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Database: UniProt
Entry: D7T6I2_VITVI
LinkDB: D7T6I2_VITVI
Original site: D7T6I2_VITVI 
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
//
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