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Database: UniProt
Entry: A0A0V1D4U8_TRIBR
LinkDB: A0A0V1D4U8_TRIBR
Original site: A0A0V1D4U8_TRIBR 
ID   A0A0V1D4U8_TRIBR        Unreviewed;       696 AA.
AC   A0A0V1D4U8;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU366025};
DE            EC=3.4.19.12 {ECO:0000256|RuleBase:RU366025};
DE   Flags: Fragment;
GN   Name=usp46 {ECO:0000313|EMBL:KRY56493.1};
GN   ORFNames=T03_12041 {ECO:0000313|EMBL:KRY56493.1};
OS   Trichinella britovi (Parasitic roundworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=45882 {ECO:0000313|EMBL:KRY56493.1, ECO:0000313|Proteomes:UP000054653};
RN   [1] {ECO:0000313|EMBL:KRY56493.1, ECO:0000313|Proteomes:UP000054653}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS120 {ECO:0000313|EMBL:KRY56493.1};
RA   Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT   "Evolution of Trichinella species and genotypes.";
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|RuleBase:RU366025};
CC   -!- SIMILARITY: Belongs to the heparin-binding growth factors family.
CC       {ECO:0000256|ARBA:ARBA00007936}.
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:KRY56493.1}.
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DR   EMBL; JYDI01000042; KRY56493.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V1D4U8; -.
DR   Proteomes; UP000054653; Unassembled WGS sequence.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008083; F:growth factor activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd02663; Peptidase_C19G; 1.
DR   Gene3D; 2.80.10.50; -; 1.
DR   Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR   InterPro; IPR002209; Fibroblast_GF_fam.
DR   InterPro; IPR008996; IL1/FGF.
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; PF00167; FGF; 1.
DR   Pfam; PF00443; UCH; 1.
DR   SMART; SM00442; FGF; 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   SUPFAM; SSF50353; Cytokine; 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:KRY56493.1};
KW   Protease {ECO:0000256|RuleBase:RU366025};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054653};
KW   Thiol protease {ECO:0000256|RuleBase:RU366025};
KW   Ubl conjugation pathway {ECO:0000256|RuleBase:RU366025}.
FT   DOMAIN          338..694
FT                   /note="USP"
FT                   /evidence="ECO:0000259|PROSITE:PS50235"
FT   REGION          454..481
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        460..481
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KRY56493.1"
SQ   SEQUENCE   696 AA;  80990 MW;  9A0055EFA5F56017 CRC64;
     LPFSWFGYRT MPFWVLNGHS EQQPRETAID CRYLLRQIIK LSVVFYIATK LPLTFLSFQT
     DSSMALNFCT NFSLNITAPY VTNMSMTVCL AGTCFLNKIN INMNSIQIAE EIPLQNHVTR
     LYRLYNRCSG RYLQMYVKAI NARGKSKSPL TLLKVETDCY GGRVRIQSKK FRKYLCFNRK
     LRVTARYNGR SENCVFVERI SENFYTELES ASQKGAFLGF NSRGLFLHPT MRSREPHCFQ
     FIKEEQINPI EEFRGIDYGP SRRIRSRAKW KKKNHTQPNI TLTPQLFELL YHSENRSCCC
     CCFYWAQKRK RVNFDMGQNA SHLEKETTDE FPANDHFYGL VNFGNTCYCN SVIQALYFCR
     PFREKVLNYK SQMKKAGNQK ENLLLCLADL FHSISTQKRR VGTIAPKKFI GRLKKENDLF
     DNYMQQDAHE FLNYLLNTVA DILLEEKRHE KRISGGHKVG SKGTTDTVSQ TDGFGDNASS
     NQTQVKDKLA EHTWVHDVFQ GTLTNETRCL NCETVSSKDE DFLDLSVDVQ QNTSITHCLR
     EFSATETLCN EHKYYCDICC SKQEAQKRMR IKKLPLILAL HLKRFKYVEQ YNRYTKLSYR
     VLFPLELRLF NTSHDAVNPD RMYDLVAVVV HCGSTPNRGH YITVVKSQGF WLLFDDDVVD
     KMDHINIEDF FGMAADGSLQ KNSESGYILF YQARDI
//
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