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Database: UniProt
Entry: W2QN94_PHYPN
LinkDB: W2QN94_PHYPN
Original site: W2QN94_PHYPN 
ID   W2QN94_PHYPN            Unreviewed;      1001 AA.
AC   W2QN94;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   RecName: Full=subtilisin {ECO:0000256|ARBA:ARBA00023619};
DE            EC=3.4.21.62 {ECO:0000256|ARBA:ARBA00023619};
GN   ORFNames=PPTG_07472 {ECO:0000313|EMBL:ETN14421.1};
OS   Phytophthora parasitica (strain INRA-310).
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC   Phytophthora.
OX   NCBI_TaxID=761204 {ECO:0000313|EMBL:ETN14421.1, ECO:0000313|Proteomes:UP000018817};
RN   [1] {ECO:0000313|Proteomes:UP000018817}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=INRA-310 {ECO:0000313|Proteomes:UP000018817};
RG   The Broad Institute Genome Sequencing Platform;
RA   Russ C., Tyler B., Panabieres F., Shan W., Tripathy S., Grunwald N.,
RA   Machado M., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA   Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Chapman S.B.,
RA   Gearin G., Goldberg J., Griggs A., Gujja S., Hansen M., Heiman D.,
RA   Howarth C., Larimer J., Lui A., MacDonald P.J.P., McCowen C.,
RA   Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., Roberts A.,
RA   Saif S., Shea T., Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RL   Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ETN14421.1, ECO:0000313|Proteomes:UP000018817}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=INRA-310 {ECO:0000313|EMBL:ETN14421.1,
RC   ECO:0000313|Proteomes:UP000018817};
RG   The Broad Institute Genomics Platform;
RA   Russ C., Tyler B., Panabieres F., Shan W., Tripathy S., Grunwald N.,
RA   Machado M., Johnson C.S., Arredondo F., Hong C., Coffey M., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L.,
RA   Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA   Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA   Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA   Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Phytophthora parasitica INRA-310.";
RL   Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
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.
CC       {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240}.
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DR   EMBL; KI669572; ETN14421.1; -; Genomic_DNA.
DR   RefSeq; XP_008899999.1; XM_008901751.1.
DR   AlphaFoldDB; W2QN94; -.
DR   STRING; 761204.W2QN94; -.
DR   EnsemblProtists; ETN14421; ETN14421; PPTG_07472.
DR   GeneID; 20177342; -.
DR   VEuPathDB; FungiDB:PPTG_07472; -.
DR   OMA; ICRAMPC; -.
DR   OrthoDB; 2441948at2759; -.
DR   Proteomes; UP000018817; Unassembled WGS sequence.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008240; F:tripeptidyl-peptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd04857; Peptidases_S8_Tripeptidyl_Aminopeptidase_II; 1.
DR   Gene3D; 1.25.40.710; -; 1.
DR   Gene3D; 2.60.40.3170; -; 1.
DR   Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 2.
DR   InterPro; IPR000209; Peptidase_S8/S53_dom.
DR   InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR   InterPro; IPR022398; Peptidase_S8_His-AS.
DR   InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR   InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR   InterPro; IPR034051; TPP_II_domain.
DR   InterPro; IPR046939; TPPII_C_sf.
DR   InterPro; IPR048384; TPPII_GBD.
DR   InterPro; IPR048383; TPPII_Ig-like-1.
DR   InterPro; IPR046940; TPPII_Ig-like_sf.
DR   PANTHER; PTHR43806; PEPTIDASE S8; 1.
DR   PANTHER; PTHR43806:SF14; TRIPEPTIDYL-PEPTIDASE 2; 1.
DR   Pfam; PF00082; Peptidase_S8; 1.
DR   Pfam; PF21316; TPPII_GBD; 1.
DR   Pfam; PF21223; TPPII_Ig-like-1; 1.
DR   PRINTS; PR00723; SUBTILISIN.
DR   SUPFAM; SSF52743; Subtilisin-like; 1.
DR   PROSITE; PS51892; SUBTILASE; 1.
DR   PROSITE; PS00137; SUBTILASE_HIS; 1.
DR   PROSITE; PS00138; SUBTILASE_SER; 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:UP000018817};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}.
FT   DOMAIN          29..497
FT                   /note="Peptidase S8/S53"
FT                   /evidence="ECO:0000259|Pfam:PF00082"
FT   DOMAIN          523..640
FT                   /note="Tripeptidyl-peptidase II first Ig-like"
FT                   /evidence="ECO:0000259|Pfam:PF21223"
FT   DOMAIN          655..751
FT                   /note="Tripeptidyl-peptidase II galactose-binding"
FT                   /evidence="ECO:0000259|Pfam:PF21316"
FT   ACT_SITE        38
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        260
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        446
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ   SEQUENCE   1001 AA;  110580 MW;  FFAADC6B17E849B0 CRC64;
     MKSFPTASLL PKEETLADRF LQQYPDYDGR NAVVAIFDTG VDPGAIGLQT TPDGRPKIID
     VVDATGAGDV DTSTVIEAKD GQLTLANDRV LTLNPDWKPS QDGKYHVGTV AGYHLFPGPL
     VTRLKTERKE KFDIEQRAAV NAVQEQLAKW SKENSATTND TAKLREKKDL QTRLKQLEEL
     AKSYEDPGPI YDAVVFYDGT CWRAALDTKE TGDFTGIPVL TNFKDERQYA TFSGESQLNY
     VLNIYDEGNT LSVVNDVGAH GTHVAGIVAA YHPDQSECNG VAPGAQIVAV KIGDGRLGSM
     ETSSALSRAI LAVMDANVDV VNMSYGEYAS QHNYGRIVEL SNELVDEHNV TFVVSAGNNG
     PALGTVGAPG GTTSSMLAVG AYVSPKMMEG EYIMRDSALS GIAYTWSSRG PTFDGDLGVN
     ICAPGAAIAP VPNWTLNKKQ LMNGTSMSSP NCAGNIALLI SAMKAQGVEY TPYSIRRALE
     NTAVKVPNVE VYAQGKGLIQ VLPAFKYLAG SNSFDGGRKF PLHYEIKTSS GDGKARGIFL
     RDSVDFAHDS TEVNVTVTPK FHKKAVQDDK VHFEQHVRLV PSARWIDVGR NLALMHGGRA
     FKVLVKTKHL TAGEHYGEIV AYDTKNEARG ALFTIPVTVI KPEDAKSVVT YQTKFQPGDI
     SRRFFTPAQD STWADIIFSR ANENDREVES NASGKLYMFD ALQFQPFVRQ SSSSFHKAFF
     LKPGEEVAFS MDLLGGLTTE FCLGQFWSAL GDSIVQIEIR FHGVKPDQEK IVPKDERDEE
     EIANEAVRDL LLERVTKLVG KSTFLPAWQR LVDQFPNYLP AMQAKLHHFD FEANRSTQLA
     AVIEAADAVL ALIKQDELAL FFGTRSVPGD QPATEKKLRK EKEKAILVDA LARKARALGD
     SSQWDDFLLA YADLQKWEDV EAATYLHVSL LHDRHFDAFG LALQRLRKVQ DMEQADKTKI
     ISDEKLAAEI NSTLDALQWQ HWTKYETQWE RRRAPTSYRI F
//
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