ID A0A0D2KGX7_9EURO Unreviewed; 398 AA.
AC A0A0D2KGX7;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE SubName: Full=Vacuolar protease A {ECO:0000313|EMBL:KIY02730.1};
GN ORFNames=Z520_01195 {ECO:0000313|EMBL:KIY02730.1};
OS Fonsecaea multimorphosa CBS 102226.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Fonsecaea.
OX NCBI_TaxID=1442371 {ECO:0000313|EMBL:KIY02730.1, ECO:0000313|Proteomes:UP000053411};
RN [1] {ECO:0000313|EMBL:KIY02730.1, ECO:0000313|Proteomes:UP000053411}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 102226 {ECO:0000313|EMBL:KIY02730.1,
RC ECO:0000313|Proteomes:UP000053411};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Fonsecaea multimorphosa CBS 102226.";
RL Submitted (JAN-2015) 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; KN848063; KIY02730.1; -; Genomic_DNA.
DR RefSeq; XP_016636852.1; XM_016771713.1.
DR AlphaFoldDB; A0A0D2KGX7; -.
DR STRING; 1442371.A0A0D2KGX7; -.
DR GeneID; 27706941; -.
DR VEuPathDB; FungiDB:Z520_01195; -.
DR OrthoDB; 615305at2759; -.
DR Proteomes; UP000053411; Unassembled 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: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, ECO:0000313|EMBL:KIY02730.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000053411};
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_5002245721"
FT DOMAIN 86..395
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 104
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 287
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 117..122
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT DISULFID 321..354
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 398 AA; 43295 MW; AD3BF1531A4402BE CRC64;
MKNSLVIAAA ALLGAADAGM HRMKLQKVPL AEQLSAANIG DHMRALRHKY TQKPMGGASE
DIFRDTSIRP DSPHDVPVEN FLNAQYFSTI ALGTPPQEFK VVLDTGSSNL WVPSTQCGSI
ACYLHQKYDS SASSTFKKNG SEFGIRYGSG EVAGFISQDL LRIGDLKIKD QLFGEVTSEP
GLAFAFGRFD GILGLGYDTI SVNHIPPPFY NMVDQKLLDE PVFAFYLGNT EDGTESEATF
GGIDSNHYTG KMIKIPLRRK AYWEVNLDSI TLGKDSADLD NTGVILDTGT SLIALPSTLA
ELLNKEIGAK KGFNGQYTVE CDKRDSLPDI TFTLSGYNFS ITAHDYILEV QGSCISSFMG
MDFPAPTGPL AILGDSFLRK WYSVYDLGND AVALAKSK
//