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Database: UniProt
Entry: A0A0G2IZX1_9EURO
LinkDB: A0A0G2IZX1_9EURO
Original site: A0A0G2IZX1_9EURO 
ID   A0A0G2IZX1_9EURO        Unreviewed;       717 AA.
AC   A0A0G2IZX1;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   05-JUN-2019, entry version 23.
DE   RecName: Full=Ubiquitinyl hydrolase 1 {ECO:0000256|SAAS:SAAS01044305};
DE            EC=3.4.19.12 {ECO:0000256|SAAS:SAAS01044305};
GN   ORFNames=EMCG_03675 {ECO:0000313|EMBL:KKZ61819.1};
OS   Emmonsia crescens UAMH 3008.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Emmonsia.
OX   NCBI_TaxID=1247875 {ECO:0000313|EMBL:KKZ61819.1, ECO:0000313|Proteomes:UP000034164};
RN   [1] {ECO:0000313|Proteomes:UP000034164}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UAMH 3008 {ECO:0000313|Proteomes:UP000034164};
RX   PubMed=26439490; DOI=10.1371/journal.pgen.1005493;
RA   Munoz J.F., Gauthier G.M., Desjardins C.A., Gallo J.E., Holder J.,
RA   Sullivan T.D., Marty A.J., Carmen J.C., Chen Z., Ding L., Gujja S.,
RA   Magrini V., Misas E., Mitreva M., Priest M., Saif S., Whiston E.A.,
RA   Young S., Zeng Q., Goldman W.E., Mardis E.R., Taylor J.W.,
RA   McEwen J.G., Clay O.K., Klein B.S., Cuomo C.A.;
RT   "The dynamic genome and transcriptome of the human fungal pathogen
RT   Blastomyces and close relative Emmonsia.";
RL   PLoS Genet. 11:E1005493-E1005493(2015).
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:KKZ61819.1}.
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DR   EMBL; LCZI01001233; KKZ61819.1; -; Genomic_DNA.
DR   EnsemblFungi; KKZ61819; KKZ61819; EMCG_03675.
DR   Proteomes; UP000034164; Unassembled WGS sequence.
DR   GO; GO:0004843; F:thiol-dependent ubiquitin-specific protease activity; IEA:InterPro.
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; IPR015940; UBA.
DR   InterPro; IPR009060; UBA-like_sf.
DR   InterPro; IPR016652; Ubiquitinyl_hydrolase.
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   PIRSF; PIRSF016308; UBP; 1.
DR   SMART; SM00165; UBA; 2.
DR   SMART; SM00290; ZnF_UBP; 1.
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:UP000034164};
KW   Hydrolase {ECO:0000256|SAAS:SAAS01044238};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR016308-3,
KW   ECO:0000256|SAAS:SAAS01044152};
KW   Protease {ECO:0000256|SAAS:SAAS01044292};
KW   Thiol protease {ECO:0000256|SAAS:SAAS01044269};
KW   Ubl conjugation pathway {ECO:0000256|SAAS:SAAS01044331};
KW   Zinc {ECO:0000256|PIRSR:PIRSR016308-3, ECO:0000256|SAAS:SAAS01044373};
KW   Zinc-finger {ECO:0000256|SAAS:SAAS01044352}.
FT   DOMAIN       96    169       UBP-type. {ECO:0000259|PROSITE:PS50271}.
FT   DOMAIN      225    717       USP. {ECO:0000259|PROSITE:PS50235}.
FT   DOMAIN      517    558       UBA. {ECO:0000259|PROSITE:PS50030}.
FT   DOMAIN      581    622       UBA. {ECO:0000259|PROSITE:PS50030}.
FT   ZN_FING      96    169       UBP-type. {ECO:0000256|PROSITE-ProRule:
FT                                PRU00502}.
FT   REGION        1     22       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A0G2IZX1}.
FT   REGION      389    410       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A0G2IZX1}.
FT   REGION      623    648       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A0G2IZX1}.
FT   ACT_SITE    234    234       Nucleophile. {ECO:0000256|PIRSR:
FT                                PIRSR016308-1}.
FT   ACT_SITE    671    671       Proton acceptor. {ECO:0000256|PIRSR:
FT                                PIRSR016308-1}.
FT   METAL        98     98       Zinc. {ECO:0000256|PIRSR:PIRSR016308-3}.
FT   METAL       101    101       Zinc. {ECO:0000256|PIRSR:PIRSR016308-3}.
FT   METAL       118    118       Zinc. {ECO:0000256|PIRSR:PIRSR016308-3}.
FT   METAL       131    131       Zinc. {ECO:0000256|PIRSR:PIRSR016308-3}.
SQ   SEQUENCE   717 AA;  79442 MW;  1B72CF8FACB02F91 CRC64;
     MQRDEPPPKM SKLAITAERE EDRYDTTTRV NCHSCQASDI DKSAGKLPAV VDGVMKAVTF
     SRKEEVKAWE QEYKSCQHIL SLVQDQSNQA MPKDLSRCSS CDLKENLWLC LECGNLGCGR
     SQFGGVGGNS HGLAHADASS HGVAVKLGSI TPEGSADVFC YKCNDEILDP DLASHLKHWN
     INIADREKTE QSLVEMQIEQ NLKWDFSMTG QDGHESKPLF GKGLTGLKNL GNSCYISSAL
     QCLFSLPEFK TRYTQSMGEP PSVSSPAEDL ETQLRKLSDG IHSGRYSFPD PDAAISTDSP
     DVVYQKGLAP AMFKHLVGRG HDEFSTMRQQ DSFEFLMHLF KLITRSKHTG GLQDPVGSFQ
     FALEQRLQCL ACKKVRYTVD EQDNISVPVP ARHVKPSNNA TAGTEHQNSP DTLEFETVTL
     KECLDIFTGD ERVELTCTAC GSKEGFLKRS RFKTFPRNLV VNARRFSLVN WVPTKLNIPV
     EVDDNPFDMS AYMSSGLQEG EELLPEDSST SQPTAFVPNQ NVLDQILAMG FPEVRCKKAL
     HATGNSDGEA AMNWLISHME DPDIDMPVEL TTGSATSDDQ PMDDPDKIAQ LNEMGIDAAK
     ARKALRETDG DVMRAVDWVF SHPDDTGTLE DSPDDTPAGN AKETPGSKEL PAEFQLQSII
     CHKGASVHAG HYVAFVRKLL PGSDTPQWVL FNDEKVVEAS DVEEMKQFAY VYFFRRL
//
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