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Database: UniProt
Entry: A0A024GPE6_9STRA
LinkDB: A0A024GPE6_9STRA
Original site: A0A024GPE6_9STRA 
ID   A0A024GPE6_9STRA        Unreviewed;       374 AA.
AC   A0A024GPE6;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=Peptidase A1 domain-containing protein {ECO:0000259|PROSITE:PS51767};
GN   ORFNames=BN9_092890 {ECO:0000313|EMBL:CCI48227.1};
OS   Albugo candida.
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Albuginales; Albuginaceae; Albugo.
OX   NCBI_TaxID=65357 {ECO:0000313|EMBL:CCI48227.1, ECO:0000313|Proteomes:UP000053237};
RN   [1] {ECO:0000313|EMBL:CCI48227.1, ECO:0000313|Proteomes:UP000053237}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ac Nc2 {ECO:0000313|EMBL:CCI48227.1,
RC   ECO:0000313|Proteomes:UP000053237};
RA   Gardiner A., Kemen E., Schultz-Larsen T., MacLean D., Van Oosterhout C.,
RA   Jones J.D.G.;
RT   "Recombination and specialization in a pathogen metapopulation.";
RL   Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase A1 family.
CC       {ECO:0000256|ARBA:ARBA00007447}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:CCI48227.1}.
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DR   EMBL; CAIX01000210; CCI48227.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A024GPE6; -.
DR   STRING; 65357.A0A024GPE6; -.
DR   InParanoid; A0A024GPE6; -.
DR   Proteomes; UP000053237; Unassembled WGS sequence.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   Gene3D; 2.40.70.10; Acid Proteases; 2.
DR   InterPro; IPR001461; Aspartic_peptidase_A1.
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   SUPFAM; SSF50630; Acid proteases; 1.
DR   PROSITE; PS51767; PEPTIDASE_A1; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053237}.
FT   DOMAIN          63..371
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
SQ   SEQUENCE   374 AA;  42750 MW;  B18290AF5F5914BF CRC64;
     MTILSTLIGF SVLPGFRDQS INSPMTTVER IPISIVGQGN ISTGNSLSEF AMNANVYWSS
     QHYLLTISVG KPANPLTIET SRDFRIKVVT DSTVFWIPQK FYDQNLFRRR WWTSYVSIPG
     ENNIQIDGYY ARDDLQLGKM QARNEKIIIA SAGAPLDSMK RDQYQGVLGS GYKTTTNLNM
     YDTPFYHFLK SRQYTLNVYS FYIYNESYGE LVIGEVDPIH GALSYVAVCD TDEPWTIEFS
     QVKLDHEAIL DNHLMIAQFN PARAGILVPK MELNTIILAL DREGFSFAFL NGRYVALCHN
     EKLPTLRFQF GEALVNLTSD DYMFRSGNYC VLALSAQTDR KTWVFGQVFF RIMYTVFEWG
     TGKQIPKMGF AKYR
//
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