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Database: UniProt
Entry: H0EIW9_GLAL7
LinkDB: H0EIW9_GLAL7
Original site: H0EIW9_GLAL7 
ID   H0EIW9_GLAL7            Unreviewed;       497 AA.
AC   H0EIW9;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   08-MAY-2019, entry version 29.
DE   SubName: Full=Putative Tripeptidyl-peptidase sed1 {ECO:0000313|EMBL:EHL01600.1};
GN   ORFNames=M7I_2487 {ECO:0000313|EMBL:EHL01600.1};
OS   Glarea lozoyensis (strain ATCC 74030 / MF5533).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Helotiaceae; Glarea.
OX   NCBI_TaxID=1104152 {ECO:0000313|EMBL:EHL01600.1};
RN   [1] {ECO:0000313|EMBL:EHL01600.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=74030 {ECO:0000313|EMBL:EHL01600.1};
RX   PubMed=22302591; DOI=10.1128/EC.05302-11;
RA   Youssar L., Gruening B.A., Erxleben A., Guenther S., Huettel W.;
RT   "Genome sequence of the fungus Glarea lozoyensis: the first genome
RT   sequence of a species from the Helotiaceae family.";
RL   Eukaryot. Cell 11:250-250(2012).
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000256|PROSITE-ProRule:PRU01032};
CC       Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000256|PROSITE-
CC       ProRule:PRU01032};
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:EHL01600.1}.
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DR   EMBL; AGUE01000049; EHL01600.1; -; Genomic_DNA.
DR   MEROPS; S53.007; -.
DR   InParanoid; H0EIW9; -.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR   CDD; cd04056; Peptidases_S53; 1.
DR   InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR   InterPro; IPR015366; S53_propep.
DR   InterPro; IPR030400; Sedolisin_dom.
DR   Pfam; PF09286; Pro-kuma_activ; 1.
DR   SUPFAM; SSF52743; SSF52743; 1.
DR   PROSITE; PS51695; SEDOLISIN; 1.
PE   4: Predicted;
KW   Calcium {ECO:0000256|PROSITE-ProRule:PRU01032};
KW   Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01032};
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU01032};
KW   Protease {ECO:0000256|PROSITE-ProRule:PRU01032};
KW   Serine protease {ECO:0000256|PROSITE-ProRule:PRU01032}.
FT   DOMAIN       92    497       Peptidase S53. {ECO:0000259|PROSITE:
FT                                PS51695}.
FT   ACT_SITE    168    168       Charge relay system.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01032}.
FT   ACT_SITE    172    172       Charge relay system.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01032}.
FT   ACT_SITE    415    415       Charge relay system.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01032}.
FT   METAL       456    456       Calcium. {ECO:0000256|PROSITE-ProRule:
FT                                PRU01032}.
FT   METAL       457    457       Calcium; via carbonyl oxygen.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01032}.
FT   METAL       475    475       Calcium; via carbonyl oxygen.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01032}.
FT   METAL       477    477       Calcium. {ECO:0000256|PROSITE-ProRule:
FT                                PRU01032}.
SQ   SEQUENCE   497 AA;  52097 MW;  C49D5922259968C4 CRC64;
     MEVEIIKTSS SAHDSPRYGK HYTAEEVADL FAPSKSTTNA IYEWLVSFGI PREYHVPPHI
     QEHVDYISPG IKLHTPGRGR AGSANLGKRI FGVTSAKGNI MYNITPPVLA APGNKMGIFE
     DLGDVYSQAD LNSFYAKYAT NIPKGTAPTL NAIDGAVAPV AVTAAGAESN LDFQIAWPII
     YPQGTVLYQT DDPVYENNYV FSGFLNTFLD ALDGSYCSTV DPLDPKYPDT SSKAGAYKGA
     LQCGVYKPTN VISISYGGDE AGLPVAYQRR QCNEFMKLGL QGVSILVASG DSGVAGSQCL
     GSTATCPYIT AVGGTYLPAG ANVAIDAEVA VTRFPSGGGF SNIYAIPSYQ SSAVASYLKN
     YPPTYKSYQT VNSTNVGANS GIYNSAGRAY PDVSAVGDNV VIFTGGSEGL IGGTSASSPA
     FGAILNRINE ERIAAGKSTI GFVNPTLYAH PGVLHDIVKG TNAGCGTKGF SASPGWDPVT
     GLGTPNYPAM LSLFMSL
//
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