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Database: UniProt
Entry: G0PF26_CAEBE
LinkDB: G0PF26_CAEBE
Original site: G0PF26_CAEBE 
ID   G0PF26_CAEBE            Unreviewed;       902 AA.
AC   G0PF26;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   24-JAN-2024, entry version 57.
DE   RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU366025};
DE            EC=3.4.19.12 {ECO:0000256|RuleBase:RU366025};
GN   ORFNames=CAEBREN_19011 {ECO:0000313|EMBL:EGT53487.1};
OS   Caenorhabditis brenneri (Nematode worm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=135651 {ECO:0000313|Proteomes:UP000008068};
RN   [1] {ECO:0000313|Proteomes:UP000008068}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PB2801 {ECO:0000313|Proteomes:UP000008068};
RG   Caenorhabditis brenneri Sequencing and Analysis Consortium;
RA   Wilson R.K.;
RL   Submitted (JUL-2011) 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 peptidase C19 family.
CC       {ECO:0000256|RuleBase:RU366025}.
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DR   EMBL; GL380341; EGT53487.1; -; Genomic_DNA.
DR   AlphaFoldDB; G0PF26; -.
DR   STRING; 135651.G0PF26; -.
DR   MEROPS; C19.A33; -.
DR   EnsemblMetazoa; CBN19011.1; CBN19011.1; WBGene00157736.
DR   eggNOG; KOG1870; Eukaryota.
DR   HOGENOM; CLU_001060_8_2_1; -.
DR   InParanoid; G0PF26; -.
DR   OMA; PCHAQQS; -.
DR   Proteomes; UP000008068; Unassembled WGS sequence.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.90.70.10; Cysteine proteinases; 2.
DR   Gene3D; 3.30.2230.10; DUSP-like; 1.
DR   InterPro; IPR035927; DUSP-like_sf.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR006615; Pept_C19_DUSP.
DR   InterPro; IPR001394; Peptidase_C19_UCH.
DR   InterPro; IPR018200; USP_CS.
DR   InterPro; IPR028889; USP_dom.
DR   PANTHER; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR   PANTHER; PTHR21646:SF24; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR   Pfam; PF06337; DUSP; 1.
DR   Pfam; PF00443; UCH; 1.
DR   SMART; SM00695; DUSP; 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   SUPFAM; SSF143791; DUSP-like; 1.
DR   PROSITE; PS51283; DUSP; 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};
KW   Protease {ECO:0000256|RuleBase:RU366025};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008068};
KW   Thiol protease {ECO:0000256|RuleBase:RU366025};
KW   Ubl conjugation pathway {ECO:0000256|RuleBase:RU366025}.
FT   DOMAIN          23..131
FT                   /note="DUSP"
FT                   /evidence="ECO:0000259|PROSITE:PS51283"
FT   DOMAIN          281..849
FT                   /note="USP"
FT                   /evidence="ECO:0000259|PROSITE:PS50235"
FT   REGION          1..30
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          239..261
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          854..902
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        8..30
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        872..890
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   902 AA;  102630 MW;  0D8DCB3FCC3409E4 CRC64;
     MPTPDDVSME EADVKGAEGS DEESNNPTRD ELRRLLTEVE QTEMLENESW FLISQKWWNS
     LLKAVRDGFV DDLPPIDNSN ISECRQGSFF LKQRLAEQVD YTPVPSKVFK RLETFYQVED
     PRRDYITRQV VPKNGSLCLE VYPRIVHVAL ARNRDMKADV TLKSDDTMAS LRERVITELN
     LEANQNVRFY VMSSDNPELI DTTQSIDSYF DTVQKVLVDV EENGEFFFRG KNAVQPQSKT
     LYGNQASSSS SSSLGGHSVS NSYNTASPTH GVVTRTTPGA CGLSNLGNTC FMASAFQCLS
     NIPPLRDYFI NEEYLQDLNE ENPLGTHGNL AVAVGDLMKG MWSGEYASIN PRKFKGIIGQ
     FAPRFNGYSQ QDAHELMAYV LDGLHEDLNR IKKKPYIEDN DEDAKLPEAE YAAKSWQVYK
     MRNDSIIVDT LHGQLRSTLI CPVCQKISIK FDPFGYLSLP LPPKEQIVKQ TVIVMFLNRK
     WAKFSLGITD TTTVEEAESL MLEKLQLEEP HHFVFFHVPS AYHDDIAILQ PGDRVRMQGR
     EVYVAQVEHD LSVKGTRIFV AYNRVKIVKP ASLPMIYSLA PGFPLTRGFL NDHVFNTTKR
     LFINQKIATE LNGNDDDSMS GNSSDEREPY KLFVGDPGSQ TPLPISSTND PIPFPDEMSN
     DLYRNYLQVI FQWKDIKLFN QYKGADLVER EMTVATRRRV LLEETLNWFT KKEQLGEQDS
     WYCPQCKKHE RASKQLDLWK LPEILILHLK RFQYTKWSRE KLTWDVVIPV RGLDLTAKVA
     NPNHEAAVYD LIAVSRHYGS LSGGHYTAIG FNDKAQKWFD FNDSSSNVSS PPNEPYESSD
     PYILVYRRRK LDDKGVPIEP AAPVESNNRH KRGAAPSISS ATTSNGSSSR HHLDENMEME
     ED
//
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