ID M7XPW9_RHOT1 Unreviewed; 1156 AA.
AC M7XPW9;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 56.
DE SubName: Full=Chromatin remodelling complex ATPase chain ISW1 {ECO:0000313|EMBL:EMS22233.1};
GN ORFNames=RHTO_00987 {ECO:0000313|EMBL:EMS22233.1};
OS Rhodotorula toruloides (strain NP11) (Yeast) (Rhodosporidium toruloides).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX NCBI_TaxID=1130832 {ECO:0000313|EMBL:EMS22233.1, ECO:0000313|Proteomes:UP000016926};
RN [1] {ECO:0000313|EMBL:EMS22233.1, ECO:0000313|Proteomes:UP000016926}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NP11 {ECO:0000313|EMBL:EMS22233.1,
RC ECO:0000313|Proteomes:UP000016926};
RX PubMed=23047670; DOI=10.1038/ncomms2112;
RA Zhu Z., Zhang S., Liu H., Shen H., Lin X., Yang F., Zhou Y.J., Jin G.,
RA Ye M., Zou H., Zou H., Zhao Z.K.;
RT "A multi-omic map of the lipid-producing yeast Rhodosporidium toruloides.";
RL Nat. Commun. 3:1112-1112(2012).
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; KB722652; EMS22233.1; -; Genomic_DNA.
DR RefSeq; XP_016273352.1; XM_016414671.1.
DR AlphaFoldDB; M7XPW9; -.
DR GeneID; 27365000; -.
DR eggNOG; KOG0385; Eukaryota.
DR HOGENOM; CLU_000315_0_2_1; -.
DR OrthoDB; 5482994at2759; -.
DR Proteomes; UP000016926; 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; cd00167; SANT; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 1.10.10.60; Homeodomain-like; 2.
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}.
FT DOMAIN 219..384
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 545..696
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 907..959
FT /note="SANT"
FT /evidence="ECO:0000259|PROSITE:PS51293"
FT REGION 1..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 151..190
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 810..831
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1078..1156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..47
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 50..65
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 66..89
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1080..1103
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1156 AA; 130132 MW; BA38DD1EB2451DDD CRC64;
MASTSASKFP TPSVDGADTL SDYIPQSAEI SRVPSTAGFN DTPAQASAVV SDEDDEEEDD
DEYDSEGDKV MKPVKGGKKR ERAQAKKEAK LRVNATLQAR GEAQEALKSA DSIKRFTYLL
GQTDLFKHFC DLKAQRDPTF AKLLAEAENA GKAKGRRGKA AQSRGRKSEK EEDNELLQAE
EGTDGLAEGD GPFVFTESPA YVKGGKMREY QIQGLNWMVG LHYNGINGIL ADEMGLGKTL
QTISFLGYLK FIRNTHGPHL VVVPKSTLDN WAREIDRWVP GFSVVLLKGT KEERQELIQD
RILPGDFDIC LASYEICLRE KSSLKRIPWE YIVIDEAHRI KNVDSMLSQI VRVFKSRGRL
LITGTPLQNN LHELWALLNF LLPDVFSDVA DFDAWFDKQG DTSDKAVEAA STEATAPSTA
DAAKDAKATE DASNNVVKQL HSVLRPFLLR RVKMDVEKSL LPKKEINVYV GMTDLQRKWY
KMILEKDIDA VNGAGGKKES KTRLQNIVMQ LRKCCNHPYL FDGAEPGPPF TTDEHLVEAA
GKMVVLDKLL KSMKAKGSRV LIFSQMSRVL DILEDYCLFR EYQYCRLDGG TAHEDRMEQI
DAYNKPDSEK FIFLLTTRAG GLGINLVTAD VVVLYDSDWN PQADLQAMDR AHRIGQTKQV
YVFRFVTENA VEEKVLERAA QKLRLDQLVI QQGRAQVSNK AANKDELVDM IQHGADKIIN
SSESMAVADD IDEIIRHGEE KTAKLNSKFS QLSFDELQIF NTGPQATTTQ WEGEEYGGRK
AGGKPGLLWI EPSKRERKTT TNYSIDEYYR GQLKGGSGRP GVPRGPRRPR QVATDDFKFF
PARLQELQEK EQLYHKKTKG EQAQLRVDPN LTPEELEAER QAEQEAIDEA EPLNEEELKE
KEELRELGFD TWHKREFQAF IRGMELYGRD NYELIHRDLP TKTIEEIKEY ADVFWTRYQE
IEDHERLIAK IENAEGRRDK EGALWGLIKR KVAETKYPLT QLKIVYANQT KGKSYSEDED
RFLVVELAKY GVGKDDTYER IKRDINEWPA FRFDWFMKSR TAQEIGRRCQ TLTNLIDREY
NPGEDGDGPL TGKARRGRKS TAKDGDNAST ASGGRKRKAP GAATPALGGA DDGASNASAS
RASTPAAGPA PKKVKK
//