ID A0A0D9XIH1_9ORYZ Unreviewed; 431 AA.
AC A0A0D9XIH1;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
OS Leersia perrieri.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Leersia.
OX NCBI_TaxID=77586 {ECO:0000313|EnsemblPlants:LPERR10G03770.1, ECO:0000313|Proteomes:UP000032180};
RN [1] {ECO:0000313|EnsemblPlants:LPERR10G03770.1, ECO:0000313|Proteomes:UP000032180}
RP NUCLEOTIDE SEQUENCE.
RA Wing R.A.;
RT "Oryza genome evolution.";
RL Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:LPERR10G03770.1, ECO:0000313|Proteomes:UP000032180}
RP NUCLEOTIDE SEQUENCE.
RA Yu Y., Lee S., de Baynast K., Wissotski M., Liu L., Talag J.,
RA Goicoechea J., Angelova A., Jetty R., Kudrna D., Golser W., Rivera L.,
RA Zhang J., Wing R.;
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblPlants:LPERR10G03770.1}
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 -!- SIMILARITY: Belongs to the RING-type zinc finger family. LOG2
CC subfamily. {ECO:0000256|ARBA:ARBA00025721}.
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DR AlphaFoldDB; A0A0D9XIH1; -.
DR STRING; 77586.A0A0D9XIH1; -.
DR EnsemblPlants; LPERR10G03770.1; LPERR10G03770.1; LPERR10G03770.
DR Gramene; LPERR10G03770.1; LPERR10G03770.1; LPERR10G03770.
DR eggNOG; KOG4265; Eukaryota.
DR HOGENOM; CLU_016631_0_0_1; -.
DR Proteomes; UP000032180; 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; cd16789; mRING-HC-C3HC5_MGRN1-like; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR045195; LOG2-like_mRING_C3HC5.
DR InterPro; IPR045194; MGRN1/RNF157-like.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR22996:SF27; E3 UBIQUITIN-PROTEIN LIGASE LOG2-RELATED; 1.
DR PANTHER; PTHR22996; MAHOGUNIN; 1.
DR Pfam; PF13920; zf-C3HC4_3; 1.
DR PIRSF; PIRSF036836; RNase_bind_SBP1; 2.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Reference proteome {ECO:0000313|Proteomes:UP000032180};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00175}.
FT DOMAIN 350..389
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 403..431
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..27
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 60..95
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 431 AA; 47821 MW; 906A739EA037FE5C CRC64;
MGNMGSSGGH RRRSNGHGRH HHHHHSQAPA PPPPSQQQQQ QQQPEAAAPN RYVFAAASPY
PPQYPNPNPP PPQYYPQYGN FYPPPPPPSM PGPLPAPYDH HHRGGGGPVQ QPPPPPIHAA
GEFPPVMLQQ QHPQYHGWGG SFSYGPPPPA SATPPYVEHQ KAVTIRNDVN LKKETLRIEP
DDECPGRFLV AFTFDATVAG SMTIYFFAKE ELNCNLMATK EELLKPVTVT FNEGLGQKFR
QPSGTGIDFS LFEDAELFKE GDMDVYPLAV KAETELSTGQ FSKGEEHKSQ TPNSQITQAV
FERKEHGDYH VRVVKQILWV NGTRYELQEI YGIGNSVEGD SEGNDPGKEC VICLSEPRDT
TVLPCRHMCM CSECAKVLRY QTNRCPICRQ PVERLLEIKV NNKGEEQQLQ TPQSPSAPST
APPQQLQEAQ A
//
