ID   A0A0A1V417_9HYPO        Unreviewed;       434 AA.
AC   A0A0A1V417;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=Peptidase family A1-like protein {ECO:0000313|EMBL:EXV04386.1};
GN   ORFNames=X797_002059 {ECO:0000313|EMBL:EXV04386.1};
OS   Metarhizium robertsii.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium.
OX   NCBI_TaxID=568076 {ECO:0000313|EMBL:EXV04386.1, ECO:0000313|Proteomes:UP000030151};
RN   [1] {ECO:0000313|EMBL:EXV04386.1, ECO:0000313|Proteomes:UP000030151}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ARSEF 2575 {ECO:0000313|EMBL:EXV04386.1,
RC   ECO:0000313|Proteomes:UP000030151};
RA   Giuliano Garisto Donzelli B., Roe B.A., Macmil S.L., Krasnoff S.B.,
RA   Gibson D.M.;
RT   "The genome sequence of the entomopathogenic fungus Metarhizium robertsii
RT   ARSEF 2575.";
RL   Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase A1 family.
CC       {ECO:0000256|ARBA:ARBA00007447}.
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:EXV04386.1}.
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DR   EMBL; JELW01000002; EXV04386.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0A1V417; -.
DR   eggNOG; ENOG502SMFH; Eukaryota.
DR   HOGENOM; CLU_039077_0_0_1; -.
DR   OrthoDB; 2342359at2759; -.
DR   Proteomes; UP000030151; Unassembled WGS sequence.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   CDD; cd05471; pepsin_like; 1.
DR   Gene3D; 2.40.70.10; Acid Proteases; 2.
DR   InterPro; IPR001461; Aspartic_peptidase_A1.
DR   InterPro; IPR034164; Pepsin-like_dom.
DR   InterPro; IPR033121; PEPTIDASE_A1.
DR   InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR   PANTHER; PTHR47966; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR   PANTHER; PTHR47966:SF51; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR   Pfam; PF00026; Asp; 1.
DR   SUPFAM; SSF50630; Acid proteases; 1.
DR   PROSITE; PS51767; PEPTIDASE_A1; 1.
PE   3: Inferred from homology;
KW   Disulfide bond {ECO:0000256|PIRSR:PIRSR601461-2};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..434
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5001992287"
FT   DOMAIN          65..430
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   DISULFID        355..391
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ   SEQUENCE   434 AA;  49205 MW;  0F7AC37BB7C5E630 CRC64;
     MPYKAILASC LLLLRTAYAV PAAVPPNGVD EARWGPGGRW SDRPGSWNPR GGQYDLPLDW
     DPLGFASRIG VGSPRFDYKV FVDWTWVSNI VTTPKCYGQW NPSLCLHPQQ PYWDPRNSTT
     FKNLTSEYAD RSWRPNHFFM QDPMSIEYGS DLLHIGPVTG EAVLQLTDLQ FNVSAKYGTP
     FPFTGIFGMS PVFRGDDVDY QSAYYQQWMN GRWRTAHTGF VYCHEESRKP VCNGHDGIQT
     MGGIRRDLIK NQKIWWYDVR LYPDVNTLDF VYNPPVYNYW GIELAGLKIG TEVQKIEPTS
     NSSGKGAIFD HAAYGRGTPL TPNAYARLAQ ITGGKPVELK EPPNNGEQKF FSVDCSKLKS
     FPSIKYKFTG SSREWAVTPE MYVEKMKDGS CVLNVRTLAS GDKFIGNFGE TFAKEKYIIL
     DFEKNRVGIA DMQW
//