PANTHER; PTHR15710:SF237; F6A14.12 PROTEIN-RELATED; 1.
DR Pfam; PF13639; zf-RING_2; 1.
DR Pfam; PF14369; zinc_ribbon_9; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000026960};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 280..321
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 25..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 119..139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 157..179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 331..414
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 120..139
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 381..399
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 414 AA; 43019 MW; A975AA8350AD8B8D CRC64;
MTSFTTPTRS GGSDPVVMTV GVRRDGLGLA HHQPPPRPRD RRPPPCPNPA AYYAAVARKQ
YFCYQCNRTV LLPASAAAAG ALSCPECSGD FIEEVNVPPR HHPLPLRFPP MMPTATSASA
AAAAAASPTQ SSSSSAATSP SSDLSAFLNS MLGPLNLRTD ERMPGTTSAA GTATPEDEPD
GFDAVTFFQN YLQNLMDGGA NIQVLLDDAS VGLAPGIGRV GGASFGDYFV GPGLEQLIEQ
LAENDPNRYG TPPAAKSALS TLPDVVVTDA MVAAADGAEC AVCKEDFSPG EGAKQMPCKH
IYHADCIMSW LDLHNSCPIC RFELPTDDPD YEGRKKSNPQ PAAGVDAGAA SGSSTAAEER
EESGESARLV ERRFNVSLPW PFSGLGSQTP QQDGSNGGAG ASGSKDGGAS SDKK
//
