ID A0A151GMV7_9HYPO Unreviewed; 442 AA.
AC A0A151GMV7;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 08-NOV-2023, entry version 24.
DE SubName: Full=Eukaryotic aspartyl protease {ECO:0000313|EMBL:KYK58439.1};
GN ORFNames=DCS_05455 {ECO:0000313|EMBL:KYK58439.1};
OS Drechmeria coniospora.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Drechmeria.
OX NCBI_TaxID=98403 {ECO:0000313|EMBL:KYK58439.1, ECO:0000313|Proteomes:UP000076580};
RN [1] {ECO:0000313|EMBL:KYK58439.1, ECO:0000313|Proteomes:UP000076580}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ARSEF 6962 {ECO:0000313|EMBL:KYK58439.1,
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}.
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:KYK58439.1}.
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DR EMBL; LAYC01000002; KYK58439.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A151GMV7; -.
DR STRING; 98403.A0A151GMV7; -.
DR InParanoid; A0A151GMV7; -.
DR OrthoDB; 4940213at2759; -.
DR Proteomes; UP000076580; Chromosome 02.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd05471; pepsin_like; 1.
DR Gene3D; 2.40.70.10; Acid Proteases; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR034164; Pepsin-like_dom.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR PANTHER; PTHR47966; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR PANTHER; PTHR47966:SF47; ENDOPEPTIDASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_3G01220)-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 Hydrolase {ECO:0000313|EMBL:KYK58439.1};
KW Protease {ECO:0000313|EMBL:KYK58439.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000076580};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..442
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007580734"
FT DOMAIN 98..439
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 116
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 330
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ SEQUENCE 442 AA; 47897 MW; BF8E4CBAA8232B47 CRC64;
MKTLRFASLA SLLVGLAALA GAAWDVSQPL NGISFQRIKA VQAPTPDRPS MKFSRLRNVK
GKPGVLTTTS ALGRVLRTPP LHHQHTYQNV STAGDFSTQY AIQCGWDGVP LWLLFDTGSS
DTWTVQTGFE CNGGGRYEQS ACGFGPTTVD GFKDGPIDDL HFLLRYGSGE KVHGPMGYSD
IACGGVHVSR QQVGLANYTL WHGNNLTVGI LGLAYPSLTS AFYGPIGTEA PWNAITYTPF
LTKAIMQGTI DPVFSVAILK NSSEGMLAWG GLPPMERPRG SFAATDLIID KANLIGQSET
SWRYSFYTII PDGVKWGQST DTTKFPYIVD TGTTMNYLPP PLAEAIAMAF QPRAVFMYQW
GSYFAPCHAI PPHFAIIISG VEFWINPADL IYQDLKDPLT GYCAVAIASG GSGPYILGDV
FLQNVVAVFD VGAAQMRFYA RE
//