ID A0A0D1YAW2_9EURO Unreviewed; 895 AA.
AC A0A0D1YAW2;
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=PV08_09315 {ECO:0000313|EMBL:KIW12041.1};
OS Exophiala spinifera.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=91928 {ECO:0000313|EMBL:KIW12041.1, ECO:0000313|Proteomes:UP000053328};
RN [1] {ECO:0000313|EMBL:KIW12041.1, ECO:0000313|Proteomes:UP000053328}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 89968 {ECO:0000313|EMBL:KIW12041.1,
RC ECO:0000313|Proteomes:UP000053328};
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 spinifera CBS89968.";
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,
CC ECO:0000256|RuleBase:RU366025};
CC -!- SIMILARITY: Belongs to the peptidase C19 family.
CC {ECO:0000256|RuleBase:RU366025}.
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DR EMBL; KN847498; KIW12041.1; -; Genomic_DNA.
DR RefSeq; XP_016232257.1; XM_016383634.1.
DR AlphaFoldDB; A0A0D1YAW2; -.
DR STRING; 91928.A0A0D1YAW2; -.
DR GeneID; 27336398; -.
DR VEuPathDB; FungiDB:PV08_09315; -.
DR HOGENOM; CLU_008279_3_0_1; -.
DR OrthoDB; 55585at2759; -.
DR Proteomes; UP000053328; 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; cd02257; Peptidase_C19; 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; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR24006:SF687; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 10; 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:UP000053328};
KW Thiol protease {ECO:0000256|RuleBase:RU366025};
KW Ubl conjugation pathway {ECO:0000256|RuleBase:RU366025}.
FT DOMAIN 434..814
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 71..199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 212..380
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 564..585
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 819..879
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 75..92
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 118..172
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 246..260
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 267..298
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 322..337
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 567..585
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 840..878
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 895 AA; 97980 MW; 210E17A11A08EC6F CRC64;
MQQNHHPYGQ HPMPMQPPQR RHEGSYPSPI RPHPGYQPFY PQQLGPMMPQ YPQHYAPNWY
GYQQHHMHPM HGQRPPYYPQ QPMPPPQYAP HHGPIIVPSQ PHALASPRLP QGPSSIVPPP
QASSSASTTS TTLVQTPPSP PLSTSSTVNT KKDGVSPSIS PAPQQTVQSP LVEVPQEPFE
PPIPWLSVQD QAFPPRAPRQ RRRILRSKLG TSPVVYPAPE PVVTAPTADT VPAQEEEPAE
IPSTEHAASD ASTTLPSGAP SDAPSDALSD AVSTQPSSLS PAVDVASAKS QQTPTQPKAR
LAGPVLPAVP ILPPSPTATR RPHRDSAVST QTKLSEPAPS AAEKDEVAAG VESSDDKQGL
TEEASPVTSA PAPPKSWANL FRSNSTQAGS FASAVSHPAS VASGTGRSEA LSDVLNDMNS
GFEPPTKISF LKPRGLVNTG NMCYMNSVLQ VLVFSLPFYD FLAKVAQRAR HAFKSDTPLI
DAIVMFVQEY PIICSAKNVE QLRLQLKPED YENYGDSFIP EYVYSAIKDL PRFREMRRGH
QQDAQEFLGF LLEELHEECA RAMKTGPGSN SGRTTPAGSV SNFSEQPDAE AGWMEVGHKQ
KPSVTRSSGA VSTESPINNI FGGKLRSELK ISGNKLSVTL EPYSPLQLDI GSPQVHNIID
ALKGLTRPES MQGDFFTTRG QKATATKQVF IDTLPPLLIL HLKRFHYDNT TKRAEKIWKK
VGYPLELEIP KEVFPMQARN KYIAHGGLPK YQLTGVIYHH GKNANGGHYT VDIRRQDGRE
WIRMDDTLLR RIRAEDVAEG GSEEDPKVLA AALERHKTSG NRFEQIDQEE DEEDGSDKVW
SQVNGHSRSK STMSSVVNGT ATPVKNSSGK QTPNPKQGIK DNKVAYLLFY QRIGN
//
