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Database: UniProt
Entry: A0A0D9QS45_PLAFR
LinkDB: A0A0D9QS45_PLAFR
Original site: A0A0D9QS45_PLAFR 
ID   A0A0D9QS45_PLAFR        Unreviewed;       450 AA.
AC   A0A0D9QS45;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   08-NOV-2023, entry version 41.
DE   RecName: Full=Peptidase A1 domain-containing protein {ECO:0000259|PROSITE:PS51767};
GN   ORFNames=AK88_01785 {ECO:0000313|EMBL:KJP88506.1};
OS   Plasmodium fragile.
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC   Plasmodiidae; Plasmodium; Plasmodium (Plasmodium).
OX   NCBI_TaxID=5857 {ECO:0000313|EMBL:KJP88506.1, ECO:0000313|Proteomes:UP000054561};
RN   [1] {ECO:0000313|EMBL:KJP88506.1, ECO:0000313|Proteomes:UP000054561}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=nilgiri {ECO:0000313|Proteomes:UP000054561};
RG   The Broad Institute Genomics Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Neafsey D., Duraisingh M., Young S.K., Zeng Q., Gargeya S., Abouelleil A.,
RA   Alvarado L., Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A.,
RA   Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., Pearson M.,
RA   Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S., Wortman J.,
RA   Nusbaum C., Birren B.;
RT   "The Genome Sequence of Plasmodium fragile nilgiri.";
RL   Submitted (MAR-2014) 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; KQ001660; KJP88506.1; -; Genomic_DNA.
DR   RefSeq; XP_012334843.1; XM_012479420.1.
DR   AlphaFoldDB; A0A0D9QS45; -.
DR   MEROPS; A01.021; -.
DR   EnsemblProtists; KJP88506; KJP88506; AK88_01785.
DR   GeneID; 24267099; -.
DR   VEuPathDB; PlasmoDB:AK88_01785; -.
DR   OMA; KMPSIRD; -.
DR   OrthoDB; 1120702at2759; -.
DR   Proteomes; UP000054561; 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   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        40..63
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          139..446
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   ACT_SITE        157
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   ACT_SITE        337
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   DISULFID        170..175
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT   DISULFID        372..408
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ   SEQUENCE   450 AA;  51661 MW;  2D7FA36A8E2F8807 CRC64;
     MDIAVKEQDY SNGLIKNSAS FENLKFTNIK NFKVQKRFQI LYFILFVLVT GIFFFFLITT
     YFFTPNYKIN KIVQNTEHLT LPFKIQRPYD KVLKNVSKNN LKNYIKETYN LFKSGYMKQN
     YLGSDNDSIE LDDVANIMFY GEGEVGDNHQ KFTLIFDTGS ANLWVPSKKC TSIGCSIKNL
     YDSSKSKSYE KDGTKVDITY GSGTVKGFFS KDLVTLGHLS MPYKFIEVTD TDELEPIYSS
     VEFDGILGLG WKDLSIGSID PIVVELKNQN KIDNALFTFY LPIHDVHAGY LTIGGIEDKF
     YEGNITYEKL NHDLYWQIDL DVHFGKHTME KANVIVDSGT TTITAPTEFL NKFFANLNVI
     KVPFLPFYVT TCDNKEMPTL EFKSANNTYT LEPEYYMNPL LEVDDTLCMI TMLPVDIDSN
     TFILGDPFMR KYFTVFDYDQ ESVGFAIAKN
//
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