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Database: UniProt
Entry: G4Z299_PHYSP
LinkDB: G4Z299_PHYSP
Original site: G4Z299_PHYSP 
ID   G4Z299_PHYSP            Unreviewed;       477 AA.
AC   G4Z299;
DT   14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2011, sequence version 1.
DT   27-MAR-2024, entry version 48.
DE   RecName: Full=subtilisin {ECO:0000256|ARBA:ARBA00023619};
DE            EC=3.4.21.62 {ECO:0000256|ARBA:ARBA00023619};
GN   ORFNames=PHYSODRAFT_354184 {ECO:0000313|EMBL:EGZ19243.1};
OS   Phytophthora sojae (strain P6497) (Soybean stem and root rot agent)
OS   (Phytophthora megasperma f. sp. glycines).
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC   Phytophthora.
OX   NCBI_TaxID=1094619 {ECO:0000313|EMBL:EGZ19243.1, ECO:0000313|Proteomes:UP000002640};
RN   [1] {ECO:0000313|EMBL:EGZ19243.1, ECO:0000313|Proteomes:UP000002640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=P6497 {ECO:0000313|EMBL:EGZ19243.1,
RC   ECO:0000313|Proteomes:UP000002640};
RX   PubMed=16946064; DOI=10.1126/science.1128796;
RA   Tyler B.M., Tripathy S., Zhang X., Dehal P., Jiang R.H., Aerts A.,
RA   Arredondo F.D., Baxter L., Bensasson D., Beynon J.L., Chapman J.,
RA   Damasceno C.M., Dorrance A.E., Dou D., Dickerman A.W., Dubchak I.L.,
RA   Garbelotto M., Gijzen M., Gordon S.G., Govers F., Grunwald N.J., Huang W.,
RA   Ivors K.L., Jones R.W., Kamoun S., Krampis K., Lamour K.H., Lee M.K.,
RA   McDonald W.H., Medina M., Meijer H.J., Nordberg E.K., Maclean D.J.,
RA   Ospina-Giraldo M.D., Morris P.F., Phuntumart V., Putnam N.H., Rash S.,
RA   Rose J.K., Sakihama Y., Salamov A.A., Savidor A., Scheuring C.F.,
RA   Smith B.M., Sobral B.W., Terry A., Torto-Alalibo T.A., Win J., Xu Z.,
RA   Zhang H., Grigoriev I.V., Rokhsar D.S., Boore J.L.;
RT   "Phytophthora genome sequences uncover evolutionary origins and mechanisms
RT   of pathogenesis.";
RL   Science 313:1261-1266(2006).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of proteins with broad specificity for peptide
CC         bonds, and a preference for a large uncharged residue in P1.
CC         Hydrolyzes peptide amides.; EC=3.4.21.62;
CC         Evidence={ECO:0000256|ARBA:ARBA00023529};
CC   -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000256|PROSITE-
CC       ProRule:PRU01240}.
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DR   EMBL; JH159153; EGZ19243.1; -; Genomic_DNA.
DR   RefSeq; XP_009521960.1; XM_009523665.1.
DR   AlphaFoldDB; G4Z299; -.
DR   STRING; 1094619.G4Z299; -.
DR   EnsemblProtists; EGZ19243; EGZ19243; PHYSODRAFT_354184.
DR   GeneID; 20649561; -.
DR   KEGG; psoj:PHYSODRAFT_354184; -.
DR   InParanoid; G4Z299; -.
DR   OMA; INAPDVW; -.
DR   Proteomes; UP000002640; Unassembled WGS sequence.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR   InterPro; IPR000209; Peptidase_S8/S53_dom.
DR   InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR   InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR   PANTHER; PTHR43399; SUBTILISIN-RELATED; 1.
DR   PANTHER; PTHR43399:SF4; TK-SUBTILISIN; 1.
DR   Pfam; PF00082; Peptidase_S8; 1.
DR   PRINTS; PR00723; SUBTILISIN.
DR   SUPFAM; SSF52743; Subtilisin-like; 1.
DR   PROSITE; PS51892; SUBTILASE; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW   ProRule:PRU01240};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}; Reference proteome {ECO:0000313|Proteomes:UP000002640};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..477
FT                   /note="subtilisin"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003471748"
FT   DOMAIN          191..468
FT                   /note="Peptidase S8/S53"
FT                   /evidence="ECO:0000259|Pfam:PF00082"
FT   ACT_SITE        200
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        236
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        406
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
SQ   SEQUENCE   477 AA;  50159 MW;  A586A4F9ADF14F51 CRC64;
     MVRALSWLAA AVIMAIGLSA EAPMAATTTT TAVRNGMDLG QSTKSRTQQR MHKRANVMVT
     MKSTGNDILA KIKGQKFTSR GHRVAALKDG LEGFAKESQR GIHELLGKVS DSFARSKSFW
     ITNQIYVQQA TPDLVKQLEK VPGVLSVEYE MVFPASMPVL STQSMSSSTS AAQWGVSKIN
     APDVWATGNT GQGVVIGSID TGVRGTHEAL ASNYRQTYGW YDPETKSSAP YDSTGHGTHV
     MGIMAGQFGF GVAPGATWIA CKGCRAQGCY GSDLLACFQF MLCPTTPSGG SKDCSKAPNI
     VNNSWGGGQG LTMFDGVINA WRAAGIIPVV AAGNTGPNCG TIASPGDSAS VITVGATDIN
     DVLASFSSKG PTVRGLRKPD VAAPGALILS SCWTDDSSYC FKSGSSMASP HVAGAIALYL
     SANPGTSYEK IKDLLQSRSV TTTLTTPTGF TCGNTQDRNF PNNQYGYGRI DIFNTLS
//
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