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Database: UniProt
Entry: A0A0V0ZEW0_9BILA
LinkDB: A0A0V0ZEW0_9BILA
Original site: A0A0V0ZEW0_9BILA 
ID   A0A0V0ZEW0_9BILA        Unreviewed;      1042 AA.
AC   A0A0V0ZEW0;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   05-JUN-2019, entry version 17.
DE   RecName: Full=Ubiquitinyl hydrolase 1 {ECO:0000256|SAAS:SAAS01044305};
DE            EC=3.4.19.12 {ECO:0000256|SAAS:SAAS01044305};
GN   Name=cps-6 {ECO:0000313|EMBL:KRY11041.1};
GN   ORFNames=T12_628 {ECO:0000313|EMBL:KRY11041.1};
OS   Trichinella patagoniensis.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=990121 {ECO:0000313|EMBL:KRY11041.1, ECO:0000313|Proteomes:UP000054783};
RN   [1] {ECO:0000313|EMBL:KRY11041.1, ECO:0000313|Proteomes:UP000054783}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS2496 {ECO:0000313|EMBL:KRY11041.1};
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,
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}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:KRY11041.1}.
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DR   EMBL; JYDQ01000208; KRY11041.1; -; Genomic_DNA.
DR   Proteomes; UP000054783; Unassembled WGS sequence.
DR   GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
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; IPR018524; DNA/RNA_endonuclease_AS.
DR   InterPro; IPR001604; DNA/RNA_non-sp_Endonuclease.
DR   InterPro; IPR020821; Extracellular_endonuc_su_A.
DR   InterPro; IPR040255; Non-specific_endonuclease.
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; PTHR13966; PTHR13966; 1.
DR   Pfam; PF01223; Endonuclease_NS; 1.
DR   Pfam; PF00443; UCH; 1.
DR   Pfam; PF02148; zf-UBP; 1.
DR   SMART; SM00892; Endonuclease_NS; 1.
DR   SMART; SM00477; NUC; 1.
DR   SMART; SM00290; ZnF_UBP; 1.
DR   SUPFAM; SSF54001; SSF54001; 1.
DR   PROSITE; PS01070; NUCLEASE_NON_SPEC; 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:UP000054783};
KW   Endonuclease {ECO:0000313|EMBL:KRY11041.1};
KW   Hydrolase {ECO:0000256|SAAS:SAAS01044238};
KW   Metal-binding {ECO:0000256|SAAS:SAAS01044152};
KW   Nuclease {ECO:0000313|EMBL:KRY11041.1};
KW   Protease {ECO:0000256|SAAS:SAAS01044292};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054783};
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       89    160       UBP-type. {ECO:0000259|PROSITE:PS50271}.
FT   DOMAIN      221    735       USP. {ECO:0000259|PROSITE:PS50235}.
FT   ZN_FING      89    160       UBP-type. {ECO:0000256|PROSITE-ProRule:
FT                                PRU00502}.
FT   REGION      404    440       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A0V0ZEW0}.
FT   REGION      470    495       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A0V0ZEW0}.
FT   REGION      675    697       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A0V0ZEW0}.
FT   COMPBIAS    404    424       Basic. {ECO:0000256|MobiDB-lite:
FT                                A0A0V0ZEW0}.
FT   COMPBIAS    426    440       Polar. {ECO:0000256|MobiDB-lite:
FT                                A0A0V0ZEW0}.
SQ   SEQUENCE   1042 AA;  118982 MW;  0DAC66FBD7922656 CRC64;
     MFLCFENEVQ QQYSSNGWKL FPCSVMEKIS KKYEEVYNKY FAGSKNGFSE NEGKLAAERD
     VILCPHIYSS LNLSPIQKHL QSSPLFQCHI CVQEQCRRAG TTENIQSESL LCLGCGYQFC
     TDRSFHHALR HFQKAESHCL TLSLTTLEIL CFRCGKFVDT GQSSQLIEVR NLVEKCKKAE
     CSSENSSPHL EKYFAVEERN CNITFSKRKM AKNSGISLPV SGLINFGNTC YFNAVLQVLM
     RTKSFCLLLA KCMSDENSQL LDPESVWQCS LFILFKCLWI GKAAHYFRGN QQHDSHELLR
     YFLDELRDEE LVCMKDGIKQ CCELTEDEEG KEKLKAYMLC CKTTAVDQVF GGQLLQSIRC
     LTCNHRSYKL DPFLDLSLAL QNDDCDDNDF QACNTAKTVP MSKHRMKKLK RQKKKEKRGK
     IRRQRVSSGT GEQQFLKDSV KNDQMNTVNN VNGDVSSLCE DMNDLTVEDK ENCNDDDSGS
     FYLESDDGGD SSQFESDDYD ELMEKLQPGP KHPVMMSSLK SVDACLNNFM IEELLTGSSK
     FACDNCAEIS GDKDETKLSD AKKSSLIFSP PAVLTLHLKR FENNGKTNRK IYGHVVFSTE
     LDMSRFCCRK GRRIFDSRVL YSLYGVICHS GSMYGGHYIA YVKVEDRDDA SWKRFLEKVS
     QVETIIFDPD DVGWQTKQRR RKTPSGSGNH KRSVSDGRRL SRAPTWYMLN DNITSKVPES
     AVLKAEAYML FYEPCIASGA SCAAIAGCFG FWLGNKQENK NTKVFPYLVA SAASAIDTRL
     PDVVPLIQAP AKPDSVAEKV DIPSRVSEIM RFGFPGFDNL RTFEDFVVSY DRKTRTVHWV
     LEHLTPDRMI YDPSVDRSKC MFREDESIHS YFRSTNEDYK ARSGYDRGHM AAAGNHRRTQ
     NAIDQTFLLS NMAPQVGKGF NRDKWNELEK HVRRMARKNK NVYICTGPLY LPKRDLDGKM
     RVTYEVIGKQ HVAVPTHFFK VILVENPESR YFIECYVMPN QSIDDSIPLN KFYAPLESVE
     RSAGFFIFSN MPRNKLISIN GK
//
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