ID A0A0E0JDH4_ORYPU Unreviewed; 640 AA.
AC A0A0E0JDH4;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE SubName: Full=E3 ubiquitin-protein ligase {ECO:0000313|EnsemblPlants:OPUNC01G01290.1};
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:OPUNC01G01290.1};
RN [1] {ECO:0000313|EnsemblPlants:OPUNC01G01290.1}
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:OPUNC01G01290.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (APR-2015) to UniProtKB.
CC -!- FUNCTION: E3 ubiquitin-protein ligase that mediates ubiquitination and
CC subsequent proteasomal degradation of target proteins. E3 ubiquitin
CC ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the
CC form of a thioester and then directly transfers the ubiquitin to
CC targeted substrates. It probably triggers the ubiquitin-mediated
CC degradation of different substrates. {ECO:0000256|ARBA:ARBA00024004}.
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DR AlphaFoldDB; A0A0E0JDH4; -.
DR STRING; 4537.A0A0E0JDH4; -.
DR EnsemblPlants; OPUNC01G01290.1; OPUNC01G01290.1; OPUNC01G01290.
DR Gramene; OPUNC01G01290.1; OPUNC01G01290.1; OPUNC01G01290.
DR eggNOG; KOG3002; Eukaryota.
DR HOGENOM; CLU_512298_0_0_1; -.
DR OMA; HENACMF; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000026962; Chromosome 1.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR InterPro; IPR044286; SINL_plant.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR013010; Znf_SIAH.
DR PANTHER; PTHR46632:SF16; E3 UBIQUITIN-PROTEIN LIGASE SINA-LIKE 10; 1.
DR PANTHER; PTHR46632; E3 UBIQUITIN-PROTEIN LIGASE SINA-LIKE 4; 1.
DR Pfam; PF21361; Sina_ZnF; 1.
DR SUPFAM; SSF49599; TRAF domain-like; 2.
DR PROSITE; PS50089; ZF_RING_2; 1.
DR PROSITE; PS51081; ZF_SIAH; 2.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00455};
KW Reference proteome {ECO:0000313|Proteomes:UP000026962};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00455};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00455}.
FT DOMAIN 46..82
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 99..154
FT /note="SIAH-type"
FT /evidence="ECO:0000259|PROSITE:PS51081"
FT DOMAIN 460..516
FT /note="SIAH-type"
FT /evidence="ECO:0000259|PROSITE:PS51081"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 356..393
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..36
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 360..393
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 640 AA; 68573 MW; D98FB2B40ACE7DAC CRC64;
MAKTNEKTAM GDHGTPKRLR TEKGQQQQDG EEETGGYSID RDALECAICS MPFQAEIYMC
NNGHAACGSC CAGVNKACPS CREPIGDIRC RPLEKAVVAI SSPCKFRASG CMKTLGYTDK
SVVPARPHAP CRCPFDGCTY QGLLLYHHIQ DEHAKDGVAM TRRTTVTVHK TKPFHVLLNR
RGGGTRVFVL INGGGVPKGR SLSLVSVGPP PLPPPPKCKA AYTITVGAVG GRLGCLSFSG
TVPRVRSVQE FEGTSFLFVP DVYWGSSGTI AVIEDSRVLL LLNGGDVPKG RSLSVVCVGP
RPAAGAGEAE LYTMAVSGGV PGALSLSASG SVPRVRQWVR YPTGFLFLRR QRLRMKKRCG
KKPTMDQSTP KKSRSEKKAA GLSTDQQDEE NETTKMTYSI DSDSLECGIC FLAFEARVYM
CKNGHAACGS CCVGMSRACP FCHEPIGDIR CRPLEKVLAA MSAPCKFRSS GCTEIVAYTE
RRSHEASCPH VPCRCPFDGC NYQGHLLYSH IQDEHATDAV VAMGCLRGTT VTVHKGKPFH
VLFHRGGTRV FLLLNGGDVL SGRSLSLVSV GHPPPANCEL LYKIELAAAG PGPGTGELSL
SASGTVPCVR RLEGFEAKAF LFVPDSYWGS SGTVSVTVHV
//