ID A0A059CBD4_EUCGR Unreviewed; 1845 AA.
AC A0A059CBD4;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Protein CHROMATIN REMODELING 4 {ECO:0008006|Google:ProtNLM};
GN ORFNames=EUGRSUZ_E04303 {ECO:0000313|EMBL:KCW75544.1};
OS Eucalyptus grandis (Flooded gum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Myrtales; Myrtaceae; Myrtoideae; Eucalypteae; Eucalyptus.
OX NCBI_TaxID=71139 {ECO:0000313|EMBL:KCW75544.1};
RN [1] {ECO:0000313|EMBL:KCW75544.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf extractions {ECO:0000313|EMBL:KCW75544.1};
RA Schmutz J., Hayes R., Myburg A., Tuskan G., Grattapaglia D., Rokhsar D.S.;
RT "The genome of Eucalyptus grandis.";
RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. ISWI subfamily.
CC {ECO:0000256|ARBA:ARBA00009687}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KK198757; KCW75544.1; -; Genomic_DNA.
DR EnsemblPlants; KCW75544; KCW75544; EUGRSUZ_E04303.
DR Gramene; KCW75544; KCW75544; EUGRSUZ_E04303.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR CDD; cd18660; CD1_tandem; 1.
DR CDD; cd18659; CD2_tandem; 1.
DR CDD; cd11660; SANT_TRF; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 2.40.50.40; -; 2.
DR Gene3D; 1.10.10.60; Homeodomain-like; 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; IPR016197; Chromo-like_dom_sf.
DR InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR InterPro; IPR023780; Chromo_domain.
DR InterPro; IPR009463; DUF1087.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001005; SANT/Myb.
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:SF28; PROTEIN CHROMATIN REMODELING 4; 1.
DR Pfam; PF00385; Chromo; 1.
DR Pfam; PF06465; DUF1087; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00298; CHROMO; 2.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM01147; DUF1087; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF54160; Chromo domain-like; 2.
DR SUPFAM; SSF46689; Homeodomain-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS50013; CHROMO_2; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS50090; MYB_LIKE; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..1845
FT /note="Protein CHROMATIN REMODELING 4"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001569090"
FT DOMAIN 154..214
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 228..290
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 333..510
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 640..799
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 1319..1375
FT /note="Myb-like"
FT /evidence="ECO:0000259|PROSITE:PS50090"
FT REGION 84..110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 806..829
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 974..1007
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1020..1100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1173..1197
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1381..1402
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1651..1682
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1696..1730
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1765..1845
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 84..103
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1055..1072
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1707..1729
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1803..1817
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1818..1845
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1845 AA; 205252 MW; C6788D72E67FC9A7 CRC64;
MVQVHCFLFL LLVPEKQDRH PDSTSGEINL DAGNRVALAD EKQADISNGS DIKLHNLNVH
ESSLTKDCKN SSCMDSLKSD TEHLASETDV LEDCDESSKA TDDQRGPDAG VMADSVNFIK
LNGNDKGEVT TTGEMRVSVE ENDKGVQDEG GTGLSPESIN QEPELAECAS VDQESPSYEF
LVKWVGKSNI HNRWLPESQL KILARRKLEN YKAKYGTSVI NICEERWKQP QRIIALRASK
DGTREAFVKW TGLPYDECTW EKLDEPILKE SSNLIDVFNQ LEQQTLEKDS SRHDSHGDRA
GHPSEIMTLT EQPSELKGGS LFPHQLEALN WLRKCWCKSK NVILADEMGL GKTVSACAFI
SSLYCEFKAS LPCLVLVPLS TMPNWLSEFS LWAPGLNVVE YHGSAKARAV IRQHEWHASD
PIDGNRKTVS HKFNVLLTTY EMVLADSSHL RGVPWEVLVV DEGHRLKNSS SKLFTLLNTF
SFQHRVLLTG TPLQNNLGEM YNLLSFLQPA SFPSISLFEE NFNDLTTAEK VEELKKLVAP
HMLRRLKKDA MQNIPPKTER VVPVELSSIQ AEYYRAILTK NYQLLRNIGK GVAQQSMLNI
VMQLRKVCNH PYLIPGTEPD SGSVEFLHEM RIKASAKLTL LHSMLKAFFK EGHRVLIFSQ
MTKLLDVLED YLTIEFGPKT YERVDGSVCV TDRQAAISRF NLDKSRFVFL LSTRSCGLGI
NLATADTVII YDSDFNPHAD IQAMNRAHRI GQSNRLLVYR LVVRASVEER ILQLAKKKLM
LDQLFVNKSG SQKEVEDILR WGTEELFGDS SNGGKESSDN DNGKTEPMLD AEHKHRKRAG
TLGDVYKDKC ADGSNKIVWD DNAILKLLDR SNLQDGSTEC TEGENDMLGS VKSLEWNDEL
MEERGEGESP PVLSEDVCVA NSVKKEDSVV TVPEENEWDR LLRVRWEKYQ SEEEAALGRG
KRVRKAVSYR EAYAAHPSEM ANESGDEEER VPEQEPEREY TPAGRALKEK YAKLRARQKE
RLARRNQIEE SQPSGGPLGP EGTIQCPPDV QNDGTKAEHP SQKTNVHSDP SFSPLSRPPD
ILPLHQHDGQ HEGTVYPSSE SDKLLPVLGL CAPNANQVEL SRRNSTRPNA RQSRPVGLEF
PFSLAPFSGN LMGTHLKGLE PTLDRLKVPD GPGEVSQLHP YPPAPLHDSG RLENAGVNSS
DFRDMMMTPK YVEETLMPRF QVPAKGVLPQ HDFLPTLSLG SRVEAGRESI QDFPPIPPLP
HFKFPPQDVA RYGHQRERET VPSLGLNQMP TFSSIPENHR KVLENIMLRT GSGSSNLHRK
KSRVDGWSED ELDFLWIGVR RHGRGNWDSM LRDPRLRFSK NKTPEDLSAR WEEEQVKLFD
GSSLPMPKPT RPLKPGKSSS FPGFTDGMMT RALQGSKLAM PPKFQSHLTD MKLGFGEVGP
PLPPFGASDQ LSLQNEHLAA LLPHNNPDKL RETFVRRYYG GPSDLPGTSL SMPFEKPFMP
NCFGSGMGSV GVVGSSSFQP RDDEQIPYPK LPGLLGKPLN MLPELRNNYG GESSGTVLLP
DPDKLVNHQF HSKGKEVIDE GASKKNLPHW LREAVTAPPP APDPELPPNV SAIAQSVRLL
YGEDKPTIPP FVIPGPPPSR PKDPRLILKK RKKSEQMRPI QAELQESRQL PPRNLLGDDA
ASSSIPLVPE LNAFPPSVAT MPDPAQKEAS LNASTSAMHQ PSKEKMNAEL SPSSEVLKLV
ASSIGPGQQL ALFLPTKSLD LTGSDVSSMK HSLDPAGNSE PNHAGGKEQP HPVDGLADPQ
KLGQPESGNS FGKTRSVLSR TDHLDAEEVS SEETVSDHPE SDNDP
//
