ID A0A1V8TRD1_9PEZI Unreviewed; 1177 AA.
AC A0A1V8TRD1;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN ORFNames=B0A48_00770 {ECO:0000313|EMBL:OQO13895.1};
OS Rachicladosporium antarcticum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Cladosporiales; Cladosporiaceae; Rachicladosporium.
OX NCBI_TaxID=1507870 {ECO:0000313|EMBL:OQO13895.1, ECO:0000313|Proteomes:UP000192596};
RN [1] {ECO:0000313|Proteomes:UP000192596}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCFEE 5527 {ECO:0000313|Proteomes:UP000192596};
RA Coleine C., Masonjones S., Stajich J.E.;
RT "Genomes of endolithic fungi from Antarctica.";
RL Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OQO13895.1}.
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DR EMBL; NAJO01000002; OQO13895.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V8TRD1; -.
DR STRING; 1507870.A0A1V8TRD1; -.
DR InParanoid; A0A1V8TRD1; -.
DR OrthoDB; 51419at2759; -.
DR Proteomes; UP000192596; Unassembled WGS sequence.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd02659; peptidase_C19C; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR InterPro; IPR002083; MATH/TRAF_dom.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR008974; TRAF-like.
DR InterPro; IPR024729; USP7_ICP0-binding_dom.
DR InterPro; IPR029346; USP_C.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR PANTHER; PTHR24006; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR24006:SF644; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 7; 1.
DR Pfam; PF00443; UCH; 1.
DR Pfam; PF14533; USP7_C2; 1.
DR Pfam; PF12436; USP7_ICP0_bdg; 1.
DR SMART; SM00061; MATH; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF49599; TRAF domain-like; 1.
DR PROSITE; PS50144; MATH; 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 Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000192596};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT DOMAIN 74..205
FT /note="MATH"
FT /evidence="ECO:0000259|PROSITE:PS50144"
FT DOMAIN 231..557
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
SQ SEQUENCE 1177 AA; 134702 MW; E2AA6DAC8F2F1F96 CRC64;
MDQIGSDMQL DSDYDEKTYV NDTESVALIT NDDADSMLDE SLPPAEPAKP MADDHEAMKE
RFLPASPDYE TEAEAIFTWD ITDWRSLPKR THGPTFNCAG HPWRVLFFPA GNAASESVSF
YLEQGFGDEK PAEDWYACAQ FMLVLSNPND PSIYIHHEAN HRFTLEEGDW GFTRFADKNK
IFAASYDGAD RPLVEGDTAR VTAYIRVLKD PTGVLWHNFV NYDSKKETGM VGLRNQGATC
YLNSLLQSLY LTGAFRKAVY QIPTSTEQER TNSTSAYALQ RLFYRLQADQ VAVSTQELTH
SFGWESRQIF EQQDVQELSR ILMEKLETHM KGTEAEKALP DMFVGKMKTY LKCINVDYES
SRTEEYWDLQ LNVSGCKSVD ESFRDYIQVE TLEGDNKYAA EGYGLQEAKK GVIFESFPNV
LHLQLKRFEY DFQRDAMMKV NDRYEFPDVL DCTPYLDETA DKSEPCIYHL HGVLVHSGDL
NAGHYYAFLK PSKDGDFFRF DDDRVTRATK REAIDDNFGG DYATNGINGA AKGQNPYTRQ
WSTKRSNNAY MLVYIRASQL DRILPPEDQM QPPEHLPIRI QEERVAAERR RKEREEAHLY
MNVYVATEAS YRAYEGTDII NWTSESETDL SAPKIYRLLR SMTVADFTAF LAQEQNADAK
SIRPWIMVNR QNGTVRPDHP LPWADMTLQE AADKFSTRNS GFRIFVEAAE KGEEGDYTWP
NEVVSTPSSP NMQGVRQPSS TQPMIIFLKY FDVERQTLRG VGHVYMSPSD RVQDLAPKIL
DRMGWEVGVL LDLYEEIKQT YVEQMKPKLT LAASEIQDGD IICFQRHLNE DEAKAVRQTT
PSAVLTAKEF YDFLINRVYV KFVPKATQNL SVRNDDDQAF SISLSRKDTY DTLATKVAEQ
LTLVSEHAVE PSHLRFTTAN VQSGKPRTIV KPQQGTTILS ILFGAAGAGY SYQPAQQTDS
LFYEVLEMSL KDLEQRKTVK IIWLPEGITK EEPYDVLVPK SAQFTEVLPL LQKRANLPDE
ILDSIRFYEA HSGKVYKVLP PTTPIVSLNE FLTIYAERIP EEEATLTPDS KDRLVWCFHF
EKEPSKHHSV PFIFAMKEGE VFSETKERLS KRIGIKGKGF EKIRFAVVKG GQAYSRPVWI
EDEDVLSDKL GPDDHLGLEE PNRQRNQWNK YESLNIR
//