ID G0S6C0_CHATD Unreviewed; 1886 AA.
AC G0S6C0;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 24-JAN-2024, entry version 57.
DE SubName: Full=Helicase-like protein {ECO:0000313|EMBL:EGS20784.1};
GN ORFNames=CTHT_0026210 {ECO:0000313|EMBL:EGS20784.1};
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:EGS20784.1, 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).
RN [2] {ECO:0007829|PDB:6G7E}
RP X-RAY CRYSTALLOGRAPHY (3.21 ANGSTROMS) OF 1-1836.
RX PubMed=30289385; DOI=10.7554/eLife.37774;
RA Butryn A., Woike S., Shetty S.J., Auble D.T., Hopfner K.P.;
RT "Crystal structure of the full Swi2/Snf2 remodeler Mot1 in the resting
RT state. .";
RL Elife 7:e37774-e37774(2018).
RN [3] {ECO:0007829|PDB:7Z7N, ECO:0007829|PDB:7Z8S}
RP STRUCTURE BY ELECTRON MICROSCOPY (2.80 ANGSTROMS) OF 1-1837.
RX PubMed=37106137; DOI=10.1038/s41594-023-00966-0;
RA Woike S., Eustermann S., Jung J., Wenzl S.J., Hagemann G., Bartho J.D.,
RA Lammens K., Butryn A., Herzog F., Hopfner K.-P.;
RT "Structural basis for TBP displacement from TATA box DNA by the Swi2/Snf2
RT ATPase Mot1.";
RL Nat. Struct. Mol. Biol. 30:640-649(2023).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; GL988041; EGS20784.1; -; Genomic_DNA.
DR RefSeq; XP_006693080.1; XM_006693017.1.
DR PDB; 6G7E; X-ray; 3.21 A; B=1-1836.
DR PDB; 7Z7N; EM; 5.10 A; E=1-1886.
DR PDB; 7Z8S; EM; 3.90 A; E=1-1886.
DR PDB; 7ZB5; EM; 2.80 A; E/H=1-1837.
DR PDB; 7ZKE; EM; 3.60 A; E=1-1886.
DR PDBsum; 6G7E; -.
DR SMR; G0S6C0; -.
DR STRING; 759272.G0S6C0; -.
DR GeneID; 18256659; -.
DR KEGG; cthr:CTHT_0026210; -.
DR eggNOG; KOG0392; Eukaryota.
DR HOGENOM; CLU_000315_1_0_1; -.
DR OMA; WYSDIAC; -.
DR OrthoDB; 180798at2759; -.
DR Proteomes; UP000008066; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0017025; F:TBP-class protein binding; IEA:InterPro.
DR CDD; cd17999; DEXHc_Mot1; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 2.
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; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR044972; Mot1.
DR InterPro; IPR044078; Mot1_ATP-bd.
DR InterPro; IPR022707; Mot1_central_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR000330; SNF2_N.
DR PANTHER; PTHR36498; TATA-BINDING PROTEIN-ASSOCIATED FACTOR 172; 1.
DR PANTHER; PTHR36498:SF1; TATA-BINDING PROTEIN-ASSOCIATED FACTOR 172; 1.
DR Pfam; PF12054; DUF3535; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 1: Evidence at protein level;
KW 3D-structure {ECO:0007829|PDB:6G7E, ECO:0007829|PDB:7Z7N};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Helicase {ECO:0000313|EMBL:EGS20784.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000008066};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 1309..1482
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1654..1805
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 76..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 176..264
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 674..731
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 192..209
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 687..703
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 704..731
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1886 AA; 210306 MW; 22E385CB8BC98C29 CRC64;
MATRLDRLVT ILETGSTRLI RDTAVNQLAD WQKQHPEELF NLLSRVVPYL RHKDWETRTT
AAKAIGKIIE NAPLYDPNAG QDEAAPEPTN GSFEVKKEEE KDVLEQDNFF RLESLDVATI
VKYGRPLLRG GPVDYNLAAL DPQKRLAHLK KTLNGRLGLL GRVFEDEEMP VEQIASPITP
NDAAGANGVG RQDGASNDNQ SQAIDESKMS ARQLNVLKRK RKREAQKAAQ GKSGFGDLSL
RRSTTAGSDA FGEDTPMPDA DSKKNKLAEY FSLDRPENTE EDTKIVSEFK GPVLPIKSEI
EADDSLEGAE WPFERLCEFL KVDLFDPQWE TRHGAAMGLR EVIRVHGAGA GRRRGKTRKE
NNDLNRQWLD DLAYRLLCVL MLDKFTDYSS DTSVAPIRET VGQTLGAVLR HISVESVHAI
YRLLYCMVTQ EDLPSEQNMW AVCHGGMVGL RYVVAVRKDL LLQDGDMIDG VVRCVMQGLG
DIDDDVRSVS AATLIPMAKE FVMMRRSALD SLINIVWESL SNLGDDLSAS TGKIMDLLAT
LCSFPEVLEA MKVSASQDEE RSFTLLVPRL YPFLRHTITS VRLAVLKALM TFANLGGETS
QGWLNGRILR LIFQNIIVER DQDTLNMSLE LWTTLVRRLA ARDPAILADE FEAHAEPMMQ
LALHPIGVPR HPIPMNPALF QKPSGGTYSL PGASQTNSRR SSPPEGERAT KRRRKSTKAE
DVAPSTHTHD VDGHMIQGEV DLVGVDVLIR SRISAAKAMG LIMSFIPTPR LASYDTAVLQ
ALSSPYASTQ LAAAMVIDEY AKNCSTPEVA SRFIEPLQKI IDLERPSHYR DLVTYVQRVR
SASQQLINLF RDHGKVSQGK LPTLAVVVQG EPEAGPGAFS IANAEKVVNE DFERLKRLMA
PGQRLIALPQ LNEAREQTVE VIEEAKAAKE ARDARIKAAA ACALVAMKVL PKKPSPLIKA
IMDSIKTEEN QELQSRSAAT IARLVQLFTE SGRRGPAEKV VANLVKFSCV EVAETPEFPI
HAHKTNVILS MQKEEDRVDH PDAVKYAREA KAARITRRGA KEALEILSKN FGAELLERVP
TLRTFMEEPL VRAFSGDLPP EARDPENAFG QEIVDAMSVI RTMTPTLHPA LHPFVMQQVP
LVIKALRSDL SVFRYMAAKC MATICSVITV DGMTALVEKV LPSINNPLDL SFRQGAIEVI
YHLIAVMGDA ILPYVIFLIV PVLGRMSDSD NQIRLIATTS FATLVKLVPL EAGIPDPPGL
SEELLKGRDR ERTFIAQLLD PKKIEPFKIP VAIKAELRSY QQEGVNWLAF LNKYHLHGIL
CDDMGLGKTL QTICIVASDH HQRAEEFART GAPEVRKLPS LIICPPTLSG HWQQEIKTYA
PFLTVTAYVG SPAERRAMKD SLDKTDIVIT SYDVCRNDID VIEKYNWNYC VLDEGHLIKN
PKAKITLAVK RLTSNHRLIL TGTPIQNNVL ELWSLFDFLM PGFLGAEKVF LDRFAKPIAN
SRYSKASSKE QEAGALAIEA LHKQVLPFLL RRLKEEVLND LPPKILQNYY CDLSDLQRKL
FEDFTKREGK KITETAGRDD KEAKQHIFQA LQYMRKLCNS PALVMKPGHK AYEDTQKYLA
KHGTTLEDPI HAPKLGALRD LLVDCGIGVE GQESSDPLYT PIKPHRALIF CQMKEMLDMV
QNTVLKQMLP SVSYLRLDGS VEANKRQDIV NKFNSDPSYD VLLLTTSVGG LGLNLTGADT
VIFVEHDWNP QKDLQAMDRA HRIGQKKVVN VYRIITRGTL EEKILSLQRF KIDVASTVVN
QQNAGLATMD TDQILDLFNL GESGPSLITD NKESIEGREE DMVDIETGDV RRPGKKAAWL
EGLGELWDNA QYEESFDLDG FLKTMQ
//