ID A0A1D6MT73_MAIZE Unreviewed; 1094 AA.
AC A0A1D6MT73;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=ISWI chromatin-remodeling complex ATPase CHR11 {ECO:0000313|EMBL:ONM32108.1};
GN ORFNames=ZEAMMB73_Zm00001d040831 {ECO:0000313|EMBL:ONM32108.1};
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577 {ECO:0000313|EMBL:ONM32108.1};
RN [1] {ECO:0000313|EMBL:ONM32108.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Seedling {ECO:0000313|EMBL:ONM32108.1};
RG Maize Genome Sequencing Project;
RA Ware D.;
RT "Update maize B73 reference genome by single molecule sequencing
RT technologies.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. ISWI subfamily.
CC {ECO:0000256|ARBA:ARBA00009687}.
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DR EMBL; CM007649; ONM32108.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1D6MT73; -.
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: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; 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:SF49; SWI_SNF RELATED, MATRIX ASSOCIATED, ACTIN DEPENDENT REGULATOR OF CHROMATIN, SUBFAMILY A, MEMBER 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT REGION 1..124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 175..202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1034..1065
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 33..72
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 85..100
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 101..124
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 178..198
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1094 AA; 126359 MW; 1072C90A3DA30EB3 CRC64;
MAKPVKYDDE EEISSSSAEE DDDQSAAAAS GSGEEGDDDE EDAAALPTEE EEAEGEGQQE
EEVDEEEIEA VTTGAGAEDG EDASAATAAE GEEESQSTED DESVARDKDN GDETDAVVGK
REKTRLKELQ KMKKQKIQEI LDTQNAAIDA DMNNKGKGRL KYLLQQTEIF AHFAKGSQSN
EKKPRGRGRH ASKMTEEEED EEYLKEEEDA LAGAGGTRLV SQPSCIKGKM RDYQLAGLNW
LIRLYENGIN GILADEMGLG KTLQTISLLG YLHEFRGIAG PHMVVAPKST LGNWMKEIQR
FCPILRAVKF LGNPEERNHI RDNLLQPGKF DVCVTSFEMA IKEKSALRRF SWRYIIIDEA
HRIKNENSLL SKTMRIYNTN YRLLITGTPL QNNLHELWAL LNFLLPEIFS SAETFDEWFQ
ISGENDQQEV VQQLHKVLRP FLLRRLKSDV EKGLPPKKET ILKVGMSQMQ KQYYRALLQK
DLEVINAGGE RKRLLNIAMQ LRKCCNHPYL FQGAEPGPPY TTGEHLIENA GKMVLLDKLL
PKLKERDSRV LIFSQMTRLL DILEDYLMYR GYQYCRIDGN TGGEDRDASI EAFNSPGSEK
FVFLLSTRAG GLGINLATAD VVVLYDSDWN PQADLQAQDR AHRIGQKKEV QVFRFCTEYT
IEEKVIERAY KKLALDALVI QQGRLAEQKT VNKDDLLQMV RFGAEMVFSS KDSTITDEDI
DRIIAKGEET TAELDAKMKK FTEDAIKFKM DDNAELYDFD DEKDENKVDF KKLVSDNWIE
PPRRERKRNY SESDYFKQAL RQGAPAKPRE PRIPRMPHLH DFQFFNNQRL NELYEKEVRY
LMQANQKKDT IDGEDEDQLE PLTAEEQEEK EQLLEEGFAS WTRRDFNTFI RACEKYGRND
IKSISSEMEG KTEEEVQRYA RVFKERYKEL SDYDRIIKNI ERGEARISRK DEIMKAIGKK
LDRYKNPWLE LKIQYGQNKG KFYNEECDRF MLCMVHKLGY GNWDELKAAF RMSPLFRFDW
FVKSRTTQEL ARRCDTLIRL VEKENQEYDE QERQARKEKR LAKANPKLIR YSSLESVREA
DHVWHPPLDM PSLQ
//
