ID A0A0V1BWH1_TRISP Unreviewed; 702 AA.
AC A0A0V1BWH1;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU366025};
DE EC=3.4.19.12 {ECO:0000256|RuleBase:RU366025};
GN Name=USP46 {ECO:0000313|EMBL:KRY41493.1};
GN ORFNames=T01_4744 {ECO:0000313|EMBL:KRY41493.1};
OS Trichinella spiralis (Trichina worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6334 {ECO:0000313|EMBL:KRY41493.1, ECO:0000313|Proteomes:UP000054776};
RN [1] {ECO:0000313|EMBL:KRY41493.1, ECO:0000313|Proteomes:UP000054776}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS3 {ECO:0000313|EMBL:KRY41493.1};
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:KRY41493.1}.
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DR EMBL; JYDH01000007; KRY41493.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1BWH1; -.
DR STRING; 6334.A0A0V1BWH1; -.
DR eggNOG; KOG1864; Eukaryota.
DR InParanoid; A0A0V1BWH1; -.
DR Proteomes; UP000054776; 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:KRY41493.1};
KW Protease {ECO:0000256|RuleBase:RU366025};
KW Reference proteome {ECO:0000313|Proteomes:UP000054776};
KW Thiol protease {ECO:0000256|RuleBase:RU366025};
KW Ubl conjugation pathway {ECO:0000256|RuleBase:RU366025}.
FT DOMAIN 344..700
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 460..487
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 466..487
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 702 AA; 80761 MW; 41DC12BD47C2530E CRC64;
MDTLSNNRGK LLKIADICCA RLSNSLLYFT LPMYTHKDAA AAVMDVIHFC VNLPSTVQTK
LEPTFTDLTF TKLPLTFLSL ETDSSMALNF CPNFSLNITT PSVTNMSMTV CLAGTCFLNK
ININMNSIQI AEEIPLQNHV TRLYRLYNRC SGRYLQMYVK AINARGKSKS PLTLLKVETD
CYGGRVRIQS KKFRKYLCFN RKLRVTARPS LKYNGRSENC VFVERISENF YTEFESASQK
GAFLGFNSRG LFLHPTMRSR EPHCFQFIKE EQINPIEEFR GIDYGPSRRI RSRAKWKKKN
HTQPNITLTP QLFELPKIEA VVGQNASHLE KETTDEFPAN DHFYGLVNFG NTCYCNSVIQ
ALYFCRPFRE KVLNYKSQMK KAGNQKENLL LCLADLFHSI STQKRRVGTI APKKFIGRLK
KENDLFDNYM QQDAHEFLNY LLNTVADILL EEKRHEKRIS GGHKVGSKGT TDTVSQTDGF
GDNASSNQTQ VKDKLAEHTW VHDVFQGTLT NETRCLNCET VSSKDEDFLD LSVDVQQNTS
ITHCLREFSA TETLCNEHKY YCDICCSKQE AQKRMRIKKL PLILALHLKR FKYVEQYNRY
TKLSYRVLFP LELRLFNTSH DAVNPDRMYD LVAVVVHCGS TPNRGHYITV VKSQGFWLLF
DDDVVDKMDH INIEDFFGMA ADGSLQKNSE SGYILFYQAR DI
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