GenomeNet

Database: UniProt
Entry: A0A024VFK3_PLAFA
LinkDB: A0A024VFK3_PLAFA
Original site: A0A024VFK3_PLAFA 
ID   A0A024VFK3_PLAFA        Unreviewed;       453 AA.
AC   A0A024VFK3;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   08-NOV-2023, entry version 40.
DE   SubName: Full=Plasmepsin-2 {ECO:0000313|EMBL:ETW26955.1};
GN   ORFNames=PFFCH_05654 {ECO:0000313|EMBL:ETW26955.1};
OS   Plasmodium falciparum FCH/4.
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC   Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX   NCBI_TaxID=1036724 {ECO:0000313|EMBL:ETW26955.1, ECO:0000313|Proteomes:UP000030656};
RN   [1] {ECO:0000313|EMBL:ETW26955.1, ECO:0000313|Proteomes:UP000030656}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FCH/4 {ECO:0000313|EMBL:ETW26955.1,
RC   ECO:0000313|Proteomes:UP000030656};
RG   The Broad Institute Genome Sequencing Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Neafsey D., Hoffman S., Volkman S., Rosenthal P., Walker B., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W.,
RA   Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J.,
RA   Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A.,
RA   Ireland A., Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W.,
RA   Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J.,
RA   Nusbaum C., Birren B.;
RT   "The Genome Annotation of Plasmodium falciparum FCH/4.";
RL   Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ETW26955.1, ECO:0000313|Proteomes:UP000030656}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FCH/4 {ECO:0000313|EMBL:ETW26955.1,
RC   ECO:0000313|Proteomes:UP000030656};
RG   The Broad Institute Genome Sequencing Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Neafsey D., Cheeseman I., Volkman S., Adams J., Walker B., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A.,
RA   Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C.,
RA   Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA   Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Plasmodium falciparum FCH/4.";
RL   Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase A1 family.
CC       {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
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DR   EMBL; KI928152; ETW26955.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A024VFK3; -.
DR   SMR; A0A024VFK3; -.
DR   MEROPS; A01.023; -.
DR   EnsemblProtists; ETW26955; ETW26955; PFFCH_05654.
DR   Proteomes; UP000030656; Unassembled 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; NAPSIN-A; 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   Disulfide bond {ECO:0000256|PIRSR:PIRSR601461-2};
KW   Hydrolase {ECO:0000256|RuleBase:RU000454};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Protease {ECO:0000256|RuleBase:RU000454};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030656};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        41..59
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          140..447
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   ACT_SITE        158
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   ACT_SITE        338
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   DISULFID        171..176
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT   DISULFID        373..409
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ   SEQUENCE   453 AA;  51490 MW;  0D78A8A65D0C80B5 CRC64;
     MDITVREHDF KHGFIKSNST FDGLNIDNSK NKKKIQKGFQ ILYVLLFCSV MCGLFYYVYE
     NVWLQRDNEM NEILKNSEHL TIGFKVENAH DRILKTIKTH KLKNYIKESV NFLNSGLTKT
     NYLGSSNDNI ELVDFQNIMF YGDAEVGDNQ QPFTFILDTG SANLWVPSVK CTTAGCLTKH
     LYDSSKSRTY EKDGTKVEMN YVSGTVSGFF SKDLVTVGNL SLPYKFIEVI DTNGFEPTYT
     ASTFDGILGL GWKDLSIGSV DPIVVELKNQ NKIENALFTF YLPVHDKHTG FLTIGGIEER
     FYEGPLTYEK LNHDLYWQIT LDAHVGNIML EKANCIVDSG TSAITVPTDF LNKMLQNLDV
     IKVPFLPFYV TLCNNSKLPT FEFTSENGKY TLEPEYYLQH IEDVGPGLCM LNIIGLDFPV
     PTFILGDPFM RKYFTVFDYD NHSVGIALAK KNL
//
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