ID A0A0D2AUZ4_9PEZI Unreviewed; 398 AA.
AC A0A0D2AUZ4;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Vacuolar protease A {ECO:0000313|EMBL:KIW02964.1};
GN ORFNames=PV09_05627 {ECO:0000313|EMBL:KIW02964.1};
OS Verruconis gallopava.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Venturiales; Sympoventuriaceae; Verruconis.
OX NCBI_TaxID=253628 {ECO:0000313|EMBL:KIW02964.1, ECO:0000313|Proteomes:UP000053259};
RN [1] {ECO:0000313|EMBL:KIW02964.1, ECO:0000313|Proteomes:UP000053259}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 43764 {ECO:0000313|EMBL:KIW02964.1,
RC ECO:0000313|Proteomes:UP000053259};
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 Ochroconis gallopava CBS43764.";
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; KN847546; KIW02964.1; -; Genomic_DNA.
DR RefSeq; XP_016212833.1; XM_016359154.1.
DR AlphaFoldDB; A0A0D2AUZ4; -.
DR STRING; 253628.A0A0D2AUZ4; -.
DR GeneID; 27313600; -.
DR VEuPathDB; FungiDB:PV09_05627; -.
DR HOGENOM; CLU_013253_3_4_1; -.
DR InParanoid; A0A0D2AUZ4; -.
DR OrthoDB; 615305at2759; -.
DR Proteomes; UP000053259; Unassembled WGS sequence.
DR GO; GO:0000324; C:fungal-type vacuole; IEA:InterPro.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd05488; Proteinase_A_fungi; 1.
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 InterPro; IPR033819; Saccharopepsin.
DR PANTHER; PTHR47966; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR PANTHER; PTHR47966:SF89; SACCHAROPEPSIN; 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:KIW02964.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000053259}.
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; 43301 MW; B0889B5BA6F23387 CRC64;
MKYSSAVAAA ALLGSASAGV HKMKLKKVPL SEQLEHHDIG QHARALGQKY MGIRPQSHAE
EMFSDTRYKG EGAHPVPVSN FLNAQYFSEI SVGTPPQNFK VVLDTGSSNL WVPSSECGSI
ACYLHSKYDH DSSSTYKKNG SEFAIQYGSG SLSGYVSRDT VRIGDLTIKD QLFAEATSEP
GLAFAFGRFD GILGLAYDTI SVNKIPPPFY SMIDQKLIDE PVFAFYLSDT KDGDDSEAVF
GGIDKSHYTG DITYIPLRRK AYWEVDLDAI TFGDATAEIE NTGVILDTGT SLIALPSTMA
ELLNKEIGAK KSFNGQYTVE CEKRDSLPDL TFTLTGHNFT IGPYDYILEV QGSCISAFMG
MDIPEPAGPL AILGDAFLRK WYSIYDLGKD AVGIAKSA
//
