ID F1LKT9_METAN Unreviewed; 390 AA.
AC F1LKT9;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE SubName: Full=Subtilisin-like protease Pr1A {ECO:0000313|EMBL:ACV71835.1};
GN Name=pr1A {ECO:0000313|EMBL:ACV71835.1};
OS Metarhizium anisopliae (Entomophthora anisopliae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium.
OX NCBI_TaxID=5530 {ECO:0000313|EMBL:ACV71835.1};
RN [1] {ECO:0000313|EMBL:ACV71835.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CG341 {ECO:0000313|EMBL:ACV71835.1};
RA Bandinelli J.B., Silva F.B., Pereira T.C.B., Fagundes N.J.R.,
RA Dallonder L.P., Yanaka F.Y., Bogo M.R.;
RT "Genetic diversity and evolutive relationships of the entomopathogen
RT Metarhizium anisopliae strains inferred from the subtilisin-like Pr1A.";
RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S8 family.
CC {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240}.
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DR EMBL; FJ659162; ACV71835.1; -; Genomic_DNA.
DR AlphaFoldDB; F1LKT9; -.
DR MEROPS; S08.056; -.
DR VEuPathDB; FungiDB:MAN_03501; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProt.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd04077; Peptidases_S8_PCSK9_ProteinaseK_like; 1.
DR Gene3D; 3.30.70.80; Peptidase S8 propeptide/proteinase inhibitor I9; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR InterPro; IPR034193; PCSK9_ProteinaseK-like.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR023827; Peptidase_S8_Asp-AS.
DR InterPro; IPR022398; Peptidase_S8_His-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR InterPro; IPR010259; S8pro/Inhibitor_I9.
DR InterPro; IPR037045; S8pro/Inhibitor_I9_sf.
DR PANTHER; PTHR43806; PEPTIDASE S8; 1.
DR PANTHER; PTHR43806:SF69; PROTEINASE T; 1.
DR Pfam; PF05922; Inhibitor_I9; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF54897; Protease propeptides/inhibitors; 1.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00136; SUBTILASE_ASP; 1.
DR PROSITE; PS00137; SUBTILASE_HIS; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU01240};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01240};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..15
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 16..390
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012722998"
FT DOMAIN 42..106
FT /note="Inhibitor I9"
FT /evidence="ECO:0000259|Pfam:PF05922"
FT DOMAIN 139..375
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT REGION 274..298
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 148
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 179
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 334
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 390 AA; 40420 MW; 8E5EE6FEA69F46E5 CRC64;
MHLSALLTLL PAVLAAPATI GRRAEPAPLF TPQAESIIAD KYIVKFKDDI ARIATDDTVS
ALTSKADFVY EHAFHGFAGS LTKEELKMLR EHPGVDFIEK DAVMRISGLT EQSGAPWGLG
RISHRNRGST TYRYDDSAGE GTCVYIIDTG IEASHPEFEG RATFLRSFIS GQETDGHGHG
THCAGTIGSK SYGVAKKAKL YGVKVLDNQG SGSYSGIISG MDYVASDSKT RGCPKGAIAS
MSLGGGYSAS VNQGAAALVN SGVFLAVAAG NDNRDAQNTS PASEPSACTV GATDSSDRRS
SFSNFGRVVD IFAPGTGVLS TWIGGSTNTI SGTSMATPHI GGLAAYLSAL QGKTTPAALC
KKIQDTATKN ALTGVPSGTV NYLAYNGNGA
//