ID   A0A059CWR7_EUCGR        Unreviewed;       430 AA.
AC   A0A059CWR7;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE            EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN   ORFNames=EUGRSUZ_C03789 {ECO:0000313|EMBL:KCW82385.1};
OS   Eucalyptus grandis (Flooded gum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Myrtales; Myrtaceae; Myrtoideae; Eucalypteae; Eucalyptus.
OX   NCBI_TaxID=71139 {ECO:0000313|EMBL:KCW82385.1};
RN   [1] {ECO:0000313|EMBL:KCW82385.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Leaf extractions {ECO:0000313|EMBL:KCW82385.1};
RA   Schmutz J., Hayes R., Myburg A., Tuskan G., Grattapaglia D., Rokhsar D.S.;
RT   "The genome of Eucalyptus grandis.";
RL   Submitted (JUL-2013) 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   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000256|ARBA:ARBA00004906}.
CC   -!- SIMILARITY: Belongs to the RING-type zinc finger family. ATL subfamily.
CC       {ECO:0000256|ARBA:ARBA00024209}.
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DR   EMBL; KK198755; KCW82385.1; -; Genomic_DNA.
DR   RefSeq; XP_010049645.1; XM_010051343.2.
DR   AlphaFoldDB; A0A059CWR7; -.
DR   EnsemblPlants; KCW82385; KCW82385; EUGRSUZ_C03789.
DR   GeneID; 104438245; -.
DR   Gramene; KCW82385; KCW82385; EUGRSUZ_C03789.
DR   KEGG; egr:104438245; -.
DR   eggNOG; KOG0800; Eukaryota.
DR   InParanoid; A0A059CWR7; -.
DR   OMA; FHKFKHK; -.
DR   OrthoDB; 472733at2759; -.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   CDD; cd16461; RING-H2_EL5-like; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR46539; E3 UBIQUITIN-PROTEIN LIGASE ATL42; 1.
DR   PANTHER; PTHR46539:SF1; E3 UBIQUITIN-PROTEIN LIGASE ATL42; 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   3: Inferred from homology;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00175};
KW   Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00175};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00175}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..430
FT                   /note="RING-type E3 ubiquitin transferase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5001569673"
FT   TRANSMEM        37..62
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          117..159
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          358..393
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          407..430
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        372..386
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   430 AA;  48922 MW;  D37A666C76ABD823 CRC64;
     MNRAHVYVLI FCWVFFLHVE AQIPPQGAVI SQDDSNVQSS LGVVMAILSL MFLIACILLV
     YAKYCLSSRS AIHSDPEALL WLTRSRSQLS GIDKTAIESL PFFRFSSLRG SKEGLECAVC
     LSKFEDVEIL RLLPQCKHAF HIECIDRWLE NHSSCPICRL RLSVEDPAIF TYSSSMRLRN
     QSSRHDDSNP ELLFVQREEG NRGSSRFGIG RSLRRMFKAD REDEVSIRDA ARNADQDPRG
     DLHKFNHRIL VPDGFFKNRW SNVSSSDLMF LNSEMLSSAS SNRFSSLEAN PGQSKTSRAN
     DEGQIGKIRE EMELKRLFES KPGPKSLTSP VLMAGLPPPM ATGRSKYLLP DEKRSMSEIT
     GVSRLGELNR KSRYTQEASS QENGGGSSRE ERMRRLWLPI ARRTAQWFAN RDRRSQDPEN
     QNLRLKPEDV
//