ID A5JS74_9HYPO Unreviewed; 390 AA.
AC A5JS74;
DT 26-JUN-2007, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2007, sequence version 1.
DT 27-MAR-2024, entry version 78.
DE SubName: Full=Serine protease {ECO:0000313|EMBL:ABQ51089.1};
OS Hirsutella minnesotensis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Hirsutella.
OX NCBI_TaxID=332947 {ECO:0000313|EMBL:ABQ51089.1};
RN [1] {ECO:0000313|EMBL:ABQ51089.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CBS115627 {ECO:0000313|EMBL:ABQ51089.1};
RA Gao L., Wei H.L., Liu X.Z.;
RT "Gene cloning of serine protease from Hirsutella minnesotania.";
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S8 family.
CC {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240,
CC ECO:0000256|RuleBase:RU003355}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; EF560594; ABQ51089.1; -; Genomic_DNA.
DR AlphaFoldDB; A5JS74; -.
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};
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_5013243275"
FT DOMAIN 40..103
FT /note="Inhibitor I9"
FT /evidence="ECO:0000259|Pfam:PF05922"
FT DOMAIN 145..356
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT ACT_SITE 147
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 178
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 333
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 390 AA; 40499 MW; 7DF1B2A7F6239B2F CRC64;
MKLSILLAIL PAVLAAPPAE RDELAPLKAP QNAKQLIEGK YIVKFKDGVS LQAVDSTLSS
FTSKAEHVYT NILRGFAGKL TADEVKTLRA RPDVDFIEQD AIFTINAIVQ QPGATWGLAR
ISSRQRGGST YSYDDSAGAG TCAYVIDTGV EASHPEFEGR ATMVRSFIPG QTKDGNGHGT
HCAGTIGSRT YGVAKKTKIY GVKVLSDQGS GSTSAIIAGM DFAVQDSRKR SCPKGVVANM
SLGGSYSAAL NNAAAKMITQ GVFLAVAAGN SNTDAASFSP ASEPTVCTVG ASDSSDRRSS
FSNYGSVLDT FAPGTSVTSL WIGGRTNTIS GTSMASPHIA GLAAYLYGLE GRSEPQALCS
RIQSLATRDV LTGIPSGTAN LLAYNGAGEE
//
