ID Q6TR88_9HYPO Unreviewed; 323 AA.
AC Q6TR88;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 89.
DE SubName: Full=Subtilisin-like serine protease PR1A {ECO:0000313|EMBL:AAR26032.1};
DE Flags: Fragment;
GN Name=pr1A {ECO:0000313|EMBL:AAR26032.1};
OS Metarhizium acridum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium.
OX NCBI_TaxID=92637 {ECO:0000313|EMBL:AAR26032.1};
RN [1] {ECO:0000313|EMBL:AAR26032.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=IMI 330189 {ECO:0000313|EMBL:AAR26032.1};
RX PubMed=15785852; DOI=10.1007/s00239-004-0147-z;
RA Wang C., Typas M.A., Butt T.M.;
RT "Phylogenetic and exon-intron structure analysis of fungal subtilisins:
RT support for a mixed model of intron evolution.";
RL J. Mol. Evol. 60:238-246(2005).
CC -!- SIMILARITY: Belongs to the peptidase S8 family.
CC {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240,
CC ECO:0000256|RuleBase:RU003355}.
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DR EMBL; AY389130; AAR26032.1; -; Genomic_DNA.
DR AlphaFoldDB; Q6TR88; -.
DR MEROPS; S08.056; -.
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; IPR023828; Peptidase_S8_Ser-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.
DR PROSITE; PS00138; SUBTILASE_SER; 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}; Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 18..82
FT /note="Inhibitor I9"
FT /evidence="ECO:0000259|Pfam:PF05922"
FT DOMAIN 115..323
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT REGION 250..270
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 124
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 155
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 310
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AAR26032.1"
FT NON_TER 323
FT /evidence="ECO:0000313|EMBL:AAR26032.1"
SQ SEQUENCE 323 AA; 33627 MW; 1541343A3D4BCDB0 CRC64;
EPAPLFTPQA ESIIADKYIV KFKDDIARIA TDDTVSALTS KADFVYEHAF HGFAGSLTKE
ELKMLREHPG VDFIEKDAVM RISGITEQSG APWGLGRISH RQKGSTTYRY DDSAGEGTCV
YIIDTGIEAS HPELEGRATF LKSFISGQTS DGHGHGTHCA GTIGSKSYGV AKKVKLYGVK
VLDNQGSGSY SGIISGMDYV AQDSKTRGCP KGAIASMSLG GGYSASVNQG AAALVNSGVF
LAVAAGNDNR DAQNTSPASE PSACTVGATD SNDNRSSFSN YGKVVDIFAP GTGVLSTWIG
GSTNTISGTS MATPHIAGLA AYL
//
