ID A0A0F4G8Y5_9PEZI Unreviewed; 462 AA.
AC A0A0F4G8Y5;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE RecName: Full=Peptidase A1 domain-containing protein {ECO:0000259|PROSITE:PS51767};
GN ORFNames=TI39_contig4248g00002 {ECO:0000313|EMBL:KJX93826.1};
OS Zymoseptoria brevis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Zymoseptoria.
OX NCBI_TaxID=1047168 {ECO:0000313|EMBL:KJX93826.1, ECO:0000313|Proteomes:UP000033647};
RN [1] {ECO:0000313|EMBL:KJX93826.1, ECO:0000313|Proteomes:UP000033647}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Zb18110 {ECO:0000313|EMBL:KJX93826.1,
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:KJX93826.1}.
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DR EMBL; LAFY01004207; KJX93826.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F4G8Y5; -.
DR STRING; 1047168.A0A0F4G8Y5; -.
DR MEROPS; A01.079; -.
DR OrthoDB; 2900143at2759; -.
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 CDD; cd06097; Aspergillopepsin_like; 1.
DR Gene3D; 2.40.70.10; Acid Proteases; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR001969; Aspartic_peptidase_AS.
DR InterPro; IPR034163; Aspergillopepsin-like_cat_dom.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR PANTHER; PTHR47966:SF1; ASPARTYL PROTEINASE; 1.
DR PANTHER; PTHR47966; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 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}; Hydrolase {ECO:0000256|RuleBase:RU000454};
KW Protease {ECO:0000256|RuleBase:RU000454};
KW Reference proteome {ECO:0000313|Proteomes:UP000033647};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..462
FT /note="Peptidase A1 domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002468247"
FT DOMAIN 150..459
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT REGION 103..149
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 103..137
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 166
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 352
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ SEQUENCE 462 AA; 49488 MW; 689B63310678C03A CRC64;
MAPSITMILL ALFEMISVAL AAPHVNSLQK RSFHAHARGR QVSGYEEIQR AHRKYWESIV
SDGAGYHHAD AVPSYSIRAS QVPVSSAPIQ LTHTVFVTAP APSATGSPEF ESSPASLKTS
TSSTSRAPTT TASNEDGEAT AVPEENESEY LTETTVGGQK VNLNLDTGSA DLWVFSSLLS
QSVLGDHSFY NPNNSDTFES YDGATWQIRY GDGSSASGVV GYDVVDIGGT TVQKQCVELA
TQLSRAFIAD DASDGLLGLG FSSISTVKPV QQKTFFENVM PQLSAPVFTA DLEETSGAGT
YEFGRIDPAK YHGEIHYTPI DNSEGWWQFD SPNYSVDGQE SPCIYCNPAI ADTGTSLVYM
DTDIVRAYYA SVSSAFPDTS QGGWLFDCTE TLPSFGLAVG DYMAVINGTD MAYAPLDDGS
GRCYGGLQEG PGDVQIIGDV FLKQFFAVFD GGENRFGVAL KN
//