ID A0A0M8N9C7_9HYPO Unreviewed; 459 AA.
AC A0A0M8N9C7;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 28-JUN-2023, entry version 33.
DE SubName: Full=Putative aspartic-type endopeptidase opsB {ECO:0000313|EMBL:KOS23424.1};
GN ORFNames=ESCO_006644 {ECO:0000313|EMBL:KOS23424.1};
OS Escovopsis weberi.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Escovopsis.
OX NCBI_TaxID=150374 {ECO:0000313|EMBL:KOS23424.1, ECO:0000313|Proteomes:UP000053831};
RN [1] {ECO:0000313|EMBL:KOS23424.1, 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, 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:KOS23424.1}.
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DR EMBL; LGSR01000001; KOS23424.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M8N9C7; -.
DR STRING; 150374.A0A0M8N9C7; -.
DR OrthoDB; 615305at2759; -.
DR Proteomes; UP000053831; 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; cd05474; SAP_like; 1.
DR Gene3D; 2.40.70.10; Acid Proteases; 3.
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; IPR033876; SAP-like.
DR PANTHER; PTHR47965:SF79; ASPARTIC PROTEINASE; 1.
DR PANTHER; PTHR47965; ASPARTYL PROTEASE-RELATED; 1.
DR Pfam; PF00026; Asp; 2.
DR PRINTS; PR00792; PEPSIN.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 1.
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:UP000053831};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..459
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005819024"
FT DOMAIN 56..373
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
SQ SEQUENCE 459 AA; 48290 MW; D6C9D4A322EC1CE8 CRC64;
MRTNPVLTTA VALASAAQAQ VVQLDINKVP RNNNLSKRAS NVFDTPAENL RTQGGYFVEV
EVGTLGQRLT LQLDTGSSDV WVPSSDASIC RKGMFNIQYV DGSGSKGDYI QDSFTMGAAN
VQNLTMGLGL STSIPNGLIG VGYRTNEASI QTTGKTYPNL PVAMQQDGLI NSIAYSLWLN
DLGASQGSIL FGGIDTEKFV GNLTTLDLQP TSSRGDAIAE FSVNLYSLDA TSSSGTDSLL
GSVPDVVAIL DSGTTLTYLP QQWAEQAWDV VGAIYEPAVQ LALVPCSMMN SEGHFTFGFA
GPNGPKVNVP MNELVLDVTG GQQPRFPSGP YKNQLVCEFG IVNETSAPYL LGDTFLRSAY
IVYDLVNDQV AIGTTNFNAT KSNIVPFSKM GAPIPSAKAV AGPLENTLTG SQKTTFSATA
GFQKSLEKEN AAGPLTTFSG ASAAVVALTL AFSLMGSAF
//