ID A0A0D2IP16_9EURO Unreviewed; 765 AA.
AC A0A0D2IP16;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU366025};
DE EC=3.4.19.12 {ECO:0000256|RuleBase:RU366025};
GN ORFNames=Z520_05212 {ECO:0000313|EMBL:KIX98751.1};
OS Fonsecaea multimorphosa CBS 102226.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Fonsecaea.
OX NCBI_TaxID=1442371 {ECO:0000313|EMBL:KIX98751.1, ECO:0000313|Proteomes:UP000053411};
RN [1] {ECO:0000313|EMBL:KIX98751.1, ECO:0000313|Proteomes:UP000053411}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 102226 {ECO:0000313|EMBL:KIX98751.1,
RC ECO:0000313|Proteomes:UP000053411};
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 multimorphosa CBS 102226.";
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KN848070; KIX98751.1; -; Genomic_DNA.
DR RefSeq; XP_016632874.1; XM_016775715.1.
DR AlphaFoldDB; A0A0D2IP16; -.
DR STRING; 1442371.A0A0D2IP16; -.
DR GeneID; 27710958; -.
DR VEuPathDB; FungiDB:Z520_05212; -.
DR OrthoDB; 227085at2759; -.
DR Proteomes; UP000053411; 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 InterPro; IPR005877; YSIRK_signal_dom.
DR PANTHER; PTHR24006:SF944; RE52890P; 1.
DR PANTHER; PTHR24006; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR Pfam; PF00443; UCH; 1.
DR Pfam; PF04650; YSIRK_signal; 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:UP000053411};
KW Thiol protease {ECO:0000256|RuleBase:RU366025};
KW Ubl conjugation pathway {ECO:0000256|RuleBase:RU366025}.
FT DOMAIN 99..522
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 56..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 146..191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 530..555
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 597..765
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..30
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 616..687
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 701..715
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 739..756
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 765 AA; 85885 MW; A044CBB852A912DF CRC64;
MTSFFGKLKS QVSQETRRIE SPSSPRTPGE GSRKISGRLY LSDCFGMVTN GLVSPQNASA
PAVGASPARK DANAPLPTPL ERMLANAGPL RTDGSDKFFG MENFGNSCYC NSILQCLYYS
VPFREHVLSY PRRSNPDAVA HAQLHAPPRV PPNQQNGAAK KPPPGPASAR NAGTPPQQQK
PEDKDSPEYK KKQAIINGPI LNVTYENSQD YDMPESLFTS LKDIFEGIVL HQSRMGVVSG
HRFLEVLRKE NEMFRSAMHQ DAHEFLNLLL NTVVENIEDH DRKLTAQKKV QELPAIEEPA
DMSRTESATV SFPSILPMPT ANSPTKWLHG LFEGTLTSET RCLTCENVSQ RDEPFLDLSV
DLEQHSSVTA CLRRFSEEEM LCERNKFHCD NCGGLQEAEK RMKIKRLPRI LALHLKRFKY
TEDFGRLQKL FHKVVYPYHL RLFNTTDDAE DPDRLYELYA VVVHIGGGPY HGHYVAVIKT
QDRGWLLFDD EMVEPVDKNF VRNFFGDKPG LACAYVLFYQ ETTLEAVQKE QRMEGKRRAS
QDLTNPLGAD AKRSAELHRV ETFSPMGSPM SPAESAQYTV LDHAVTAPAQ FKANGHVEAP
QSPTLGAARP TSPVVQSKKE KAKEEKARKA AEKQAEKERQ ESERQRRKDL ANKITEAHKR
QEAELKAAME ASKATKAEED KRNALERAHT VQANGSSHSG LDRFKRSKSL RFGSLTKRDK
PPSNPSEENM VPTVTAETAE PPEKDKEKEK KNRFSIRKKS FGVLS
//
