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Database: UniProt
Entry: A0A0N5ASV0_9BILA
LinkDB: A0A0N5ASV0_9BILA
Original site: A0A0N5ASV0_9BILA 
ID   A0A0N5ASV0_9BILA        Unreviewed;      1389 AA.
AC   A0A0N5ASV0;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=Ubiquitin carboxyl-terminal hydrolase 47 {ECO:0000256|ARBA:ARBA00026136};
DE            EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
DE   AltName: Full=Ubiquitin thioesterase 47 {ECO:0000256|ARBA:ARBA00029910};
DE   AltName: Full=Ubiquitin-specific-processing protease 47 {ECO:0000256|ARBA:ARBA00032453};
OS   Syphacia muris.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Oxyuridomorpha; Oxyuroidea; Oxyuridae; Syphacia.
OX   NCBI_TaxID=451379 {ECO:0000313|Proteomes:UP000046393, ECO:0000313|WBParaSite:SMUV_0000788401-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:SMUV_0000788401-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-2017) 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};
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DR   STRING; 451379.A0A0N5ASV0; -.
DR   WBParaSite; SMUV_0000788401-mRNA-1; SMUV_0000788401-mRNA-1; SMUV_0000788401.
DR   Proteomes; UP000046393; Unplaced.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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; IPR045578; USP47_C.
DR   InterPro; IPR018200; USP_CS.
DR   InterPro; IPR028889; USP_dom.
DR   PANTHER; PTHR24006; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR   PANTHER; PTHR24006:SF702; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 47; 1.
DR   Pfam; PF00443; UCH; 1.
DR   Pfam; PF19718; USP47_C; 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   4: Predicted;
FT   DOMAIN          117..525
FT                   /note="USP"
FT                   /evidence="ECO:0000259|PROSITE:PS50235"
FT   REGION          1..88
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1358..1389
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        11..38
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        52..88
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1358..1373
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1374..1389
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1389 AA;  157060 MW;  F04AA17EEE3C2241 CRC64;
     MARKEDHNTL STSSFKNLIP QPSAASPLPG TSTSEVPEDG DQVACPPLME SSLSYDTRNI
     STGEDNGNQL EIITNDNSNS PTDGSPTSIP ALAFPTSSVP ITSPSLGHLD DNGHCYVGLV
     NQAMTCYLNS LIQTLYMTPE FRNAIYEWKF SGAQSEEARS IPCQLQKLFL LLQTSNRESL
     ETRELTRSFG WGAGEAYDQH DVQELCRIMF DALEQKWRKT NNSSLIQNLY RYLKLCYYHF
     YLKNNIRKFR GSMEDFVKCL ACSTESVKND VFLDLPLAIK QFGVLEAYKS VEEALQAFIK
     PEILDGNNQY FCEKCGKKQD AQKGLRITEF PYLLTIQLKR FDFDYNTLHR IKLNDRMVFP
     FLLNLNGFVY DSSKDSDCEA KRKKISWASV AAGTKKVTEP AVVPPVDYGR FSLKAGFFPK
     FFFTGIRIGR AENQHPHIEI KEVEELLKKD GPYVYELFSV MVHQGSATGG HYYAYIKNMD
     QDAWFCFNDS SVTVATVDDI HRTYGGSFGG WACNTNAYML MYRRIDKAKN AKFLKTCDLP
     DHLKTILKRW ETTEEEKRLK KEYEESLVKV GDTIIMVHVL INGISLNAFC GMERSIRIPY
     TSKLKDIFDQ TIEITFVDSE LTSANRFRLI ECSDSTFSMK RAFSSLELEN VSLNDLYPKY
     ARTLKTYRQD AFFILDCVPI NSDFFEVMSS KEACTCKLYP VDIAKKTILT SIFIQFSLSC
     TVFEMRKKIG EYFGFNKELY QKTRVVIDKK SALTLPSFLL LENDDESCST LINTAGTRLL
     SIYFDTSISS DLVEEDRRKN FEKSRLLALL ERKRLAMTLT IHLPAENDYK QAGIAPLDFS
     NIDSIILNCA SSNDVECSTT VDSSNDGHGL EHSMKGDCKN EVTQIHREHH SPAPATEVAS
     LPVASASSAT MSNNYPLSAS LTNSQLSSTS SLVSEDDREP ILMEFDHSGT SSPFFTPIVS
     PSVSDSDDAC LEGSNTLNTM KERYERIFNA VADMKDMTEV EGLSPVDLDL ISSTAESSED
     TVTMGAQTVN SAVGSETSGS NYEVVVLSRS SENGVNEIVV ELDGRQSVSS LKEWLSKLLA
     VDVNRFVVLK HYKKGDDGYE NIFYDNETVR DYYSSVVYIS INLRSPLKEN ERVIRVSQFV
     LDTAEYERWP YLFSIVVSPD TKVHDMLLKC RDLLKATCNL DYELRRLRLR ELDVAIGAPV
     MNSGDTMGRR GGEWSRSVYL QILSEKEADE WEECGTTSYP VAVQRWNPST LEVSPRSELV
     VAADLEDQTA ALKGAIASHF HVPVEKIELS EPYPSNVWTK YPYTKDRLEL LDTVYFSSRT
     INVNNFNGKL VYFKLNDELP KRLTEAERRA IRIKDSSAKS MDVTKRRKEK PLRIQLSSSV
     SEDNTFSLP
//
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