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Database: UniProt
Entry: A0A1V8TRD1_9PEZI
LinkDB: A0A1V8TRD1_9PEZI
Original site: A0A1V8TRD1_9PEZI 
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
//
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