ID D7T6I2_VITVI Unreviewed; 1080 AA.
AC D7T6I2;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 24-JAN-2024, entry version 87.
DE RecName: Full=ISWI chromatin-remodeling complex ATPase CHR11 {ECO:0008006|Google:ProtNLM};
GN OrderedLocusNames=VIT_05s0020g01780 {ECO:0000313|EMBL:CBI26103.3};
OS Vitis vinifera (Grape).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; Vitales; Vitaceae; Viteae; Vitis.
OX NCBI_TaxID=29760 {ECO:0000313|EMBL:CBI26103.3, ECO:0000313|Proteomes:UP000009183};
RN [1] {ECO:0000313|Proteomes:UP000009183}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Pinot noir / PN40024 {ECO:0000313|Proteomes:UP000009183};
RX PubMed=17721507; DOI=10.1038/nature06148;
RG The French-Italian Public Consortium for Grapevine Genome Characterization.;
RA Jaillon O., Aury J.-M., Noel B., Policriti A., Clepet C., Casagrande A.,
RA Choisne N., Aubourg S., Vitulo N., Jubin C., Vezzi A., Legeai F.,
RA Hugueney P., Dasilva C., Horner D., Mica E., Jublot D., Poulain J.,
RA Bruyere C., Billault A., Segurens B., Gouyvenoux M., Ugarte E.,
RA Cattonaro F., Anthouard V., Vico V., Del Fabbro C., Alaux M.,
RA Di Gaspero G., Dumas V., Felice N., Paillard S., Juman I., Moroldo M.,
RA Scalabrin S., Canaguier A., Le Clainche I., Malacrida G., Durand E.,
RA Pesole G., Laucou V., Chatelet P., Merdinoglu D., Delledonne M.,
RA Pezzotti M., Lecharny A., Scarpelli C., Artiguenave F., Pe M.E., Valle G.,
RA Morgante M., Caboche M., Adam-Blondon A.-F., Weissenbach J., Quetier F.,
RA Wincker P.;
RT "The grapevine genome sequence suggests ancestral hexaploidization in major
RT angiosperm phyla.";
RL Nature 449:463-467(2007).
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; FN595749; CBI26103.3; -; Genomic_DNA.
DR RefSeq; XP_002275787.1; XM_002275751.4.
DR AlphaFoldDB; D7T6I2; -.
DR STRING; 29760.D7T6I2; -.
DR PaxDb; 29760-VIT_05s0020g01780-t01; -.
DR EnsemblPlants; Vitvi05g00345_t001; Vitvi05g00345_P001; Vitvi05g00345.
DR GeneID; 100244281; -.
DR Gramene; Vitvi05g00345_t001; Vitvi05g00345_P001; Vitvi05g00345.
DR KEGG; vvi:100244281; -.
DR eggNOG; KOG0385; Eukaryota.
DR HOGENOM; CLU_000315_0_0_1; -.
DR InParanoid; D7T6I2; -.
DR OMA; VHDYQFF; -.
DR OrthoDB; 5482994at2759; -.
DR Proteomes; UP000009183; Chromosome 5.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008094; F:ATP-dependent activity, acting on DNA; IBA:GO_Central.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
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:UP000009183}.
FT DOMAIN 216..381
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 509..660
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 854..906
FT /note="SANT"
FT /evidence="ECO:0000259|PROSITE:PS51293"
FT REGION 1..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 148..192
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 823..844
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1029..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 27..41
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 70..85
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 86..103
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1029..1043
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1048..1062
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1080 AA; 125073 MW; D4814FFE14C37304 CRC64;
MAKPSKSQVS SDEALSNGSN SSEEEQLNDQ INDEEDEEEL EAVTRTAVSE DEDEEAADGG
NSPATEDDAA GDSSDGEEDE EDGNAVGGTE ISKREKARLK EMQKMKKQKI QEILDAQNAA
IDADMNNRGK GRLKYLLQQT EIFAHFAKGD QSTSQKKTKG RGRHASKVTE EEEDEECLKE
EEDGLSGTGN TRLVTQPSCI QGKMRDYQLA GLNWLIRLYE NGINGILADE MGLGKTLQTI
SLLGYLHEFR GITGPHMVVA PKSTLGNWMN EIRRFCPVLR AVKFLGNPDE RRHIRDNLLV
AGKFDVCVTS FEMAIKEKTT LRRFSWRYII IDEAHRIKNE NSLLSKTMRL YSTNYRLLIT
GTPLQNNLHE LWSLLNFLLP EIFNSAETFD EWFQISGDND QQEVVQQLHK VLRPFLLRRL
KSDVEKGLPP KKETILKVGM SQLQKQFYRA LLQKDLEVVN AGGERKRLLN IAMQLRKCCN
HPYLFQGAEP GPPYTTGEHL ITNSGKMVLL DKLLPKLKER DSRVLIFSQM TRLLDILEDY
LMFRGYLYCR IDGNTGGEDR DASIDAFNKP GSEKFVFLLS TRAGGLGINL ATADVVILYD
SDWNPQVDLQ AQDRAHRIGQ KKEVQVFRFC TEYTIEEKVI ERAYKKLALD ALVIQQGRLA
EQKTVNKDEL LQMVRFGAEM VFSSKDSTIT DEDIDRIIAK GEEATAELDA KMKKFTEDAI
KFKMDDTAEL YDFDDEKDEN KFDFKKIVSE NWIEPPKRER KRNYSESEYF KQTMRQGAPA
KQREPRIPRM PQLHDFQFFN TQRLNELYEK EVRYLMQTHQ KNQLKDSIDV DEPEDLGDPL
TAEEQEEKER LLEEGFSSWS RRDFNTFIRA CEKYGRNDVK SIASEMEGKT EEEVERYAKA
FKERYKELND YDRIIKNIER GEARISRKDE IMKAIGKKLD RYKNPWLELK IQYGQNKGKL
YNEECDRFMI CMVHKLGYGN WDELKAAFRT SPLFRFDWFV KSRTTQELAR RCDTLIRLVE
RENQEFDERE RQARKEKKLA KNMTPSKRAM ARQATESPTS VKKRKQLLMD DYVSSGKRRK
//