ID   A0A1I8PG54_STOCA        Unreviewed;      1054 AA.
AC   A0A1I8PG54;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE            EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN   Name=106081148 {ECO:0000313|EnsemblMetazoa:SCAU007760-PB};
OS   Stomoxys calcitrans (Stable fly) (Conops calcitrans).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Muscoidea;
OC   Muscidae; Stomoxys.
OX   NCBI_TaxID=35570 {ECO:0000313|EnsemblMetazoa:SCAU007760-PB, ECO:0000313|Proteomes:UP000095300};
RN   [1] {ECO:0000313|EnsemblMetazoa:SCAU007760-PB}
RP   IDENTIFICATION.
RC   STRAIN=USDA {ECO:0000313|EnsemblMetazoa:SCAU007760-PB};
RG   EnsemblMetazoa;
RL   Submitted (MAY-2020) to UniProtKB.
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   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC       center, centrosome {ECO:0000256|ARBA:ARBA00004300}. Cytoplasm,
CC       perinuclear region {ECO:0000256|ARBA:ARBA00004556}.
CC   -!- SIMILARITY: Belongs to the peptidase C19 family.
CC       {ECO:0000256|ARBA:ARBA00009085}.
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DR   RefSeq; XP_013098375.1; XM_013242921.1.
DR   RefSeq; XP_013098376.1; XM_013242922.1.
DR   AlphaFoldDB; A0A1I8PG54; -.
DR   STRING; 35570.A0A1I8PG54; -.
DR   EnsemblMetazoa; SCAU007760-RB; SCAU007760-PB; SCAU007760.
DR   EnsemblMetazoa; SCAU007760-RC; SCAU007760-PC; SCAU007760.
DR   KEGG; scac:106081148; -.
DR   VEuPathDB; VectorBase:SCAU007760; -.
DR   OrthoDB; 5397179at2759; -.
DR   Proteomes; UP000095300; Unassembled WGS sequence.
DR   GO; GO:0005813; C:centrosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:InterPro.
DR   CDD; cd02670; Peptidase_C19N; 1.
DR   Gene3D; 2.30.30.190; CAP Gly-rich-like domain; 1.
DR   Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR   InterPro; IPR036859; CAP-Gly_dom_sf.
DR   InterPro; IPR000938; CAP-Gly_domain.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR001394; Peptidase_C19_UCH.
DR   InterPro; IPR028889; USP_dom.
DR   PANTHER; PTHR11830; 40S RIBOSOMAL PROTEIN S3A; 1.
DR   PANTHER; PTHR11830:SF3; CYLINDROMATOSIS, ISOFORM D; 1.
DR   Pfam; PF01302; CAP_GLY; 1.
DR   Pfam; PF00443; UCH; 1.
DR   SMART; SM01052; CAP_GLY; 1.
DR   SUPFAM; SSF74924; Cap-Gly domain; 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   PROSITE; PS50235; USP_3; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          690..1048
FT                   /note="USP"
FT                   /evidence="ECO:0000259|PROSITE:PS50235"
FT   REGION          310..338
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          408..484
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        314..336
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        408..459
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1054 AA;  117991 MW;  19CE302FE02E2021 CRC64;
     MDSCTISKYG IVNRKTKLRM HYSSEIPPEK GVCRDSNSDE LEVPAGTLIK YFQTNGPIKS
     GFKVWSTVQV RDFINSRPIY ENLYECPLSN LTKVDENLWP FVIGIVDPDE RLRLIINTDH
     CKWFLYLKEN SLVSVPGEMF LKPGLRFDCI VRYIGPVKEL QSVGYFFGLE LLHLESGNSP
     QADNIPFSKE YIGCEPHLAI FATANYICNI PKDVQKKFSA REFISGTFEK LKSAIGPTSS
     VTGCIGSNSS SPKWNKATKG KGKESTSQFY DNLRDAILLS KNEMDTKSES SIVAQAAGGE
     DGKQVENYER SLERKSTNTV QTQTQPQSGI LKNKNSKDQI KPSHVLAFGG PDIVVIDNKD
     IDESVRNEGE VIVLQKTQDV DLVELLGSDW PKTAGDAAAM LNQQKYQNST LTRQSSTGGS
     GCNDSSNTGT YKRSRNKSSN PLSHIGAASS SNAKKMNDYV SGPNKSGDMK IQKPHQKAAR
     DSSCSSKNFY ENYDNIENQP LYANTPSDDM IATDAYDATN TLLPAVLDAD FTESPMQELE
     DTGLGVGSMV EVNDPESDSH LYGVIRWIGV PPGSHPVMVG VELEEDYINK QLITTDGGFN
     GISLFKCPVG RGLFVTPDQC SCDRRFLAEE GAIGNDVSVA NNNYKTKQMN GTQDEQQTFG
     HMDCPVVPGA IAPIKCFSSK DLEELCGKFK GIQGHHNSCY LDVTLFSMFT FTPVFDAVLY
     RPPEKEDISS YAEVQTVLRE EIVNPLRKNM FVRADRVMKL RQLLDKLSSV SGLTSEEKDP
     EEFLNCILAQ ILRAEPFLKL NSGQDAYYYQ LFVEKDDRLS FPSVQQLFEQ SFYTSDIKLK
     EVPSCLIIQM PRFGKNYKMY PRILPSQVLD VTDIIEDSPR QCSVCGKLAE FECRDCFGVL
     QSGVGLESTS FCPKCLETVH MHVKRSNHKY RELSVPQDFR VMANHMTVPR LYMELFAVVC
     IETSHYVTFV KAGSGPDAPW CFFDSMADRK GEQNGYNIPE MITVPDLPQW LSEEGSRIVN
     ETSANDKMLP EHAKRLFCDA YMCMYQSTDV MMYR
//