ID A0A151GG86_9HYPO Unreviewed; 402 AA.
AC A0A151GG86;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 28-JUN-2023, entry version 27.
DE SubName: Full=Secreted aspartic proteinase {ECO:0000313|EMBL:KYK56105.1};
GN ORFNames=DCS_08071 {ECO:0000313|EMBL:KYK56105.1};
OS Drechmeria coniospora.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Drechmeria.
OX NCBI_TaxID=98403 {ECO:0000313|EMBL:KYK56105.1, ECO:0000313|Proteomes:UP000076580};
RN [1] {ECO:0000313|EMBL:KYK56105.1, ECO:0000313|Proteomes:UP000076580}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ARSEF 6962 {ECO:0000313|EMBL:KYK56105.1,
RC ECO:0000313|Proteomes:UP000076580};
RX PubMed=26975455; DOI=10.1038/srep23122;
RA Zhang L., Zhou Z., Guo Q., Fokkens L., Miskei M., Pocsi I., Zhang W.,
RA Chen M., Wang L., Sun Y., Donzelli B.G., Gibson D.M., Nelson D.R.,
RA Luo J.G., Rep M., Liu H., Yang S., Wang J., Krasnoff S.B., Xu Y.,
RA Molnar I., Lin M.;
RT "Insights into Adaptations to a Near-Obligate Nematode Endoparasitic
RT Lifestyle from the Finished Genome of Drechmeria coniospora.";
RL Sci. Rep. 6:23122-23122(2016).
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:KYK56105.1}.
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DR EMBL; LAYC01000003; KYK56105.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A151GG86; -.
DR STRING; 98403.A0A151GG86; -.
DR InParanoid; A0A151GG86; -.
DR OrthoDB; 2900143at2759; -.
DR Proteomes; UP000076580; Chromosome 03.
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:SF2; ASPERGILLOPEPSIN-1-RELATED; 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; 1.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 3: Inferred from homology;
KW Aspartyl protease {ECO:0000256|ARBA:ARBA00022750,
KW ECO:0000256|RuleBase:RU000454};
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR601461-2};
KW Hydrolase {ECO:0000256|RuleBase:RU000454};
KW Protease {ECO:0000256|RuleBase:RU000454};
KW Reference proteome {ECO:0000313|Proteomes:UP000076580};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..402
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007580571"
FT DOMAIN 90..399
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 108
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 291
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 327..362
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 402 AA; 42543 MW; 552F4E2E3C667819 CRC64;
MHTLAAFLLS LLLGGQLVAS LPTVESPAEF SVVAARNEKH KRHGPSALAK AYRKYGKSLP
NDLAAAVDQL EKRQSTGSVT TTPQKYDSEY LAAVQIGTPP QTLQLDFDTG SSDLWVFSTE
LPARAVKGQT LYNPASSSTA SQLRGASWSI TYGDHSSSSG DVYADVVSIG GLKVKNQAVE
AAKKISAQFT ADASSGLLGL AFSSINTVRP KKQQTFFDNA QSSLKKPVFT ANLKHQADGK
YNFGSIDSTQ YQGKITYTPV DNSQGFWAWT SSGYAVGKGA VNDHPITGIA DTGTSLLLLP
SEVVSDYYAD VDGADYDDSQ GGFTFPCGTR LPDFTFGVET STITVPASFL SYAPTDGSGK
TCFGAMQSSD EIGISIFGDV ALKAAFVVFD GGNMQLGWAS KL
//