ID A0A059BY29_EUCGR Unreviewed; 633 AA.
AC A0A059BY29;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
DE AltName: Full=Deubiquitinating enzyme MINDY-3 {ECO:0000256|ARBA:ARBA00033208};
GN ORFNames=EUGRSUZ_F04241 {ECO:0000313|EMBL:KCW71143.1};
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:KCW71143.1};
RN [1] {ECO:0000313|EMBL:KCW71143.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf extractions {ECO:0000313|EMBL:KCW71143.1};
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 -!- FUNCTION: Hydrolase that can remove 'Lys-48'-linked conjugated
CC ubiquitin from proteins. {ECO:0000256|ARBA:ARBA00002107}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide
CC and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-
CC residue protein attached to proteins as an intracellular targeting
CC signal).; EC=3.4.19.12; Evidence={ECO:0000256|ARBA:ARBA00000707};
CC -!- SIMILARITY: Belongs to the MINDY deubiquitinase family. FAM188
CC subfamily. {ECO:0000256|ARBA:ARBA00011074}.
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DR EMBL; KK198758; KCW71143.1; -; Genomic_DNA.
DR RefSeq; XP_010063873.1; XM_010065571.2.
DR AlphaFoldDB; A0A059BY29; -.
DR STRING; 71139.A0A059BY29; -.
DR EnsemblPlants; KCW71143; KCW71143; EUGRSUZ_F04241.
DR GeneID; 104450864; -.
DR Gramene; KCW71143; KCW71143; EUGRSUZ_F04241.
DR KEGG; egr:104450864; -.
DR eggNOG; KOG2871; Eukaryota.
DR InParanoid; A0A059BY29; -.
DR OMA; NEFWQVL; -.
DR OrthoDB; 72090at2759; -.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR GO; GO:1990380; F:K48-linked deubiquitinase activity; IEA:InterPro.
DR Gene3D; 1.10.238.10; EF-hand; 1.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR025257; MINDY-3/4_CD.
DR InterPro; IPR039785; MINY3/4.
DR PANTHER; PTHR12473:SF8; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE MINDY-3; 1.
DR PANTHER; PTHR12473; UNCHARACTERIZED; 1.
DR Pfam; PF13898; MINDY-3_4_CD; 1.
DR SMART; SM01174; DUF4205; 1.
DR SUPFAM; SSF47473; EF-hand; 1.
PE 3: Inferred from homology;
FT DOMAIN 136..506
FT /note="Deubiquitinating enzyme MINDY-3/4 conserved"
FT /evidence="ECO:0000259|SMART:SM01174"
FT REGION 1..126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 579..606
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 633 AA; 67826 MW; BC9B9B677EDF3427 CRC64;
MADQEEEDLK MALRLSMQPS PPEPKRSKPR DAAAGGGAAV AAAVAASSSS SPEDGRRMQR
ELMAAAAEKR MLASRGAGGA PSPAPSPSPA QSQSPAPLLA PNNEKSKPLP QREGGAGVDD
GRTGRGLSSE EACQLFSMVF GSDVSKGILA QWSNQGIRFS PDPETSMGLV QHEGGPCGVL
AAVQAFVLKY LLFFPDDFRK GASTISPFHG TKASSRRQFQ GSDNFASLTD NEKLRALIRS
MSEILFHCGS NKRAVIATLS VTGKELEGAA DGSKDESIIK ALEGLSIESA SDLQSILRVE
TYSVQATVFQ RLEATLPVFQ SRMGALLFLI SALLSRGLDA VQADRDDPSL PLVTAPFGHA
SQEIVNLLLC GQAVPNVFDG RMDLGGGMFL KGVSTSVEVG FLTLLESLNF CKVGQHLKCP
IWPIWVVGSE SHYTVLFALD TVVQEENELE ERESQIRRAF DAQDQSGGGG FIGVEGFHQV
LRETDIRLTS EKVDQLCSSG FIVWSEFWQA ILDLDSSMGG LKDSSGLMGK KVFDLYHFNG
IAKSDLNGQA NLGNEAPVQR PRLTKLRVSV PPRWTPEEFM AAAPSGSGGD QSSAKDAEVA
KQEPPQHAPL VDCIRTRWPR AVCNWVGDPP SIV
//
