ID A0A0D2GRE2_9EURO Unreviewed; 723 AA.
AC A0A0D2GRE2;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU366025};
DE EC=3.4.19.12 {ECO:0000256|RuleBase:RU366025};
GN ORFNames=Z517_02768 {ECO:0000313|EMBL:KIW83523.1};
OS Fonsecaea pedrosoi CBS 271.37.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Fonsecaea.
OX NCBI_TaxID=1442368 {ECO:0000313|EMBL:KIW83523.1, ECO:0000313|Proteomes:UP000053029};
RN [1] {ECO:0000313|EMBL:KIW83523.1, ECO:0000313|Proteomes:UP000053029}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 271.37 {ECO:0000313|EMBL:KIW83523.1,
RC ECO:0000313|Proteomes:UP000053029};
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 Fonsecaea pedrosoi CBS 271.37.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Ubiquitin thioesterase component of the regulatory network
CC controlling carbon source utilization through ubiquitination and
CC deubiquitination involving creA, creB, creC, creD and acrB.
CC Deubiquitinates the creA catabolic repressor and the quinate permease
CC qutD. Also plays a role in response to carbon starvation and the
CC control of extracellular proteases activity.
CC {ECO:0000256|ARBA:ARBA00037075}.
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|RuleBase:RU366025};
CC -!- SUBUNIT: Interacts with creA, creC and qutD.
CC {ECO:0000256|ARBA:ARBA00038752}.
CC -!- SIMILARITY: Belongs to the peptidase C19 family.
CC {ECO:0000256|RuleBase:RU366025}.
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DR EMBL; KN846970; KIW83523.1; -; Genomic_DNA.
DR RefSeq; XP_013287331.1; XM_013431877.1.
DR AlphaFoldDB; A0A0D2GRE2; -.
DR STRING; 1442368.A0A0D2GRE2; -.
DR GeneID; 25302258; -.
DR VEuPathDB; FungiDB:Z517_02768; -.
DR HOGENOM; CLU_008279_0_2_1; -.
DR OrthoDB; 227085at2759; -.
DR Proteomes; UP000053029; Unassembled WGS sequence.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd02663; Peptidase_C19G; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR PANTHER; PTHR24006:SF944; RE52890P; 1.
DR PANTHER; PTHR24006; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR Pfam; PF00443; UCH; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 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|RuleBase:RU366025};
KW Protease {ECO:0000256|RuleBase:RU366025};
KW Reference proteome {ECO:0000313|Proteomes:UP000053029};
KW Thiol protease {ECO:0000256|RuleBase:RU366025};
KW Ubl conjugation pathway {ECO:0000256|RuleBase:RU366025}.
FT DOMAIN 54..479
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 101..146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 487..506
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 548..723
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..21
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 574..645
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 659..673
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 697..714
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 723 AA; 81348 MW; B3F85E4C326B5060 CRC64;
MTSFFGKLKS QNASSPAVGA STAKKDANAP LPTPLERMLA NAGPLRNDGS DKFFGMENFG
NSCYCNSILQ CLYYSVPFRE HVLSYPRRSN PDAVAHAQLH APPRVPPNQQ NGAAKKPPPG
PASSRNAGTP PQQQQKPEDK DSPEYKKKQA ILNGPILNMT YDNSQDYDMP ESLFTSMKDI
FEAIVLHQSR MGVVSGHRFL EVLRKENEMF RSAMHQDAHE FLNLLLNTVV ENIEDHDRKV
TAQKKSEEPS PAIEPATDMA RTESATVSFP SILPVPTANS PTKWLHGLFE GTLTSETRCL
TCENVSQRDE PFLDLSVDLE QHSSVTACLR RFSEEEMLCE RNKFHCDNCG GLQEAEKRMK
IKRLPRILAL HLKRFKYTED FGRLQKLFHK VVYPYHLRLF NTTDDAEDPD RLYELYAVVV
HIGGGPYHGH YVAVIKTQDR GWLLFDDEMV EPVDKNFVRN FFGDKPGLAC AYVLFYQETT
VEAVQKEQRM EGKRRASQDL TNPLGVDANH SAELHRVETF SPTGSPASTA EAAQYAALDH
AVTAPPQFKA NGHVETPQSP PNFTPARPTS PVVQSKKEKA KEEKARKAAE KQAEKERQEA
ERQRRKDLAN KITEAHKRQE AELKAAMEAS KATKAEEDRR NALERAHTVQ ANGSSHSGLD
RFKRSKSLRF GSLTRRDKPP SNPSEENMVP SVTPESADPP EKEKEKEKRN RFSIRKKSFG
VLS
//