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Database: UniProt
Entry: A0A0G4INX4_PLABS
LinkDB: A0A0G4INX4_PLABS
Original site: A0A0G4INX4_PLABS 
ID   A0A0G4INX4_PLABS        Unreviewed;       777 AA.
AC   A0A0G4INX4;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   08-MAY-2019, entry version 24.
DE   RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|PIRNR:PIRNR016308};
DE            EC=3.4.19.12 {ECO:0000256|PIRNR:PIRNR016308};
GN   ORFNames=PBRA_005476 {ECO:0000313|EMBL:CEO96872.1}, PLBR_LOCUS9044
GN   {ECO:0000313|EMBL:SPR01829.1};
OS   Plasmodiophora brassicae (Clubroot disease).
OG   Mitochondrion {ECO:0000313|EMBL:SPR01829.1}.
OC   Eukaryota; Rhizaria; Cercozoa; Imbricatea; Plasmodiophorida;
OC   Plasmodiophoridae; Plasmodiophora.
OX   NCBI_TaxID=37360 {ECO:0000313|EMBL:CEO96872.1, ECO:0000313|Proteomes:UP000039324};
RN   [1] {ECO:0000313|EMBL:CEO96872.1, ECO:0000313|Proteomes:UP000039324}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E3 {ECO:0000313|EMBL:CEO96872.1};
RA   Chooi Y.-H.;
RL   Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:SPR01829.1, ECO:0000313|Proteomes:UP000290189}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Fogelqvist J.;
RL   Submitted (MAR-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|PIRNR:PIRNR016308,
CC         ECO:0000256|SAAS:SAAS01117307};
CC   -!- SIMILARITY: Belongs to the peptidase C19 family.
CC       {ECO:0000256|PIRNR:PIRNR016308, ECO:0000256|SAAS:SAAS01045498}.
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DR   EMBL; CDSF01000077; CEO96872.1; -; Genomic_DNA.
DR   EMBL; OVEO01000019; SPR01829.1; -; Genomic_DNA.
DR   EnsemblProtists; CEO96872; CEO96872; PBRA_005476.
DR   OMA; ECGNLGC; -.
DR   OrthoDB; 556111at2759; -.
DR   Proteomes; UP000039324; Unassembled WGS sequence.
DR   Proteomes; UP000290189; Unassembled WGS sequence.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-KW.
DR   GO; GO:0004843; F:thiol-dependent ubiquitin-specific protease activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016579; P:protein deubiquitination; IEA:InterPro.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR   CDD; cd14298; UBA2_scUBP14_like; 1.
DR   Gene3D; 3.30.40.10; -; 2.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR001394; Peptidase_C19_UCH.
DR   InterPro; IPR015940; UBA.
DR   InterPro; IPR009060; UBA-like_sf.
DR   InterPro; IPR033864; UBA2_scUBP14-like.
DR   InterPro; IPR016652; Ubiquitinyl_hydrolase.
DR   InterPro; IPR041432; UBP13_Znf-UBP_var.
DR   InterPro; IPR018200; USP_CS.
DR   InterPro; IPR028889; USP_dom.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR001607; Znf_UBP.
DR   Pfam; PF00627; UBA; 2.
DR   Pfam; PF00443; UCH; 1.
DR   Pfam; PF02148; zf-UBP; 1.
DR   Pfam; PF17807; zf-UBP_var; 1.
DR   PIRSF; PIRSF016308; UBP; 1.
DR   SMART; SM00165; UBA; 2.
DR   SMART; SM00290; ZnF_UBP; 2.
DR   SUPFAM; SSF46934; SSF46934; 1.
DR   SUPFAM; SSF54001; SSF54001; 1.
DR   PROSITE; PS50030; UBA; 2.
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:UP000039324,
KW   ECO:0000313|Proteomes:UP000290189};
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR016308,
KW   ECO:0000256|SAAS:SAAS01044238};
KW   Metal-binding {ECO:0000256|PIRNR:PIRNR016308,
KW   ECO:0000256|PIRSR:PIRSR016308-3, ECO:0000256|SAAS:SAAS01044152};
KW   Mitochondrion {ECO:0000313|EMBL:SPR01829.1};
KW   Protease {ECO:0000256|PIRNR:PIRNR016308,
KW   ECO:0000256|SAAS:SAAS01044292};
KW   Reference proteome {ECO:0000313|Proteomes:UP000039324};
KW   Thiol protease {ECO:0000256|PIRNR:PIRNR016308,
KW   ECO:0000256|SAAS:SAAS01044269};
KW   Ubl conjugation pathway {ECO:0000256|PIRNR:PIRNR016308,
KW   ECO:0000256|SAAS:SAAS01044331};
KW   Zinc {ECO:0000256|PIRNR:PIRNR016308, ECO:0000256|PIRSR:PIRSR016308-3,
KW   ECO:0000256|SAAS:SAAS01044373};
KW   Zinc-finger {ECO:0000256|SAAS:SAAS01044352}.
FT   DOMAIN      177    249       UBP-type. {ECO:0000259|PROSITE:PS50271}.
FT   DOMAIN      305    776       USP. {ECO:0000259|PROSITE:PS50235}.
FT   DOMAIN      577    633       UBA. {ECO:0000259|PROSITE:PS50030}.
FT   DOMAIN      654    694       UBA. {ECO:0000259|PROSITE:PS50030}.
FT   ZN_FING     177    249       UBP-type. {ECO:0000256|PROSITE-ProRule:
FT                                PRU00502}.
FT   ACT_SITE    314    314       Nucleophile. {ECO:0000256|PIRSR:
FT                                PIRSR016308-1}.
FT   ACT_SITE    736    736       Proton acceptor. {ECO:0000256|PIRSR:
FT                                PIRSR016308-1}.
FT   METAL       179    179       Zinc. {ECO:0000256|PIRSR:PIRSR016308-3}.
FT   METAL       182    182       Zinc. {ECO:0000256|PIRSR:PIRSR016308-3}.
FT   METAL       199    199       Zinc. {ECO:0000256|PIRSR:PIRSR016308-3}.
FT   METAL       212    212       Zinc. {ECO:0000256|PIRSR:PIRSR016308-3}.
SQ   SEQUENCE   777 AA;  85842 MW;  470E70950DC15A34 CRC64;
     MSSCSHWPNE DSLALPGSSA VVVNDECSQC FRTPVDADSL YICIRCYNGG CLTHAVQHAK
     VAQHSVAVRL KKTVKPSTEE SRPQKVTKLA IGVEGGFSVP KPPEYDVETS FTCMACPDHP
     QKPITAATKA FVDAIVGHRS MAATSQVDTW VEERVTCSHV VDLEQHSGVH LQPKNLAHCA
     SCDLTENLWL CMTCGALGCG RPIYGGGGGR GHALEHYQQT GHPTSCKVGT ITADGADIYC
     YNCDEMRLDE QLAAHMATFG IAIHEQRKTA QTTEEMELER NLNYEWSKVI EKGDAMQLLW
     GPGHTGLINL GNSCYMAASV QVLFSLDAFR QRYYEQGRAH IASCTSQQPY NCFSCQMAKL
     AHGLWSGEYS KRPEGLDDEP QSTVCNDELP AQVVSQPGVS PKMFKRLVAE SHAEFRSTRQ
     QDAQEFIQYF LQFVRQQEHR LQGPDPTDAL EFVMETRLQC LNCHRVRYRS INTTELSVTL
     PTDAPAPKSD DDETSIPFKD VIAQFLGSSR VEDFKCPQCS SRTTAETSVR LATFPEILMV
     HVRRFVHDGW VPRKLTAKID VPTSPFSLEP LRSHGMQADE QPLPEDAPAR FTPNPALVEQ
     LRQMGFTENA CGRALQAVNN SGAEEAMEWL FAHVDDPNLN DPVPPPSSAA TSASADPGAI
     ANLAAMGFEE QRCAYALQQT SGDVERALDW LFSHEGEPID DSKGAPPRLP GVKDAPATYA
     LAAVITHLGE STSHGHYVAH VHRPDEHKWI YFNDNKVSDS ARPPIKQGYL YFFRRCS
//
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