ID A0A1B6QEB1_SORBI Unreviewed; 2224 AA.
AC A0A1B6QEB1;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Protein CHROMATIN REMODELING 4 {ECO:0008006|Google:ProtNLM};
GN ORFNames=SORBI_3002G308700 {ECO:0000313|EMBL:KXG36264.1};
OS Sorghum bicolor (Sorghum) (Sorghum vulgare).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Sorghinae; Sorghum.
OX NCBI_TaxID=4558 {ECO:0000313|EMBL:KXG36264.1, ECO:0000313|Proteomes:UP000000768};
RN [1] {ECO:0000313|EMBL:KXG36264.1, ECO:0000313|Proteomes:UP000000768}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. BTx623 {ECO:0000313|Proteomes:UP000000768};
RX PubMed=19189423; DOI=10.1038/nature07723;
RA Paterson A.H., Bowers J.E., Bruggmann R., Dubchak I., Grimwood J.,
RA Gundlach H., Haberer G., Hellsten U., Mitros T., Poliakov A., Schmutz J.,
RA Spannagl M., Tang H., Wang X., Wicker T., Bharti A.K., Chapman J.,
RA Feltus F.A., Gowik U., Grigoriev I.V., Lyons E., Maher C.A., Martis M.,
RA Narechania A., Otillar R.P., Penning B.W., Salamov A.A., Wang Y., Zhang L.,
RA Carpita N.C., Freeling M., Gingle A.R., Hash C.T., Keller B., Klein P.,
RA Kresovich S., McCann M.C., Ming R., Peterson D.G., Mehboob-ur-Rahman,
RA Ware D., Westhoff P., Mayer K.F., Messing J., Rokhsar D.S.;
RT "The Sorghum bicolor genome and the diversification of grasses.";
RL Nature 457:551-556(2009).
RN [2] {ECO:0000313|Proteomes:UP000000768}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. BTx623 {ECO:0000313|Proteomes:UP000000768};
RX PubMed=29161754; DOI=10.1111/tpj.13781;
RA McCormick R.F., Truong S.K., Sreedasyam A., Jenkins J., Shu S., Sims D.,
RA Kennedy M., Amirebrahimi M., Weers B.D., McKinley B., Mattison A.,
RA Morishige D.T., Grimwood J., Schmutz J., Mullet J.E.;
RT "The Sorghum bicolor reference genome: improved assembly, gene annotations,
RT a transcriptome atlas, and signatures of genome organization.";
RL Plant J. 93:338-354(2018).
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. ISWI subfamily.
CC {ECO:0000256|ARBA:ARBA00009687}.
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DR EMBL; CM000761; KXG36264.1; -; Genomic_DNA.
DR STRING; 4558.A0A1B6QEB1; -.
DR EnsemblPlants; KXG36264; KXG36264; SORBI_3002G308700.
DR Gramene; KXG36264; KXG36264; SORBI_3002G308700.
DR eggNOG; KOG0383; Eukaryota.
DR InParanoid; A0A1B6QEB1; -.
DR OMA; INICEDK; -.
DR Proteomes; UP000000768; Chromosome 2.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR GO; GO:0042735; C:endosperm protein body; IEA:EnsemblPlants.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IBA:GO_Central.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006338; P:chromatin remodeling; IBA:GO_Central.
DR CDD; cd18660; CD1_tandem; 1.
DR CDD; cd18659; CD2_tandem; 1.
DR CDD; cd15532; PHD2_CHD_II; 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 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; IPR001005; SANT/Myb.
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; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS50090; MYB_LIKE; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 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 Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000000768};
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 74..121
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 501..552
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 668..845
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 975..1134
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 1675..1727
FT /note="Myb-like"
FT /evidence="ECO:0000259|PROSITE:PS50090"
FT REGION 19..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 129..349
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 395..474
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1229..1268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1394..1421
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1985..2028
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2105..2133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..47
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 48..63
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 142..183
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 192..239
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 246..282
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 283..301
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 302..316
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 408..429
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 444..474
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1405..1420
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2105..2122
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2224 AA; 247098 MW; B28B77D1938224DD CRC64;
MKERSSLCES AADGNWGLKY KRKRSKLTSP SNENEATSPT SDSPMSHAST KKKLKHDTNI
SPSAKKIRGH DGYFFECVEC DLGGNLLCCD SCPRVYHLEC LNPPLKRAPP GNWQCPRCRP
KKGSLKLLGN VEADTSKHER STRMYAGTTS DSPPSHTKVS FKTRNSTQDK TGSNEQGKHS
SGGTMKGGDS GMKNNEVEKK KTLILHLKKR STKELSENAK SSKTEFVGEP SEEKTVKHGS
VLKLKKHPHR MDLSPNKSKS RRQNSQRESK RSGTKKLKYS TSDDDSVSSS EPSTSLDNSE
SPPKRKPSDG KAPSSSTKKG KKKVKFVEKK HSEEQGVAGD KITTPQEDQQ VDRILGCRLQ
TSQINPTSHA SLEQFESANL KVDGMESSRN GTVEDVCADG SANHSGHSLE MQKDRNSKSH
EKETIKQEQA KKILSVCSGD ETSIMKDDQV DRENVSPSKK GEDETRTDLP AEKDDTKLAV
TRADTMVRTN QEHTDESKQH GKIEEITDKD YNDAGYEFLI KWVGKSNIHN SWVAESEVKI
LAKRKLENYK AKYGTSLINI CKEQWCQPQR VIALRASVDE VEEALIKWCG LPYDECTWER
IDEPTLMKYS HLVTQFKNFE CQALDKDMVK DYANTRNRQE LNVLVDQPKE LQGGMLFPHQ
LEALNWLRKC WYKSKNVILA DEMGLGKTVS ACAFLSSLCC EFKISLPCLV LVPLSTMPNW
MAEFASWAPH LNVVEYHGSA RSRSIIRQYE WHAGDASQIG KTKRSYKFNV LLTTYEMVLV
DAAYLRSVSW EVLIVDEGHR LKNSSSKLFS LLNSLSFQHR VLLTGTPLQN NIGEMYNLLN
FLQPTSFPSL SSFEEKFNDL TTAEKVEELK KLVAPHMLRR LKKDAMQNIP PKTERMVPVE
LTSIQAEYYR AMLTKNYQVL RNIGKGGAHQ SLLNIVMQLR KVCNHPYLIP GTEPESGSPE
FLHDMRIKAS AKLALLHSML KILHKEGHRV LIFSQMTKLL DILEDYLTLE FGPKTFERVD
GSVSVAERQA AIARFNQDKT RFVFLLSTRS CGLGINLATA DTVIIYDSDF NPHADIQAMN
RAHRIGQSNR LLVYRLVVRA SVEERILQLA KKKLMLDQLF VNKSESQKEV EDIIRWGTEE
LFGSSDSVDD KDSNEASGPV ADVEFKHRRK TGGLGDVYED KCIGGSTKLV WDENAILKLL
DRSNLPSSLA EGTDGDLDND MLGTVKSIDW NDELNDDPGA NEDIAPIDND GSEQASESKQ
GATNRSEENE WDKLLRVRWE QYQIEEEASL GRGKRLRKAV SYRETFATLP NEALSEDSDE
GDEPKREYTA AGLALKEKYG KLRARQKERI AQRHIIKNYA DDNLEEFMTA YDSIANGPAE
NPLIIVEDPN SSQLSGAKRF SESTGEMRQS SKKSKRYSDI PQDIYARIPG NAASSKHHSK
ATDVFNPGTP DHLLPVLGLC APNADQVNSY KNSLCAPSIK EHKRASGDIV NKQLSTSADH
SNEHRNEAQP ASDKAIFPGA SEEALRRISN MIPESYFPFS HIPPVSGKGV DPVENPGPSI
ASFQGKLGLP NFSLEDNTPL KHIKPVPDIF PNLSLGAHKD YIRSSVPELP ESSLLPNFMA
DIAGTSKQKS FMSGLLPGLG LSPGQPIHSA MPDNHKKVLD NIMMRAQYAS NKFLKKRSKL
DYWSEDELDA LWIGVRRHGR GNWDAMLRDP KLKFLNNRTS EELASRWILE EQKIIDEPMS
TATRRSNSTA FPGISDAMMS RALNESNFSK MRMEQPKLQS HLTDIQLGSS DILSRFPHIE
AANYINSGEG GTPQIPWQDF KHRSSYGGDF HGGAFDKLEK PDVGPIPPFM PNPFMTDSIG
SLPINRKNNS SIPHSEIRSS SRENIHLSGV SDGQINLLHE MQRRVRSGKQ PMEMNLNHID
HSNSQLDNTS DLGGLKSNKL PHWLQEAVRA PSSKPPEREL PATVSAIAQS VCLLLGEQEP
SIPPFLIPEA PLSRPKDPRI NSKKRKLRKA QQSTSHVEHS KIGSGEGDCI TTPAPPSLEA
IATPSVHCND GAPSLNLNSA SLSSLAGSKG QDELPPTFEE SNQTVDCSEA LAAKLEAPEI
ACQITSSSPV DDKASESSGS PVKDTPDAGV RLQGSDNSAM AFSALPLVDE APGTSSRAAG
MPVACDCNDL KEDVPLDNAE STGNLEEPTD ELTLVDTDAV VASTFLSAKT ANEDRVDEMT
SDEH
//
