ID A8I437_MAIZE Unreviewed; 1435 AA.
AC A8I437;
DT 04-DEC-2007, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 2.
DT 27-MAR-2024, entry version 60.
DE SubName: Full=Mutant required to maintain repression 1 {ECO:0000313|EMBL:ABV80241.2};
GN Name=rmr1 {ECO:0000313|EMBL:ABV80241.2};
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:ABV80241.2};
RN [1] {ECO:0000313|EMBL:ABV80241.2}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=17941719; DOI=10.1371/journal.pbio.0050275;
RA Hale C.J., Stonaker J.L., Gross S.M., Hollick J.B.;
RT "A novel Snf2 protein maintains trans-generational regulatory states
RT established by paramutation in maize.";
RL PLoS Biol. 5:e275-e275(2007).
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DR EMBL; EU155003; ABV80241.2; -; Genomic_DNA.
DR ExpressionAtlas; A8I437; baseline and differential.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0080188; P:gene silencing by RNA-directed DNA methylation; IEA:InterPro.
DR CDD; cd18793; SF2_C_SNF; 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; IPR044567; CLSY/DRD1.
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 PANTHER; PTHR45821; SNF2 DOMAIN-CONTAINING PROTEIN CLASSY 2-RELATED; 1.
DR PANTHER; PTHR45821:SF26; SNF2_N DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT DOMAIN 883..1070
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1222..1379
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 97..255
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 305..337
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 364..397
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 460..512
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 600..653
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..39
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 102..117
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 128..142
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 148..210
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 305..327
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 460..502
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 600..615
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1435 AA; 161311 MW; F60BE9557A462A3C CRC64;
MDRATPRVCG RRGVSQAAVE AAPSSSRARR RDKAPAVVMD LGDDDCGGGG ARKTVGGAAG
RCEGSTKAPS PMLPPMMVPA GAVALRTRSR RRAMLAAAVV EEAPTKKKKK EGAIPDAAEA
TRGHGSKAAA TSMATSSHKR RAGTSRSTSR DKRRARSGRA SEPARVGRAR KRKRNELEAP
ARRERVKAPC VSESDDNSGR GDDASHDGDA EPRGGVAIGT DLVNGDHPAA KEVVEGAGDE
DTGDGGNSGL ASTADVVAEE MAPFEDDYDD EMLEEQLVGD VIRAYSNGRN LDSDGVDWEA
EDEMEFNDDA DNSDFMDDAD DSDFMDDAYE GGNSKPIQNH AKLEIQDWVN QKVVLSGGRC
EVRGEGDLEE ELGVGKEADE EDVEPKSEAA PGSDKRVLQL EILGSDEEIK VLENMSSAPS
RKASVQSKLP TIPSCVAWRT RSSWGVNQDR LSYDTYFEEL SDEPKEDDDD TEVELDEVED
DNNDDDSSDA YDKDDEEKEE EEEEAERRKL NNRICTSDED MINITVPTSR YDMFKKKNSS
RYDIEWVEDE DASVDMLQPV SFKKDSSWKP VAVGNDTFTE QQKRSRFTWE LERRKKLKLE
MKTNPLHERD LDSDPNSSGS DQIRKYGFKS DGSHKVDRKK KHTSPKSGKK PSSAIILKRQ
SLLKLLVDKM SGDKSLASFP FDQNPQLQFI FKEMHPLVFS FGDEDLVAAD RPEQDVGLDM
LWADFDFALE SENIGTYYDD ECQEGNQLDF SLASVTPCSR GKHEFVIDDQ IGIRCKYCSL
VNLEIKFMFP SLVSVFGEKS AWPNDKGVKN TLMFHDLYEQ GVNDTEQSQD IHQYGTVWNL
IPGVISTMYE HQREAFEFMW TNLVGDIRLD EIKHGAKPDV VGGCVICHAP GTGKTRLAIV
FIQTYMKVFP DCRPVIIAPR GMLFAWDEEF KKWNVDVPFH ILNTTDYTGK EDRDICKLIK
KEHRTEKLTR LVKLLSWNKG HGILGISYGL YTKLTSEKPG CTEENKVRSI LLDNPGLLVL
DEGHTPRNER NVMWKTLGNV KTEKRIILSG TPFQNNFLEL YNILCLVRPR FGEMFLTKSR
VGRRHYVSKK QKDKFSDKYE KGVWASLTSN VTDDNAEKVR SILKPFVHIH NGNILRTLPG
LRESVIILKP LPLQKSIIKK VENIGSGNNF EHEYVISLAS THPSLVTAIN MSEEEASLID
KPMLAKVRSN PYEGVKTRFV IEVVRLSEAL REKVLIFSQF IQPLELIKEH LRKFFKWREG
KEILQMDGKI LPRYRQASIE AFNNPNNDSR VLLASTRACC EGISLTGASR IVLLDVVWNP
AVGRQAISRA FRIGQKKFVY TYNLITYGTG EGDKYDRQAE KDHLSKLVFS TEDEFNNVRN
MLSKAEMEHC SKFISEDKVL EEMTSHDQLK GMFLKIHYPP TESNIVYSYN QIATE
//
