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Database: UniProt
Entry: K5WXX5_AGABU
LinkDB: K5WXX5_AGABU
Original site: K5WXX5_AGABU 
ID   K5WXX5_AGABU            Unreviewed;      1630 AA.
AC   K5WXX5;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   27-MAR-2024, entry version 51.
DE   RecName: Full=Histone deacetylase interacting domain-containing protein {ECO:0000259|SMART:SM00761};
GN   ORFNames=AGABI1DRAFT_46078 {ECO:0000313|EMBL:EKM75658.1};
OS   Agaricus bisporus var. burnettii (strain JB137-S8 / ATCC MYA-4627 / FGSC
OS   10392) (White button mushroom).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Agaricineae; Agaricaceae; Agaricus.
OX   NCBI_TaxID=597362 {ECO:0000313|EMBL:EKM75658.1, ECO:0000313|Proteomes:UP000008493};
RN   [1] {ECO:0000313|Proteomes:UP000008493}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JB137-S8 / ATCC MYA-4627 / FGSC 10392
RC   {ECO:0000313|Proteomes:UP000008493};
RX   PubMed=23045686; DOI=10.1073/pnas.1206847109;
RA   Morin E., Kohler A., Baker A.R., Foulongne-Oriol M., Lombard V., Nagy L.G.,
RA   Ohm R.A., Patyshakuliyeva A., Brun A., Aerts A.L., Bailey A.M.,
RA   Billette C., Coutinho P.M., Deakin G., Doddapaneni H., Floudas D.,
RA   Grimwood J., Hilden K., Kuees U., LaButti K.M., Lapidus A., Lindquist E.A.,
RA   Lucas S.M., Murat C., Riley R.W., Salamov A.A., Schmutz J., Subramanian V.,
RA   Woesten H.A.B., Xu J., Eastwood D.C., Foster G.D., Sonnenberg A.S.,
RA   Cullen D., de Vries R.P., Lundell T., Hibbett D.S., Henrissat B.,
RA   Burton K.S., Kerrigan R.W., Challen M.P., Grigoriev I.V., Martin F.;
RT   "Genome sequence of the button mushroom Agaricus bisporus reveals
RT   mechanisms governing adaptation to a humic-rich ecological niche.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:17501-17506(2012).
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC       ECO:0000256|PROSITE-ProRule:PRU00810}.
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DR   EMBL; JH971410; EKM75658.1; -; Genomic_DNA.
DR   RefSeq; XP_007333674.1; XM_007333612.1.
DR   STRING; 597362.K5WXX5; -.
DR   GeneID; 18829626; -.
DR   KEGG; abp:AGABI1DRAFT46078; -.
DR   eggNOG; KOG0069; Eukaryota.
DR   eggNOG; KOG4204; Eukaryota.
DR   HOGENOM; CLU_001360_2_2_1; -.
DR   InParanoid; K5WXX5; -.
DR   OMA; GRFQTWL; -.
DR   OrthoDB; 199155at2759; -.
DR   Proteomes; UP000008493; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR   GO; GO:0003714; F:transcription corepressor activity; IEA:InterPro.
DR   CDD; cd05301; GDH; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR   Gene3D; 1.20.1160.11; Paired amphipathic helix; 3.
DR   InterPro; IPR006139; D-isomer_2_OHA_DH_cat_dom.
DR   InterPro; IPR029753; D-isomer_DH_CS.
DR   InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR   InterPro; IPR013194; HDAC_interact_dom.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR003822; PAH.
DR   InterPro; IPR036600; PAH_sf.
DR   InterPro; IPR039774; Sin3-like.
DR   InterPro; IPR031693; Sin3_C.
DR   PANTHER; PTHR12346:SF0; SIN3A, ISOFORM G; 1.
DR   PANTHER; PTHR12346; SIN3B-RELATED; 1.
DR   Pfam; PF00389; 2-Hacid_dh; 1.
DR   Pfam; PF02826; 2-Hacid_dh_C; 1.
DR   Pfam; PF02671; PAH; 3.
DR   Pfam; PF08295; Sin3_corepress; 1.
DR   Pfam; PF16879; Sin3a_C; 1.
DR   SMART; SM00761; HDAC_interact; 1.
DR   SUPFAM; SSF52283; Formate/glycerate dehydrogenase catalytic domain-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   SUPFAM; SSF47762; PAH2 domain; 3.
DR   PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 1.
DR   PROSITE; PS51477; PAH; 2.
PE   4: Predicted;
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PROSITE-
KW   ProRule:PRU00810}; Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008493}.
FT   DOMAIN          876..975
FT                   /note="Histone deacetylase interacting"
FT                   /evidence="ECO:0000259|SMART:SM00761"
FT   REGION          378..491
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          674..731
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1174..1210
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1222..1241
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1574..1630
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        469..491
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        679..694
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1183..1204
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1582..1601
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1630 AA;  182896 MW;  C44E1C4D2087461E CRC64;
     MSKPASFVQP IPNSNAQTNR LTTINSHLRN LPKIVVTRDL GPEASALIQP KDSFEIIQWS
     ENRACGRDWI LKNVPGAVAL VVTVVDKILT LVLVAGSNLK IVSTMSVGYE HLDVQAILSR
     GIRIGYTPEV LTDAVADICV MLALMAGRNV RETMHIVDDG KWPSFGWAPF LFCGPQLGAS
     PVSPRRTAGF IGFGRIAQAT LTRLIPFGIT DCIYSKSSGS KPDLDRDEAL RKTMGLQSLR
     CVDLDELARE SDAVFVLAPG GAPTYHVVNE EFLRKMKKTA ILVNGARGSL VDSDALAKAL
     REKWIWGAGV DVVEGEPHIT PDHPLVRERR CAVLPHIASA TTETRVGMAT LAIENMMAVL
     TGKPIPKELL PHKLAGPAAV LSSSPPSTPM DTDDSKQMAL DDVPPGLPHP SRGPSPSRLG
     TPRRHPDQVT ASESTYTAGE KDVEMGRPSA APPDIPPNPS DPQPSIAMLV DDPQSSRRQS
     PIDPQSYPSI DRPLNVTDAL SYLDAVKIQF HDQPDVYNQF LDIMKEFKNE LIDTPGVIKR
     VSQLFNGHSA LIQGFNTFLP VGYRIECSTD ANDSSYITVT TPTGTMMQTT NNGPGRGPIF
     GTYDGRAIEP AVQYVQKIKN RCDPETYRQF LDILSRYHHK PETIDEEEVS RQIARLFKDA
     PDLRADFRVF MPEQSRQLLD ESPPRTSPRT GTPLNEARNK RKLDAVASSM SLPPKRKRRA
     PEKETVPSKP AQVVAVSMKI PPSAERTTLG YGNKNIAGPS SPHMVHSQLP PGPRPPLPVD
     ETHFFERVKR ALDSRDTYNE FLKVVNLFTQ DFIDTARLVK ESKHFLGDGD LYRQFRDILG
     WDELKEREYF MAEFQNNWTK PTPVQLPSRV SRIDPSVKYG SYRRLSASEA NVLCTGRDEM
     CRSVLNDEWV SHPTWSSEDS GFISHKKNIY EEALHRSEEE RHEYDFHIEA ITRTISLLEP
     LHHKIAQLSA EDRANFKLKP HIGGSWKPIH TRVIKKIYGR DLGLEVISSM QDSPVLAIPV
     VLKRLKQKED EWKRSQREWN KVWREVDARN YTKSLDHQSI IFKTMDKKAI TTKALVNQIE
     GAREEQMAKR ASLIDPLFAR TRQRHQLEYV IDDIRIVQDA LKLTFSFLDR TQGQINFAER
     KRIEGFLRSF VPLFFILDPV TFNTAFLIHE TNESDGSEDI TDDVETSSVA SGSRNSSRSR
     RGGNISNGGD LRKKLLKSEQ AKLTGRKTRA QEAAASPAVS RLASPALEND DSAAQAAIAN
     KRKRNIFFTN TTFYALLRLI ELLYSRLYSF RDLATKLGKE KPDQKFPTKE AISAGMANQA
     HDAIANFGER AKNPETFYEL LLVSCERLFD NEIEQHAFED QMRFMFGIKE AHRIFNVDKV
     IGAIIKQVQA IVSDTRSQEL LENLKRERSV ASFTSQDQIN SRRSAEKILG PDENLFRVDW
     LSDSKMMTIQ LIGKDDSSFD DAEVLTGRWQ AYIDSYVSSE NTAGVSQTRV RYPYLRRNIP
     AKVRDIQPEA VTQDGQEIKV CVRTYRLFFV PGKEDFLWKV RSKEEMEEAA ANLTKRNILR
     KQWLEKLRMT PAAFPKSPVR TDKTPTPLSS TTSNITGPPA VTETESEPKG ITAESIPPPH
     QPPVAETTTV
//
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