ID A0A014MXW9_9HYPO Unreviewed; 387 AA.
AC A0A014MXW9;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Peptidase S1 domain protein {ECO:0000313|EMBL:EXU96374.1};
GN ORFNames=X797_010491 {ECO:0000313|EMBL:EXU96374.1};
OS Metarhizium robertsii.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium.
OX NCBI_TaxID=568076 {ECO:0000313|EMBL:EXU96374.1, ECO:0000313|Proteomes:UP000030151};
RN [1] {ECO:0000313|EMBL:EXU96374.1, ECO:0000313|Proteomes:UP000030151}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ARSEF 2575 {ECO:0000313|EMBL:EXU96374.1,
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 S1 family.
CC {ECO:0000256|ARBA:ARBA00007664}.
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:EXU96374.1}.
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DR EMBL; JELW01000050; EXU96374.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A014MXW9; -.
DR eggNOG; KOG3627; Eukaryota.
DR HOGENOM; CLU_006842_7_5_1; -.
DR OrthoDB; 2486832at2759; -.
DR Proteomes; UP000030151; 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; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 1.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001314; Peptidase_S1A.
DR InterPro; IPR001254; Trypsin_dom.
DR InterPro; IPR018114; TRYPSIN_HIS.
DR InterPro; IPR033116; TRYPSIN_SER.
DR PANTHER; PTHR24276:SF91; AT26814P-RELATED; 1.
DR PANTHER; PTHR24276; POLYSERASE-RELATED; 1.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Hydrolase {ECO:0000256|RuleBase:RU363034};
KW Protease {ECO:0000256|RuleBase:RU363034};
KW Serine protease {ECO:0000256|RuleBase:RU363034};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..387
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001472397"
FT DOMAIN 27..294
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
SQ SEQUENCE 387 AA; 41402 MW; 0D5208C5399C9BDC CRC64;
MVRSTAITLA ATFFATLAAA ATIDKRIVGG EDVPDGEIKF IVSLCDENGT HVCGGSLLDS
TTVLTAAHCL ISDEIQIVSV TAGTVSTKTG GVNATVASVE KHPNYKPGAP SDCPVDLPWD
ECRRRADLPG GREENDIAIV KLSTPIEKSD TIDYAGLPPA GGDAVVNSTG IAAGWGSQTP
LESTVPKDGE MKPIILAEKL SKVVLHIHAR EDCAAKYKNQ RVGDRDTIIC AGGQGKNPCK
GDSGGPLFHP ETRELLGVVS WSIKDRYEDD LCNKTPTVFT RVGSYIDWIN DNLGSRASSR
LAAVRHCTRP ENDVIPCFNA LLFCQAREVS PDAPELEFLE CIDRIQICAG QDTRADQCVA
NAKVCKEQEK LNVGDLVNLA RCAKQDL
//
