ID A0A5D3A342_GOSMU Unreviewed; 1063 AA.
AC A0A5D3A342;
DT 13-NOV-2019, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2019, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Chromatin-remodeling complex ATPase {ECO:0008006|Google:ProtNLM};
GN ORFNames=E1A91_A02G054200v1 {ECO:0000313|EMBL:TYJ45422.1};
OS Gossypium mustelinum (Cotton).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Malvoideae; Gossypium.
OX NCBI_TaxID=34275 {ECO:0000313|EMBL:TYJ45422.1, ECO:0000313|Proteomes:UP000323597};
RN [1] {ECO:0000313|EMBL:TYJ45422.1, ECO:0000313|Proteomes:UP000323597}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1408120.09 {ECO:0000313|EMBL:TYJ45422.1};
RA Chen Z.J., Sreedasyam A., Ando A., Song Q., De L., Hulse-Kemp A., Ding M.,
RA Ye W., Kirkbride R., Jenkins J., Plott C., Lovell J., Lin Y.-M., Vaughn R.,
RA Liu B., Li W., Simpson S., Scheffler B., Saski C., Grover C., Hu G.,
RA Conover J., Carlson J., Shu S., Boston L., Williams M., Peterson D.,
RA Mcgee K., Jones D., Wendel J., Stelly D., Grimwood J., Schmutz J.;
RT "WGS assembly of Gossypium mustelinum.";
RL Submitted (JUL-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. ISWI subfamily.
CC {ECO:0000256|ARBA:ARBA00009687}.
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DR EMBL; CM017637; TYJ45422.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5D3A342; -.
DR Proteomes; UP000323597; Chromosome a02.
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; IPR049730; SNF2/RAD54-like_C.
DR InterPro; IPR000330; SNF2_N.
DR PANTHER; PTHR45623; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 3-RELATED-RELATED; 1.
DR PANTHER; PTHR45623:SF49; SWI_SNF RELATED, MATRIX ASSOCIATED, ACTIN DEPENDENT REGULATOR OF CHROMATIN, SUBFAMILY A, MEMBER 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:UP000323597}.
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..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 132..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 1007..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..90
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1007..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; 123534 MW; 9428A1665DE3B27D CRC64;
MAKSSKPASS DEELYNGSSS SEEERMSAQV NGEEDDEEEI EAVARSADAS DEDDDAVPEE
NADDADYDES NGADPETSKR EKERLKEMQK LKKQKIQEIL DTQNAAIDAD MNNKGRGRLK
YLLQQTELFS HFAKGDPNSS QKKVKGRGRH ASKITEEEED EEYLKEEEDG LSGNTRLVTQ
PSCIQGKMRD YQLAGLNWLI RLYENGINGI LADEMGLGKT LQTISLLGYL HEYRGITGPH
MVVAPKSTLG NWMNEIRRFC PVLRAVKFLG NPEERRYIRE ELLVAGKFDV CVTSFEMAIK
EKCALRRFSW 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 TIDVDEPEER GDPLTAEELE EKERLLEEGF
SSWSRRDFNT FIRACEKYGR NDIKSIASEM EGKTEEEVER YAKVFKERYK ELNDYDRIIK
NIERGEARIS RRDEIMKAIG KKLDRYKNPW LELKIQYGQN KGKLYNEECD RFMICMVHKL
GYGNWEELKA AFRASPLFRF DWFVKSRTTQ ELARRCDTLI RLVEKENQEN DERERQARKE
KKLAKNMTPS KRSGKQPTES PNQLKKRKQL SMDDNANSGK RRK
//
