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Database: UniProt
Entry: A0A151GFI3_9HYPO
LinkDB: A0A151GFI3_9HYPO
Original site: A0A151GFI3_9HYPO 
ID   A0A151GFI3_9HYPO        Unreviewed;       515 AA.
AC   A0A151GFI3;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   05-JUN-2019, entry version 16.
DE   RecName: Full=Ubiquitinyl hydrolase 1 {ECO:0000256|SAAS:SAAS01044305};
DE            EC=3.4.19.12 {ECO:0000256|SAAS:SAAS01044305};
GN   ORFNames=DCS_07822 {ECO:0000313|EMBL:KYK55857.1};
OS   Drechmeria coniospora.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae;
OC   Drechmeria.
OX   NCBI_TaxID=98403 {ECO:0000313|EMBL:KYK55857.1, ECO:0000313|Proteomes:UP000076580};
RN   [1] {ECO:0000313|EMBL:KYK55857.1, ECO:0000313|Proteomes:UP000076580}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ARSEF 6962 {ECO:0000313|EMBL:KYK55857.1,
RC   ECO:0000313|Proteomes:UP000076580};
RX   PubMed=26975455; DOI=10.1038/srep23122;
RA   Zhang L., Zhou Z., Guo Q., Fokkens L., Miskei M., Pocsi I., Zhang W.,
RA   Chen M., Wang L., Sun Y., Donzelli B.G., Gibson D.M., Nelson D.R.,
RA   Luo J.G., Rep M., Liu H., Yang S., Wang J., Krasnoff S.B., Xu Y.,
RA   Molnar I., Lin M.;
RT   "Insights into Adaptations to a Near-Obligate Nematode Endoparasitic
RT   Lifestyle from the Finished Genome of Drechmeria coniospora.";
RL   Sci. Rep. 6:23122-23122(2016).
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:KYK55857.1}.
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DR   EMBL; LAYC01000003; KYK55857.1; -; Genomic_DNA.
DR   EnsemblFungi; KYK55857; KYK55857; DCS_07822.
DR   OrthoDB; 929408at2759; -.
DR   Proteomes; UP000076580; Chromosome 03.
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:0016578; P:histone 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; IPR037798; UBP8.
DR   InterPro; IPR018200; USP_CS.
DR   InterPro; IPR028889; USP_dom.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR001607; Znf_UBP.
DR   PANTHER; PTHR21646:SF33; PTHR21646:SF33; 1.
DR   Pfam; PF00443; UCH; 1.
DR   Pfam; PF02148; zf-UBP; 1.
DR   SUPFAM; SSF54001; SSF54001; 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:UP000076580};
KW   Hydrolase {ECO:0000256|SAAS:SAAS01044238,
KW   ECO:0000313|EMBL:KYK55857.1};
KW   Metal-binding {ECO:0000256|SAAS:SAAS01044152};
KW   Protease {ECO:0000256|SAAS:SAAS01044292};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076580};
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       64    127       UBP-type. {ECO:0000259|PROSITE:PS50271}.
FT   DOMAIN      180    512       USP. {ECO:0000259|PROSITE:PS50235}.
FT   ZN_FING      64    127       UBP-type. {ECO:0000256|PROSITE-ProRule:
FT                                PRU00502}.
FT   REGION        1     21       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A151GFI3}.
SQ   SEQUENCE   515 AA;  58540 MW;  75CF468FB725FA53 CRC64;
     MSTRPTTPAS PKNAKIKSPA PGTPMFGCEH VQLLLSQGQE VMNSSIAHYK MILRGIFDTP
     PIVPQTSTNQ EGRPITSLTS NYLCLQCPTT VTEEDRLEHG TERQHRFYVD SRSGSLYCQI
     CDDMVWDPTL EELRVRKIGT GSFSGRKRKH DELFTDSIKE DPRYIASNTT TASCRANGLR
     GIYNAGATCY QNVVLQSFLH NPLLRNFYLS DGHQSNDCSV PHCLSCAMDD MFQDFYALEN
     TNGYTAANIL SGFWISEKKA FENLVTTKEQ DAHEFFQFLA EELHERNGDG KRPETGCEHS
     CNCIVHQTFY GKMQTTTACQ NCSGTTHAVQ SFLDLSLGLD ALTQRRIKKT GQKKPVLTLT
     DCLDEEYVKF DKCEYRCHSC ASSQQARRYT CIKRLPNVLS IQLKRFEYKQ GRHDRAASKI
     DNVVQFPLQL NMLPYTNRVR TRDSRENLEL ERSCTYDLLS VVVHVGEIET GHYVSYCRVG
     DQWFKFNDHK VELASISDVL GAQAYLLFYI IRSLA
//
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