ID A0A0D2SBJ5_GOSRA Unreviewed; 1063 AA.
AC A0A0D2SBJ5;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 49.
DE RecName: Full=Chromatin-remodeling complex ATPase {ECO:0008006|Google:ProtNLM};
GN ORFNames=B456_005G058400 {ECO:0000313|EMBL:KJB28615.1};
OS Gossypium raimondii (New World cotton).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Malvoideae; Gossypium.
OX NCBI_TaxID=29730 {ECO:0000313|EMBL:KJB28615.1, ECO:0000313|Proteomes:UP000032304};
RN [1] {ECO:0000313|EMBL:KJB28615.1, ECO:0000313|Proteomes:UP000032304}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23257886; DOI=10.1038/nature11798;
RA Paterson A.H., Wendel J.F., Gundlach H., Guo H., Jenkins J., Jin D.,
RA Llewellyn D., Showmaker K.C., Shu S., Udall J., Yoo M.J., Byers R.,
RA Chen W., Doron-Faigenboim A., Duke M.V., Gong L., Grimwood J., Grover C.,
RA Grupp K., Hu G., Lee T.H., Li J., Lin L., Liu T., Marler B.S., Page J.T.,
RA Roberts A.W., Romanel E., Sanders W.S., Szadkowski E., Tan X., Tang H.,
RA Xu C., Wang J., Wang Z., Zhang D., Zhang L., Ashrafi H., Bedon F.,
RA Bowers J.E., Brubaker C.L., Chee P.W., Das S., Gingle A.R., Haigler C.H.,
RA Harker D., Hoffmann L.V., Hovav R., Jones D.C., Lemke C., Mansoor S.,
RA ur Rahman M., Rainville L.N., Rambani A., Reddy U.K., Rong J.K.,
RA Saranga Y., Scheffler B.E., Scheffler J.A., Stelly D.M., Triplett B.A.,
RA Van Deynze A., Vaslin M.F., Waghmare V.N., Walford S.A., Wright R.J.,
RA Zaki E.A., Zhang T., Dennis E.S., Mayer K.F., Peterson D.G., Rokhsar D.S.,
RA Wang X., Schmutz J.;
RT "Repeated polyploidization of Gossypium genomes and the evolution of
RT spinnable cotton fibres.";
RL Nature 492:423-427(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; CM001744; KJB28615.1; -; Genomic_DNA.
DR EMBL; CM001744; KJB28616.1; -; Genomic_DNA.
DR RefSeq; XP_012482089.1; XM_012626635.1.
DR AlphaFoldDB; A0A0D2SBJ5; -.
DR STRING; 29730.A0A0D2SBJ5; -.
DR EnsemblPlants; KJB28615; KJB28615; B456_005G058400.
DR EnsemblPlants; KJB28616; KJB28616; B456_005G058400.
DR GeneID; 105796815; -.
DR Gramene; KJB28615; KJB28615; B456_005G058400.
DR Gramene; KJB28616; KJB28616; B456_005G058400.
DR KEGG; gra:105796815; -.
DR eggNOG; KOG0385; Eukaryota.
DR OMA; KEIYVSC; -.
DR OrthoDB; 5482994at2759; -.
DR Proteomes; UP000032304; Chromosome 5.
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; 1.20.5.1190; 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 Reference proteome {ECO:0000313|Proteomes:UP000032304}.
FT DOMAIN 200..365
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 493..644
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 838..890
FT /note="SANT"
FT /evidence="ECO:0000259|PROSITE:PS51293"
FT REGION 1..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 133..170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 747..771
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1010..1063
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..26
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 52..71
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..88
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1010..1027
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1029..1045
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1046..1063
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1063 AA; 123419 MW; E55DFBF51166A5FF CRC64;
MAKSSKPASS DEELYNGSSS SEEERMNAQV NGEEDDEEEI EAVARSADAS DEDDDAVPEE
IAGDADDDES NGADPEISKR EKERLKEMQK IKKQKIQEIL DTQNAAIDAD MNNKGKGRLK
YLLQQTELFS HFAKGDPNSS QKKVKGRGRH ASKITEEEED EEYLKEEEDG LSGNTRLVTQ
PSCIQGKMRD YQLAGLNWLI RLYENGINGI LADEMGLGKT LQTISLLGYL HEYRGITGPH
MVVAPKSTLG NWMNEIRRFC PVLRAVKFLG NPEERRYIRE ELLVAGKFDV CVTSFEMAIK
EKSALRRFSW RYIIIDEAHR IKNENSLLSK TMRLYNTNYR LLITGTPLQN NLHELWSLLN
FLLPEIFSSA ETFDEWFQIS GENDQQEVVQ QLHKVLRPFL LRRLKSDVEK GLPPKKETIL
KVGMSQMQKQ YYRALLQKDL EVVNAGGERK RLLNIAMQLR KCCNHPYLFQ GAEPGPPYTT
GDHLVTSAGK MVLLDKLLPK LKERDSRVLI FSQMTRLLDI LEDYLMFRGY QYCRIDGNTG
GEDRDASIEA FNKPGSEKFV FLLSTRAGGL GINLATADVV ILYDSDWNPQ VDLQAQDRAH
RIGQKKEVQV FRFCTEYTIE EKVIERAYKK LALDALVIQQ GRLAEQKTVN KDELLQMVRF
GAEMVFSSKD STITDEDIDR IIAKGEAATA ELDAKMKKFT EDAIKFKMDD TAELYEFDDD
KDENKFDIKK IVSENWIEPP KRERKRNYSE SEYFKQTLRQ GGPAKPKEPR IPRMPQLLDF
QFFNTQRLSE LYEKEVRYLM QTHQKNQVKD TIDVDEPEET GDPLTAEELE EKERLLEEGF
SSWSRRDFNT FIRACEKYGR NDIMSIASEM EGKTEEEVER YAKVFKERYK ELNDYDRIIK
NIERGEARIS RRDEIMKAIG KKLDRYKNPW LELKIQYGQN KGKLYNEECD RFMICMVHKL
GYGNWEELKA AFRASPLFRF DWFVKSRTTQ ELARRCDTLI RLVEKENQEY DERERQARKE
KKLAKNMTPS KRSGKQPTES PNQLKKRKQL SMDDNANSGK RRK
//