ID W4IV69_PLAFP Unreviewed; 449 AA.
AC W4IV69;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=Peptidase A1 domain-containing protein {ECO:0000259|PROSITE:PS51767};
GN ORFNames=PFUGPA_03578 {ECO:0000313|EMBL:ETW53704.1};
OS Plasmodium falciparum (isolate Palo Alto / Uganda).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX NCBI_TaxID=57270 {ECO:0000313|EMBL:ETW53704.1, ECO:0000313|Proteomes:UP000019103};
RN [1] {ECO:0000313|EMBL:ETW53704.1, ECO:0000313|Proteomes:UP000019103}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Palo Alto/Uganda {ECO:0000313|EMBL:ETW53704.1,
RC ECO:0000313|Proteomes:UP000019103};
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 Palo Alto/Uganda.";
RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ETW53704.1, ECO:0000313|Proteomes:UP000019103}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Palo Alto/Uganda {ECO:0000313|EMBL:ETW53704.1,
RC ECO:0000313|Proteomes:UP000019103};
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 Palo Alto/Uganda.";
RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004606}; Single-
CC pass type II membrane protein {ECO:0000256|ARBA:ARBA00004606}. Vacuole
CC lumen {ECO:0000256|ARBA:ARBA00004410}.
CC -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
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DR EMBL; KI927384; ETW53704.1; -; Genomic_DNA.
DR AlphaFoldDB; W4IV69; -.
DR EnsemblProtists; ETW53704; ETW53704; PFUGPA_03578.
DR OMA; CRVHQKF; -.
DR Proteomes; UP000019103; 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; 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 Disulfide bond {ECO:0000256|PIRSR:PIRSR601461-2};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000454};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|RuleBase:RU000454};
KW Reference proteome {ECO:0000313|Proteomes:UP000019103};
KW Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 40..62
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 137..444
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 155
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 335
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 168..173
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT DISULFID 370..406
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 449 AA; 51070 MW; 27CAB55D2CE11B9C CRC64;
MAHTVKEEEF SNTLIKNASA FDRLKLGNLK NLKIQKKLQF LYLILFVLIT GVFFFFLIGN
FYSHRKLYQV IKNTKHTTIG FKIDRPHDKV LSSVLKNKLS TYVKESFKFF KSGYAQKGYL
GSENDSIELD DVANLMFYGE GQIGTNKQPF MFIFDTGSAN LWVPSVNCDS IGCSTKHLYD
ASASKSYEKD GTKVEISYGS GTVRGYFSKD VISLGDLSLP YKFIEVTDAD DLEPIYSGSE
FDGILGLGWK DLSIGSIDPV VVELKKQNKI DNALFTFYLP VHDKHVGYLT IGGIESDFYE
GPLTYEKLNH DLYWQIDLDI HFGKYVMQKA NAVVDSGTST ITAPTSFLNK FFRDMNVIKV
PFLPLYVTTC DNDDLPTLEF HSRNNKYTLE PEFYMDPLSD IDPALCMLYI LPVDIDDNTF
ILGDPFMRKY FTVFDYEKES VGFAVAKNL
//
