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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   24-JAN-2024, entry version 41.
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, ECO:0000313|Proteomes:UP000005446};
RN   [1] {ECO:0000313|EMBL:EHL01600.1, ECO:0000313|Proteomes:UP000005446}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 74030 / MF5533 {ECO:0000313|Proteomes:UP000005446};
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 sequence
RT   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   -!- SUBCELLULAR LOCATION: Secreted, extracellular space
CC       {ECO:0000256|ARBA:ARBA00004239}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EHL01600.1}.
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DR   EMBL; AGUE01000049; EHL01600.1; -; Genomic_DNA.
DR   AlphaFoldDB; H0EIW9; -.
DR   MEROPS; S53.007; -.
DR   HOGENOM; CLU_013783_4_0_1; -.
DR   InParanoid; H0EIW9; -.
DR   Proteomes; UP000005446; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd04056; Peptidases_S53; 1.
DR   Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR   InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR   InterPro; IPR015366; S53_propep.
DR   InterPro; IPR030400; Sedolisin_dom.
DR   PANTHER; PTHR14218; PROTEASE S8 TRIPEPTIDYL PEPTIDASE I CLN2; 1.
DR   PANTHER; PTHR14218:SF19; SERINE PROTEASE AORO, PUTATIVE (AFU_ORTHOLOGUE AFUA_6G10250)-RELATED; 1.
DR   Pfam; PF09286; Pro-kuma_activ; 1.
DR   SUPFAM; SSF54897; Protease propeptides/inhibitors; 1.
DR   SUPFAM; SSF52743; Subtilisin-like; 1.
DR   PROSITE; PS51695; SEDOLISIN; 1.
PE   4: Predicted;
KW   Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|PROSITE-
KW   ProRule:PRU01032}; Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01032};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW   ProRule:PRU01032}; Protease {ECO:0000256|PROSITE-ProRule:PRU01032};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005446};
KW   Serine protease {ECO:0000256|PROSITE-ProRule:PRU01032}.
FT   DOMAIN          92..497
FT                   /note="Peptidase S53"
FT                   /evidence="ECO:0000259|PROSITE:PS51695"
FT   ACT_SITE        168
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT   ACT_SITE        172
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT   ACT_SITE        415
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT   BINDING         456
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT   BINDING         457
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT   BINDING         475
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT   BINDING         477
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PROSITE-ProRule: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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