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
//