ID W7HSY5_9PEZI Unreviewed; 1142 AA.
AC W7HSY5;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN ORFNames=DRE_04347 {ECO:0000313|EMBL:EWC46404.1};
OS Drechslerella stenobrocha 248.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Orbiliomycetes;
OC Orbiliales; Orbiliaceae; Drechslerella.
OX NCBI_TaxID=1043628 {ECO:0000313|EMBL:EWC46404.1, ECO:0000313|Proteomes:UP000024837};
RN [1] {ECO:0000313|EMBL:EWC46404.1, ECO:0000313|Proteomes:UP000024837}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=248 {ECO:0000313|EMBL:EWC46404.1,
RC ECO:0000313|Proteomes:UP000024837};
RA Liu X., Zhang W., Liu K.;
RT "Drechslerella stenobrocha genome reveals carnivorous origination and
RT mechanical trapping mechanism of predatory fungi.";
RL Submitted (MAY-2013) 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}.
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DR EMBL; KI966418; EWC46404.1; -; Genomic_DNA.
DR AlphaFoldDB; W7HSY5; -.
DR HOGENOM; CLU_005922_0_0_1; -.
DR Proteomes; UP000024837; Unassembled WGS sequence.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:InterPro.
DR GO; GO:0019538; P:protein metabolic process; IEA:UniProt.
DR CDD; cd02674; Peptidase_C19R; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR Gene3D; 3.40.250.10; Rhodanese-like domain; 1.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR001763; Rhodanese-like_dom.
DR InterPro; IPR036873; Rhodanese-like_dom_sf.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR PANTHER; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR21646:SF95; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 4-RELATED; 1.
DR Pfam; PF00443; UCH; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF52821; Rhodanese/Cell cycle control phosphatase; 1.
DR PROSITE; PS50206; RHODANESE_3; 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:UP000024837}.
FT DOMAIN 362..488
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
FT DOMAIN 769..1139
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 148..234
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 272..342
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 655..692
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 720..751
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 151..169
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 206..231
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 309..325
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 671..688
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1142 AA; 127172 MW; 8E661D3811166959 CRC64;
MPAVVPSLTP TVNHSSPRPL GASVQAMDVD LPPASGGQKR TLKHIDELKA KIDADKPRQS
LSINALMMLA SRRFKSALMN IEFNRIDLAY VDFNIALDTL INAIPRHREY PTWLTRPNAP
PSEFKKLRAD MVKHMDRMEE IKRIIIADNL ENGTQPPSID SQPTAKSPPS APHEGQKAEA
KDTSPPIEIK QPPPRPAKPK DLQNYHPGSA RTSTDRPPSR GYANDDTQDP KPSQTDLLKE
RFEKLMLPTN PPNSANRAST DQASLRRRLL KPALSTDITP LPRPPEPTYS PIRQYPENGT
FLPGESQPRP LIRTSSSTSL DNYRPSSHAP APPQPSKPST GDITISAERL SEYLFNTPDL
SVLVIDVRER SEFDQGHIFA RDIICIEPTA LRDNMSAEQL EDALSLSPDR EHSMFNGRHV
YDYVVYYDQS TYALNTYQRG TDKQAQRALK VLVQAIYDLA YDKQLRNLPK LLVGGLDAWI
EYNGAASLVQ TASQKVGGLS RNGAKTTATS LSTIAARRKE RARAALPGQV LPDAERSEHL
TSAHPINQEE EAQWIARLKR ENTSLTIKNP LTIESSNTKS RNRAASLVTL DFERSPDIEE
FFQRFPAVVQ EYAEVPPMPA RGPPSPPVEG SLQQGAAYPV LPVLGSIQRT AVSPAPSIHP
EEQEQLPHHM EPPVRTPPPV PPPVPTKEPT ETTLTRRNTI IDHMFHGFTD VQNPQFHPIA
PPSPLRPPPA VPKKSYSGVS EHHQPQAPVL DPVTSPFIAT VAPSGFGTTG LKNLGNTCYM
NSIIQCMSGT VPLARYFLSG SYRAHVNREN RLGSRGIFAE AFANLNRNLW EETYSFVSPV
TIKDISGRLN SQFRGRDQQD AQEYLEFFLD YLHEDMNASA GKSKLRDLTE DEERYREKLP
IQLASYYEWG RYTHTNLSMI VKWFQGQFRS QLKCLKCGHT STTYSPFMYL SLPIPASAKG
SSGTCTLKDC MDEFTKQEIL DGDDAWHCPI CKKPRRASKQ LSISRMPIVL IIHLKRFSSH
GMWRDKVNTM VNFSKSVDLT QYVPPPLDPG QVPGGKALPV TIETTPPFHY SLYAITNHYG
SLTSGHYTAF VRVSGGSGGG GGQVGAGSVW HRFDDTKATK MESDDVVNRN AYILFWVRNG
VM
//
