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Database: UniProt
Entry: A0A0N5CJD0_THECL
LinkDB: A0A0N5CJD0_THECL
Original site: A0A0N5CJD0_THECL 
ID   A0A0N5CJD0_THECL        Unreviewed;       518 AA.
AC   A0A0N5CJD0;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   05-JUN-2019, entry version 20.
DE   RecName: Full=Ubiquitinyl hydrolase 1 {ECO:0000256|SAAS:SAAS01044305};
DE            EC=3.4.19.12 {ECO:0000256|SAAS:SAAS01044305};
GN   ORFNames=TCLT_LOCUS131 {ECO:0000313|EMBL:VDM94975.1};
OS   Thelazia callipaeda (Oriental eyeworm) (Parasitic nematode).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Spiruromorpha; Thelazioidea; Thelaziidae; Thelazia.
OX   NCBI_TaxID=103827 {ECO:0000313|Proteomes:UP000046394, ECO:0000313|WBParaSite:TCLT_0000013001-mRNA-1};
RN   [1] {ECO:0000313|Proteomes:UP000046394, ECO:0000313|WBParaSite:TCLT_0000013001-mRNA-1}
RP   NUCLEOTIDE SEQUENCE.
RG   Helminth Genomes Consortium;
RL   Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|WBParaSite:TCLT_0000013001-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-2017) to UniProtKB.
RN   [3] {ECO:0000313|EMBL:VDM94975.1, ECO:0000313|Proteomes:UP000276776}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   Pathogen Informatics;
RL   Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Thiol-dependent hydrolysis of ester, thioester, amide,
CC         peptide and isopeptide bonds formed by the C-terminal Gly of
CC         ubiquitin (a 76-residue protein attached to proteins as an
CC         intracellular targeting signal).; EC=3.4.19.12;
CC         Evidence={ECO:0000256|SAAS:SAAS01117307};
CC   -!- SIMILARITY: Belongs to the peptidase C19 family.
CC       {ECO:0000256|SAAS:SAAS01045498}.
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DR   EMBL; UYYF01000008; VDM94975.1; -; Genomic_DNA.
DR   WBParaSite; TCLT_0000013001-mRNA-1; TCLT_0000013001-mRNA-1; TCLT_0000013001.
DR   OMA; KCDDHLI; -.
DR   Proteomes; UP000046394; Genome Assembly.
DR   Proteomes; UP000276776; Unassembled WGS sequence.
DR   GO; GO:0036459; F:thiol-dependent ubiquitinyl hydrolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0016579; P:protein deubiquitination; IEA:InterPro.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR   Gene3D; 3.30.40.10; -; 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   Pfam; PF00443; UCH; 1.
DR   Pfam; PF02148; zf-UBP; 1.
DR   SUPFAM; SSF54001; SSF54001; 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   Complete proteome {ECO:0000313|Proteomes:UP000046394,
KW   ECO:0000313|Proteomes:UP000276776};
KW   Hydrolase {ECO:0000256|SAAS:SAAS01044238};
KW   Metal-binding {ECO:0000256|SAAS:SAAS01044152};
KW   Protease {ECO:0000256|SAAS:SAAS01044292};
KW   Reference proteome {ECO:0000313|Proteomes:UP000276776};
KW   Thiol protease {ECO:0000256|SAAS:SAAS01044269};
KW   Ubl conjugation pathway {ECO:0000256|SAAS:SAAS01044331};
KW   Zinc {ECO:0000256|SAAS:SAAS01044373};
KW   Zinc-finger {ECO:0000256|SAAS:SAAS01044352}.
FT   DOMAIN       65    124       UBP-type. {ECO:0000259|PROSITE:PS50271}.
FT   DOMAIN      178    513       USP. {ECO:0000259|PROSITE:PS50235}.
FT   ZN_FING      65    124       UBP-type. {ECO:0000256|PROSITE-ProRule:
FT                                PRU00502}.
SQ   SEQUENCE   518 AA;  59505 MW;  15BF607B09A37F72 CRC64;
     MANIVAVQCV RAQVAYCTRN KRKLMPHSCV HLTKHKRTLM KALSVVHSVI FPCNTMSRGL
     HAKFVRCMQC RTRINALMCS CCECSTFACL KHMKGHMINQ RHGFAVSVGE GFLYCIGCDD
     FIYNRKMEKN RRDAENVHRR SLNLSTRSVW YPSTAIANAF RDTSGIILFS KSSVRGLRGL
     VNLGNTCFMN CIIQAIVHTP QLKDYFLTDQ HRRSSASHSK AHCLMCELAN TFQEFYSGNT
     TPYKPNRFLN LVWTHARHLA GYEQQDAHEF FIAALDVLHR HSGSSSPNFT PNDCNCIIDW
     IFTGKLQSDL TCSICGCVST TVDPFWDISL DVAQEVLLSS DAAFNSPDMT LEDCLRRYIM
     PEHLGSNAKT RCARCETYEE STKQLTLKTL PMVACFHLKR FEHNHNDRKK MDTVIKYPQF
     IDMTPFTASY HERPTCSPEN TFSVVSDLLK KNRNKYELFG VVNHLGTMES GHYTCYIRHQ
     TNQWFQCDDQ KVSRVSMEEV LSSQGYLLFY HKCHSDYY
//
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