ID G3B649_CANTC Unreviewed; 1018 AA.
AC G3B649;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 13-SEP-2023, entry version 67.
DE RecName: Full=Chromatin remodelling complex ATPase chain ISW1 {ECO:0008006|Google:ProtNLM};
GN ORFNames=CANTEDRAFT_106017 {ECO:0000313|EMBL:EGV63380.1};
OS Candida tenuis (strain ATCC 10573 / BCRC 21748 / CBS 615 / JCM 9827 / NBRC
OS 10315 / NRRL Y-1498 / VKM Y-70) (Yeast) (Yamadazyma tenuis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Yamadazyma.
OX NCBI_TaxID=590646 {ECO:0000313|Proteomes:UP000000707};
RN [1] {ECO:0000313|EMBL:EGV63380.1, ECO:0000313|Proteomes:UP000000707}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10573 / BCRC 21748 / CBS 615 / JCM 9827 / NBRC 10315 /
RC NRRL Y-1498 / VKM Y-70 {ECO:0000313|Proteomes:UP000000707};
RX PubMed=21788494; DOI=10.1073/pnas.1103039108;
RA Wohlbach D.J., Kuo A., Sato T.K., Potts K.M., Salamov A.A., LaButti K.M.,
RA Sun H., Clum A., Pangilinan J.L., Lindquist E.A., Lucas S., Lapidus A.,
RA Jin M., Gunawan C., Balan V., Dale B.E., Jeffries T.W., Zinkel R.,
RA Barry K.W., Grigoriev I.V., Gasch A.P.;
RT "Comparative genomics of xylose-fermenting fungi for enhanced biofuel
RT production.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:13212-13217(2011).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. ISWI subfamily.
CC {ECO:0000256|ARBA:ARBA00009687}.
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DR EMBL; GL996524; EGV63380.1; -; Genomic_DNA.
DR RefSeq; XP_006687173.1; XM_006687110.1.
DR AlphaFoldDB; G3B649; -.
DR STRING; 590646.G3B649; -.
DR GeneID; 18245856; -.
DR KEGG; cten:CANTEDRAFT_106017; -.
DR eggNOG; KOG0385; Eukaryota.
DR HOGENOM; CLU_000315_0_2_1; -.
DR OrthoDB; 5482994at2759; -.
DR Proteomes; UP000000707; 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:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0031491; F:nucleosome binding; IEA:InterPro.
DR CDD; cd17997; DEXHc_SMARCA1_SMARCA5; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 1.10.10.60; Homeodomain-like; 2.
DR Gene3D; 1.20.5.1190; iswi atpase; 1.
DR Gene3D; 1.10.1040.30; ISWI, HAND domain; 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; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR044754; Isw1/2_DEXHc.
DR InterPro; IPR015194; ISWI_HAND-dom.
DR InterPro; IPR036306; ISWI_HAND-dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001005; SANT/Myb.
DR InterPro; IPR017884; SANT_dom.
DR InterPro; IPR015195; SLIDE.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR000330; SNF2_N.
DR PANTHER; PTHR45623; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 3-RELATED-RELATED; 1.
DR PANTHER; PTHR45623:SF49; ISW-1; 1.
DR Pfam; PF09110; HAND; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF09111; SLIDE; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00717; SANT; 2.
DR SUPFAM; SSF101224; HAND domain of the nucleosome remodeling ATPase ISWI; 1.
DR SUPFAM; SSF46689; Homeodomain-like; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51293; SANT; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
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:UP000000707}.
FT DOMAIN 151..316
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 448..599
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 819..871
FT /note="SANT"
FT /evidence="ECO:0000259|PROSITE:PS51293"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 92..112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 995..1018
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..38
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1004..1018
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1018 AA; 118337 MW; FEBC4B4F6D863003 CRC64;
MTGKVIDRDE VDVPSPSPQP VVSIPQDTST STNVGQNRQK YFVTSDKPRL DAEDTAKRFK
YLLGLTDLFK HFINAKAEKD AGIRKILNKV ESERTGEQVP NHRGRKTEKE EDAELLNDEI
ETPAITEFTE SPAYVHGTLR PYQIQGLNWL VSLYENNLSG ILADEMGLGK TLQTISFLGY
LRYFKGINGP HIIITPKSTL DNWAREFARW TPDVRVLVLQ GDKDQRNQLI NQRLMTCDFD
VVISSYEIVI REKSALKRFK WEYIIIDEAH RIKNEESLLS QIIRMFHSNN RLLITGTPLQ
NNLHELWALL NFILPDVFGD SEAFDSWFQD NEGQDENSVV QQLHKVLKPF LLRRIKSEVE
KSLLPKEELN VYVKMTDMQK KWYQKILEKD IDAVNGASGK KESKTRLLNI VMQLRKCCNH
PYLFEGAEPG PPYTTDEHLV FNAQKMIILD KLLKKFKQEG SRVLIFSQMS RMLDILEDYL
LFREYEYCRI DGQTDHADRV NSIDDYNKPG SSKFAFLLTT RAGGLGINLT TADIVILFDS
DWNPQADLQA MDRAHRIGQT KQVKVFRFIT EHAIEEKVIE RAAQKLRLDQ LVIQQGRHAP
NISNQSNKAA SKDELLNMIQ HGAAEMFKSD STSKAGTVEP EDDDIDAILA KSEAKTSELN
QKYEKLNINA LQNFTNDESV YEWNGENFKK KEPTAITNIG HAWINPGKRE RKENYSIDMY
YKDVLNTGGS RSTIKSGPKP PKQHNIYDHQ FFPAKLLELL ELEKNYYKKQ IKYQVPLKSG
PPNTLDERQL EQKLEQEEIE KSRPLTEEEK QLKDELLTQG FGNWNRRDFQ HFITLNIKYG
RNSIQLITNE FEDKTIDEVR DYAKSFWKKY EEIDGYERYI NQIETGEEKI IKIKLQKEAL
RRKLSQFKYP LQELTLKFPP ASSNRKVWSE DEDRFLLVQL YRFGIDRPDI YERIKEAIRD
SILFKFDFFF QSRNTTEISR RCQTLLGCVL REMNPPVTGS KRKSETPDVG EKTKKPKK
//