ID A0A0F4GTC0_9PEZI Unreviewed; 495 AA.
AC A0A0F4GTC0;
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=Aspartic-type endopeptidase (OpsB) like protein {ECO:0000313|EMBL:KJY00474.1};
GN ORFNames=TI39_contig328g00021 {ECO:0000313|EMBL:KJY00474.1};
OS Zymoseptoria brevis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Zymoseptoria.
OX NCBI_TaxID=1047168 {ECO:0000313|EMBL:KJY00474.1, ECO:0000313|Proteomes:UP000033647};
RN [1] {ECO:0000313|EMBL:KJY00474.1, ECO:0000313|Proteomes:UP000033647}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Zb18110 {ECO:0000313|EMBL:KJY00474.1,
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}.
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:KJY00474.1}.
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DR EMBL; LAFY01000320; KJY00474.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F4GTC0; -.
DR STRING; 1047168.A0A0F4GTC0; -.
DR OrthoDB; 615305at2759; -.
DR Proteomes; UP000033647; Unassembled WGS sequence.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd05474; SAP_like; 1.
DR Gene3D; 2.40.70.10; Acid Proteases; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR InterPro; IPR033876; SAP-like.
DR PANTHER; PTHR47966; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR PANTHER; PTHR47966:SF81; PEPTIDASE A1 DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00026; Asp; 1.
DR PRINTS; PR00792; PEPSIN.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000033647};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..495
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002468992"
FT DOMAIN 78..404
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT REGION 444..470
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 96
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 290
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ SEQUENCE 495 AA; 53385 MW; DB8B1B041AE49A4A CRC64;
MPEFFTIAAV LAGYLLGADA IQLGTLDENR APKVVQQHLY RHPVADAVER DRRRFLHKRQ
NDNVNAVDVP LRNDLFLYYM NVSVGTPPQD FEVHIDTGSS DLWLNVPTSE FCSLPVDPCT
TGTYDANVSS TYEYVNSLFE ILYVDKTTSN GDYARDIVRL TDSNVSLPAQ QFGVGYESTT
QDGILGIGYP TNEAQISFGG PLYDNIPVSM VKEGYINTLA YSLWLNNIDA DEGDILFGGV
NTAKYQGDLV SLPVIPDRGL YRDFTIEMNS LGLSGDEEAF SSSPLEVHLD SGASLTYLPD
DVTDRIYSKV GATYDARYGI NIVDCNIANQ NETMDFVFSN ITIKVPMSEM VVPYANFGAQ
ELCVFGVLPT ITSSLGNEYI ILGDTFLRSA YVVYDMTNHE ISLAQTVFGV DAADDKIVEI
SSSGDGKPVE TGIASLVTPV GTIGSGSGSG AGTGTKNGSG SGSSSRTGEK GIASRFGGQM
GLVGMTFVAC ILSLW
//
