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Database: UniProt
Entry: D0N2H4_PHYIT
LinkDB: D0N2H4_PHYIT
Original site: D0N2H4_PHYIT 
ID   D0N2H4_PHYIT            Unreviewed;       512 AA.
AC   D0N2H4;
DT   15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT   15-DEC-2009, sequence version 1.
DT   27-MAR-2024, entry version 75.
DE   SubName: Full=Aspartyl protease family A01A, putative {ECO:0000313|EMBL:EEY68503.1};
GN   ORFNames=PITG_04975 {ECO:0000313|EMBL:EEY68503.1};
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:EEY68503.1, 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; DS028123; EEY68503.1; -; Genomic_DNA.
DR   RefSeq; XP_002905662.1; XM_002905616.1.
DR   AlphaFoldDB; D0N2H4; -.
DR   STRING; 403677.D0N2H4; -.
DR   GeneID; 9479122; -.
DR   KEGG; pif:PITG_04975; -.
DR   VEuPathDB; FungiDB:PITG_04975; -.
DR   eggNOG; KOG1339; Eukaryota.
DR   HOGENOM; CLU_033035_0_0_1; -.
DR   InParanoid; D0N2H4; -.
DR   OrthoDB; 52999at2759; -.
DR   Proteomes; UP000006643; Partially assembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd05471; pepsin_like; 1.
DR   Gene3D; 2.40.70.10; Acid Proteases; 2.
DR   InterPro; IPR001461; Aspartic_peptidase_A1.
DR   InterPro; IPR001969; Aspartic_peptidase_AS.
DR   InterPro; IPR034164; Pepsin-like_dom.
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; 1.
DR   PRINTS; PR00792; PEPSIN.
DR   SUPFAM; SSF50630; Acid proteases; 1.
DR   PROSITE; PS00141; ASP_PROTEASE; 2.
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   Membrane {ECO:0000256|SAM:Phobius};
KW   Protease {ECO:0000256|RuleBase:RU000454, ECO:0000313|EMBL:EEY68503.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006643};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        434..456
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          3..390
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   REGION          473..512
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        21
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   ACT_SITE        236
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ   SEQUENCE   512 AA;  55947 MW;  F613C4BA1D5E6F84 CRC64;
     MQFFGSIGVG SPPQRFQVIF DTGSSDIWLP ESSCADCAGS RRYHAAVSRS HEPLNEPFRL
     EYGSGNASGR VVREQVSLFG GDEQSLTLSR VHMGSTTKTT KSLQRFQADG IVGLGLEALA
     VITKPSLLKS DPRLGLFSIY INPLPGALPP AQLIFGGVDD SLPIAHIPHA NEAQVSWHHF
     PLVRYPSSRR AHGFWAIRLH RLTVGNFDSR SKSSPKKLAG SGDGIVAVSA AVAIVDSGTS
     LLLLPRRAFD TTITEIQQHL RVQHSKELRV NPHAVSGYAC VDCTAEMFPA LRFSFVIEET
     PAGSQSKTQT LVLKGTDYAR CDDLMCAPQL DVHALFTSKS KSKVPTPAAS AMTTNIPQGT
     EHEDVVVLGV TFMRAYYVQF DSQRKTVGFA CVDSATSSAV CSGGWAPKLQ FHSAHFLDAE
     ASAWRAGWVF WSRVYLGIGV LLLLVAFALL WLILVVPSSE VKKVFNWFYG PSDKSRRRQQ
     QTDNRDDETA EPDSEPESPP APSRRKSVSF DV
//
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