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Database: UniProt
Entry: G0SI27_CHATD
LinkDB: G0SI27_CHATD
Original site: G0SI27_CHATD 
ID   G0SI27_CHATD            Unreviewed;       625 AA.
AC   G0SI27;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 55.
DE   SubName: Full=Putative sequence-specific DNA binding protein {ECO:0000313|EMBL:EGS17097.1};
GN   ORFNames=CTHT_0074260 {ECO:0000313|EMBL:EGS17097.1};
OS   Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719)
OS   (Thermochaetoides thermophila).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Chaetomiaceae; Thermochaetoides.
OX   NCBI_TaxID=759272 {ECO:0000313|Proteomes:UP000008066};
RN   [1] {ECO:0000313|EMBL:EGS17097.1, ECO:0000313|Proteomes:UP000008066}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 1495 / CBS 144.50 / IMI 039719
RC   {ECO:0000313|Proteomes:UP000008066};
RX   PubMed=21784248; DOI=10.1016/j.cell.2011.06.039;
RA   Amlacher S., Sarges P., Flemming D., van Noort V., Kunze R., Devos D.P.,
RA   Arumugam M., Bork P., Hurt E.;
RT   "Insight into structure and assembly of the nuclear pore complex by
RT   utilizing the genome of a eukaryotic thermophile.";
RL   Cell 146:277-289(2011).
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC       ECO:0000256|PROSITE-ProRule:PRU00089}.
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DR   EMBL; GL988048; EGS17097.1; -; Genomic_DNA.
DR   RefSeq; XP_006697679.1; XM_006697616.1.
DR   AlphaFoldDB; G0SI27; -.
DR   STRING; 759272.G0SI27; -.
DR   GeneID; 18261464; -.
DR   KEGG; cthr:CTHT_0074260; -.
DR   eggNOG; KOG2294; Eukaryota.
DR   HOGENOM; CLU_437418_0_0_1; -.
DR   OrthoDB; 5385885at2759; -.
DR   Proteomes; UP000008066; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IEA:UniProt.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR   InterPro; IPR001766; Fork_head_dom.
DR   InterPro; IPR030456; TF_fork_head_CS_2.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR45881; CHECKPOINT SUPPRESSOR 1-LIKE, ISOFORM A-RELATED; 1.
DR   PANTHER; PTHR45881:SF5; FORK-HEAD DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00250; Forkhead; 1.
DR   SMART; SM00339; FH; 1.
DR   SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR   PROSITE; PS00658; FORK_HEAD_2; 1.
DR   PROSITE; PS50039; FORK_HEAD_3; 1.
PE   4: Predicted;
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|PROSITE-
KW   ProRule:PRU00089};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PROSITE-
KW   ProRule:PRU00089}; Reference proteome {ECO:0000313|Proteomes:UP000008066};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT   DOMAIN          253..360
FT                   /note="Fork-head"
FT                   /evidence="ECO:0000259|PROSITE:PS50039"
FT   DNA_BIND        253..360
FT                   /note="Fork-head"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00089"
FT   REGION          1..32
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          97..119
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          179..253
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          313..334
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          351..381
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          415..438
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        221..246
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        315..334
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        351..376
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        416..438
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   625 AA;  68189 MW;  34071C8287F2BAEA CRC64;
     MVSIEASNAS PPRQVSQTSA PTDPTTTVAT TTGEQIMATA DMESLQSHNS QVMRSYLSSH
     SAAQSSEPIW SVCFEQQQAN SSTDDCDNYA LHSSPVMSSL NPATDRTSAQ SSPRTWTTSP
     EQCNAINWEP APEYTTLDPQ FSYRPTSYPS RVPLVTSEEF HDIGRSHIET YPAGYYHNSP
     MDGAPPTPMS PCSSTLDLTA PDSIPSPPET AEDSDSRPAS KDKIISSNSK SGHKKNQSGD
     IKNGSSTDGS GKKEDEPYAQ LIYKAFLSTP RHAMTLQEIY QWFRENTDKG KDDSKGWQNS
     IRHNLSMNMA FTKRERRLST SEDSKDGKDS ASAKKSTEWY LEPWAVEQGV QSTTRYRKSN
     ASRRNATLSS TASRSHHHHS SIYRHHAYLS THPGSRKVVA ATAATAGLLA AGSLGTSTRL
     RGSSPRSTPL RSNSTSAGSL AATAYHHQLQ QIQHQQTQRY YQLLQQQHQL NAVHPVYVTR
     AAAAAGYFTR HDYEHQHHHE TYHQQAHQQH QQYPTDPQLF PATPGPLTPE PSAFGGDGML
     AMADIQAASI NASGIVTTTV TTQGLPATPS PSPYHPLMYE GYASEHRVAE PWTAAVTSQS
     TQALAAVVTC EADTTNGTTV TTGGY
//
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