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Database: UniProt
Entry: A0A445FCH0_GLYSO
LinkDB: A0A445FCH0_GLYSO
Original site: A0A445FCH0_GLYSO 
ID   A0A445FCH0_GLYSO        Unreviewed;       496 AA.
AC   A0A445FCH0;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=E3 ubiquitin-protein ligase RGLG2 isoform A {ECO:0000313|EMBL:RZB46542.1};
DE   SubName: Full=E3 ubiquitin-protein ligase RGLG2 isoform B {ECO:0000313|EMBL:RZB46543.1};
DE   SubName: Full=E3 ubiquitin-protein ligase RGLG2 isoform C {ECO:0000313|EMBL:RZB46544.1};
DE   SubName: Full=E3 ubiquitin-protein ligase RGLG2 isoform D {ECO:0000313|EMBL:RZB46545.1};
DE   SubName: Full=E3 ubiquitin-protein ligase RGLG2 isoform E {ECO:0000313|EMBL:RZB46546.1};
GN   ORFNames=D0Y65_050535 {ECO:0000313|EMBL:RZB46542.1};
OS   Glycine soja (Wild soybean).
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; Glycine;
OC   Glycine subgen. Soja.
OX   NCBI_TaxID=3848 {ECO:0000313|EMBL:RZB46542.1, ECO:0000313|Proteomes:UP000289340};
RN   [1] {ECO:0000313|EMBL:RZB46542.1, ECO:0000313|Proteomes:UP000289340}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. W05 {ECO:0000313|Proteomes:UP000289340};
RC   TISSUE=Hypocotyl of etiolated seedlings {ECO:0000313|EMBL:RZB46542.1};
RA   Xie M., Chung C.Y.L., Li M.-W., Wong F.-L., Chan T.-F., Lam H.-M.;
RT   "A high-quality reference genome of wild soybean provides a powerful tool
RT   to mine soybean genomes.";
RL   Submitted (SEP-2018) to the EMBL/GenBank/DDBJ databases.
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   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RZB46542.1}.
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DR   EMBL; QZWG01000019; RZB46542.1; -; Genomic_DNA.
DR   EMBL; QZWG01000019; RZB46543.1; -; Genomic_DNA.
DR   EMBL; QZWG01000019; RZB46544.1; -; Genomic_DNA.
DR   EMBL; QZWG01000019; RZB46545.1; -; Genomic_DNA.
DR   EMBL; QZWG01000019; RZB46546.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A445FCH0; -.
DR   SMR; A0A445FCH0; -.
DR   OrthoDB; 3641271at2759; -.
DR   Proteomes; UP000289340; Chromosome 19.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR   GO; GO:0070534; P:protein K63-linked ubiquitination; IEA:InterPro.
DR   CDD; cd16729; RING-HC_RGLG_plant; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR010734; Copine_C.
DR   InterPro; IPR045317; RING-HC_RGLG1/2.
DR   InterPro; IPR002035; VWF_A.
DR   InterPro; IPR036465; vWFA_dom_sf.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR45751; COPINE FAMILY PROTEIN 1; 1.
DR   PANTHER; PTHR45751:SF51; E3 UBIQUITIN-PROTEIN LIGASE RGLG2; 1.
DR   Pfam; PF07002; Copine; 1.
DR   Pfam; PF13920; zf-C3HC4_3; 1.
DR   SMART; SM00184; RING; 1.
DR   SMART; SM00327; VWA; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   SUPFAM; SSF53300; vWA-like; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00175};
KW   Reference proteome {ECO:0000313|Proteomes:UP000289340};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00175};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00175}.
FT   DOMAIN          453..486
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          1..94
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          424..443
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..33
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        56..72
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   496 AA;  54041 MW;  F83EA20970C51C04 CRC64;
     MGGNNSKEDN NNWRQNSSVR SSSSASSWGS YPDPQSGYGH GGYAYEPQQP SYPTQQPYYA
     QPPPPPPNYG NEPQPHASGR VAGHRNEKRL DRKYSRITDN YNSIDEVTEA LARAGLESSN
     LILGIDFTKS NEWTGKHSFN RKSLHHIGNG PNPYEQAISI IGKTLAAFDE DNLIPCFGFG
     DASTHDQDVF SFYPDERICN GFEEVLSRYR EIVPIIRLAG PTSFAPIVEM AMTIVEQTGG
     QYHVLVIVAD GQVTRSIDTE HGRLSPQEQS TVDAIVEASK FPLSIILVGV GDGPWDMMKE
     FDDNIPARVF DNFQFVNFTE IMSKNIPPSR KEAAFALAAL MEIPSQYKAT IELNLLGGRN
     ANAPQRVALP TPSYGSASMG ISKPYGSASF GASKPYGSAS FDAPKPYGSA SFSSSKPSHA
     ASFEQSAPSY YDNTDPVGTA PPAPSSSYDN QLCPICLTNS KDMAFGCGHQ TCCECGQDLQ
     SCPICRSPIN TRIKLY
//
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