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Database: UniProt/TrEMBL
Entry: G0S896_CHATD
LinkDB: G0S896_CHATD
Original site: G0S896_CHATD 
ID   G0S896_CHATD            Unreviewed;      1119 AA.
AC   G0S896;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   24-JAN-2024, entry version 53.
DE   SubName: Full=Histone deacetylase-like protein {ECO:0000313|EMBL:EGS21930.1};
GN   ORFNames=CTHT_0038040 {ECO:0000313|EMBL:EGS21930.1};
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:EGS21930.1, 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).
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DR   EMBL; GL988041; EGS21930.1; -; Genomic_DNA.
DR   RefSeq; XP_006694226.1; XM_006694163.1.
DR   AlphaFoldDB; G0S896; -.
DR   STRING; 759272.G0S896; -.
DR   GeneID; 18257842; -.
DR   KEGG; cthr:CTHT_0038040; -.
DR   eggNOG; KOG1343; Eukaryota.
DR   HOGENOM; CLU_001880_0_0_1; -.
DR   OMA; MTHGLTH; -.
DR   OrthoDB; 10780at2759; -.
DR   Proteomes; UP000008066; Unassembled WGS sequence.
DR   GO; GO:0010468; P:regulation of gene expression; IEA:UniProt.
DR   CDD; cd09998; HDAC_Hos3; 1.
DR   Gene3D; 3.40.800.20; Histone deacetylase domain; 1.
DR   InterPro; IPR000286; His_deacetylse.
DR   InterPro; IPR023801; His_deacetylse_dom.
DR   InterPro; IPR037138; His_deacetylse_dom_sf.
DR   InterPro; IPR023696; Ureohydrolase_dom_sf.
DR   PANTHER; PTHR47558; HISTONE DEACETYLASE HOS3; 1.
DR   PANTHER; PTHR47558:SF1; HISTONE DEACETYLASE HOS3; 1.
DR   Pfam; PF00850; Hist_deacetyl; 1.
DR   PRINTS; PR01270; HDASUPER.
DR   SUPFAM; SSF52768; Arginase/deacetylase; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000008066}.
FT   DOMAIN          257..589
FT                   /note="Histone deacetylase"
FT                   /evidence="ECO:0000259|Pfam:PF00850"
FT   REGION          1..99
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          598..639
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          762..857
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          950..1119
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        9..30
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        604..619
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        782..804
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        831..857
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        995..1065
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1080..1095
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1119 AA;  120755 MW;  9B1BAA3B8784CE79 CRC64;
     MARTSDAHAT STSRDDRQDH HNDLTESMEK LRINKTSPSA KTARPGRPGP VNSAAMNPLA
     ENLPNTPRPG SAMRTPLRSA SAAVKEPHSR SGTPTLVRKA SMTSLHSVAT TATTHGPSRR
     ASIAHISSVA KSRSGTSPLR DISPEPIIIP TPHSVASAHF KAELDIHHGP EPTRRVETVV
     ILQDACYGHR YSRPRASKSL LSTIVERPER IKACILGIAA AYVRLGERHQ DGAFPIHPDS
     DPATLPTIPF RIQKSFRRVP LTSQVVTNVH GVKWMEELRH MCDTAETKLA SGGKELERPD
     MDRGPNAGEP QAFHEGDLYL CEDSRDALEG ALGGVCDAVD IVFNPHGPQR AFVAIRPPGH
     HCSASHPSGF CWINNVHVGI MHAILAHGLT HAAIIDFDLH HGDGSQAIAW QHNTRTINSA
     KNAALWKKTS IGYFSLHDIN SFPCETGDEE KVRNASICID NAHGQTVWNV HLEPWKTESD
     FWTIYNTKYS ALLERARGYL KAQTEKLRAA GLNSKAAIFI SAGFDASQWE DPGMQRHNVN
     VPTDFYAKFT RDIVRIAAEE GTSVEGRIIS VLEGGYSDRA LCSGVFAHLC GLAGDGASNE
     PRSRPASVDF SQLPQGTPVP TSMPLRGRKD SSASERGSRR YEPSWWSAAE LERLEVTVAT
     PAPQPRVIRN ITPPTYSSPT QASIAKAKAP PRFPSAGLAS NGAEIRSLPP SSPCLDIPWT
     IATHELSKLL IPTDRQTNSC TAEELNAEAT RLRRERQIAL GTLAPPPQPA VPPTVPEEGR
     APTRTGLRER KPKVAEDAIG GDVESKSRRQ TVSGAGDLSG KMMRATSRRL SAASAVASSS
     EVPARPPSSG SVSVAGSNGL TVKKTRSTAT LRKEPSVASL KKDSTASTTA ARTTIKVKKT
     PAVNGTTSDK KDGGEEVDKI AGDMKRIKIT VIQKAQKDAR ERERLVREKL AQAQGQRMDV
     PASESIAEEE EEEQASTPQA QAPPAQPLPS PTPSLSLSPC SLAPGQTQSF LYQQQQVIHD
     QPSQVQTQEP GLASPPTSAP RTVPSSPASS VEPACSASIS PGTDGQPKRN KLPDWPPKPL
     NQQASLPPKP QPMPIKRENL PIFSSKGHIP FAPRPEEQK
//
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