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Database: UniProt
Entry: F0U899_AJEC8
LinkDB: F0U899_AJEC8
Original site: F0U899_AJEC8 
ID   F0U899_AJEC8            Unreviewed;       398 AA.
AC   F0U899;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   24-JAN-2024, entry version 52.
DE   SubName: Full=Aspartic endopeptidase Pep2 {ECO:0000313|EMBL:EGC40857.1};
GN   Name=PEP2 {ECO:0000313|EMBL:QSS52701.1};
GN   ORFNames=HCEG_00219 {ECO:0000313|EMBL:EGC40857.1}, I7I53_08429
GN   {ECO:0000313|EMBL:QSS52701.1};
OS   Ajellomyces capsulatus (strain H88) (Darling's disease fungus) (Histoplasma
OS   capsulatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX   NCBI_TaxID=544711 {ECO:0000313|Proteomes:UP000008142};
RN   [1] {ECO:0000313|EMBL:EGC40857.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H88 {ECO:0000313|EMBL:EGC40857.1};
RG   The Broad Institute Genome Sequencing Platform;
RA   Champion M., Cuomo C., Ma L.-J., Henn M.R., Sil A., Goldman B., Young S.K.,
RA   Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., Berlin A., Borenstein D.,
RA   Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA   Gujja S., Heiman D., Hepburn T., Howarth C., Jen D., Larson L., Lewis B.,
RA   Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA   Sisk P., Stolte C., Sykes S., Walk T., White J., Yandava C., Klein B.,
RA   McEwen J.G., Puccia R., Goldman G.H., Felipe M.S., Nino-Vega G.,
RA   San-Blas G., Taylor J., Mendoza L., Galagan J., Nusbaum C., Birren B.;
RT   "Annotation of Ajellomyces capsulatus strain H88.";
RL   Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000008142}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H88 {ECO:0000313|Proteomes:UP000008142};
RA   Champion M., Cuomo C., Ma L.-J., Henn M.R., Sil A., Goldman B., Young S.K.,
RA   Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., Berlin A., Borenstein D.,
RA   Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA   Gujja S., Heiman D., Hepburn T., Howarth C., Jen D., Larson L., Lewis B.,
RA   Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA   Sisk P., Stolte C., Sykes S., Walk T., White J., Yandava C., Klein B.,
RA   McEwen J.G., Puccia R., Goldman G.H., Felipe M.S., Nino-Vega G.,
RA   San-Blas G., Taylor J., Mendoza L., Galagan J., Nusbaum C., Birren B.;
RT   "Annotation of Ajellomyces capsulatus strain H88.";
RL   Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:QSS52701.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=H88 {ECO:0000313|EMBL:QSS52701.1};
RA   Voorhies M., Cohen S., Shea T.P., Petrus S., Munoz J.F., Poplawski S.,
RA   Goldman W.E., Michael T., Cuomo C.A., Sil A., Beyhan S.;
RT   "Chromosome-level genome assembly of a human fungal pathogen reveals
RT   clustering of transcriptionally co-regulated genes.";
RL   Submitted (JAN-2021) 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; DS990636; EGC40857.1; -; Genomic_DNA.
DR   EMBL; CP069103; QSS52701.1; -; Genomic_DNA.
DR   AlphaFoldDB; F0U899; -.
DR   STRING; 544711.F0U899; -.
DR   MEROPS; A01.018; -.
DR   VEuPathDB; FungiDB:I7I53_08429; -.
DR   HOGENOM; CLU_013253_3_4_1; -.
DR   OMA; KYDHDAS; -.
DR   Proteomes; UP000008142; Unassembled WGS sequence.
DR   Proteomes; UP000663419; Chromosome 2.
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: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|ARBA:ARBA00022750,
KW   ECO:0000256|RuleBase:RU000454};
KW   Disulfide bond {ECO:0000256|PIRSR:PIRSR601461-2};
KW   Hydrolase {ECO:0000256|RuleBase:RU000454};
KW   Protease {ECO:0000256|RuleBase:RU000454};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008142};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..398
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5033972481"
FT   DOMAIN          85..395
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   ACT_SITE        103
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   ACT_SITE        287
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   DISULFID        116..121
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT   DISULFID        321..354
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ   SEQUENCE   398 AA;  43041 MW;  9D21133BF76EA7E4 CRC64;
     MKPTLLLAAT ALLGVSSAKV HKLKLQKIPL SEQFANVNID AHVRALGQKY MGVKPNQNVQ
     DVFGDPAKAS GGHSLPVDNF LNAQYFSEIG IGTPPQTFKV VLDTGSSNLW VPSSECGSIA
     CYLHNKYDSS ASSTHKKNGS EFSITYGSGS LTGFVSQDCL TIGDLVVENQ VFAEATSEPG
     LAFAFGRFDG ILGLGYDTIS VNKIVPPFYE MLNKDLLDEP MFSFYLGDAN IDDDQSEVVF
     GGMNKDRFTG ELTKIPLRRK AYWEVDLDSI TFGKQTAMMT NTGVILDTGT SLIALPSTIA
     ELLNKEIGAK KSFNGQYTVE CAKRDSLPNL TFGLSGHNFT IGPYDYTLEV QGTCISSFMG
     MDFPAPVGPL AILGDAFLRR YYTVYDLGND AVGLAPVK
//
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