ID A0A3B6TEW7_WHEAT Unreviewed; 1306 AA.
AC A0A3B6TEW7;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=CHD3-type chromatin-remodeling factor PICKLE {ECO:0008006|Google:ProtNLM};
GN ORFNames=CFC21_107879 {ECO:0000313|EMBL:KAF7107217.1};
OS Triticum aestivum (Wheat).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX NCBI_TaxID=4565 {ECO:0000313|EnsemblPlants:TraesCS7D02G148900.1};
RN [1] {ECO:0000313|EMBL:KAF7107217.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf {ECO:0000313|EMBL:KAF7107217.1};
RX PubMed=29069494;
RA Zimin A.V., Puiu D., Hall R., Kingan S., Clavijo B.J., Salzberg S.L.;
RT "The first near-complete assembly of the hexaploid bread wheat genome,
RT Triticum aestivum.";
RL Gigascience 6:1-7(2017).
RN [2] {ECO:0000313|EnsemblPlants:TraesCS7D02G148900.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Chinese Spring
RC {ECO:0000313|EnsemblPlants:TraesCS7D02G148900.1};
RX PubMed=30115783; DOI=10.1126/science.aar7191;
RG International wheat genome sequencing consortium (IWGSC);
RT "Shifting the limits in wheat research and breeding using a fully annotated
RT reference genome.";
RL Science 361:EAAR7191-EAAR7191(2018).
RN [3] {ECO:0000313|EnsemblPlants:TraesCS7D02G148900.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (OCT-2018) to UniProtKB.
RN [4] {ECO:0000313|EMBL:KAF7107217.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf {ECO:0000313|EMBL:KAF7107217.1};
RA Zimin A.V., Puiu D., Shumante A., Alonge M., Salzberg S.L.;
RT "The second near-complete assembly of the hexaploid bread wheat (Triticum
RT aestivum) genome.";
RL Submitted (MAR-2020) to the EMBL/GenBank/DDBJ databases.
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; CM022231; KAF7107217.1; -; Genomic_DNA.
DR EnsemblPlants; TraesCS7D02G148900.1; TraesCS7D02G148900.1; TraesCS7D02G148900.
DR Gramene; TraesCS7D02G148900.1; TraesCS7D02G148900.1; TraesCS7D02G148900.
DR Gramene; TraesCS7D03G0334000.1; TraesCS7D03G0334000.1.CDS; TraesCS7D03G0334000.
DR Gramene; TraesRN7D0100347500.1; TraesRN7D0100347500.1; TraesRN7D0100347500.
DR Proteomes; UP000019116; Chromosome 7D.
DR Proteomes; UP000815260; Chromosome 7D.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:0003677; F:DNA binding; 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; cd18793; SF2_C_SNF; 1.
DR Gene3D; 2.40.50.40; -; 2.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
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; IPR009462; CHD_II_SANT-like.
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; 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; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR45623:SF17; CHD3-TYPE CHROMATIN-REMODELING FACTOR CHR7-RELATED; 1.
DR PANTHER; PTHR45623; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 3-RELATED-RELATED; 1.
DR Pfam; PF06461; CHDII_SANT-like; 1.
DR Pfam; PF00385; Chromo; 2.
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; SM01146; DUF1086; 1.
DR SMART; SM01147; DUF1087; 1.
DR SMART; SM00249; PHD; 1.
DR SUPFAM; SSF54160; Chromo domain-like; 2.
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:UP000019116};
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 55..101
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 103..184
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 194..254
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 290..477
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 605..784
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 15..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 849..911
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1277..1306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 849..877
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 888..911
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1306 AA; 149475 MW; F5ED9B49F078761F CRC64;
MSSLVERLRV RSDKRPRYTL DESDDDFPPR GGNGKGKDRD GDPPVKQIER EDAKEDACRK
CGLSDNLVSC TTCTYAFHRK CLVPCLNITS DKWSCPECVS PLTEMEKILD CETKVASEET
SSSESGSNKK PVKQYLIKWK GLSHIHCTWV SEDEYFEAAK IHPRLKTRLN NFNRQFESTD
KSDDDYVPIR PEWTTVDRVL ASRKNSSGER EYYVKWKELS YDECTWESES DISVFQPQIE
RYNEILSKRK KSTDKSKNAD RAMRHAEGTP EFLTGGTLHP YQLEGLNFLR YSWSINKRVI
LGDEMGLGKT IQSIAFLASV SEDKFGPHLV VAPLSTLRNW EREFATWAPQ MNVIMYFGSG
SSRDIIKKYE FYYSKDNPKK LKKNKSSSSN DEKKQSRIKF DVLLTSYEMI NMDSAVLKTI
EWECMIVDEG HRLKNKDSKL FGLLKDYHTQ HRVLLTGTPV QNNLDELFML MHFLEGETFG
SISDLQEEFK DINQDKQVEK LHGMLKPHLL RRFKKDVMKE LPPKKELILR VELTSKQKEY
YKAILTKNYA VLSRRGGGHV SLINVVMELR KLCCHGFMTD EPDTEPASPE EGLRRLLDSS
GKMQLLDKMM VKLKEQGHRV LIYSQFQHML DLLEDYLSYR KWSYERIDGK IGGAERQIRI
DRFNAKTSTS DWNPHADLQA MARAHRLGQT SKVMIYRLVS RGTIEERMMQ LTKKKMILEH
LVVGRLTKAS NVNQEELDDI IRYGSKELFD DDEDEAGKSR QIHYDDAAID RLLDRDQVDE
EEYLEDEEDD EFLKGFKVAN FEYIDEAKAL AAKEEARKKA EAEAASNKAN YWEELLKDRC
VEQEVEEIAM GKGKRSRKQM AAADEDDITG LHELSSEDED YSYDDDVSDN DTSLPANVSG
RKAQYSKKNS RNVDSLPLME GEGRALKVYG FNHVQRTQFL QTLMRYGFQN YDWKEYLPRL
KGKSVEEIQR YGELVMAHLV EDTNDSPTYA DGVPKEMRAD ETLVRLAKIS LVEEKVAAME
QGKITKLFPN YLLHEFTGLS GGRIWKGEHD LLLLKALIKH GYARWQYISD DRDNGLFETA
RRELNLPSAN ELISSQSNNE ANGNLENTQE VQVNPTSLSQ YRDIQRKIVE FIRKRYHILE
KCLDIEYAVI KTNTPVPDDL TEQNVPMGHS PAVPDISEVL RELPPLVPIS AKEVASDGST
DQAHLSHLYN KMCGVLEDSG PRALNSFCGD KAASASLANS LHQFEKVCED VDRVLRVQEN
GAATPKEQVV DASVEEAKPP QDAGVVAANG VGPSTVKPED KMEIDG
//
