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Database: UniProt
Entry: D0NBJ4_PHYIT
LinkDB: D0NBJ4_PHYIT
Original site: D0NBJ4_PHYIT 
ID   D0NBJ4_PHYIT            Unreviewed;       815 AA.
AC   D0NBJ4;
DT   15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT   15-DEC-2009, sequence version 1.
DT   27-MAR-2024, entry version 77.
DE   SubName: Full=Aspartyl protease family A01A, putative {ECO:0000313|EMBL:EEY55423.1};
GN   ORFNames=PITG_09387 {ECO:0000313|EMBL:EEY55423.1};
OS   Phytophthora infestans (strain T30-4) (Potato late blight agent).
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC   Phytophthora.
OX   NCBI_TaxID=403677 {ECO:0000313|EMBL:EEY55423.1, ECO:0000313|Proteomes:UP000006643};
RN   [1] {ECO:0000313|Proteomes:UP000006643}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T30-4 {ECO:0000313|Proteomes:UP000006643};
RX   PubMed=19741609; DOI=10.1038/nature08358;
RG   The Broad Institute Genome Sequencing Platform;
RA   Haas B.J., Kamoun S., Zody M.C., Jiang R.H., Handsaker R.E., Cano L.M.,
RA   Grabherr M., Kodira C.D., Raffaele S., Torto-Alalibo T., Bozkurt T.O.,
RA   Ah-Fong A.M., Alvarado L., Anderson V.L., Armstrong M.R., Avrova A.,
RA   Baxter L., Beynon J., Boevink P.C., Bollmann S.R., Bos J.I., Bulone V.,
RA   Cai G., Cakir C., Carrington J.C., Chawner M., Conti L., Costanzo S.,
RA   Ewan R., Fahlgren N., Fischbach M.A., Fugelstad J., Gilroy E.M., Gnerre S.,
RA   Green P.J., Grenville-Briggs L.J., Griffith J., Grunwald N.J., Horn K.,
RA   Horner N.R., Hu C.H., Huitema E., Jeong D.H., Jones A.M., Jones J.D.,
RA   Jones R.W., Karlsson E.K., Kunjeti S.G., Lamour K., Liu Z., Ma L.,
RA   Maclean D., Chibucos M.C., McDonald H., McWalters J., Meijer H.J.,
RA   Morgan W., Morris P.F., Munro C.A., O'Neill K., Ospina-Giraldo M.,
RA   Pinzon A., Pritchard L., Ramsahoye B., Ren Q., Restrepo S., Roy S.,
RA   Sadanandom A., Savidor A., Schornack S., Schwartz D.C., Schumann U.D.,
RA   Schwessinger B., Seyer L., Sharpe T., Silvar C., Song J., Studholme D.J.,
RA   Sykes S., Thines M., van de Vondervoort P.J., Phuntumart V., Wawra S.,
RA   Weide R., Win J., Young C., Zhou S., Fry W., Meyers B.C., van West P.,
RA   Ristaino J., Govers F., Birch P.R., Whisson S.C., Judelson H.S.,
RA   Nusbaum C.;
RT   "Genome sequence and analysis of the Irish potato famine pathogen
RT   Phytophthora infestans.";
RL   Nature 461:393-398(2009).
CC   -!- SIMILARITY: Belongs to the peptidase A1 family.
CC       {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
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DR   EMBL; DS028131; EEY55423.1; -; Genomic_DNA.
DR   RefSeq; XP_002903647.1; XM_002903601.1.
DR   AlphaFoldDB; D0NBJ4; -.
DR   SMR; D0NBJ4; -.
DR   STRING; 403677.D0NBJ4; -.
DR   GeneID; 9474942; -.
DR   KEGG; pif:PITG_09387; -.
DR   VEuPathDB; FungiDB:PITG_09387; -.
DR   eggNOG; KOG1339; Eukaryota.
DR   HOGENOM; CLU_013253_3_4_1; -.
DR   InParanoid; D0NBJ4; -.
DR   OrthoDB; 615305at2759; -.
DR   Proteomes; UP000006643; Partially assembled WGS sequence.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 2.40.70.10; Acid Proteases; 3.
DR   Gene3D; 3.30.70.141; Nucleoside diphosphate kinase-like domain; 1.
DR   InterPro; IPR001461; Aspartic_peptidase_A1.
DR   InterPro; IPR001969; Aspartic_peptidase_AS.
DR   InterPro; IPR036850; NDK-like_dom_sf.
DR   InterPro; IPR033121; PEPTIDASE_A1.
DR   InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR   PANTHER; PTHR47966; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR   PANTHER; PTHR47966:SF51; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR   Pfam; PF00026; Asp; 2.
DR   PRINTS; PR00792; PEPSIN.
DR   SUPFAM; SSF50630; Acid proteases; 1.
DR   SUPFAM; SSF54919; Nucleoside diphosphate kinase, NDK; 1.
DR   PROSITE; PS00141; ASP_PROTEASE; 1.
DR   PROSITE; PS51767; PEPTIDASE_A1; 1.
PE   3: Inferred from homology;
KW   Aspartyl protease {ECO:0000256|RuleBase:RU000454};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000454};
KW   Protease {ECO:0000256|RuleBase:RU000454, ECO:0000313|EMBL:EEY55423.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006643};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..815
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003012482"
FT   DOMAIN          83..370
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
SQ   SEQUENCE   815 AA;  90037 MW;  86DEF3051BF45E38 CRC64;
     MMLRCSVLCS LLLALSSAAV MRVPMIKRSD DEFVSSLLHD VHAMQRPVVW SPDASPINNQ
     NEGQSTVEGS ASVVIRDFQN AQYYGEISIG TPPQPFAVIF DTGSSNLWVP DKKFGSHNVY
     DHDKSSTYKP NGTAFDIMYG SGPVSGFLSQ DKLELGGLTV PDQYFAEVNV TKGLGPAYYL
     GKFDGLFGLA FDTISVDHLK TPFHRMVQEG LLDEPVFAFY LGDQKDGELT FGGVDKAHYK
     GEIEYVDVTS ATYWSVKLGH CGLWHLAHRW TEDQVAKLAA LVGAHKFIMG EYLISCTAAA
     PDISFVLNGK TYTLTKEEYT LKSGPICLFA FMGIDIPAPA GPLWILGDVF MRKHYTVFDW
     GTDSRKPRAA QLSVLALQAD ALEHDEAVRQ ELKRSGFVVR QQALVHLSID AARQFVLEVC
     NPHSAMYRPP PLEENEDEKL QATSEQHDAV SRASNVKANL EMTEEDNEIL EHAIHALASG
     PALILGVEKP NAVAELLQLV GPGDPSAWTE GASSCLRARF AKDAPRKLGL RCSTHEKTAT
     HELAFLLAHS GNKTHAYGQG HAAVTPPNGR SGGRTSAMGL DQLLNFLFPD HLQHPTSAGR
     LFVFGLYGPL DKCSRLRSGE KGLHVVTDRE LTTMSARMER EDILAVYGIC SLSQEEEEEV
     VRQVDNLLKR FPQYTPRDIE TLFAPLPRDS DGHMSFHDMQ QAVLKERLRR VVCMKERLHP
     ALAEPVRNRF SRTLTRLTAT KTAGLINGAP SSFFLRDIGA TNVENVSLVS RLLSTRSSQI
     CQMEDGNSPA LTQNVRLARP DKAQGFTERE PWNPT
//
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