ID B2B5A5_PODAN Unreviewed; 358 AA.
AC B2B5A5;
DT 20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT 20-MAY-2008, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE SubName: Full=Acyl-protein thioesterase 1 {ECO:0000313|EMBL:CDP25380.1};
DE SubName: Full=Podospora anserina S mat+ genomic DNA chromosome 2, supercontig 2 {ECO:0000313|EMBL:CAP72980.1};
GN ORFNames=PODANS_2_4040 {ECO:0000313|EMBL:CAP72980.1};
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:CAP72980.1};
RN [1] {ECO:0000313|EMBL:CAP72980.1, 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:CAP72980.1};
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:CAP72980.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=S mat+ {ECO:0000313|EMBL:CAP72980.1};
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:CDP25380.1}
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 AB hydrolase superfamily. AB hydrolase 2
CC family. {ECO:0000256|ARBA:ARBA00006499}.
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DR EMBL; CU640366; CAP72980.1; -; Genomic_DNA.
DR EMBL; FO904937; CDP25380.1; -; Genomic_DNA.
DR RefSeq; XP_001911155.1; XM_001911120.1.
DR AlphaFoldDB; B2B5A5; -.
DR GeneID; 6195679; -.
DR KEGG; pan:PODANSg8197; -.
DR VEuPathDB; FungiDB:PODANS_2_4040; -.
DR eggNOG; KOG2112; Eukaryota.
DR HOGENOM; CLU_049413_2_1_1; -.
DR OrthoDB; 910288at2759; -.
DR Proteomes; UP000001197; Chromosome 2.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR001375; Peptidase_S9.
DR InterPro; IPR003140; PLipase/COase/thioEstase.
DR PANTHER; PTHR10655:SF64; ABHYDROLASE_2 DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR10655; LYSOPHOSPHOLIPASE-RELATED; 1.
DR Pfam; PF02230; Abhydrolase_2; 1.
DR Pfam; PF00326; Peptidase_S9; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000001197}.
FT DOMAIN 83..234
FT /note="Phospholipase/carboxylesterase/thioesterase"
FT /evidence="ECO:0000259|Pfam:PF02230"
FT DOMAIN 279..350
FT /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00326"
FT REGION 29..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 236..264
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 248..263
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 358 AA; 39558 MW; 4B0FB1A9D584419D CRC64;
MGIASSSVVC IQNLPAFISS SLSYRLCRQS KSPTNQQTKP QRTKTYRLSP SIPHSSPSLT
QFMSHKMSPP FPDPLILPPL NPPHSFTLVL LHGRGNSPSS LLPFCSPLQQ SFPSLKIILP
TAPKSRATIY ARSLITQWFD GWHLDSPASV LNPGQDEWRS IDGLQQTTSY LHDLLRQEIA
LVGGDSRRMF LGGLSQGCAA SLMALLLWEG EPLGRCVGMC GWLPFVRTVQ RATKDFASRK
GDTEEDEFDP FGGNGEDDED KPQDVEAAAV QALRESLELE GNSPITRPNS FDTPVFLAHG
TEDDKVLIAH GKEAASTLSE LSVNTSWNEY PGLGHWFYPE MITDITAFLK SQIPQHRR
//
