ID M7XP08_RHOT1 Unreviewed; 1760 AA.
AC M7XP08;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE SubName: Full=Helicase SWR1 {ECO:0000313|EMBL:EMS21923.1};
GN ORFNames=RHTO_01138 {ECO:0000313|EMBL:EMS21923.1};
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:EMS21923.1, ECO:0000313|Proteomes:UP000016926};
RN [1] {ECO:0000313|EMBL:EMS21923.1, ECO:0000313|Proteomes:UP000016926}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NP11 {ECO:0000313|EMBL:EMS21923.1,
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. SWR1 subfamily.
CC {ECO:0000256|ARBA:ARBA00009220}.
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DR EMBL; KB722653; EMS21923.1; -; Genomic_DNA.
DR RefSeq; XP_016273042.1; XM_016414821.1.
DR GeneID; 27365151; -.
DR eggNOG; KOG0391; Eukaryota.
DR HOGENOM; CLU_000315_24_3_1; -.
DR OrthoDB; 5475375at2759; -.
DR Proteomes; UP000016926; 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:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR CDD; cd18003; DEXQc_SRCAP; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 1.20.120.850; SWI2/SNF2 ATPases, N-terminal domain; 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; IPR014012; HSA_dom.
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; PTHR45685:SF1; HELICASE SRCAP; 1.
DR PANTHER; PTHR45685; HELICASE SRCAP-RELATED; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF07529; HSA; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00573; HSA; 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.
DR PROSITE; PS51204; HSA; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Helicase {ECO:0000313|EMBL:EMS21923.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT DOMAIN 456..528
FT /note="HSA"
FT /evidence="ECO:0000259|PROSITE:PS51204"
FT DOMAIN 939..1104
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1479..1629
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..91
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 215..328
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 577..699
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 716..846
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 858..914
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..48
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 586..615
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 669..683
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 684..699
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 728..755
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 763..787
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 793..808
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 883..906
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1760 AA; 194262 MW; 9782032653A5326A CRC64;
MARTARRSTA KAAAAEPADP PPRADQDGEN STTGTAEGVA TTATGVGEGQ PSEGAAHDPS
DAVGGEKSHL EGVPADASTP MELDAAAEGH SDGSAAVVNG VMDGSVAAQT ASTAIAPPVF
ASPANLPPIP STSQQPPPKR EYTAEEVHVW REQQIDAKQA ELAEIVDRHD DFVRELFHLD
RFVTLVGYDP AVAKADRSDV FQSFQANYDL FLNATPDGAA EGSGRRGTRR ATTERKIGAL
ATPDTGGRWG DPKGKGKARE DSSGPMFEAS GSGRAGGKKA VGPRGKMAGS GSPAPSSYYG
GGSPSPAPSA DTPYKKRPSD VLTPSRSTSQ IPFNLPPLPA LPVGVGYKPV VANLADLPGM
LKDDLPPLSP RSVKRRRLYA ASDVTYSHMS QLPPDSEFDF SLPAFLSSWV SLDDDTDIAP
PPPEEELDAR AEYEHDILQQ VEAIRAEGRE LCNPDRTQSA EAKRPKDHQD WLVDHALYFS
QLVMQERKSH IALARKTARM VMKHFEEIRG KEDREQKEIE RNQKALSRWT LREVRKKWKM
AVNVVRARRK AEQQKEAKRL GKQQLDLMLN KSTTMLQAQQ QEMAGEGSSD EEEEEEDGEE
GEDEEDEEED EGDAESTSQA ASTPADSSPA ATPPPKANGR RARRTARSRL STSATPGDAD
EDAGDAFAGA EDDAERDKED NVFAAEMEAE DEDDDDEMAG LAAEADMPIE ELLRRSGYAA
MMAEEAAGGG EAEEEEGEED EEEEEGEDDA SIADVVDDAA SEQDSAVKST SSTNAAPSPS
TPGTSAPAGP ELTAEEKEAE AMSEFGSEAG DDERDDEDAR MAKEMEAEEG ESDDEEMKGL
AAEADMPIEE LMRKYGYGGG ESAEATAGEP DGAVKAEEEE RKVSPEPEEE DEGDEAKGEE
DAEDKPEDGA DRQIVHLKPP FLLRATLRPY QQAGLEWLAS LYTSGVNGIL ADEMGLGKTI
QTISLLAHLA CDKGQWGPHL VVVPTSVMLN WEMEFRKFFP GFKLLTYYGT QKERKKKREG
WNTENAFNVC ITSYQLVLAD QHIFRRKPWH YLILDEAHHI KNFRSQRWQT LLGFNARHRL
LLTGTPLQNN LMELWSLLYF LMPHGLITDG SGPFAEHADF QAWFSNPMEK AIESGEVMDA
EMQATVNKLH TILRPYLLRR LKAEVETQMP GKTESVIYCR MSKRQRFLYD DFMSRAQTRD
TLASGHFLSI INCLMQLRKV CNHPDLFEVR PIVTSFSMQR SVVSGFEPSE LLVRKRLLED
EPIAKMDWTT LTLVKPWQEE TTSTVAGQIR LHLDASTSFP YLHRVPMDVN LASPPPRDTK
TIAGWRRYRA WQEHHAILSR LNRLAVVNRR RCLSSTPYFG ADLLHLLREP SRSSQLLPTD
AIRPDREALS RPSIVPNMIL SHEQRASALE ETVSLFSFAT PKVRAHDMKH HALPGMSQDD
VDDIEEEAPA ELLHAASTKL TVAFPDRSLL QYDCGKLQKL DELLRECKAG GHRALIFTQM
TKVLDILEEF LSYQGYRYLR LDGSTKIEQR QALTERFNSN DKILCFISST RAGGLGINLQ
GADTVIFYDS DWNPALDRQC QDRAHRIGQT REVRIWRFVT EHSIEENMLK KANQKRKLDQ
MVIAEGEFTT DHLQKLDWRD YLDDGQLAEL GVDAGSNEQG DTGTGASAMQ SAAEIRQALA
AAEDAEDVAA AKAAEQEIEI DRTDFGNEGQ QASRTAATFG KDGLVNTTAA GQKEEEEDPL
AGTIDGVMVK WVEEDWDYFA
//
