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Database: UniProt
Entry: A0A369GJC1_9HYPO
LinkDB: A0A369GJC1_9HYPO
Original site: A0A369GJC1_9HYPO 
ID   A0A369GJC1_9HYPO        Unreviewed;       866 AA.
AC   A0A369GJC1;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=HTH APSES-type domain-containing protein {ECO:0000259|PROSITE:PS51299};
GN   ORFNames=CP532_1526 {ECO:0000313|EMBL:RDA85438.1};
OS   Ophiocordyceps camponoti-leonardi (nom. inval.).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Ophiocordyceps.
OX   NCBI_TaxID=2039875 {ECO:0000313|EMBL:RDA85438.1, ECO:0000313|Proteomes:UP000252748};
RN   [1] {ECO:0000313|EMBL:RDA85438.1, ECO:0000313|Proteomes:UP000252748}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BCC 80369 {ECO:0000313|EMBL:RDA85438.1,
RC   ECO:0000313|Proteomes:UP000252748};
RA   Kobmoo N., Wichadakul D., Arnamnart N., Rodriguez De La Vega R.C.,
RA   Luangsa-Ard J.-J., Giraud T.;
RT   "A genome scan of diversifying selection in the zombie-ant fungus
RT   Ophiocordyceps unilateralis complex supports a role of enterotoxins in
RT   coevolution and host-specificity.";
RL   Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RDA85438.1}.
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DR   EMBL; PDHP01000076; RDA85438.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A369GJC1; -.
DR   STRING; 2039875.A0A369GJC1; -.
DR   Proteomes; UP000252748; 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; PF13637; Ank_4; 1.
DR   Pfam; PF04383; KilA-N; 1.
DR   SMART; SM00248; ANK; 3.
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; 1.
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}; Conidiation {ECO:0000256|ARBA:ARBA00023321};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000252748};
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          39..145
FT                   /note="HTH APSES-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51299"
FT   REPEAT          436..468
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          579..611
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          202..330
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          350..389
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..23
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        218..281
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        294..318
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        350..375
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   866 AA;  95100 MW;  EFA9129FE0EDC961 CRC64;
     MPSSSQPSSQ NFSMSQSSQP RHAASFHHDY HAAAEGPKIY SASYSGVDVY EMEVNGIVVM
     RRRQDSCLNA TQILKVAGVD KGKRTKILEK EIQTGEHEKV QGGYGKYQGT WIKFERGVEV
     CRQYGVEELL RPLLTYDMGQ DGGVPGRGDL NTPTKEQAMA AQRKRMYNSG VDARPNNGLA
     GTFFKNISST ASHAVAAISK ARFDSPGPRG RSGPARVPSF SRQPSMANGD EFPGNSQQSF
     TSDYSQQGDH AYSSQQQQQQ QSQQPQPSQN SQHLQHSQHQ QHQQQHHQHQ EQQEQQQQHQ
     QQHQQHQQQQ QQQHQHAVAA ENEPPRKRQR VAVTPADSFG NYGQSVDLYS TAFPGSPTEP
     NESFMETQAT APSDRPTGED TRGPLAPMPY VKTPEIEAKR SMLMGLFLEP DASDATKHEM
     LRSLSPAELD MPIDQQSHTV LHWAATLARM SLLRALVEAG ASPYRVNTSG ETPLMRACLV
     TNSMDHGSFP ELLEVLGGTI EARDHKGRTV LHHITVTSAV KGRNAASKYY LESLLEWVVR
     HGSVPNSQIS QANGSSQLEA PKMGIARFMS EIVNAQDSSG DTALNIVARI GNRSIISQLL
     EVGADPWIAN RVGLRPVDFN IGVDIAGEPA NSNGEAVVES NGAPASGHRT RESSDGIVSS
     VTHLLNETGS EFQQELKAKQ ASLDALHVTL RAALGQLSEA RRNVDHLTAT AKKQQLSRQR
     VANLAHARED EQMRLMKEQS MSSQPNPSSS WETELSAMLE AAEESSATGP GGFHNEGLLP
     SSAMLKARIR AIEGRRDVTR KMVQALKGRS RELEVKYRRV VSLCTGVAHD EVDAVVDSLL
     KAVESEREEL DVGRVKRFLT GVAAVH
//
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