ID B2AQD7_PODAN Unreviewed; 412 AA.
AC B2AQD7;
DT 20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT 20-MAY-2008, sequence version 1.
DT 08-NOV-2023, entry version 72.
DE SubName: Full=Podospora anserina S mat+ genomic DNA chromosome 4, supercontig 4 {ECO:0000313|EMBL:CAP67077.1};
GN ORFNames=PODANS_4_4490 {ECO:0000313|EMBL:CAP67077.1};
OS Podospora anserina (strain S / ATCC MYA-4624 / DSM 980 / FGSC 10383)
OS (Pleurage anserina).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Podosporaceae; Podospora;
OC Podospora anserina.
OX NCBI_TaxID=515849 {ECO:0000313|EMBL:CAP67077.1};
RN [1] {ECO:0000313|EMBL:CAP67077.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S mat+ {ECO:0000313|EMBL:CAP67077.1};
RX PubMed=18460219; DOI=10.1186/gb-2008-9-5-r77;
RA Espagne E., Lespinet O., Malagnac F., Da Silva C., Jaillon O., Porcel B.M.,
RA Couloux A., Aury J.-M., Segurens B., Poulain J., Anthouard V.,
RA Grossetete S., Khalili H., Coppin E., Dequard-Chablat M., Picard M.,
RA Contamine V., Arnaise S., Bourdais A., Berteaux-Lecellier V., Gautheret D.,
RA de Vries R.P., Battaglia E., Coutinho P.M., Danchin E.G.J., Henrissat B.,
RA El Khoury R., Sainsard-Chanet A., Boivin A., Pinan-Lucarre B., Sellem C.H.,
RA Debuchy R., Wincker P., Weissenbach J., Silar P.;
RT "The genome sequence of the model ascomycete fungus Podospora anserina.";
RL Genome Biol. 9:R77.1-R77.22(2008).
RN [2] {ECO:0000313|EMBL:CAP67077.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=S mat+ {ECO:0000313|EMBL:CAP67077.1};
RA Genoscope - CEA;
RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000256|ARBA:ARBA00007447}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CU633895; CAP67077.1; -; Genomic_DNA.
DR RefSeq; XP_001906410.1; XM_001906375.1.
DR AlphaFoldDB; B2AQD7; -.
DR GeneID; 6189961; -.
DR KEGG; pan:PODANSg3439; -.
DR VEuPathDB; FungiDB:PODANS_4_4490; -.
DR HOGENOM; CLU_035052_1_0_1; -.
DR OrthoDB; 4940213at2759; -.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
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; 2.
DR PRINTS; PR00792; PEPSIN.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 3: Inferred from homology;
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..412
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002775307"
FT DOMAIN 79..407
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 95
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 298
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ SEQUENCE 412 AA; 45004 MW; 0CB7DE0D50B0B798 CRC64;
MKSSLLAFLA VGVAHSAGRL LHATRHGLVP DTVTSNVIPM RKHIVPSSEH RSSVVKPVYR
RTADVNHPAN LTNVHDVYYI VDIVVGNQTL AVSVDTGSSD TWFVSDYFEC VRFWWQGPEY
KPNCGLADGF TGNLSGGVLD NPPFVRSYMD TTFVSGYYGF EDVTVGSITA KNQRVGVVNY
TFWAGDGLTS ALRSPGRVGT RARPDGEVRT PEGSYLALGG LPPVEVDEES WARTKIHGVD
AIPEWMFEQS DLGLYIIKPD SWVYGRETED VTPAEADQGA VTTHGLTTNT TQFPVLIDVG
ATLSLLPKGL VQKLYAAFDP PAKYLSTNGL FFALCNATIP KFGVNIGENT FYFAPEDLLR
QTARDPSGEY CRIGVTDVNG GPYVLGVSFL SSVVAVFDIE NTEMRFASRT KY
//