ID A0A059CZY1_EUCGR Unreviewed; 444 AA.
AC A0A059CZY1;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 31.
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_B00656 {ECO:0000313|EMBL:KCW83784.1};
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:KCW83784.1};
RN [1] {ECO:0000313|EMBL:KCW83784.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf extractions {ECO:0000313|EMBL:KCW83784.1};
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};
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DR EMBL; KK198754; KCW83784.1; -; Genomic_DNA.
DR RefSeq; XP_010045619.1; XM_010047317.1.
DR AlphaFoldDB; A0A059CZY1; -.
DR EnsemblPlants; KCW83784; KCW83784; EUGRSUZ_B00656.
DR GeneID; 104434379; -.
DR Gramene; KCW83784; KCW83784; EUGRSUZ_B00656.
DR KEGG; egr:104434379; -.
DR eggNOG; KOG0800; Eukaryota.
DR InParanoid; A0A059CZY1; -.
DR OrthoDB; 473485at2759; -.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR CDD; cd16454; RING-H2_PA-TM-RING; 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; PTHR15710; E3 UBIQUITIN-PROTEIN LIGASE PRAJA; 1.
DR PANTHER; PTHR15710:SF108; RING-TYPE DOMAIN-CONTAINING PROTEIN; 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 Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 393..434
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 444 AA; 48130 MW; 6170F3F506782FF8 CRC64;
MSAAEPPSPS GRRHRRRRSG LRRSLSLEPG PSPRHRRRRA RRSLDLYDSD DDLTLPVRDP
AAAADDRIED LLDVDFASDP DSGDRLRKIG GEGGCGVDLF VEDLQLAGGA DSASEEVNGL
DFGVIDANDD VCMDIVDVDL RIGLGLGVGG NEDVGFADED CCEDEFFMET GASGFNSCEA
GLTACEMEQC WSGVRDVEFD SDLELADALG VCGVSEDELS LDHVIDEDDY FCGVPLCWGD
PLPVEADGGE VEDLDLEWEE VESCVDDREV LSLFVDALND DGSISVSSTP IIADEGEEDA
SVEVVGDFGN LEWEVLLNSD NLVATAGLNH ELETYFDDDD DYLYSAEYET MFGQFTENES
SLVGGSPASE AVIRNLPKLA LTQEDVDGKD GLCPVCKDEF SAGNIATQLP CSHKYHTNCI
LTWLHVKNTC PVCRHELPAD GAES
//
