ID   B2B358_PODAN            Unreviewed;       865 AA.
AC   B2B358;
DT   20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT   20-MAY-2008, sequence version 1.
DT   27-MAR-2024, entry version 99.
DE   SubName: Full=Podospora anserina S mat+ genomic DNA chromosome 6, supercontig 2 {ECO:0000313|EMBL:CAP71544.1};
DE   Flags: Fragment;
GN   ORFNames=PODANS_6_990 {ECO:0000313|EMBL:CAP71544.1};
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:CAP71544.1};
RN   [1] {ECO:0000313|EMBL:CAP71544.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S mat+ {ECO:0000313|EMBL:CAP71544.1};
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:CAP71544.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=S mat+ {ECO:0000313|EMBL:CAP71544.1};
RA   Genoscope - CEA;
RL   Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000256|ARBA:ARBA00004286}.
CC   -!- SIMILARITY: Belongs to the HIBADH-related family.
CC       {ECO:0000256|ARBA:ARBA00009080}.
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DR   EMBL; CU638744; CAP71544.1; -; Genomic_DNA.
DR   RefSeq; XP_001910409.1; XM_001910374.1.
DR   AlphaFoldDB; B2B358; -.
DR   GeneID; 6194668; -.
DR   KEGG; pan:PODANSg7447; -.
DR   VEuPathDB; FungiDB:PODANS_6_990; -.
DR   HOGENOM; CLU_344833_0_0_1; -.
DR   OrthoDB; 1121581at2759; -.
DR   GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:InterPro.
DR   GO; GO:0042054; F:histone methyltransferase activity; IEA:InterPro.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   CDD; cd19473; SET_SUV39H_DIM5-like; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   Gene3D; 2.170.270.10; SET domain; 1.
DR   InterPro; IPR002204; 3-OH-isobutyrate_DH-rel_CS.
DR   InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR   InterPro; IPR013328; 6PGD_dom2.
DR   InterPro; IPR006115; 6PGDH_NADP-bd.
DR   InterPro; IPR029154; HIBADH-like_NADP-bd.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR003616; Post-SET_dom.
DR   InterPro; IPR007728; Pre-SET_dom.
DR   InterPro; IPR001214; SET_dom.
DR   InterPro; IPR046341; SET_dom_sf.
DR   PANTHER; PTHR43060; 3-HYDROXYISOBUTYRATE DEHYDROGENASE-LIKE 1, MITOCHONDRIAL-RELATED; 1.
DR   PANTHER; PTHR43060:SF15; 3-HYDROXYISOBUTYRATE DEHYDROGENASE-LIKE 1, MITOCHONDRIAL-RELATED; 1.
DR   Pfam; PF14833; NAD_binding_11; 1.
DR   Pfam; PF03446; NAD_binding_2; 1.
DR   Pfam; PF05033; Pre-SET; 1.
DR   Pfam; PF00856; SET; 1.
DR   SMART; SM00468; PreSET; 1.
DR   SMART; SM00317; SET; 1.
DR   SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 2.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   SUPFAM; SSF82199; SET domain; 1.
DR   PROSITE; PS00895; 3_HYDROXYISOBUT_DH; 1.
DR   PROSITE; PS50868; POST_SET; 1.
DR   PROSITE; PS50867; PRE_SET; 1.
DR   PROSITE; PS50280; SET; 1.
PE   3: Inferred from homology;
KW   Chromosome {ECO:0000256|ARBA:ARBA00022454};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          604..691
FT                   /note="Pre-SET"
FT                   /evidence="ECO:0000259|PROSITE:PS50867"
FT   DOMAIN          694..829
FT                   /note="SET"
FT                   /evidence="ECO:0000259|PROSITE:PS50280"
FT   DOMAIN          849..865
FT                   /note="Post-SET"
FT                   /evidence="ECO:0000259|PROSITE:PS50868"
FT   REGION          497..516
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:CAP71544.1"
SQ   SEQUENCE   865 AA;  93728 MW;  11F3546A7F36E2EA CRC64;
     YCMQSLGRVS SHQHQLTPRV PQLLHFEPNI TTMADQKPPV AFIGLGAMGF GMATHLIKQG
     YPVTGFDVWA PTLKRFEEAG GSTATTPAEA VLNKEHVVVM VATAQQAQTV LLDGPNAAVP
     KLPQGAVVLL CSTVPCDYVQ ALQVQLNSIG RSDILLIDSP VSGGAARAAD GTLSIMAGMS
     AAALEKGRPL LAELSDPAKL YIVEGGIGAG SNMKMVHQVL AANQILGASE VMGFAERLGL
     DLAKAQKAVL ESDAWNFMFE HRTPRIFTEF QPVASAVQII VKDTSIITSE GRRSSFATPM
     TSAAEQIYFT AVGRGWAMDD DSSLVRLYTE GNGKVGPVYG TAESEEDKTA LVLALMRGIL
     LCAAAESLAF AHTVSLDLDQ VLDLCVNAAG GSKVLEKLGP AIIKELGGAG DASSGESSLE
     DVFSGLSAAV EEAQRIKTPL YLGTQALSIL QRVTQSKGTG SAGVVVKEGY SPHQQNKPAC
     PTLYCSIPIP APSRVFSSQH ASHDQISPRA SSTPVEQPHQ LPKMEEAMKQ HFFHHGKPDT
     DPSEAEKCHW CQIRSFKTHK KLPITIVNEA KGDERKEVLN PDFKFIDHSI PSDDVPIAGA
     SFRTGCNCAD DEQCMYSTCE CLDEMAPDSD EDMSDAPPAR GRRIQKFQYY HSGTKAGLLK
     SRILDSREPI YECHDGCSCS KNCPNRVVER GRTVPLQIFR TKNRGWGVKC PVDIKKGQFV
     DKYLGEIITS EEANRRRAES TVSDKKDVYL FALDKFSDPD SPDPLLRAPP FEVDGEWMSG
     PTRFINHSCD PNMRIFARVG DAVDKHVHDL ALFAIRDIPA GEELTFDYVD GGLAEEDAGG
     LVPDDKKKDM TKCLCGTKKC RGFLW
//