ID A0A3Q7HY98_SOLLC Unreviewed; 175 AA.
AC A0A3Q7HY98;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
OS Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC Solanum subgen. Lycopersicon.
OX NCBI_TaxID=4081 {ECO:0000313|EnsemblPlants:Solyc09g007620.2.1};
RN [1] {ECO:0000313|EnsemblPlants:Solyc09g007620.2.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Heinz 1706 {ECO:0000313|EnsemblPlants:Solyc09g007620.2.1};
RX PubMed=22660326; DOI=10.1038/nature11119;
RG Tomato Genome Consortium;
RT "The tomato genome sequence provides insights into fleshy fruit
RT evolution.";
RL Nature 485:635-641(2012).
RN [2] {ECO:0000313|EnsemblPlants:Solyc09g007620.2.1}
RP IDENTIFICATION.
RC STRAIN=cv. Heinz 1706 {ECO:0000313|EnsemblPlants:Solyc09g007620.2.1};
RG EnsemblPlants;
RL Submitted (JAN-2019) 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; A0A3Q7HY98; -.
DR STRING; 4081.A0A3Q7HY98; -.
DR PaxDb; 4081-Solyc09g007620-1-1; -.
DR EnsemblPlants; Solyc09g007620.2.1; Solyc09g007620.2.1; Solyc09g007620.2.
DR Gramene; Solyc09g007620.2.1; Solyc09g007620.2.1; Solyc09g007620.2.
DR InParanoid; A0A3Q7HY98; -.
DR OMA; RIDCGHM; -.
DR Proteomes; UP000004994; Chromosome 9.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR045191; MBR1/2-like.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR22937; E3 UBIQUITIN-PROTEIN LIGASE RNF165; 1.
DR PANTHER; PTHR22937:SF205; 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; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000004994};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 102..143
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..35
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 175 AA; 19602 MW; EACB9842E449E98A CRC64;
MESYNSNGAM NGDGSSNAPI SDNREGVTNV INPNVPENEG GEVRDSEVDR RNFLYQEVVE
RAISELEEHA RAGFRAIPPL LNINLHVYEA ANSTFSEPKD KCSVCLEEFC DKEELARIDC
GHMYHIDCLK KWNLVVNTCP ICRRRVAVIC HFTLKIRAYL DRLAAANQLS SGSVN
//