ID B2AWU0_PODAN Unreviewed; 480 AA.
AC B2AWU0;
DT 20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT 20-MAY-2008, sequence version 1.
DT 24-JAN-2024, entry version 90.
DE SubName: Full=Candidapepsin {ECO:0000313|EMBL:CDP32336.1};
DE SubName: Full=Podospora anserina S mat+ genomic DNA chromosome 7, supercontig 1 {ECO:0000313|EMBL:CAP68864.1};
GN ORFNames=PODANS_7_8310 {ECO:0000313|EMBL:CAP68864.1};
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:CAP68864.1};
RN [1] {ECO:0000313|EMBL:CAP68864.1, 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:CAP68864.1};
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:CAP68864.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=S mat+ {ECO:0000313|EMBL:CAP68864.1};
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:CDP32336.1}
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 (SEP-2014) 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; CU633900; CAP68864.1; -; Genomic_DNA.
DR EMBL; FO904942; CDP32336.1; -; Genomic_DNA.
DR RefSeq; XP_001908191.1; XM_001908156.1.
DR AlphaFoldDB; B2AWU0; -.
DR GeneID; 6191907; -.
DR KEGG; pan:PODANSg5226; -.
DR VEuPathDB; FungiDB:PODANS_7_8310; -.
DR eggNOG; KOG1339; Eukaryota.
DR HOGENOM; CLU_013253_9_3_1; -.
DR OrthoDB; 615305at2759; -.
DR Proteomes; UP000001197; Chromosome 7.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd05474; SAP_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; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR InterPro; IPR033876; SAP-like.
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; 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:UP000001197};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..480
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007639043"
FT DOMAIN 79..408
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT REGION 24..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 421..450
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..38
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 97
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 290
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 325..372
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 480 AA; 50773 MW; C0B600BCAB37215F CRC64;
MKTATSLLVV AASLAGQTID ALSLPSTTPT QQQQRRDGSG PRVVGMDIQR RTPKNPLHRD
HLRKRGSVEV DLDNQETLYF INGTIGTPPK SLRLHLDTGS SDLWVNTPSS SLCTQSSAPC
KYAGTYSANG SSTYEYIGSW FNISYVDGSG ASGDYVSDTV TFGDATLDRL QFGIGYSSNN
AQGILGIGYP INEVQVGRAG MRPYNNLPAQ MVADGLIQTN AYSLWLNDLD ADTGNILFGG
VDTEKFVPPL MSLPVESEAG VYAEFMITLT KVELGSAQVG GDLALAVLLD TGSSLTYLPD
RMVQDIFDLV DAQYDPEANA AYVPCSLADN ETAVLSFTFT EPTINVGMDE LVLDLVTSSG
RRPVFSDGTE ACLFGIAPAG EGTNVLGDTF LRSAYVVYDL ENNEISLAAT RFNSTGTRVE
EIGKGEGGVP GATKVENPTK ATEGLDGPNG LGGISAGNKR GLEVGVVWLV AGMVGVLLVV
//
