ID B2ARA8_PODAN Unreviewed; 645 AA.
AC B2ARA8;
DT 20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT 20-MAY-2008, sequence version 1.
DT 27-MAR-2024, entry version 78.
DE SubName: Full=Podospora anserina S mat+ genomic DNA chromosome 4, supercontig 4 {ECO:0000313|EMBL:CAP66686.1};
GN ORFNames=PODANS_4_8090 {ECO:0000313|EMBL:CAP66686.1};
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:CAP66686.1};
RN [1] {ECO:0000313|EMBL:CAP66686.1, 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:CAP66686.1};
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:CAP66686.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=S mat+ {ECO:0000313|EMBL:CAP66686.1};
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:CDP28421.1}
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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; CU633895; CAP66686.1; -; Genomic_DNA.
DR EMBL; FO904939; CDP28421.1; -; Genomic_DNA.
DR RefSeq; XP_001906020.1; XM_001905985.1.
DR AlphaFoldDB; B2ARA8; -.
DR STRING; 515849.B2ARA8; -.
DR GeneID; 6190536; -.
DR KEGG; pan:PODANSg3048; -.
DR VEuPathDB; FungiDB:PODANS_4_8090; -.
DR eggNOG; ENOG502SVCF; Eukaryota.
DR HOGENOM; CLU_424592_0_0_1; -.
DR OrthoDB; 1945096at2759; -.
DR Proteomes; UP000001197; Chromosome 4.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd00067; GAL4; 1.
DR CDD; cd04301; NAT_SF; 1.
DR Gene3D; 3.40.630.30; -; 1.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR021858; Fun_TF.
DR InterPro; IPR000182; GNAT_dom.
DR InterPro; IPR001138; Zn2Cys6_DnaBD.
DR PANTHER; PTHR47784; STEROL UPTAKE CONTROL PROTEIN 2; 1.
DR PANTHER; PTHR47784:SF4; ZN(II)2CYS6 TRANSCRIPTION FACTOR (EUROFUNG); 1.
DR Pfam; PF13673; Acetyltransf_10; 1.
DR Pfam; PF11951; Fungal_trans_2; 1.
DR SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
DR PROSITE; PS51186; GNAT; 1.
PE 4: Predicted;
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000001197}.
FT DOMAIN 434..642
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51186"
FT REGION 50..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 50..86
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 645 AA; 72651 MW; 403BEF2AF96594D7 CRC64;
MMRRRHKKSR RGFVLDHYTE TCSTADNGLQ CDETRPRCIN CTTVERECQY STPGYQSPSE
TSGSPAPVSQ QTPFQGSVST PASGAASDHS MPAPALSPEA PAPPMLDMRT FPHTGDMNGK
VDIVHMQLFY HYVTNHSVIY PFVDYDGRLK RIIVEVALRE PFLLHSILAM ASRHLSMTGT
GNTAYYHDLA IELQTQALSL FNSFDVEHFA QSIERRVPVF LFSAILGFHA LCDMLAYQDD
TYPSNLARLT GYFRLHRGIL SVMEGHWEDL KKTELSILFD HIVPRWYEIS DDDGGSDCDD
IKQRVRESPD LDDGQREAFF KVLKYLQWVF DATPNYRSRA HMLCSFAPFV DAVEAGKPEA
LAILAYFYVA LHFCRDIWLI GNSGQFLLTS VATHLNQLGP EWSAWLEKPC QMLRDVVCVC
VCVCVCTAAM GHDIVISRPS EADAGRIAEI HISAMGSNPL LHAQFPTPEG LQALRRFLEA
ETLDEIRDAV SGVLVSRDGP DGPVTGFVKW TSPSHPQDVK LERGDIVHLE GCCRRFLDEY
ASLAEQAKER SVRDEPPCYR LSFVCADPEY QGRGIGTQLT RKVLELAEED NLAVYLESTD
VAVSIYQRLG FRAIDSFEMQ IPGRQETERV VYKEVCMIWY PSGKR
//
