ID A0A014N8L2_9HYPO Unreviewed; 356 AA.
AC A0A014N8L2;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 08-NOV-2023, entry version 32.
DE SubName: Full=Peptidase A1family protein {ECO:0000313|EMBL:EXU96275.1};
GN ORFNames=X797_010660 {ECO:0000313|EMBL:EXU96275.1};
OS Metarhizium robertsii.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium.
OX NCBI_TaxID=568076 {ECO:0000313|EMBL:EXU96275.1, ECO:0000313|Proteomes:UP000030151};
RN [1] {ECO:0000313|EMBL:EXU96275.1, ECO:0000313|Proteomes:UP000030151}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ARSEF 2575 {ECO:0000313|EMBL:EXU96275.1,
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:EXU96275.1}.
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DR EMBL; JELW01000052; EXU96275.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A014N8L2; -.
DR eggNOG; KOG1339; Eukaryota.
DR HOGENOM; CLU_037868_1_0_1; -.
DR OrthoDB; 4946at2759; -.
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; NAPSIN-A; 1.
DR Pfam; PF00026; Asp; 1.
DR PRINTS; PR00792; PEPSIN.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 3: Inferred from homology;
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..356
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001473978"
FT DOMAIN 58..353
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
SQ SEQUENCE 356 AA; 37156 MW; 3C62C2821C325726 CRC64;
MSLKTLLLLA AAHLAQADSS HALFYKVVDR ETAQRIASIK GLAAAGNDTP VSKNQGFWFS
HFTVGASPDL EILIDTGSSD AILNPGVYKP SPGSVNANRR FRISYATTNP DGSGTLTASG
NVYQDVITQL SANLTVANQT LGDIQDPTSP PTFPRDGLIG YASQQGSALR GSPFINSLCD
QGALSTCRFG LALRPNKTGE LYYGTLATDT FTEPLTTVPL AQGEWAVQGD VTVDGTPVQH
GASIITDSGT TVIFGPTHRV ADVFARAGIQ AVSTSTGLAG YYNCSAPPTI GFSFAGANFD
ILPSALAFAS DGDNCTAAVH GSDAFGDNWL VGQAFFQGRY VDHNVADGTM GFANLK
//