ID B6KGS0_TOXGV Unreviewed; 643 AA.
AC B6KGS0; A0A0F7VEJ1; B9QDN8; S8EV53;
DT 16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT 16-DEC-2008, sequence version 1.
DT 27-MAR-2024, entry version 78.
DE SubName: Full=Aspartyl protease ASP3 {ECO:0000313|EMBL:ESS34201.1};
DE EC=3.4.23.1 {ECO:0000313|EMBL:ESS34201.1};
DE SubName: Full=Eukaryotic aspartyl protease, putative {ECO:0000313|EMBL:CEL78331.1};
GN ORFNames=BN1205_005440 {ECO:0000313|EMBL:CEL78331.1}, TGVEG_246550
GN {ECO:0000313|EMBL:ESS34201.1};
OS Toxoplasma gondii (strain ATCC 50861 / VEG).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Sarcocystidae; Toxoplasma.
OX NCBI_TaxID=432359 {ECO:0000313|EMBL:ESS34201.1, ECO:0000313|Proteomes:UP000002226};
RN [1] {ECO:0000313|EMBL:ESS34201.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=VEG {ECO:0000313|EMBL:ESS34201.1};
RA Paulsen I.;
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000002226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 50861 / VEG {ECO:0000313|Proteomes:UP000002226};
RA Lorenzi H., Inman J., Amedeo P., Brunk B., Roos D., Caler E.;
RT "Annotation of Toxoplasma gondii VEG.";
RL Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:ESS34201.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=VEG {ECO:0000313|EMBL:ESS34201.1};
RA Sibley D., Venepally P., Karamycheva S., Hadjithomas M., Khan A., Brunk B.,
RA Roos D., Caler E., Lorenzi H.;
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:CEL78331.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=VEG {ECO:0000313|EMBL:CEL78331.1};
RX PubMed=25875305; DOI=10.1371/journal.pone.0124473;
RA Ramaprasad A., Mourier T., Naeem R., Malas T.B., Moussa E., Panigrahi A.,
RA Vermont S.J., Otto T.D., Wastling J., Pain A.;
RT "Comprehensive Evaluation of Toxoplasma gondii VEG and Neospora caninum LIV
RT Genomes with Tachyzoite Stage Transcriptome and Proteome Defines Novel
RT Transcript Features.";
RL PLoS ONE 10:e0124473-e0124473(2015).
CC -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
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DR EMBL; LN714502; CEL78331.1; -; Genomic_DNA.
DR EMBL; AAYL02000080; ESS34201.1; -; Genomic_DNA.
DR AlphaFoldDB; B6KGS0; -.
DR SMR; B6KGS0; -.
DR STRING; 432359.B6KGS0; -.
DR PaxDb; 5811-TGME49_046550; -.
DR EnsemblProtists; ESS34201; ESS34201; TGVEG_246550.
DR VEuPathDB; ToxoDB:TGVEG_246550; -.
DR eggNOG; KOG1339; Eukaryota.
DR OMA; THIRKED; -.
DR Proteomes; UP000002226; Partially assembled WGS sequence.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 2.40.70.10; Acid Proteases; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR001969; Aspartic_peptidase_AS.
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:SF28; PLASMEPSIN X; 1.
DR Pfam; PF00026; Asp; 1.
DR PRINTS; PR00792; PEPSIN.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 1.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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, ECO:0000313|EMBL:ESS34201.1};
KW Protease {ECO:0000256|RuleBase:RU000454, ECO:0000313|EMBL:ESS34201.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002226};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..31
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 32..643
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010106554"
FT DOMAIN 281..600
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT REGION 87..116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 299
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 490
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 312..317
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 643 AA; 69156 MW; 094EDD0710978633 CRC64;
MEGRTTAGRA TPAGFWLFSC CLASLLWSAN ALIPAGKSAG SSFLAATSSQ PSEEAPREFP
GHLSNSQIAS ETGSALKIEE IASSGSAPEV SGAAGASASK TSEKPIRPYH TGPSSRSSAY
SASSGIPLCH TCSSFDAANG GCRLCVHGEV ASDFLMPMMP IRNIDTHREE TLSRLEANHR
THLNEKKNFY VLRGKGPFGS LGNLPGTPGL DAAIAFGLSS PDLPSASFAQ IKNKDSSDSG
DVAAVGEETD SAVADGSKTL DLDLKLAETS VPILQMKDSQ YVGVIGIGTP PQFVQPIFDT
GSTNLWVVGS KCTDDTCTKV TRFDPSASKT FRAANPPVHL DITFGTGRIE GSTGIDDFTV
GPFLVKGQSF GLVESEGGHN MHGNIFKTIN FEGIVGLAFP EMSSTGTVPI YDNIISQGTL
KENEFAFYMA KGSQVSALFF GGVDPRFYEA PIHMFPVTRE HYWETSLDAI YIGDKKFCCE
EGTKNYVILD SGTSFNTMPS GELGKLLDMI PSKECNLDDP EFTSDFPTIT YVIGGVKFPL
TPEQYLVRSK KNECKPAYMQ IDVPSQFGHA YILGSVAFMR HYYTVFRRSD GTRPSLVGIA
RAVHNDDNSA YLSNVLNEYP GAHIRKEDLM MERSMSAPSM REL
//
