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Database: UniProt
Entry: Q2HDV6_CHAGB
LinkDB: Q2HDV6_CHAGB
Original site: Q2HDV6_CHAGB 
ID   Q2HDV6_CHAGB            Unreviewed;       843 AA.
AC   Q2HDV6;
DT   21-MAR-2006, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2006, sequence version 1.
DT   27-MAR-2024, entry version 73.
DE   RecName: Full=Helicase C-terminal domain-containing protein {ECO:0000259|PROSITE:PS51194};
GN   ORFNames=CHGG_01598 {ECO:0000313|EMBL:EAQ93363.1};
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:EAQ93363.1, 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; CH408029; EAQ93363.1; -; Genomic_DNA.
DR   RefSeq; XP_001220819.1; XM_001220818.1.
DR   AlphaFoldDB; Q2HDV6; -.
DR   STRING; 306901.Q2HDV6; -.
DR   GeneID; 4386422; -.
DR   VEuPathDB; FungiDB:CHGG_01598; -.
DR   eggNOG; KOG0389; Eukaryota.
DR   HOGENOM; CLU_000315_16_2_1; -.
DR   InParanoid; Q2HDV6; -.
DR   OrthoDB; 5482994at2759; -.
DR   Proteomes; UP000001056; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   CDD; cd18793; SF2_C_SNF; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR038718; SNF2-like_sf.
DR   InterPro; IPR049730; SNF2/RAD54-like_C.
DR   InterPro; IPR000330; SNF2_N.
DR   PANTHER; PTHR10799; SNF2/RAD54 HELICASE FAMILY; 1.
DR   PANTHER; PTHR10799:SF964; SWI_SNF-RELATED MATRIX-ASSOCIATED ACTIN-DEPENDENT REGULATOR OF CHROMATIN SUBFAMILY A CONTAINING DEAD_H BOX 1; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF00176; SNF2-rel_dom; 2.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001056}.
FT   DOMAIN          664..824
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          34..77
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          116..231
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          350..375
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        34..59
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        143..160
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   843 AA;  93868 MW;  5DCF88EBF4CDF5FE CRC64;
     MEFSSSPLAS HRRFHIEDDD DDLSVVTQSP YFTQPTQIIG RSASRAPNPT TSSPKSIVEV
     PASSPFRPQA AQQRGGRIAN LMAPAGTAFR APARQTLTIT KTAAKREFVM ISDDELDAPI
     YAGGDSSDDD EPSRGDIRPS SFQPKELKTS NSTTGSQPRA GKLPTRRRLV QGRRPGVVSP
     SSPVLKLSQH SPPRPQLIDL VSDDDADDGY KQSNASPRRG SSPVEDEEED SFDERVLNYL
     NTCDVMQLVA IANVKEDSAK LMVSRQPFDN LEEARKVTLS QKKRGKKSAK VSIGEDIVSA
     VRTYARALDD IDHIIAVCES QAESLKRDNL EMEYRPDRPA SQRLQISMTE KPDDSAQHGG
     LYETGGGAAA PAKAHGGLHD EAFPDIRAQL ALPVISLMCA IVEAWERTGQ SESNRPWPNV
     IVVPPSTLAN WAAEFKRFAP KLNVTLYQGS QAVRDEIAYE IKEDPSSHHF VEPSLFQAHF
     KNLEALFSQK VSLTAVSKGA LLHSERVARA RTILEPFILQ RRKEQVLQDL PPKTTKVVTC
     KMDPVQEAIY RSYERRFRKS DSQDANLRVK EGRENDTNNV WIQLRKSAIH PQLFRRFFKD
     RDVEKMAEVL MKRVSQAELK QPKLDHLTNE LKALSDFELH LWCRDYKCIK GYDLPDDSWT
     DCAKVKALLE LVRKYQANGD RALVFTRFAK VIEILGECLA SEGIEYLSLQ GNTDVSARQE
     LINEFNADES IPVFLLTTGS GGTGINLTAA NKVIIFDQSD NPQDDIQAEN RAHRLGQTRP
     VEIIRLISEG TVEELVYKAC EKKLELANKV VGWSTVEMTS GEMESAVKSQ LLQLAPSTPP
     NEG
//
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