(data stored in ACNUC9543 zone)

SWISSPROT: Q8IAS0_PLAF7

ID   Q8IAS0_PLAF7            Unreviewed;       573 AA.
AC   Q8IAS0;
DT   01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2003, sequence version 1.
DT   11-DEC-2019, entry version 112.
DE   SubName: Full=Plasmepsin X {ECO:0000313|EMBL:CAD51290.1};
DE            EC=3.4.23.1 {ECO:0000313|EMBL:CAD51290.1};
GN   ORFNames=PF3D7_0808200 {ECO:0000313|EMBL:CAD51290.1};
OS   Plasmodium falciparum (isolate 3D7).
OC   Eukaryota; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC   Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX   NCBI_TaxID=36329 {ECO:0000313|EMBL:CAD51290.1, ECO:0000313|Proteomes:UP000001450};
RN   [1] {ECO:0000313|Proteomes:UP000001450}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Isolate 3D7 {ECO:0000313|Proteomes:UP000001450};
RX   PubMed=12368864; DOI=10.1038/nature01097;
RA   Gardner M.J., Hall N., Fung E., White O., Berriman M., Hyman R.W.,
RA   Carlton J.M., Pain A., Nelson K.E., Bowman S., Paulsen I.T., James K.D.,
RA   Eisen J.A., Rutherford K.M., Salzberg S.L., Craig A., Kyes S., Chan M.-S.,
RA   Nene V., Shallom S.J., Suh B., Peterson J., Angiuoli S., Pertea M.,
RA   Allen J., Selengut J., Haft D., Mather M.W., Vaidya A.B., Martin D.M.A.,
RA   Fairlamb A.H., Fraunholz M.J., Roos D.S., Ralph S.A., McFadden G.I.,
RA   Cummings L.M., Subramanian G.M., Mungall C., Venter J.C., Carucci D.J.,
RA   Hoffman S.L., Newbold C., Davis R.W., Fraser C.M., Barrell B.G.;
RT   "Genome sequence of the human malaria parasite Plasmodium falciparum.";
RL   Nature 419:498-511(2002).
RN   [2] {ECO:0000313|Proteomes:UP000001450}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Isolate 3D7 {ECO:0000313|Proteomes:UP000001450};
RX   PubMed=12368867; DOI=10.1038/nature01095;
RA   Hall N., Pain A., Berriman M., Churcher C.M., Harris B., Harris D.,
RA   Mungall K.L., Bowman S., Atkin R., Baker S., Barron A., Brooks K.,
RA   Buckee C.O., Burrows C., Cherevach I., Chillingworth C., Chillingworth T.,
RA   Christodoulou Z., Clark L., Clark R., Corton C., Cronin A., Davies R.M.,
RA   Davis P., Dear P., Dearden F., Doggett J., Feltwell T., Goble A.,
RA   Goodhead I., Gwilliam R., Hamlin N., Hance Z., Harper D., Hauser H.,
RA   Hornsby T., Holroyd S., Horrocks P., Humphray S., Jagels K., James K.D.,
RA   Johnson D., Kerhornou A., Knights A., Konfortov B., Kyes S., Larke N.,
RA   Lawson D., Lennard N., Line A., Maddison M., Mclean J., Mooney P.,
RA   Moule S., Murphy L., Oliver K., Ormond D., Price C., Quail M.A.,
RA   Rabbinowitsch E., Rajandream M.A., Rutter S., Rutherford K.M., Sanders M.,
RA   Simmonds M., Seeger K., Sharp S., Smith R., Squares R., Squares S.,
RA   Stevens K., Taylor K., Tivey A., Unwin L., Whitehead S., Woodward J.R.,
RA   Sulston J.E., Craig A., Newbold C., Barrell B.G.;
RT   "Sequence of Plasmodium falciparum chromosomes 1, 3-9 and 13.";
RL   Nature 419:527-531(2002).
CC   -!- SIMILARITY: Belongs to the peptidase A1 family.
CC       {ECO:0000256|RuleBase:RU000454, ECO:0000256|SAAS:SAAS01079896}.
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DR   EMBL; AL844507; CAD51290.1; -; Genomic_DNA.
DR   RefSeq; XP_001349441.1; XM_001349405.1.
DR   SMR; Q8IAS0; -.
DR   IntAct; Q8IAS0; 2.
DR   MEROPS; A01.A93; -.
DR   PRIDE; Q8IAS0; -.
DR   EnsemblProtists; CAD51290; CAD51290; PF3D7_0808200.
DR   GeneDB; PF3D7_0808200.1:pep; -.
DR   GeneID; 2655308; -.
DR   KEGG; pfa:PF3D7_0808200; -.
DR   EuPathDB; PlasmoDB:PF3D7_0808200; -.
DR   HOGENOM; HOG000283924; -.
DR   InParanoid; Q8IAS0; -.
DR   KO; K06002; -.
DR   OMA; PQEIHPI; -.
DR   PhylomeDB; Q8IAS0; -.
DR   BioCyc; PLASMO:PF08_0108-MONOMER; -.
DR   Proteomes; UP000001450; Chromosome 8.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; ISS:GeneDB.
DR   GO; GO:0030163; P:protein catabolic process; IBA:GO_Central.
DR   GO; GO:0006508; P:proteolysis; ISS:GeneDB.
DR   CDD; cd05471; pepsin_like; 1.
DR   Gene3D; 2.40.70.10; -; 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; PTHR13683; PTHR13683; 1.
DR   Pfam; PF00026; Asp; 1.
DR   PRINTS; PR00792; PEPSIN.
DR   SUPFAM; SSF50630; SSF50630; 1.
DR   PROSITE; PS00141; ASP_PROTEASE; 1.
DR   PROSITE; PS51767; PEPTIDASE_A1; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q8IAS0.
DR   SWISS-2DPAGE; Q8IAS0.
KW   Aspartyl protease {ECO:0000256|RuleBase:RU000454};
KW   Hydrolase {ECO:0000256|RuleBase:RU000454, ECO:0000313|EMBL:CAD51290.1};
KW   Protease {ECO:0000256|RuleBase:RU000454};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001450}.
FT   DOMAIN          248..567
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   REGION          167..211
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   573 AA;  65114 MW;  1381CB0D4519A54F CRC64;
     MKRISPLNTL FYLSLFFSYT FKGLKCTRIY KIGTKALPCS ECHDVFDCTG CLFEEKESSH
     VIPLKLNKKN PNDHKKLQKH HESLKLGDVK YYVNRGEGIS GSLGTSSGNT LDDMDLINEE
     INKKRTNAQL DEKNFLDFTT YNKNKAQDIS DHLSDIQKHV YEQDAQKGNK NFTNNENNSD
     NENNSDNENN SDNENNLDNE NNLDNENNSD NSSIEKNFIA LENKNATVEQ TKENIFLVPL
     KHLRDSQFVG ELLVGTPPQT VYPIFDTGST NVWVVTTACE EESCKKVRRY DPNKSKTFRR
     SFIEKNLHIV FGSGSISGSV GTDTFMLGKH LVRNQTFGLV ESESNNNKNG GDNIFDYISF
     EGIVGLGFPG MLSAGNIPFF DNLLKQNPNV DPQFSFYISP YDGKSTLIIG GISKSFYEGD
     IYMLPVLKES YWEVKLDELY IGKERICCDE ESYVIFDTGT SYNTMPSSQM KTFLNLIHST
     ACTEQNYKDI LKSYPIIKYV FGELIIELHP EEYMILNDDV CMPAYMQIDV PSERNHAYLL
     GSLSFMRNFF TVFVRGTESR PSMVGVARAK SKN
//

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