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Database: UniProt
Entry: M7XPW9_RHOT1
LinkDB: M7XPW9_RHOT1
Original site: M7XPW9_RHOT1 
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
//
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