ID A0A0D3E741_BRAOL Unreviewed; 2271 AA.
AC A0A0D3E741;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=Protein CHROMATIN REMODELING 4 {ECO:0008006|Google:ProtNLM};
OS Brassica oleracea var. oleracea.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX NCBI_TaxID=109376 {ECO:0000313|EnsemblPlants:Bo9g068090.1, ECO:0000313|Proteomes:UP000032141};
RN [1] {ECO:0000313|EnsemblPlants:Bo9g068090.1, ECO:0000313|Proteomes:UP000032141}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=cv. TO1000 {ECO:0000313|Proteomes:UP000032141};
RX PubMed=24916971; DOI=10.1186/gb-2014-15-6-r77;
RA Parkin I.A., Koh C., Tang H., Robinson S.J., Kagale S., Clarke W.E.,
RA Town C.D., Nixon J., Krishnakumar V., Bidwell S.L., Denoeud F., Belcram H.,
RA Links M.G., Just J., Clarke C., Bender T., Huebert T., Mason A.S.,
RA Pires J.C., Barker G., Moore J., Walley P.G., Manoli S., Batley J.,
RA Edwards D., Nelson M.N., Wang X., Paterson A.H., King G., Bancroft I.,
RA Chalhoub B., Sharpe A.G.;
RT "Transcriptome and methylome profiling reveals relics of genome dominance
RT in the mesopolyploid Brassica oleracea.";
RL Genome Biol. 15:R77-R77(2014).
RN [2] {ECO:0000313|EnsemblPlants:Bo9g068090.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (MAR-2015) to UniProtKB.
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DR STRING; 109376.A0A0D3E741; -.
DR EnsemblPlants; Bo9g068090.1; Bo9g068090.1; Bo9g068090.
DR Gramene; Bo9g068090.1; Bo9g068090.1; Bo9g068090.
DR eggNOG; KOG0383; Eukaryota.
DR HOGENOM; CLU_000994_1_1_1; -.
DR OMA; INICEDK; -.
DR Proteomes; UP000032141; Chromosome C9.
DR GO; GO:0042735; C:endosperm protein body; IEA:EnsemblPlants.
DR GO; GO:0005634; C:nucleus; IEA:EnsemblPlants.
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:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd18660; CD1_tandem; 1.
DR CDD; cd18659; CD2_tandem; 1.
DR CDD; cd15532; PHD2_CHD_II; 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 Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 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; IPR038718; SNF2-like_sf.
DR InterPro; IPR049730; SNF2/RAD54-like_C.
DR InterPro; IPR000330; SNF2_N.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
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; PF00628; PHD; 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 SMART; SM00249; PHD; 1.
DR SUPFAM; SSF54160; Chromo domain-like; 2.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
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; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000032141};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 112..159
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 557..613
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 627..689
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 733..910
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1040..1199
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 27..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 160..223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 236..361
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 455..501
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 527..560
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1299..1329
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1380..1571
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1822..1845
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1896..1925
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2056..2271
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..65
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 66..100
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 170..190
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 191..216
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 296..328
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 341..355
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 469..501
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1315..1329
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1385..1426
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1460..1479
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1508..1528
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1541..1571
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1822..1839
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2089..2110
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2123..2148
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2172..2189
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2190..2234
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2271 AA; 253751 MW; 71E1D89A195A23B2 CRC64;
MTDSGSEMLD RDWVMKQKRR KLPSILDLLD QKGDSSAAAI DSSDKPTKHQ LKVGPTPERT
SKRKGQSLPE NNSLAFGSPE CTSSDKLTNQ QPSIDLTPEG TSSKRKGHDG NYFECVICDL
GGDLLCCDSC PRTYHTDCLT PPLKRIPNGK WICPKCSQDS SALKPTTRLD AISKRARTKT
SKRNSQDRPK SERASQIYCS SLVSGEPSSE KGKSISAGES KSIGKEVMDG CSAELGHVSA
DDQPDSPVIP TAYPPSCEDL PESKLSNTGK SHEAPVERVE HACSEMVVNN TIGEAETGKG
KRKKRKREHN DGETVKECKA DKKRTKKSLS KVGSPKTKTS ESSKKKKKKK NRVTLKSLSK
TQSKVEVPEK VKVCFLKYLY VLIQLYVLIM QKLSKEERRA IRDADKSSSY LDAKNSIPPT
NLQVDRVLGC RVQDPNKTSL YGALSDDLCS DNLQDNDQRG STVKDTNADT VVAEDRTDSS
SETGKSSRNS RLKDRDMDES AVGTECLVDE KEDMVSEDTF DATVSRHVDN EDKKASETPV
SVDAHHEMGE KSPVAREEVE EPVAAKVADL IGETVSYEFL VKWVGKSNIH NSWISEADLK
SLARRKLENY KSKYGTAVIN ICEDKWKQPQ RIIALRVSKE GYQEAYVKWT GLAYDECTWE
SLEEPILRES PHLMDLFQKY ERKTLERDIS KGISPRTRGE GQQSEVITLT EQPSELRGGA
LFPHQLEALN WLRRCWHKSK NVILADEMGL GKTVSASAFL SSLYFEFGVA RPCLVLVPLS
TMPNWLSEFS LWAPLLNVVE YHGGAKARAI IREYEWHAKS STETTKKMKP YKFNVLLTTY
EMVLADSSHL RGVPWEVLVV DEGHRLKNSE SKLFSLLNTF SFQHRVLLTG TPLQNNIGEM
YNLLNFLQPS SFPSLSSFEE KFHDLTSAEK VEELKKLVAP HMLRRLKKDA MQNIPPKTER
MVPVELTSIQ AEYYRAMLTK NYQILRNIGK GVAQQSMLNI VMQLRKVCNH PYLIPGTEPE
SGSLEFLHDM RIKASAKLTL LHSMLKVLHK EGHRVLIFSQ MTKLLDILED YLNVEFGPKT
FERVDGSVAV ADRQAAIARF NQDKNRFVFL LSTRACGLGI NLATADTVII YDSDFNPHAD
IQAMNRAHRI GQSKQLLVYR LVVRASVEER ILQLAKKKLM LDQLFVNKSG SQKEFEDILR
WGTEELFNDS AGANKKDTSE SNGNLDVIMD LESKSRKKGG GLGDVYQDKC TDGNGKIVWD
ETAIMKLLDR TNIQSPSTDG ADTELENDML GSVKPVEWNE ETAEEQVGAE SPPLVADDTD
EHSSERKDDD VVTFTEENDW DRLLRMRWKR YQSEEEATLG RGKRLRKAVS YREAYAPNTS
GAVVEDGGED EKEPELKKEY TPAGRALKDK FTKLRERQKN RLAKRNAVED SIPNGNVDQV
TEAANEDEES PVMMDLDDSQ QCDAQKRKSR QDPTPDLPSQ HHHGAECPPS LPPNNLPVLG
LCAPNFTQPE PSRRNYSRPS SRQNRTIPGP HFPFSLPQRS GSVEREVNNQ EPSMGNLKPH
NVKEEPSQQP PLSNMDGWLP VRPVFPSLLY LLTHLLPIHT RIKNKRILIS VLNLICTLQF
PPSGDFERPR SSGAALAEFQ EKFPLLNLPF DDKLLPRFPF QQRNMGTSHQ EIMANLSLRK
RFEGSGHSMQ DLFSMPPMPF LPNMKVPPVD PPVFSQQEEL PPLGLDQFSS ALSSIPENHR
KVLENIMLRT GSGLGHLQKK KTRVDAWSED ELDSLWIGIR RHGYGNWETI LRDPRLKFSK
FKCPEYLAAR WEEEQRKFLD SLSSLPSKSS RTDKSTKTPL FPGLPQGIMN RALHGTKYAT
PPRFQSHLTD IKLGFNDLAS TLPLFESSNH LGLRSEPFPP LDLSGDPSAG PSNTPSDKPF
PLNSLGMGNL GSLGLDSLSS LNTQRTDERR DAIKRGKLPL FLDMQLPPML DSSNNVFLGR
SANPSLLDPN RVMNLSNPMG KDVLGGTSTS ENKLPHWLRD AVTVPAAKSP EPPTLPPTVS
AIAQSVRVLY GKDSTSIPPF VIPEPPPPVP RDPRHSLRKK KKRKSRPSSQ MTTDIASSSH
NVAESSSQGN PPTPPLLPPS LSGEPFGSSQ ATSPHHNLNI TEPSSSEPIR VPAPQEDSVV
AEEPSEVPKP SLEEVTGTSK SVSPESKISE PKSTNEDGDS DLETCEKNEA DQLMIHSDDK
HLDVKQEEQQ SEDASNKQCE PTEAETPNMD AEQEDKGESV KMVIDISPGD N
//
