ID L8FYN9_PSED2 Unreviewed; 404 AA.
AC L8FYN9;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 24-JAN-2024, entry version 45.
DE RecName: Full=Peptidase A1 domain-containing protein {ECO:0000259|PROSITE:PS51767};
GN ORFNames=GMDG_01984 {ECO:0000313|EMBL:ELR06110.1};
OS Pseudogymnoascus destructans (strain ATCC MYA-4855 / 20631-21) (Bat
OS white-nose syndrome fungus) (Geomyces destructans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=658429 {ECO:0000313|EMBL:ELR06110.1, ECO:0000313|Proteomes:UP000011064};
RN [1] {ECO:0000313|Proteomes:UP000011064}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4855 / 20631-21 {ECO:0000313|Proteomes:UP000011064};
RG The Broad Institute Genome Sequencing Platform;
RA Cuomo C.A., Blehert D.S., Lorch J.M., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M.,
RA Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E.,
RA Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D.,
RA Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A., Murphy C.,
RA Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The genome sequence of Geomyces destructans 20631-21.";
RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
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DR EMBL; GL573194; ELR06110.1; -; Genomic_DNA.
DR RefSeq; XP_012740387.1; XM_012884933.1.
DR AlphaFoldDB; L8FYN9; -.
DR STRING; 658429.L8FYN9; -.
DR VEuPathDB; FungiDB:GMDG_01984; -.
DR HOGENOM; CLU_013253_0_1_1; -.
DR InParanoid; L8FYN9; -.
DR OrthoDB; 2900143at2759; -.
DR Proteomes; UP000011064; 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; 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:SF1; ASPARTYL PROTEINASE; 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; 2.
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:UP000011064};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..404
FT /note="Peptidase A1 domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003989867"
FT DOMAIN 93..401
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 109
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 292
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ SEQUENCE 404 AA; 41936 MW; D1B184E8A80F39C2 CRC64;
MVAASKLALF ATAAASVAAA PVAAPAAAKS FSVPAVHNAN YQRNGTLALL KAYAKYGLTP
SEPDSIINLL LGGLAKRQDG TVPAKPDSQN VEYICKVTIG GQTLNLDFDT GSADLWVFST
SLPATSKNNH NVFDPTKSST WQEMSGASWS IQYVDGSGSS GTVGTDTVTI GGTTVQGQAV
EIATDASAQF IAGANDGLLG LSFSSINTVQ PTQQNTFFDN AKASLDKPLF AAYLPLQASG
AYDFGAIDSS RYTGEVAYTS VDNTNGWWEF PSTTYKVGSQ AFSSAGYTAI ADTGTTLLLM
GDEQVTNYYN NVPGSRLDNN QGGYVFPCSA TLPSLSVAIG DAGDAVIPAK YLNFGPAGHS
DTDCFGSLQS SGNGQQNVYG DVFFNAFYGV FDASGPRFGF AATA
//