ID A0A0D9YYW7_9ORYZ Unreviewed; 914 AA.
AC A0A0D9YYW7;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=SWI/SNF complex subunit SWI3D {ECO:0008006|Google:ProtNLM};
OS Oryza glumipatula.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=40148 {ECO:0000313|EnsemblPlants:OGLUM02G35040.1};
RN [1] {ECO:0000313|EnsemblPlants:OGLUM02G35040.1}
RP NUCLEOTIDE SEQUENCE.
RA Wing R.A., Panaud O., Oliveira A.C.;
RT "Oryza genome evolution.";
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:OGLUM02G35040.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (APR-2015) to UniProtKB.
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DR AlphaFoldDB; A0A0D9YYW7; -.
DR STRING; 40148.A0A0D9YYW7; -.
DR EnsemblPlants; OGLUM02G35040.1; OGLUM02G35040.1; OGLUM02G35040.
DR Gramene; OGLUM02G35040.1; OGLUM02G35040.1; OGLUM02G35040.
DR eggNOG; KOG1279; Eukaryota.
DR HOGENOM; CLU_015614_0_0_1; -.
DR Proteomes; UP000026961; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProt.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0051171; P:regulation of nitrogen compound metabolic process; IEA:UniProt.
DR GO; GO:0080090; P:regulation of primary metabolic process; IEA:UniProt.
DR CDD; cd00167; SANT; 1.
DR CDD; cd02336; ZZ_RSC8; 1.
DR Gene3D; 3.30.60.90; -; 1.
DR Gene3D; 1.10.10.60; Homeodomain-like; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR017930; Myb_dom.
DR InterPro; IPR041984; Rsc8/Ssr1/Ssr2_ZZ.
DR InterPro; IPR001005; SANT/Myb.
DR InterPro; IPR017884; SANT_dom.
DR InterPro; IPR032451; SMARCC_C.
DR InterPro; IPR007526; SWIRM.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR000433; Znf_ZZ.
DR InterPro; IPR043145; Znf_ZZ_sf.
DR PANTHER; PTHR12802; SWI/SNF COMPLEX-RELATED; 1.
DR PANTHER; PTHR12802:SF179; SWI_SNF COMPLEX SUBUNIT SWI3D; 1.
DR Pfam; PF00249; Myb_DNA-binding; 1.
DR Pfam; PF04433; SWIRM; 1.
DR Pfam; PF16495; SWIRM-assoc_1; 1.
DR Pfam; PF00569; ZZ; 1.
DR SMART; SM00717; SANT; 1.
DR SMART; SM00291; ZnF_ZZ; 1.
DR SUPFAM; SSF46689; Homeodomain-like; 2.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS51294; HTH_MYB; 1.
DR PROSITE; PS50090; MYB_LIKE; 1.
DR PROSITE; PS51293; SANT; 1.
DR PROSITE; PS50934; SWIRM; 1.
DR PROSITE; PS01357; ZF_ZZ_1; 1.
DR PROSITE; PS50135; ZF_ZZ_2; 1.
PE 4: Predicted;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000026961};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00228}.
FT DOMAIN 131..228
FT /note="SWIRM"
FT /evidence="ECO:0000259|PROSITE:PS50934"
FT DOMAIN 296..350
FT /note="ZZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50135"
FT DOMAIN 353..404
FT /note="SANT"
FT /evidence="ECO:0000259|PROSITE:PS51293"
FT DOMAIN 357..404
FT /note="HTH myb-type"
FT /evidence="ECO:0000259|PROSITE:PS51294"
FT DOMAIN 357..400
FT /note="Myb-like"
FT /evidence="ECO:0000259|PROSITE:PS50090"
FT REGION 1..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 419..520
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 603..782
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 877..914
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 427..460
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 461..486
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 487..501
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 620..643
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 662..694
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 695..718
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 745..759
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 760..779
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 899..914
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 914 AA; 98596 MW; 77282AF0B3C64C45 CRC64;
MEPKSSASAA HQGGDAPAEA PRRRGGGGKR KSGGSSFTPS KRHAKERNAA FHVPPHLLHS
GPLTRAARQS PHKLAEEAAA AAAAGAGGSG AGGGKGGGDV IRLEGEEAPT EETPLVDEVF
EAVRSRGAGV HVVPTFAGWF SWKEIHPIEK QMLPSFFNGK SDKRTPEIYL GIRNFIMLKF
HANPQLQLES KDLAELSIGE ADAHQEVLKF LDHWGLINFH PFLPAGQEES KPEEAHGKSQ
SEEKASVLEQ LFKFESVQSY MIPLPKKGEV ETPAPLPSLL PDPALVEDVV SAAEPSVEYH
CNSCSVDCSK KRYHCRTQAD FDLCSDCYNE GKFDIGMAKT DFILMDSSEV SGASGTSWTD
EETLLLLEAL EIFGGKWTEI AEHVATKTKA QCMLHFLQMQ IEDRFHGDGD INQNIQENTE
QASAEKGAAE IPDKMEVEEK AEGKDTAGEK TPEKAEGNSV EAQTEDGNAI ENKDANNSGG
TDSVKSLNTD EPKKSSDADP PKISSDAEPV VKENSVDVDT SRENASNFAI DTLKSAFEAV
GYFPEHEGSF ADAGNPVMAL ASFLAGLVED DTATNSCRSS LKAISEVSPA LQLATRHCFI
LEDPPSDVKD MSGNASTTST DGDKRKDKDK TQDSIDSEVE GINKKGETVL SVEGKKSSPI
SPKGQDTDKK DECDEDPSVD PKHNNGKESD DPVSLDKSVS NNKKGNTMET SNPEMIEDKA
SSEVNPADDS SLEGKVEMKK TKDAVANATT AQEQKQSQIL ENGKMEEPKS TEDVAADEEN
SSRVTANLTD SITRLKRAAA TAISAAAVKA KLLADHEEEQ IRQLAALMID KLYRKVEAKV
SFLTEVEHLV QRTREYTEKT RKKLLMERNA IIAARMGSLP SRPNQPGAAG NRLPAGYGGP
IVRPPPNAMP RPSS
//
