ID A0A0F4GAK2_9PEZI Unreviewed; 398 AA.
AC A0A0F4GAK2;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Vacuolar protease a like protein {ECO:0000313|EMBL:KJX94022.1};
GN ORFNames=TI39_contig4225g00003 {ECO:0000313|EMBL:KJX94022.1};
OS Zymoseptoria brevis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Zymoseptoria.
OX NCBI_TaxID=1047168 {ECO:0000313|EMBL:KJX94022.1, ECO:0000313|Proteomes:UP000033647};
RN [1] {ECO:0000313|EMBL:KJX94022.1, ECO:0000313|Proteomes:UP000033647}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Zb18110 {ECO:0000313|EMBL:KJX94022.1,
RC ECO:0000313|Proteomes:UP000033647};
RA Grandaubert J., Bhattacharyya A., Stukenbrock E.H.;
RT "RNA-seq based gene annotation and comparative genomics of four
RT Zymoseptoria species reveal species-specific pathogenicity related genes
RT and transposable element activity.";
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
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:KJX94022.1}.
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DR EMBL; LAFY01004184; KJX94022.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F4GAK2; -.
DR STRING; 1047168.A0A0F4GAK2; -.
DR OrthoDB; 615305at2759; -.
DR Proteomes; UP000033647; 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: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:KJX94022.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000033647}.
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; 43148 MW; 7E8A8DDF5DC374A3 CRC64;
MKGNALLASA LVAGTASAGV HKMKLQKVPL SEQLEGYSIE EQVQHLGQKY MGIRPQGRIN
EMFKEQSYKP NKGHPVGVSN FLNAQYFSEI AIGTPPQEFK VVLDTGSSNL WVPSKDCGSI
ACYLHSKYNH GDSNTYKQNG SDFAIQYGSG SLEGYISQDT VQIGDLKIKN QLFAEATSEP
GLAFAFGRFD GILGLGYDTI SVNGIPPPFY NMIDQGLLDE KVFAFYLSST DKGDESEAIF
GGVNKDHYTG KMTNIPLRRK AYWEVDLDAI TLGDQTAELD STGAILDTGT SLIALPSTMA
ELLNKEIGAK KGYNGQYSVE CSARDSLPDL TFTLTGHNFT ISAYDYILEV QGSCISAFMG
FDIPAPAGPL AILGDAFLRR YYSVYDLGNN AVGLAKAK
//
