ID   A0A0N5A999_9BILA        Unreviewed;       719 AA.
AC   A0A0N5A999;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU366025};
DE            EC=3.4.19.12 {ECO:0000256|RuleBase:RU366025};
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_0000066901-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:SMUV_0000066901-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,
CC         ECO:0000256|RuleBase:RU366025};
CC   -!- SIMILARITY: Belongs to the peptidase C19 family.
CC       {ECO:0000256|RuleBase:RU366025}.
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DR   AlphaFoldDB; A0A0N5A999; -.
DR   STRING; 451379.A0A0N5A999; -.
DR   WBParaSite; SMUV_0000066901-mRNA-1; SMUV_0000066901-mRNA-1; SMUV_0000066901.
DR   Proteomes; UP000046393; Unplaced.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
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   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR001607; Znf_UBP.
DR   PANTHER; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR   PANTHER; PTHR21646:SF19; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 3; 1.
DR   Pfam; PF00443; UCH; 1.
DR   Pfam; PF02148; zf-UBP; 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS00972; USP_1; 1.
DR   PROSITE; PS00973; USP_2; 1.
DR   PROSITE; PS50235; USP_3; 1.
DR   PROSITE; PS50271; ZF_UBP; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|RuleBase:RU366025};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Protease {ECO:0000256|RuleBase:RU366025};
KW   Thiol protease {ECO:0000256|RuleBase:RU366025};
KW   Ubl conjugation pathway {ECO:0000256|RuleBase:RU366025};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00502}.
FT   DOMAIN          45..147
FT                   /note="UBP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50271"
FT   DOMAIN          313..716
FT                   /note="USP"
FT                   /evidence="ECO:0000259|PROSITE:PS50235"
FT   REGION          206..225
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          269..308
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        281..303
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   719 AA;  81084 MW;  6FB99E7C7F978B7B CRC64;
     MVDCPHLNNS VCIVQLDLDQ LKRLSSKSVF KDEKKFGAGD RASPNSVPTI SATQKNNLGL
     GVHFNDNNWN CVECGTTQCP WLCLSCGLIH CGRYINQDGL KHWKTYPNHS ARRYMDVFSS
     YQCDDFVGND TNDNRLASVR SSLQFYNRLR CEDHNYSSSK YDNLLEGEDV VEISADDSLP
     PFYDEGTEEE ENEVVEEVEG ANAVKFTLSN SNDNEENTEK SVISKSDLIE SRSPLSGDEF
     GKTLLSTESL QAESSTSFQS GLRKRKCENS CEGEQRVKSP YKDATSLSGL DQTPNSFPTS
     SSEKAETQDR KLRGLRNLGN TCFMNSVLQA LGCIEIFRYF MRNLPPIDFY TCTTDTVTSQ
     LPRYNTRNAL SSFNEGGVQP TFVSEELRKT LIEISRVPYT LNNAGSTAFG PVAFLEEVRK
     FAPRFRGFQQ HDAHEFLRCI LDRMQVELKN YQLPEWLLSE VFEGGSQKSN KSHFQATKDE
     NSYGSEKKCP IAFMFEGTLQ SQVTCLSCNT VSNKQDPFLD LSLDIYCSLN SSRTAVIQLS
     ECLERFFAKE ELGSDEQYLC TKCCSKQPST KQLFIKMLPN ASVLCLHLKR FRWSSFHRGK
     LDNMVEFPLK GLDMKPFMTS ICQSGNRFES SRGTSDSRSD SISSCSSCNA NDDDSKMIYD
     LTSLVVHHGG GINCGHYTAF GQRNGVWYIF NDSCVKECSA DLVTKQKAYI LFYTRRSSL
//