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Database: UniProt
Entry: A0A0M8N9C7_9HYPO
LinkDB: A0A0M8N9C7_9HYPO
Original site: A0A0M8N9C7_9HYPO 
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
//
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