ID   E9EGH0_METAQ            Unreviewed;       517 AA.
AC   E9EGH0;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   SubName: Full=Intracellular serine protease {ECO:0000313|EMBL:EFY84984.1};
GN   ORFNames=MAC_08968 {ECO:0000313|EMBL:EFY84984.1};
OS   Metarhizium acridum (strain CQMa 102).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium.
OX   NCBI_TaxID=655827 {ECO:0000313|Proteomes:UP000002499};
RN   [1] {ECO:0000313|EMBL:EFY84984.1, ECO:0000313|Proteomes:UP000002499}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CQMa 102 {ECO:0000313|EMBL:EFY84984.1,
RC   ECO:0000313|Proteomes:UP000002499};
RX   PubMed=21253567; DOI=10.1371/journal.pgen.1001264;
RA   Gao Q., Jin K., Ying S.H., Zhang Y., Xiao G., Shang Y., Duan Z., Hu X.,
RA   Xie X.Q., Zhou G., Peng G., Luo Z., Huang W., Wang B., Fang W., Wang S.,
RA   Zhong Y., Ma L.J., St Leger R.J., Zhao G.P., Pei Y., Feng M.G., Xia Y.,
RA   Wang C.;
RT   "Genome sequencing and comparative transcriptomics of the model
RT   entomopathogenic fungi Metarhizium anisopliae and M. acridum.";
RL   PLoS Genet. 7:E1001264-E1001264(2011).
CC   -!- SIMILARITY: Belongs to the peptidase S8 family.
CC       {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01240}.
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DR   EMBL; GL698595; EFY84984.1; -; Genomic_DNA.
DR   RefSeq; XP_007815308.1; XM_007817117.1.
DR   AlphaFoldDB; E9EGH0; -.
DR   GeneID; 19253279; -.
DR   KEGG; maw:MAC_08968; -.
DR   eggNOG; ENOG502S0RE; Eukaryota.
DR   HOGENOM; CLU_526834_0_0_1; -.
DR   InParanoid; E9EGH0; -.
DR   OrthoDB; 2325156at2759; -.
DR   Proteomes; UP000002499; Unassembled WGS sequence.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd00306; Peptidases_S8_S53; 1.
DR   Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR   InterPro; IPR000209; Peptidase_S8/S53_dom.
DR   InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR   PANTHER; PTHR43806:SF59; CEREVISIN-RELATED; 1.
DR   PANTHER; PTHR43806; PEPTIDASE S8; 1.
DR   Pfam; PF00082; Peptidase_S8; 1.
DR   SUPFAM; SSF52743; Subtilisin-like; 1.
DR   PROSITE; PS51892; SUBTILASE; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000313|EMBL:EFY84984.1};
KW   Protease {ECO:0000313|EMBL:EFY84984.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002499}.
FT   DOMAIN          241..460
FT                   /note="Peptidase S8/S53"
FT                   /evidence="ECO:0000259|Pfam:PF00082"
SQ   SEQUENCE   517 AA;  57346 MW;  DAD8935AE46B88A4 CRC64;
     MDMSFWQELR LMLTSTSSES SVPQREVLDE GDICALLSEP TFARLVYSID REKACFLRLR
     QPQLPELLPA PGNGLSLSDI LSRYRLTPSH RILLAYVVAH TYWQFYDSEV YCLDSKNFSQ
     YNTVQELGEP EIGKEVKKEG SPQVKGVEAR RKSLYYHVVR PLAWLANNGF RPRLGDRGYI
     SKNQSFSSLR SSVRTDGTYP HDSGLFHSSV SLGPLRWLQQ LKTISASVDD MRQATSSTRP
     VRIAILDTGL RLSIPYFQDD FDGPERKKQV ISYKDFVGQS DSDMKDLFGH GTFMMRLVAE
     SAPAAEIMVA RVAENTEGLS SCQTNIVKAI QWAGSEGADI ISMSFGFPRP IKDISDTIES
     VSRRGEGVVF VASAGNSPYE EEGFPACHPS VISVYAANSH GTFLESNSQT PSKRADVLCV
     VGEVPGEILE ELRDELPGIC QAGSSVSTAI AAGISATMLA YGDFLPHILP ARQGSSVYKR
     MHTSRGITHA SRDDTVFKSL WEARRRCQAK TKTGFNY
//