GenomeNet

Database: UniProt
Entry: G4TIP4_SERID
LinkDB: G4TIP4_SERID
Original site: G4TIP4_SERID 
ID   G4TIP4_SERID            Unreviewed;       798 AA.
AC   G4TIP4;
DT   14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2011, sequence version 1.
DT   05-JUN-2019, entry version 55.
DE   RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|PIRNR:PIRNR016308};
DE            EC=3.4.19.12 {ECO:0000256|PIRNR:PIRNR016308};
GN   ORFNames=PIIN_05123 {ECO:0000313|EMBL:CCA71187.1};
OS   Serendipita indica (strain DSM 11827) (Root endophyte fungus)
OS   (Piriformospora indica).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina;
OC   Agaricomycetes; Sebacinales; Serendipitaceae; Serendipita.
OX   NCBI_TaxID=1109443 {ECO:0000313|EMBL:CCA71187.1, ECO:0000313|Proteomes:UP000007148};
RN   [1] {ECO:0000313|EMBL:CCA71187.1, ECO:0000313|Proteomes:UP000007148}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 11827 {ECO:0000313|EMBL:CCA71187.1,
RC   ECO:0000313|Proteomes:UP000007148};
RX   PubMed=22022265; DOI=10.1371/journal.ppat.1002290;
RA   Zuccaro A., Lahrmann U., Guldener U., Langen G., Pfiffi S.,
RA   Biedenkopf D., Wong P., Samans B., Grimm C., Basiewicz M., Murat C.,
RA   Martin F., Kogel K.H.;
RT   "Endophytic Life Strategies Decoded by Genome and Transcriptome
RT   Analyses of the Mutualistic Root Symbiont Piriformospora indica.";
RL   PLoS Pathog. 7:e1002290-e1002290(2011).
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}.
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:CCA71187.1}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   EMBL; CAFZ01000109; CCA71187.1; -; Genomic_DNA.
DR   STRING; 65672.G4TIP4; -.
DR   EnsemblFungi; CCA71187; CCA71187; PIIN_05123.
DR   InParanoid; G4TIP4; -.
DR   OMA; ECGNLGC; -.
DR   OrthoDB; 556111at2759; -.
DR   Proteomes; UP000007148; Unassembled WGS sequence.
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   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; 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:UP000007148};
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   Protease {ECO:0000256|PIRNR:PIRNR016308,
KW   ECO:0000256|SAAS:SAAS01044292};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007148};
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      182    255       UBP-type. {ECO:0000259|PROSITE:PS50271}.
FT   DOMAIN      311    798       USP. {ECO:0000259|PROSITE:PS50235}.
FT   DOMAIN      602    642       UBA. {ECO:0000259|PROSITE:PS50030}.
FT   DOMAIN      661    701       UBA. {ECO:0000259|PROSITE:PS50030}.
FT   ZN_FING     182    255       UBP-type. {ECO:0000256|PROSITE-ProRule:
FT                                PRU00502}.
FT   REGION       53     91       Disordered. {ECO:0000256|MobiDB-lite:
FT                                G4TIP4}.
FT   REGION      206    209       Substrate binding. {ECO:0000256|PIRSR:
FT                                PIRSR016308-2}.
FT   COMPBIAS     77     91       Polyampholyte. {ECO:0000256|MobiDB-lite:
FT                                G4TIP4}.
FT   ACT_SITE    320    320       Nucleophile. {ECO:0000256|PIRSR:
FT                                PIRSR016308-1}.
FT   ACT_SITE    752    752       Proton acceptor. {ECO:0000256|PIRSR:
FT                                PIRSR016308-1}.
FT   METAL       184    184       Zinc. {ECO:0000256|PIRSR:PIRSR016308-3}.
FT   METAL       187    187       Zinc. {ECO:0000256|PIRSR:PIRSR016308-3}.
FT   METAL       204    204       Zinc. {ECO:0000256|PIRSR:PIRSR016308-3}.
FT   METAL       217    217       Zinc. {ECO:0000256|PIRSR:PIRSR016308-3}.
FT   BINDING     194    194       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR016308-2}.
FT   BINDING     245    245       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR016308-2}.
FT   BINDING     247    247       Substrate; via carbonyl oxygen.
FT                                {ECO:0000256|PIRSR:PIRSR016308-2}.
FT   BINDING     250    250       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR016308-2}.
SQ   SEQUENCE   798 AA;  88153 MW;  456AA1146651856D CRC64;
     MACPHLPQLQ SLQPPRLSQS VHREECTQCF DNQDMEGGVD VCLSCFNGGC PSEERHHSRN
     HQQRSGHPFT LNIRRRPKPT IKRDDGAEPP AKRLAIQEER EEDKYNHSAE LKCWLCDPQN
     GSIVSGALDN GKGAELKNAI MTSLSSARQS EVKSWEEDIE ACEHTLTLHQ PDSHPIPAEG
     LAQCSKCDLK ENLWLCLACG NLGCGRAQFG GVSGNGHALL HYNESGHAPA VKLGTITPEG
     TADVYCYKCD DSKMDLELAA HLATFGINVA TQQKTEKTMT ELQIDQNFNY EFSVTDENGK
     PFEPLFGPGL TGLQNLGNSC YMASVLQSLF ALDPFKAAYR GDHVNTCGEP LPASCILCQL
     HKMHDGLLSG RYSIPRANLP QDEPPKSNEP VFQNGLRPSM FKALIGKGHP EFATMRQQDA
     EEFMTYLFKV IRTDAKKRGI PEKNTPPESF KFGMEQRLQC QRCQKVRYKV DSHDSVSLAI
     PANKVTKIPS DENEEPKEDW EPVELESCLR IFTGGDGLEY KCPSCKETVT ASKQTRFATF
     PDILAVHAKK FQLVNWVPTK LPIPLLVNDF LILDEYVGKG LQQGEQELPN DGETGATSTE
     PEVDAEALAQ LEGLGFPTTR CKRALLANQM NAEAAVQWIF EHMDDPDIDA PLAPAASQAA
     PADPGMISML QDMGFTSAQA SKALRETGGD MERAVEWLFS HPDDMGDVEA PGESAPTQES
     VTKDYGGSGT LPARYRLKAF VSHKGPSVHS GHYVAHIRLD LPDGEKWVLF NDEKVVKADE
     ESVDALKPLA YLYIFERV
//
DBGET integrated database retrieval system