ID A0A1S3U9C3_VIGRR Unreviewed; 524 AA.
AC A0A1S3U9C3; A0A1S3U9H5;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 2.
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};
GN Name=LOC106762992 {ECO:0000313|RefSeq:XP_014502623.2,
GN ECO:0000313|RefSeq:XP_014502626.1};
OS Vigna radiata var. radiata (Mung bean) (Phaseolus aureus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Vigna.
OX NCBI_TaxID=3916 {ECO:0000313|Proteomes:UP000087766, ECO:0000313|RefSeq:XP_014502623.2};
RN [1] {ECO:0000313|RefSeq:XP_014502623.2, ECO:0000313|RefSeq:XP_014502626.1}
RP IDENTIFICATION.
RC TISSUE=Leaf {ECO:0000313|RefSeq:XP_014502623.2,
RC ECO:0000313|RefSeq:XP_014502626.1};
RG RefSeq;
RL Submitted (NOV-2023) 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 RefSeq; XP_014502623.2; XM_014647137.2.
DR RefSeq; XP_014502624.1; XM_014647138.1.
DR RefSeq; XP_014502626.1; XM_014647140.2.
DR GeneID; 106762992; -.
DR KEGG; vra:106762992; -.
DR OrthoDB; 988298at2759; -.
DR Proteomes; UP000087766; Chromosome 6.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
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:SF136; 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:UP000087766};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 470..511
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 198..306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 325..349
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 63..119
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 133..171
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 210..229
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 230..306
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 325..339
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 524 AA; 57286 MW; AA5FD28EE4959CD4 CRC64;
MDECSGRRGV DGVAVPRKGM THVFRDTANT RERTGQVCSK LGCSSRANIP KVAQVRSSEK
GKSVRPLFQS SSTSKEEIGS SSRSTSNPAK RTTEPQKILS SQFEADSPES SSVQDEPESS
ELIPPSEEIQ RGPKSRGGSS DSSNVRLMEV GSSSSVSNTR SQRNLNQRPG LRGQEIKNPG
HAVSSRYGLR NIRCNTISDV IPSGCSSSDS SHNRRKDTIK KRDGEGESSS TVRGKNIIGS
SLEGRNSGSR NGISISDSRR TRNTLSHRNS SLAPVRTQRS LSGHARGRLS SQGNENPLAT
SEFQHSGDVN PHGISCQISV ENPLTCSSSC DSPGNSSEDL PLSPPAEDDI TDSLNGDSFW
HYSMSSIEGV VLALERIEQG GELTREQILM FGTDIYENGL NFYDHHRDMR LDIDNMSYEE
LLALEERMGT VSTALSEEAL AESLKRSIYQ SPPTHDTHKN CNEDKDDIKC CICQEEYVTG
DEVGDLPCKH RFHVDCIQEW MGLKNWCPIC KLSAALSNNS SSPH
//
