ID A0A0D0AP62_9AGAM Unreviewed; 746 AA.
AC A0A0D0AP62;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=HTH APSES-type domain-containing protein {ECO:0000259|PROSITE:PS51299};
GN ORFNames=CY34DRAFT_811511 {ECO:0000313|EMBL:KIK36147.1};
OS Suillus luteus UH-Slu-Lm8-n1.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Boletales; Suillineae; Suillaceae; Suillus.
OX NCBI_TaxID=930992 {ECO:0000313|EMBL:KIK36147.1, ECO:0000313|Proteomes:UP000054485};
RN [1] {ECO:0000313|EMBL:KIK36147.1, ECO:0000313|Proteomes:UP000054485}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UH-Slu-Lm8-n1 {ECO:0000313|EMBL:KIK36147.1,
RC ECO:0000313|Proteomes:UP000054485};
RG DOE Joint Genome Institute;
RA Kuo A., Ruytinx J., Rineau F., Colpaert J., Kohler A., Nagy L.G.,
RA Floudas D., Copeland A., Barry K.W., Cichocki N., Veneault-Fourrey C.,
RA LaButti K., Lindquist E.A., Lipzen A., Lundell T., Morin E., Murat C.,
RA Sun H., Tunlid A., Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.,
RA Nordberg H.P., Cantor M.N., Hua S.X.;
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000054485}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UH-Slu-Lm8-n1 {ECO:0000313|Proteomes:UP000054485};
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.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KN835555; KIK36147.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D0AP62; -.
DR STRING; 930992.A0A0D0AP62; -.
DR HOGENOM; CLU_009666_2_0_1; -.
DR InParanoid; A0A0D0AP62; -.
DR OrthoDB; 3019647at2759; -.
DR Proteomes; UP000054485; 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:UP000054485};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 6..112
FT /note="HTH APSES-type"
FT /evidence="ECO:0000259|PROSITE:PS51299"
FT REPEAT 274..306
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 393..425
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REGION 108..131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 165..235
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 515..549
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 166..191
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 195..219
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 746 AA; 82377 MW; 3BE0CFBF33B61043 CRC64;
MPEGQIFKAT YSGIPVFEMM CKGVAVMRRR ADSWLNATQI LKVAGFDKPQ RTRVLEREVQ
KGEHEKVQGG YGKYQGTWIP LERGLALAKQ YNCEAALRPI IDFQPAAKSP PLAPKHLVST
STAARPPRRA AAAAEAAAAL AAAARSRRNV EPPVESDHEI LSVHASEDGS MTSSPSRGSS
SSRTPSPIGN KFGSADASKD RRSGNRRKPP QRHIDERYDD EGSEEEPAQP NGATDPRAYA
DQILEYFISD SNQVPQVLIS PPPDFDPNTA IDDDGHTALH WASAMGRLRI VKLLITAGAE
IFKVNKAGQT ALMRSVMFAN NYDVRKFPEL YELLHRSTLN IDNYNRTVFH HIVDVAMSKG
KTHAARYYME TVLNRLADYP KELADVINFQ DEDGETALTM AARCRSKRLV KLLIDHGANP
KIINNDGKST EDYILEDERF RSSPGPTSRL SSMSFRNAQA TLGPTTSNAM TLAYPMNGDK
PPLHHSVAGQ KASTRCVNDI TSMLDSLASS FDRELQEKER DMTQAHALLQ NIQQEILESH
RAVNQLKTKA EGLQLAKSVL GDLEGRLLDK MGRRYRLGWE KWVKDEENRE MSIRDAADGE
LRITAATVPY RTDDDIEEVA EPGKDKGKGK RKALPQEEDI SDLLALYAEV PTDPEALRVA
CDAVREEIGL HRKRRKEMFD ELASFQAEAG TGGRMAEYRK LIGAGCGGVQ PSEVDNVIGM
LLETLESEEP SASSTAWSGL KAGPMG
//
