ID H3GHE1_PHYRM Unreviewed; 577 AA.
AC H3GHE1;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=subtilisin {ECO:0000256|ARBA:ARBA00023619};
DE EC=3.4.21.62 {ECO:0000256|ARBA:ARBA00023619};
OS Phytophthora ramorum (Sudden oak death agent).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=164328 {ECO:0000313|EnsemblProtists:Phyra75336, ECO:0000313|Proteomes:UP000005238};
RN [1] {ECO:0000313|Proteomes:UP000005238}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pr102 {ECO:0000313|Proteomes:UP000005238};
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).
RN [2] {ECO:0000313|EnsemblProtists:Phyra75336}
RP IDENTIFICATION.
RC STRAIN=Pr102 {ECO:0000313|EnsemblProtists:Phyra75336};
RG EnsemblProtists;
RL Submitted (JUN-2015) to UniProtKB.
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 -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913};
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01032}.
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DR EMBL; DS566009; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; H3GHE1; -.
DR STRING; 164328.H3GHE1; -.
DR EnsemblProtists; Phyra75336; Phyra75336; Phyra75336.
DR VEuPathDB; FungiDB:PSURA_81495; -.
DR eggNOG; ENOG502QR6D; Eukaryota.
DR HOGENOM; CLU_013783_5_1_1; -.
DR InParanoid; H3GHE1; -.
DR OMA; YARSVCN; -.
DR Proteomes; UP000005238; Unassembled WGS sequence.
DR GO; GO:0004175; F:endopeptidase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0008240; F:tripeptidyl-peptidase activity; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR CDD; cd04056; Peptidases_S53; 1.
DR CDD; cd11377; Pro-peptidase_S53; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 2.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR015366; S53_propep.
DR InterPro; IPR030400; Sedolisin_dom.
DR PANTHER; PTHR14218:SF42; PEPTIDASE S53 DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR14218; PROTEASE S8 TRIPEPTIDYL PEPTIDASE I CLN2; 1.
DR Pfam; PF09286; Pro-kuma_activ; 1.
DR SMART; SM00944; Pro-kuma_activ; 1.
DR SUPFAM; SSF54897; Protease propeptides/inhibitors; 1.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51695; SEDOLISIN; 1.
PE 4: Predicted;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000005238};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..577
FT /note="subtilisin"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003585491"
FT DOMAIN 209..577
FT /note="Peptidase S53"
FT /evidence="ECO:0000259|PROSITE:PS51695"
SQ SEQUENCE 577 AA; 61976 MW; 786B38E8F5576B7B CRC64;
MAGSWLLAPA LALCSLTSAS FATVLEPPAR FGGFSSDSYV RQSRADPEKV VPLVIGLLPV
DFNAMEREFY SVSDPTHASY GQFLAQHQAD QLSRPADGAL DAVRSWVGDF AHENSAGTFS
ATSNLFKVPM KVKHMERLLG AEIHHYETNE MRGVPSTRRR RLVRAATDVS VPEHLQNIVS
FLSVNAHPLG LRALGATSAQ TPEMNGQGGG TLAAIRQTYG IPDDLVVTNA GSTQCVPSFY
DEVWNPDDLK TFYAQYLPGE SPPQIIEKGG RANRPEMAST EASLDVQYIT GVGRNASTFV
WTMNGSNPYS SEDEPFVEFA EDVLALENPP LVISISYSDD EEHIFDVSAG YARTLDTLLI
KMGLRGITVL IAGGDDGVTG LRTEFEKVPV ENMCKQSGPQ WPSSSPYITT VGATMLLTKA
QQAAKPFFRT NEEVICSVEN GGIITSGGGF SNIYPIPEYQ RKAVERYLAT RNIPTTPGFF
NTSGRAYPDV AALGAGFLVY MGGRLSSVSG NNGAPRGGNN PCEDSFSAAA GWDAVSGVGT
PNFPVISEFI ANLEDHFNIS TLGGGSNSAT YNKTEVE
//
