ID A0A0N0RTV6_9HYPO Unreviewed; 708 AA.
AC A0A0N0RTV6;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=Putative aspartic-type endopeptidase opsB {ECO:0000313|EMBL:KOS21279.1};
GN ORFNames=ESCO_006697 {ECO:0000313|EMBL:KOS21279.1};
OS Escovopsis weberi.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Escovopsis.
OX NCBI_TaxID=150374 {ECO:0000313|EMBL:KOS21279.1, ECO:0000313|Proteomes:UP000053831};
RN [1] {ECO:0000313|EMBL:KOS21279.1, ECO:0000313|Proteomes:UP000053831}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA de Man T.J., Stajich J.E., Kubicek C.P., Chenthamara K., Atanasova L.,
RA Druzhinina I.S., Birnbaum S., Barribeau S.M., Teiling C., Suen G.,
RA Currie C., Gerardo N.M.;
RT "The genome of the fungus Escovopsis weberi, a specialized disease agent of
RT ant agriculture.";
RL Submitted (JUL-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:KOS21279.1}.
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DR EMBL; LGSR01000011; KOS21279.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N0RTV6; -.
DR STRING; 150374.A0A0N0RTV6; -.
DR OrthoDB; 615305at2759; -.
DR Proteomes; UP000053831; Unassembled WGS sequence.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
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 PANTHER; PTHR47966:SF65; ASPARTIC-TYPE ENDOPEPTIDASE; 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; PS51767; PEPTIDASE_A1; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR601461-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000053831}.
FT DOMAIN 65..380
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT REGION 620..639
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 667..686
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 83
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 275
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 311..345
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 708 AA; 73319 MW; 5492FC142CBDD77E CRC64;
MRYSSSLAIL PLAAHALQSP DDNNFLQTDG ISRYPITVSG GAPNKGLHKR QSEAFLTPRK
SGFFYTIDIG IGTPPQHVSV NFDTGSSELW VNPVCGKSTD KAFCEGFGRY NESKTFVDAK
APGGVKYGTG FVDFEYGYDY IQIGTAKIRQ QLFGVATDSE FASVGILGAG PSLEGWTSPY
PFVIDTMAQQ GLIQSRAFSL DIREFGSSRG SVIFGGIDTK KFSGPLEKRP IIPAKESPDG
YTRYWVYLDG ISLHTEDGYD VSVFNKTNGQ PVLLDSGYTI SALPGPIFNE ILDAFPSAKE
DGTTGEYFVD CKVAKSEGSI NFQFGKTLIK VAYVDFIWHL DDGTCKLGVF KDDEFPVLGD
TFMRAAYIVY DWDNQNIHLA NNEDCGSNLV PIGKGPDAVP SVVGECGAPS ATSSKPPLTT
APPLRTTPLT TATASATGAS GAVSSGTASI GTNMIQSTGP QSHGPLATGF LGATGGDAGS
HATSGLWSNS TVAPTLTSTV TTSVVHTVTS CPPSVTDCPL GSVTTEVITS YITYCPVTAG
GLTATPSQFE ETTATYTIPR TYTCSKGLVT CASQSPVHVI TVSPIVTQPT PVGIPHCTSC
GIDGAPPTTT TATAPIQTAP TSSAAQTTVP TSSSVPAVPT VTRAPSSGLT TVISPCSTCG
FAPGAPAPAP APAPTQGGSP PGAPVSGASD LGMPGLAVLL VGAVFAFL
//
