ID   A0A0D1Y4F2_EXOME        Unreviewed;      1346 AA.
AC   A0A0D1Y4F2;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE            EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN   ORFNames=PV10_03170 {ECO:0000313|EMBL:KIV95526.1};
OS   Exophiala mesophila (Black yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX   NCBI_TaxID=212818 {ECO:0000313|EMBL:KIV95526.1, ECO:0000313|Proteomes:UP000054302};
RN   [1] {ECO:0000313|EMBL:KIV95526.1, ECO:0000313|Proteomes:UP000054302}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 40295 {ECO:0000313|EMBL:KIV95526.1,
RC   ECO:0000313|Proteomes:UP000054302};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA   Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Exophiala mesophila CBS40295.";
RL   Submitted (JAN-2015) 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};
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DR   EMBL; KN847521; KIV95526.1; -; Genomic_DNA.
DR   RefSeq; XP_016227100.1; XM_016367582.1.
DR   STRING; 212818.A0A0D1Y4F2; -.
DR   GeneID; 27321015; -.
DR   VEuPathDB; FungiDB:PV10_03170; -.
DR   OrthoDB; 1423057at2759; -.
DR   Proteomes; UP000054302; Unassembled WGS sequence.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:InterPro.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR   Gene3D; 3.90.70.10; Cysteine proteinases; 2.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR001394; Peptidase_C19_UCH.
DR   InterPro; IPR044635; UBP14-like.
DR   InterPro; IPR025305; UCH_repeat_domain.
DR   InterPro; IPR018200; USP_CS.
DR   InterPro; IPR028889; USP_dom.
DR   PANTHER; PTHR43982; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR   PANTHER; PTHR43982:SF6; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 2-RELATED; 1.
DR   Pfam; PF13446; RPT; 4.
DR   Pfam; PF00443; UCH; 2.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   PROSITE; PS00972; USP_1; 1.
DR   PROSITE; PS50235; USP_3; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000054302}.
FT   DOMAIN          632..1253
FT                   /note="USP"
FT                   /evidence="ECO:0000259|PROSITE:PS50235"
FT   REGION          733..760
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          781..883
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1306..1346
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        788..809
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        832..851
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        857..883
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1346 AA;  151459 MW;  509F05AF980846AB CRC64;
     MAGVQADIRS LIAPIKGSGR TAPAFLQDLT LYTPWSPDVP NLLAESPLIF SQSQHLGENV
     PLGSCRHRFS LKPRQSRLPE LDERPGPETV WTVAAFCSSC RLHLHLKVDY TVRFEDRPCP
     TPDHPLHHLV RYELQEPLEK NAWRQQIGST AEIYTYRCSA LRCSVLVTVR VTPPVLRPYD
     VQVLTDPGLL RQRTDDAFRK QEGSTEGMKY PNPTDVLCDL RSYLKNSWRA KQDPKYASIN
     VSNKRFIVRF GPGGVACKDV LEHLGFRSEA GETWKVPEPD PDEAQPFQGW NNMFIDDAEH
     EIISLLLSRP YDERQSLPDL PAPVAADREL SRVLGCQDYD KHPSSRTAKQ IAEMRTGPFV
     ALGCPSDLSD DLISKAYHWQ VQTDPQNTPT YLSNLRYIAN DRQSDLLETE VALQISQGHF
     EIESLNQAYK ALQLTGREAL VTDEDVIGCF NATLTDSPAH EHQLREYLRM IGVHRNSKRI
     YDTAQNVMET YGQALAFLDA SPTTDDEGIR TMFTVKTNDN KNVEERAIKA LRIIAKERQS
     QLLTTWIESG FTIEPSMEPA EGYQALQIDN REVDDEMILM QYKFTVDENP ASADFYTRAL
     TAIATARGST VLMDHLHSKA PQDPEGALDE PVGLENIGNT CYLNSLLQVL FTTVDLRNIV
     LNFDEYKMPL DDVSLRQKRV GQRQVSLKEV QTGQKFVDSL ATLFRGMIQT PQSSIKPEQE
     LARLTLESHS VKEKLRRRST LKTGERPSLS ETHSLPFLGP LSSAEYDKSD VGDTILLSPA
     EEVDIRSLPP NDANDHDNHE KELGAKDVHM NDNSSEATVV SKEESEPVLT EDDPEAERQA
     ITDDKENLAP IPEGDLVKSS VSTQNQSNAP LTPASPSKLN SQAGTLQVSI ATENATKEQP
     MQYLPPPGKP PPVPPRKPLE ATTITLEEYA RQQDVTEVIG HVLNQLSSAI RPTGFDKTGE
     QLDEVHDTFY GQLILHTEND NGSPGKSEQY RDIITRVFHQ PADVYAAIDN EFDLQTGGNA
     VKGYISLSSL PPILCVQLDR VAWNNQTKRQ EKLNHHVEVP ETIYMDRYLE SGPDSELMQR
     RRHTWDLKRE LATISRRRGV LEEKHGQSKD IPTLLEDAKT ALEYLAEVPA DTFGGDLDVD
     PNTIATLGAL ADSTRTELED LRVRATDISQ QIKEAFVDMR KHPYRLHAAF FHRGSAGGGH
     YWVYIYDHQK EIWRKYNDDH VTVVQNRNEI FGKPPQDSYN VPPNPYLLVY VRSDRVGEVV
     ETVKRDIVYP PPDAPPPVPA RTQMAEMPPV MAQEDVKMTG HMDVKGGEQI PQAEPDPAEF
     TIGQPQQPVA SGWNKEELTV PRRVQW
//