ID   Q5I8R5_9FUNG            Unreviewed;       257 AA.
AC   Q5I8R5;
DT   15-FEB-2005, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2005, sequence version 1.
DT   24-JAN-2024, entry version 64.
DE   SubName: Full=Trypsin-like serine protease {ECO:0000313|EMBL:AAW31593.1};
GN   Name=SP1 {ECO:0000313|EMBL:AAW31593.1};
OS   Zoophthora radicans.
OC   Eukaryota; Fungi; Fungi incertae sedis; Zoopagomycota;
OC   Entomophthoromycotina; Entomophthoromycetes; Entomophthorales;
OC   Entomophthoraceae; Zoophthora.
OX   NCBI_TaxID=42210 {ECO:0000313|EMBL:AAW31593.1};
RN   [1] {ECO:0000313|EMBL:AAW31593.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=16788723; DOI=10.1139/W06-004;
RA   Xu J., Baldwin D., Kindrachuk C., Hegedus D.D.;
RT   "Serine proteases and metalloproteases associated with pathogenesis but not
RT   host specificity in the Entomophthoralean fungus Zoophthora radicans.";
RL   Can. J. Microbiol. 52:550-559(2006).
CC   -!- SIMILARITY: Belongs to the peptidase S1 family.
CC       {ECO:0000256|ARBA:ARBA00007664}.
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DR   EMBL; AY845416; AAW31593.1; -; mRNA.
DR   AlphaFoldDB; Q5I8R5; -.
DR   MEROPS; S01.B40; -.
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   2: Evidence at transcript level;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Hydrolase {ECO:0000256|RuleBase:RU363034};
KW   Protease {ECO:0000256|RuleBase:RU363034, ECO:0000313|EMBL:AAW31593.1};
KW   Serine protease {ECO:0000256|RuleBase:RU363034};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..15
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           16..257
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5013107826"
FT   DOMAIN          27..257
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000259|PROSITE:PS50240"
SQ   SEQUENCE   257 AA;  27552 MW;  5F2394920371F00F CRC64;
     MQLLSILSVL GLVTANYKLE KLPSGRIVGG YEVTPKFQYP WIASLEYYGS HTCGGTLYNE
     KTIISAAHCN IGSTSAWSAS VHRHDLNEKA EKESGSNHKI IERISHPQYD LNDDSSNDVS
     VWKIAAPGNK TSGIVLDSGK VSSEDGTLLK VIGWGTTTSG GDVSKVLLEV KVPVFNIDKC
     KKAYSTLDTA SQFCAGYPEG GKDSCQGDSG GPIFIEEKGV ATLVGVVSWG RGCALKGYPG
     VYTRVSKVLD FIEKHAN
//