ID Q2GZ16_CHAGB Unreviewed; 798 AA.
AC Q2GZ16;
DT 21-MAR-2006, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2006, sequence version 1.
DT 27-MAR-2024, entry version 87.
DE RecName: Full=HTH APSES-type domain-containing protein {ECO:0000259|PROSITE:PS51299};
GN ORFNames=CHGG_05230 {ECO:0000313|EMBL:EAQ88611.1};
OS Chaetomium globosum (strain ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 /
OS NRRL 1970) (Soil fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Chaetomiaceae; Chaetomium.
OX NCBI_TaxID=306901 {ECO:0000313|EMBL:EAQ88611.1, ECO:0000313|Proteomes:UP000001056};
RN [1] {ECO:0000313|Proteomes:UP000001056}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 / NRRL 1970
RC {ECO:0000313|Proteomes:UP000001056};
RX PubMed=25720678; DOI=10.1128/genomeA.00021-15;
RA Cuomo C.A., Untereiner W.A., Ma L.-J., Grabherr M., Birren B.W.;
RT "Draft genome sequence of the cellulolytic fungus Chaetomium globosum.";
RL Genome Announc. 3:E0002115-E0002115(2015).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; CH408032; EAQ88611.1; -; Genomic_DNA.
DR RefSeq; XP_001224444.1; XM_001224443.1.
DR AlphaFoldDB; Q2GZ16; -.
DR STRING; 306901.Q2GZ16; -.
DR GeneID; 4393105; -.
DR VEuPathDB; FungiDB:CHGG_05230; -.
DR eggNOG; ENOG502QPWC; Eukaryota.
DR HOGENOM; CLU_009666_1_1_1; -.
DR InParanoid; Q2GZ16; -.
DR OMA; RGVEVCR; -.
DR OrthoDB; 3019647at2759; -.
DR Proteomes; UP000001056; 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 GO; GO:0048315; P:conidium formation; IEA:UniProtKB-KW.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
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:SF3; REGULATORY PROTEIN SWI6; 1.
DR Pfam; PF00023; Ank; 1.
DR Pfam; PF13637; Ank_4; 1.
DR Pfam; PF04383; KilA-N; 1.
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 Conidiation {ECO:0000256|ARBA:ARBA00023321};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000001056};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Sporulation {ECO:0000256|ARBA:ARBA00022969};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT DOMAIN 13..120
FT /note="HTH APSES-type"
FT /evidence="ECO:0000259|PROSITE:PS51299"
FT REPEAT 351..383
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 491..523
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REGION 171..272
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 527..565
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 678..698
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 600..651
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 187..234
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 546..565
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 678..697
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 798 AA; 87874 MW; FF1A0E28AFD2FAC8 CRC64;
MPQKAQNDTD MGIYSAVYSG VNVYEMEVNN VAVMRRQTDG WLNATQILKV AGVDKGRRTK
ILEKEIQTGE HEKVQGGYGK YQGTWIPFER GFEVCRQYGV EEVLMRLLTH KRGQEGGIAD
VDTPTKEQAM AAQRKRMYNA SSQENRANGL SGTFFKNISS TASHAINAIS KARFDSPGPR
NRNGPSRAPS FHRQSSMQDS SNDFPPNSQQ SFVSDYNHAD SAFGSQTTQV APGDNEQPPR
KRQRVLTPAN SFGGLTPTYP QLDGYAANYP GSPTEPNESF IYSQAGVHLE QEPNYAPGPL
RPLPYDMSPE AEAKRSMLMG LFMDPSGPDE AKRNVLRNMI PQELDAPIDT QSHTALHWAA
TLSRMPLLRA LIEAGASPFR VNSSGETALM RACIVTNSMD HNSFPELLDV LGVTIDVRDD
KGRTVLHHIA VTSAVKGRNS ASRYYLESLL EWVVRQGSAP SSQNIPGSLS APAKMGIGRF
MSEIVNAQDS SGDTALNIAA RIGNRSIVSQ LLEVGADPNI ANRAGLRPVD FGIGTDAEDN
RNGEVSDKNG ASQGGSNQKN KENSDEVVNS ITHLITESSS LFQTELKKKQ ESIDTLHSSL
RTTSAQVGEA RRTLESLQEK LKAQQLARQK VVNLKRACQE EEYELLQLEQ RHGRLDIDSA
NAWEIDLEMV LDGIAAANTQ QQQQPQQQPQ QQAPTDNGYF HGLAEEHLAR LPSSAVLRAR
VNALREQSGQ THQAVEALQA RSKDRELGYR RLVALCTRRP ESEVDMLLDT LTRAVESEKG
ELEITRVRRF LGGVEGVA
//
