ID B2AEF9_PODAN Unreviewed; 507 AA.
AC B2AEF9;
DT 20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT 20-MAY-2008, sequence version 1.
DT 24-JAN-2024, entry version 73.
DE SubName: Full=Podospora anserina S mat+ genomic DNA chromosome 5, supercontig 1 {ECO:0000313|EMBL:CAP61825.1};
GN ORFNames=PODANS_5_2710 {ECO:0000313|EMBL:CAP61825.1};
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:CAP61825.1};
RN [1] {ECO:0000313|EMBL:CAP61825.1, ECO:0000313|Proteomes:UP000001197}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S / ATCC MYA-4624 / DSM 980 / FGSC 10383
RC {ECO:0000313|Proteomes:UP000001197}, and S mat+
RC {ECO:0000313|EMBL:CAP61825.1};
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:CAP61825.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=S mat+ {ECO:0000313|EMBL:CAP61825.1};
RA Genoscope - CEA;
RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Proteomes:UP000001197}
RP GENOME REANNOTATION.
RC STRAIN=S / ATCC MYA-4624 / DSM 980 / FGSC 10383
RC {ECO:0000313|Proteomes:UP000001197};
RX PubMed=24558260; DOI=10.1534/genetics.113.159988;
RA Grognet P., Bidard F., Kuchly C., Tong L.C.H., Coppin E., Benkhali J.A.,
RA Couloux A., Wincker P., Debuchy R., Silar P.;
RT "Maintaining two mating types: Structure of the mating type locus and its
RT role in heterokaryosis in Podospora anserina.";
RL Genetics 197:421-432(2014).
RN [4] {ECO:0000313|EMBL:CDP28901.1}
RP NUCLEOTIDE SEQUENCE.
RA Grognet P., Bidard F., Kuchly C., Chan Ho Tong L., Coppin E.,
RA Ait Benkhali J., Couloux A., Wincker P., Debuchy R., Silar P.;
RT "Maintaining two mating types: Structure of the mating type locus and its
RT role in heterokaryosis in Podospora anserina.";
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000256|ARBA:ARBA00007447}.
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DR EMBL; CU633457; CAP61825.1; -; Genomic_DNA.
DR EMBL; FO904940; CDP28901.1; -; Genomic_DNA.
DR RefSeq; XP_001904048.1; XM_001904013.1.
DR AlphaFoldDB; B2AEF9; -.
DR GeneID; 6188403; -.
DR KEGG; pan:PODANSg1065; -.
DR VEuPathDB; FungiDB:PODANS_5_2710; -.
DR eggNOG; KOG1339; Eukaryota.
DR HOGENOM; CLU_013253_9_0_1; -.
DR OrthoDB; 615305at2759; -.
DR Proteomes; UP000001197; Chromosome 5.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR Gene3D; 2.40.70.10; Acid Proteases; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR PANTHER; PTHR47966:SF65; ASPARTIC-TYPE ENDOPEPTIDASE; 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; PS51767; PEPTIDASE_A1; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR601461-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000001197};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..507
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007638633"
FT DOMAIN 139..462
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT REGION 24..121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..42
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 77..117
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 157
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 352
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 386..422
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 507 AA; 55975 MW; 8DCC66F922AFE91F CRC64;
MLLHFAIYTT LFLTVSHGAS LPNLSNEHSL DDGDKGGGKR TRDPGYVRMP VSRQKFKSKG
KSKRGWHWGP PTDPHNDPSA LKSNQPFQPT HASSSTRPPP TLTRITRSPP TQQSPTLHRR
AADRRWGWSN LEELGGIAYI IQLDIGTPPQ KVRVFVDTGS YELWVNPRCS TSASDSLCQT
FGNYFPSKSN SAMHIGGNFA VTYGTGAVRG SYWSDVMSIA MLQIPHVQFA VAADSNYTFA
GILGLGYAYP YSIPYPSVLN LMVSQKMISA PIFSLGLGGD GDGFSEIIFG GVNRWKFAGP
LVPVSIWPPI KEQDPRWVQY WVNVTSVGLT KPKEAGKLYT PREGFSMPTL IDTGSTLSYI
REDLVAVIGQ QFNAEIDTQG NYFVDCKYRD VAGTVDFGFN SGAMVINVRY KDFIYQLYPG
RCMLGVQPAD YGSTYYVLGD TFIRGAYCES CPFLTVSKIS TELTHAYIVV FDQQSDVVWM
NQYYNCGDGV VTVGQTPRDT KNVVGAC
//
