ID A0A452XYF3_AEGTS Unreviewed; 1170 AA.
AC A0A452XYF3;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Chromatin-remodeling complex ATPase {ECO:0008006|Google:ProtNLM};
OS Aegilops tauschii subsp. strangulata (Goatgrass).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Aegilops.
OX NCBI_TaxID=200361 {ECO:0000313|EnsemblPlants:AET1Gv20217300.5, ECO:0000313|Proteomes:UP000015105};
RN [1] {ECO:0000313|Proteomes:UP000015105}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. AL8/78 {ECO:0000313|Proteomes:UP000015105};
RX PubMed=25035499; DOI=10.1126/science.1250092;
RG International Wheat Genome Sequencing Consortium,;
RA Marcussen T., Sandve S.R., Heier L., Spannagl M., Pfeifer M.,
RA Jakobsen K.S., Wulff B.B., Steuernagel B., Mayer K.F., Olsen O.A.;
RT "Ancient hybridizations among the ancestral genomes of bread wheat.";
RL Science 345:1250092-1250092(2014).
RN [2] {ECO:0000313|Proteomes:UP000015105}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. AL8/78 {ECO:0000313|Proteomes:UP000015105};
RX PubMed=29158546; DOI=10.1038/s41477-017-0067-8;
RA Zhao G., Zou C., Li K., Wang K., Li T., Gao L., Zhang X., Wang H., Yang Z.,
RA Liu X., Jiang W., Mao L., Kong X., Jiao Y., Jia J.;
RT "The Aegilops tauschii genome reveals multiple impacts of transposons.";
RL Nat. Plants 3:946-955(2017).
RN [3] {ECO:0000313|EnsemblPlants:AET1Gv20217300.5}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (MAR-2019) to UniProtKB.
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DR AlphaFoldDB; A0A452XYF3; -.
DR STRING; 200361.A0A452XYF3; -.
DR EnsemblPlants; AET1Gv20217300.5; AET1Gv20217300.5; AET1Gv20217300.
DR Gramene; AET1Gv20217300.5; AET1Gv20217300.5; AET1Gv20217300.
DR Proteomes; UP000015105; Chromosome 1D.
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:0042393; F:histone binding; IEA:InterPro.
DR CDD; cd18793; SF2_C_SNF; 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; IPR027417; P-loop_NTPase.
DR InterPro; IPR029295; SnAC.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR049730; SNF2/RAD54-like_C.
DR InterPro; IPR000330; SNF2_N.
DR PANTHER; PTHR10799:SF854; ATP-DEPENDENT DNA HELICASE CHR12-RELATED; 1.
DR PANTHER; PTHR10799; SNF2/RAD54 HELICASE FAMILY; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM01314; SnAC; 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.
PE 4: Predicted;
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:UP000015105}.
FT DOMAIN 493..658
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 790..951
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 130..160
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 406..455
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1095..1170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 132..146
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 406..424
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1099..1113
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1138..1170
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1170 AA; 133040 MW; 540E1F692921F02D CRC64;
IDPSKPKKLP PLPSDNTARK HNTAPLSSRK ASPRKGFERA LPRSDLNTGS GGRRPPPHRL
ASAASRGLEA ETLAMAASVD AAAAVAAPEE AGGGDAEQAR ILIGALNLLS RNLPLPPAVL
RAVSSIYHGG EDADQEEEEE EGAEGPSLVG DEGGEGDPAD AVDAAEEATL IQEFEDSIYR
NQMMHMSSSK LTALKEERFN TCIQHRLSEL EGLPSTRGED LQMKCLLELY GLKLLDLQKK
VRSDVNAEYW LHKKCAHPEK QLFDWGMMRI RYPFTMYGIG DGFSMDTDDI HRKKRFTERI
SKLEEEEKNQ AETRKRRFFT EILNAAREYQ VQTSATYKRR KQRNDGVQAW HVRARQRINR
LEKSRLQVLK AGDQEAYMRM VEESKNERLT MLLDKTNELL EGIGKAVQRQ KDAEHVSRPE
GSEDSESDES PEESPSDDDA DTHGSANTSK FNAAGRRLDS TVHSIEEKVT EQPSALVGGE
LRPYQLEGLQ WMLSLFNNNL NGILADEMGL GKTIQTIALI AYLLEKKEVT GPHLIVAPKA
VLPNWSNEFK TWAPSIGTIL YDGRPDERKS LRETNFGGQF NVLLTHYDLI LKDKKFLKKV
HWHYLIVDEG HRLKNHECAL ARTLVSGYLI RRRLLLTGTP IQNSLQELWS LLNFILPNIF
NSSGNFEEWF NAPFACDVSI NDEEELLIIH RLHQVLRPFL LRRKKDEVEK YLPSKTQVIL
KCDFSAWQKA YYEQVASKGK VALGSGLKPK AVANLSMQLR KCCNHPYLFV EQYNMYQREE
IVRASGKFEL LDRLLPKLHR AGHRVLLFSQ MTRLLNILEV YLQMYNFKYM RLDGSTKTEE
RGKLLADFNK KDSEYFIFLL STRAGGLGLN LQTADTVIIF DSDWNPQMDQ QAEDRAHRIG
QKNEVRVFVL VSVGSIEEEI LDRAKQKMGI DAKVIQAGLF NNTSTAQDRK ALLQEILKRG
TSTLGTDIPS EREINRLAAR TEEEFWLFEK MDEERRRREN YKSRLMQGPE VPEWVFDISE
TLAEKLLAEE AKNPVINTKR RRKEVVYSDS YVDQWMKSDE VYEDIPKMTP RAKRSAYLSD
IQEVDLHDRA KRLKYSDSAD GAGNSTWTPE KGRPGVSSYS KDENEDDNDE DEVTAGGLQQ
GGSFTWNTLR RKRSSHSTNP SSDPKGRSAF
//
