ID A0A421JST9_9ASCO Unreviewed; 834 AA.
AC A0A421JST9;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU366025};
DE EC=3.4.19.12 {ECO:0000256|RuleBase:RU366025};
GN ORFNames=JA1_001490 {ECO:0000313|EMBL:RLV94826.1};
OS Spathaspora sp. JA1.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Spathaspora.
OX NCBI_TaxID=2028339 {ECO:0000313|EMBL:RLV94826.1, ECO:0000313|Proteomes:UP000285775};
RN [1] {ECO:0000313|EMBL:RLV94826.1, ECO:0000313|Proteomes:UP000285775}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JA1 {ECO:0000313|EMBL:RLV94826.1,
RC ECO:0000313|Proteomes:UP000285775};
RA Formighieri E.F., Steindorff A.S., Trichez D., Almeida J.R.;
RT "Physiological and comparative genomic analysis of newly identified yeasts
RT Spathaspora sp. JA1 and Meyerozyma sp. JA9 reveals insights into xylitol
RT production.";
RL Submitted (AUG-2017) 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|RuleBase:RU366025};
CC -!- SIMILARITY: Belongs to the peptidase C19 family.
CC {ECO:0000256|RuleBase:RU366025}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RLV94826.1}.
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DR EMBL; NSGQ01000008; RLV94826.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A421JST9; -.
DR STRING; 2028339.A0A421JST9; -.
DR Proteomes; UP000285775; 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; 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; 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; 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, ECO:0000313|EMBL:RLV94826.1};
KW Protease {ECO:0000256|RuleBase:RU366025};
KW Reference proteome {ECO:0000313|Proteomes:UP000285775};
KW Thiol protease {ECO:0000256|RuleBase:RU366025};
KW Ubl conjugation pathway {ECO:0000256|RuleBase:RU366025}.
FT DOMAIN 455..834
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 341..375
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 402..440
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 834 AA; 95961 MW; 2E4DE56649DFA26F CRC64;
MKSIAELQSI SSNLVKHTIK SATGFPKLIN DQITLLQIFN KQIKTFEKIG YCDYEIAYVV
YVTAGQLLSV TSKYVNEKNK EIYQETERTL INKKSQFEEV ESVLVKSEVL VPNVDPLLNR
FNQLQGKSQT KEESDIIDKF KFQDQITAQE LHDLLDKYKI LLIDYRPKKD FLYNHINHPD
IVNIEPKQLE LDSDLEVLLQ ESLPQDQYNK FQNRHRYDLI VIYNYKYGNA DLDRFSNILI
DFPNPFEQLI EVLMYKNKYI SSRPKLLPCY LIGGVLNWYN QFGKSALVSS PAVENGSGQI
NNVKSDYLTN FGEYISNSKS HGSKEYIKPR NRKNNHEEFV VTKSIESNLP PTPRSREHTP
VSKQQVETSP SAPVVPSIPA QVAPALPKKI IPTVQGIVPY SPENNSTTSL NPPALPQKTP
LPKDKPPAYS KTTSPTSMEK SISETQINFL NSYTTGLVNL GNSCYMNCVL QCLGATQQLT
TFFFPSINNY KQHINTTNKL GSQGIVTVQF AELLANMFKS NGKTLNPKKF KMIMGSCSPN
KQFETYDQQD CIEFLNYLLD TLHEDLNQMV ILSPEEKRMI SELTPEQEKS RETLPVRLAS
TIEWERYLKL NFSIIVDYFQ GQLLSQLKCL QCRTTSTTYN SFSILSLPIP ERKQTVSLQD
CLQEFTTIEL LDDNNKWYCP NCKTFTKSTK QITITRLPQV LIINFKRFKM TPNGRFNKLE
TFVTYPVNET LDLTQYWPKE GTSINPSRND VMTIEKERQL LQTFPVRNQI PPFKYKLYGV
ANHFGNLTTG HYTSYVHKSD GRGWCYFDDA RISYNVGSDK VLNKNAYCLF FQRI
//
