ID   A0A1S3UG75_VIGRR        Unreviewed;       881 AA.
AC   A0A1S3UG75;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=E3 ubiquitin protein ligase {ECO:0000256|RuleBase:RU365038};
DE            EC=2.3.2.27 {ECO:0000256|RuleBase:RU365038};
GN   Name=LOC106764992 {ECO:0000313|RefSeq:XP_014504949.1};
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_014504949.1};
RN   [1] {ECO:0000313|RefSeq:XP_014504949.1}
RP   IDENTIFICATION.
RC   TISSUE=Leaf {ECO:0000313|RefSeq:XP_014504949.1};
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|RuleBase:RU365038};
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000256|ARBA:ARBA00004906, ECO:0000256|RuleBase:RU365038}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC       ECO:0000256|RuleBase:RU365038}.
CC   -!- SIMILARITY: Belongs to the BRE1 family. {ECO:0000256|ARBA:ARBA00005555,
CC       ECO:0000256|RuleBase:RU365038}.
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DR   RefSeq; XP_014504949.1; XM_014649463.2.
DR   AlphaFoldDB; A0A1S3UG75; -.
DR   STRING; 3916.A0A1S3UG75; -.
DR   GeneID; 106764992; -.
DR   KEGG; vra:106764992; -.
DR   OrthoDB; 53681at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000087766; Chromosome 6.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniRule.
DR   CDD; cd16499; RING-HC_Bre1-like; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR013956; E3_ubiquit_lig_Bre1.
DR   InterPro; IPR018957; Znf_C3HC4_RING-type.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   PANTHER; PTHR23163:SF7; E3 UBIQUITIN-PROTEIN LIGASE BRE1-LIKE 2; 1.
DR   PANTHER; PTHR23163; RING FINGER PROTEIN-RELATED; 1.
DR   Pfam; PF00097; zf-C3HC4; 1.
DR   SMART; SM00184; RING; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   SUPFAM; SSF57997; Tropomyosin; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   3: Inferred from homology;
KW   Chromatin regulator {ECO:0000256|ARBA:ARBA00022853,
KW   ECO:0000256|RuleBase:RU365038};
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|RuleBase:RU365038};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU365038}; Nucleus {ECO:0000256|RuleBase:RU365038};
KW   Reference proteome {ECO:0000313|Proteomes:UP000087766};
KW   Transferase {ECO:0000256|RuleBase:RU365038};
KW   Ubl conjugation pathway {ECO:0000256|RuleBase:RU365038};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU365038};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00175}.
FT   DOMAIN          829..867
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          1..35
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          46..73
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          250..277
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          407..455
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          584..807
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1..17
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        19..35
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   881 AA;  100265 MW;  85024FE64915923D CRC64;
     MENSDHDEPE KKRPHLTSVS SRTSRNSINS PTTNKTADAG VLQFQNQQLV QQIDVQKHAL
     HGLEEKIREL KGKQSSYDDL LIALNQLWTQ LVDDMILLGI QAGRGKGKDT LRYLTDIENP
     EGSLPLCPAE DIFLCRLIQK DSIKGISDDE ITGYVEEALA LRQSSTMELL KLLKDIIDDQ
     MERSGGIAQI LDGDISSEDA ITLMTKIDDM MKEEASNLQE VIDTLHAKHK EYTVGIKKFI
     NECLQEQSDI KHLAGELDEI VAELEESRRK LVNLEMQKDT SVGMNSPNAD AVNGNLSPEN
     IADRTMGLRE LKDSIEEAKI VDADRISELQ EAQEDNQTLT KQFQDLQNEL KDDKYIRSSR
     IYSLANDQLQ HWTSELARYK TLVESLQAGS VHIAKWENEL NLKLESADSA RQLLDNSDHR
     IDDLEHQLQK CIIEKNDLEI KMEEAKQDAG RKDIKSEFRV MASALSKEMG MMEAQLKRWK
     DAAHEAVSLR EKAHSLREVL NVKTSELKSL ANKCAEQVLE IRSLKMLTEK LQKENQELEF
     VLDMYGQENY DKSYSEVRES ESKAHSQAEI LKNALDEHSL ELRVKAANEA EAACEQRLSA
     AEAEIEDLRA KLDASERGIL ELTEAIKVKE AEAEAYISEI ETIGQAYEDM QTQNQNLLDQ
     VIERDDYNIK LVSDSVKAKQ AYNTLLTQKQ ALAKQLQQLN TSIENSKARI AHSEEQMKTI
     LSEAIKCNQE EKHLAVTLEF ARWELADAEK ELKLLKSSVS SSEKEYDQIQ KDTEAIEMEL
     ESERSSRKKL EEELRELNSQ IAELTSETGE TTIQKLEKEI RICKNMIKCT VCTDRPKEVV
     IVKCYHLFCN PCIQRNLELR HRKCPACGTA FGQSDVRFVK I
//