ID D5GKF1_TUBMM Unreviewed; 1176 AA.
AC D5GKF1;
DT 15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT 15-JUN-2010, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN ORFNames=GSTUM_00009508001 {ECO:0000313|EMBL:CAZ84994.1};
OS Tuber melanosporum (strain Mel28) (Perigord black truffle).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Pezizomycetes;
OC Pezizales; Tuberaceae; Tuber.
OX NCBI_TaxID=656061 {ECO:0000313|EMBL:CAZ84994.1, ECO:0000313|Proteomes:UP000006911};
RN [1] {ECO:0000313|EMBL:CAZ84994.1, ECO:0000313|Proteomes:UP000006911}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mel28 {ECO:0000313|EMBL:CAZ84994.1,
RC ECO:0000313|Proteomes:UP000006911};
RX PubMed=20348908; DOI=10.1038/nature08867;
RA Martin F., Kohler A., Murat C., Balestrini R., Coutinho P.M., Jaillon O.,
RA Montanini B., Morin E., Noel B., Percudani R., Porcel B., Rubini A.,
RA Amicucci A., Amselem J., Anthouard V., Arcioni S., Artiguenave F.,
RA Aury J.M., Ballario P., Bolchi A., Brenna A., Brun A., Buee M.,
RA Cantarel B., Chevalier G., Couloux A., Da Silva C., Denoeud F.,
RA Duplessis S., Ghignone S., Hilselberger B., Iotti M., Marcais B., Mello A.,
RA Miranda M., Pacioni G., Quesneville H., Riccioni C., Ruotolo R.,
RA Splivallo R., Stocchi V., Tisserant E., Viscomi A.R., Zambonelli A.,
RA Zampieri E., Henrissat B., Lebrun M.H., Paolocci F., Bonfante P.,
RA Ottonello S., Wincker P.;
RT "Perigord black truffle genome uncovers evolutionary origins and mechanisms
RT of symbiosis.";
RL Nature 464:1033-1038(2010).
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 peptidase C19 family.
CC {ECO:0000256|ARBA:ARBA00009085}.
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DR EMBL; FN430338; CAZ84994.1; -; Genomic_DNA.
DR RefSeq; XP_002840803.1; XM_002840757.1.
DR AlphaFoldDB; D5GKF1; -.
DR STRING; 656061.D5GKF1; -.
DR EnsemblFungi; CAZ84994; CAZ84994; GSTUM_00009508001.
DR GeneID; 9182014; -.
DR KEGG; tml:GSTUM_00009508001; -.
DR eggNOG; KOG1870; Eukaryota.
DR HOGENOM; CLU_001060_9_0_1; -.
DR InParanoid; D5GKF1; -.
DR OMA; KPRGCTG; -.
DR OrthoDB; 5474185at2759; -.
DR Proteomes; UP000006911; Unassembled WGS sequence.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR CDD; cd02674; Peptidase_C19R; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 2.
DR Gene3D; 3.30.2230.10; DUSP-like; 1.
DR InterPro; IPR035927; DUSP-like_sf.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR006615; Pept_C19_DUSP.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR028135; Ub_USP-typ.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR PANTHER; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR21646:SF24; USP DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF06337; DUSP; 1.
DR Pfam; PF14836; Ubiquitin_3; 1.
DR Pfam; PF00443; UCH; 1.
DR SMART; SM00695; DUSP; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF143791; DUSP-like; 1.
DR PROSITE; PS51283; DUSP; 1.
DR PROSITE; PS00972; USP_1; 1.
DR PROSITE; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000006911}.
FT DOMAIN 69..201
FT /note="DUSP"
FT /evidence="ECO:0000259|PROSITE:PS51283"
FT DOMAIN 388..999
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 47..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 341..385
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1006..1104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1148..1176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 356..370
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1015..1083
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1090..1104
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1176 AA; 128875 MW; 89A9DAF5377B27AC CRC64;
MPSAEEKSRR EPSVEVADGS VASSEGNGGV IHIDATSTAV SIAPSTATTI GSTQPSSASA
TPVSSVSIPS LEDQAHFIIK SKIETKPKEG DLGYIISGPW LNQLLAKFSD SGVQLTKEGA
EGEIGLIDNS DLVDTTQMQG QAKKTSDDST VEDSAVPEDF VAIKPGILGD DFEILPEEAW
NSLVSWYGLA EGSPVITRRA VNTSETNVPH IQYEIYPPTF TFYKLRDPST NITKDVLDKE
KSQSPKRITA GKTDGFQKLL RKVKKLAGVD AARKIRLWRI IESSFEHDLE PASKSSRKAG
LGAGGTIVIE EQGSDGEWIS EKPTKSVKKG GQQVTVALNG KNITGGPVKK KASARPDSPS
GSTSTAVIRS GFLNRPAERR DGRPLGKCGL SNLGNTCYMN SALQCLRSVT ELSNYFLCNK
YMEELNPSNP LSHSGKVAKA YATLLGYIFS PTCPVSVSPR EFKSTISRFS LSFSGYGQQD
TQEFLAFLLD GLHEDLNRIQ KKPYIEKPES TDKMVGDGEA IARLAQEHWT IYKRRNDSVI
ADLFGGLYQS TLVCPDCEKV SITFDPFMDL TLPLPVENVW GRDIYFYPSS ASGGGLIKIP
VEMDKNSSIK SLKEHLARKF NLDPKKTMAS EVYKGKFFKH YEDFQTVSET IRQDDDAFIY
ELDDVPTNYP PSKSKKPRRT GFYGPSYVFG LPFFIVVNRD EVRSFDAIVK KIIAKYQVLT
TRNFYESEAS PSESETEEVV EVKDELEDIN ETEEETHDGF VDVSMKDASS MVGSDRKAVK
SPRRPLPAGI EDLFTVMATK RRSGDSAVVT GWQALETAFD IRERLNHVQS ASPPRRKTSD
YFTNERKRKG IHLEDCLDEF AKEEVLSEED PWFCPRCKVH RRASKKFELW KCPDILVIHL
KRFSSSRNFR DKIDVLIDCP VTGLDLQERV GLKEEGKSLV YDLIAVDNHY GGLGGGHYTA
CAKSWIDGKW YHYDDSSVKE VGEQKVITSA AYLLFYRRRS ETTLGGPRLN WMLSEPTDSP
GSASSSRNTS PTRAGEGGPS GDSSATVLPN GRSSGGGTSG LSTIYSTPGN SNLWGNEPPP
SYSESSGMEM ILMPGTQGSP TSSKAPTVGF SFGSRGGLLR DSTDDGVFIG SLLGPAEHTD
IPTDITVDDD EGLLPTLSDG NNDTAGVHDV TDPMEP
//
