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Database: UniProt
Entry: A0A0C3NK29_PISTI
LinkDB: A0A0C3NK29_PISTI
Original site: A0A0C3NK29_PISTI 
ID   A0A0C3NK29_PISTI        Unreviewed;       723 AA.
AC   A0A0C3NK29;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=HTH APSES-type domain-containing protein {ECO:0000259|PROSITE:PS51299};
GN   ORFNames=M404DRAFT_301863 {ECO:0000313|EMBL:KIN95718.1};
OS   Pisolithus tinctorius Marx 270.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Boletales; Sclerodermatineae; Pisolithaceae; Pisolithus.
OX   NCBI_TaxID=870435 {ECO:0000313|EMBL:KIN95718.1, ECO:0000313|Proteomes:UP000054217};
RN   [1] {ECO:0000313|EMBL:KIN95718.1, ECO:0000313|Proteomes:UP000054217}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Marx 270 {ECO:0000313|EMBL:KIN95718.1,
RC   ECO:0000313|Proteomes:UP000054217};
RG   DOE Joint Genome Institute;
RA   Kuo A., Kohler A., Costa M.D., Nagy L.G., Floudas D., Copeland A.,
RA   Barry K.W., Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A.,
RA   Lipzen A., Lundell T., Morin E., Murat C., Sun H., Tunlid A., Henrissat B.,
RA   Grigoriev I.V., Hibbett D.S., Martin F., Nordberg H.P., Cantor M.N.,
RA   Hua S.X.;
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000054217}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Marx 270 {ECO:0000313|Proteomes:UP000054217};
RG   DOE Joint Genome Institute;
RG   Mycorrhizal Genomics Consortium;
RA   Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA   Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA   Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H., Tunlid A.,
RA   Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT   "Evolutionary Origins and Diversification of the Mycorrhizal Mutualists.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; KN832062; KIN95718.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0C3NK29; -.
DR   STRING; 870435.A0A0C3NK29; -.
DR   HOGENOM; CLU_009666_2_0_1; -.
DR   InParanoid; A0A0C3NK29; -.
DR   OrthoDB; 3019647at2759; -.
DR   Proteomes; UP000054217; Unassembled WGS sequence.
DR   GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IEA:UniProt.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IEA:UniProt.
DR   Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR   Gene3D; 3.10.260.10; Transcription regulator HTH, APSES-type DNA-binding domain; 1.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   InterPro; IPR036887; HTH_APSES_sf.
DR   InterPro; IPR018004; KilA/APSES_HTH.
DR   InterPro; IPR003163; Tscrpt_reg_HTH_APSES-type.
DR   PANTHER; PTHR43828; ASPARAGINASE; 1.
DR   PANTHER; PTHR43828:SF15; TRANSCRIPTION FACTOR MBP1; 1.
DR   Pfam; PF00023; Ank; 1.
DR   Pfam; PF12796; Ank_2; 1.
DR   Pfam; PF04383; KilA-N; 1.
DR   PRINTS; PR01415; ANKYRIN.
DR   SMART; SM00248; ANK; 2.
DR   SMART; SM01252; KilA-N; 1.
DR   SUPFAM; SSF48403; Ankyrin repeat; 1.
DR   SUPFAM; SSF54616; DNA-binding domain of Mlu1-box binding protein MBP1; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 2.
DR   PROSITE; PS50088; ANK_REPEAT; 2.
DR   PROSITE; PS51299; HTH_APSES; 1.
PE   4: Predicted;
KW   ANK repeat {ECO:0000256|ARBA:ARBA00023043, ECO:0000256|PROSITE-
KW   ProRule:PRU00023}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054217};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          1..93
FT                   /note="HTH APSES-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51299"
FT   REPEAT          251..283
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          370..402
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REGION          86..212
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          488..522
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        141..165
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        177..199
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   723 AA;  80149 MW;  CB8B85630D997069 CRC64;
     MCKGVAVMRR RSDSWLNATQ ILKVAGFDKP QRTRILEREV QKGEHEKVQG GYGKYQGTWI
     PLDRSLTLAR QYNCDTVLRP IIEFQPAAKS PPPAPKHLAA TATTAKPPRR TAGPDASALA
     SARSRRQLEG GEDSDQEVLS EPASEDGSMT SSPSRRSSSS RTPSPIDEGY EAAGASGDRS
     HADRRKGTRH HHDRPDNAIG IDDLSQANDA NDPRAYSDQI LEYFISDTNQ IPPILISPPA
     DFDPNMAIDD DGHTALHWAS AMGRLRIVKL LLTAGAEIFK VNKAGQTALM RSVMFANNYD
     VRKFPELYEL LHRSTLNIDN YNRTVFHHIV DVAMSKGKTH AARYYMETVL NRLADYPKEL
     ADVINFQDED GETALTMAAR CRSKRLVKLL IDHGADPKIR NRDGKSTEDY ILEDERFRSS
     PGPISRLSAM SFRNAQAALP AGVPAATLVS GERPLVHHSL AGQKASTRCV NDITNMLDSL
     AASFDRELQE KERDVTQAQV LLQNIQQEIL ESHRAVNQLR TRAEGLQVAK AMFEKLENQL
     LDKMGRRYRL GWEKWVKDEE DREKSVRDAA GGELKITAAM VPYRAADDME VDGTTELGKD
     KGKGKRKALP QEENISDLLT LYSDVPSDPE ALHSTCEALR EELGHHRKRR KELFDELTAF
     QAEAGTRGKM SEYRRLIGAG CGGVPPSEVD NLVGVLLETL ESEESNTSAV WGGMKPATTV
     PVG
//
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