ID A0A014N7S9_9HYPO Unreviewed; 408 AA.
AC A0A014N7S9;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 22-FEB-2023, entry version 36.
DE SubName: Full=Peptidase A1family protein {ECO:0000313|EMBL:EXU95858.1};
GN ORFNames=X797_011039 {ECO:0000313|EMBL:EXU95858.1};
OS Metarhizium robertsii.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium.
OX NCBI_TaxID=568076 {ECO:0000313|EMBL:EXU95858.1, ECO:0000313|Proteomes:UP000030151};
RN [1] {ECO:0000313|EMBL:EXU95858.1, ECO:0000313|Proteomes:UP000030151}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ARSEF 2575 {ECO:0000313|EMBL:EXU95858.1,
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, ECO:0000256|RuleBase:RU000454}.
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:EXU95858.1}.
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DR EMBL; JELW01000062; EXU95858.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A014N7S9; -.
DR eggNOG; KOG1339; Eukaryota.
DR HOGENOM; CLU_013253_0_1_1; -.
DR OrthoDB; 2900143at2759; -.
DR Proteomes; UP000030151; Unassembled WGS sequence.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd06097; Aspergillopepsin_like; 1.
DR Gene3D; 2.40.70.10; Acid Proteases; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR001969; Aspartic_peptidase_AS.
DR InterPro; IPR034163; Aspergillopepsin-like_cat_dom.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR PANTHER; PTHR47966:SF2; ASPERGILLOPEPSIN-1-RELATED; 1.
DR PANTHER; PTHR47966; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR Pfam; PF00026; Asp; 1.
DR PRINTS; PR00792; PEPSIN.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 1.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 3: Inferred from homology;
KW Aspartyl protease {ECO:0000256|ARBA:ARBA00022750,
KW ECO:0000256|RuleBase:RU000454}; Hydrolase {ECO:0000256|RuleBase:RU000454};
KW Protease {ECO:0000256|RuleBase:RU000454}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..408
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001472984"
FT DOMAIN 93..404
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 111
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 296
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ SEQUENCE 408 AA; 43304 MW; CEC44A36F5C796D5 CRC64;
MQTFGRFLVS LVAASSLAAG APKESFPSKN GKFSITAKHN VNFERNGPLA LAKAYNKLDK
PVPQDIADAV TRIQQKRETG SVTNTPNKHD QAYLAPVQIG TPPQTLNLIF DTGSADFWVF
SNETASNEVK GQIPYDPKKS STSKRMSGAS WSIKYADNGT SVSGDVYTEI VTVGGLSVKS
QAFASAKNIS AYLSKSLAAS GVLGLAFSKA NRIKPQKQQT FFDNAKATLD APLFTVDLKH
QADGKYNFGY IDSSAHTGPI AYTSVDSTIG GWGFTSPGFA VGDGSFTNLS ISGIIDTGAT
LLLLPENVVM AYYSKVKGAS YDESERGYTF GCSTTLPSFS FWVGNSTITI PGSYMNYQAT
NDSGKTCFGG LQSSSGYGVS IFGDVALKAA FVVFDAGNNR LGWAAKNL
//