ID A0A493SZY1_ANAPP Unreviewed; 997 AA.
AC A0A493SZY1;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 1 {ECO:0000313|Ensembl:ENSAPLP00000019068.1};
GN Name=SMARCA1 {ECO:0000313|Ensembl:ENSAPLP00000019068.1};
OS Anas platyrhynchos platyrhynchos (Northern mallard).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Anseriformes; Anatidae;
OC Anatinae; Anas.
OX NCBI_TaxID=8840 {ECO:0000313|Ensembl:ENSAPLP00000019068.1, ECO:0000313|Proteomes:UP000016666};
RN [1] {ECO:0000313|Ensembl:ENSAPLP00000019068.1, ECO:0000313|Proteomes:UP000016666}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Hou Z.-C., Zhou Z.-K., Zhu F., Hou S.-S.;
RT "A new Pekin duck reference genome.";
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSAPLP00000019068.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. ISWI subfamily.
CC {ECO:0000256|ARBA:ARBA00009687}.
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DR AlphaFoldDB; A0A493SZY1; -.
DR Ensembl; ENSAPLT00000024184.1; ENSAPLP00000019068.1; ENSAPLG00000013149.2.
DR GeneTree; ENSGT00940000157297; -.
DR OMA; TAFYRKE; -.
DR Proteomes; UP000016666; Chromosome 10.
DR GO; GO:0005634; C:nucleus; IEA:InterPro.
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:0031491; F:nucleosome binding; IEA:InterPro.
DR CDD; cd18065; DEXHc_SMARCA1; 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; 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; IPR044755; SMARCA1_N.
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; 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 Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000016666}.
FT DOMAIN 172..337
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 467..618
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 782..834
FT /note="SANT"
FT /evidence="ECO:0000259|PROSITE:PS51293"
FT REGION 1..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 739..772
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 958..997
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..32
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 754..772
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 982..997
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 997 AA; 115774 MW; FD3150D1DCE31D47 CRC64;
MDPGPGSPGA PAAARSDGEV PSTSTSGAQE PGSEEKNDPP FQLKPPPKAA RPEKEIDPEY
EEKMKADRAK RFEFLLKQTE LFAHFIQPAA QKSPTSPLKV KLGRPRIKKD EKQCLISAGD
YRHRRTEQEE DEELLSESRK TSNVCIRFEE SPSYVKGGTL RDYQVRGLNW MISLYENGVN
GILADEMGLG KTLQTIALLG YLKHYRNIPG PHMVLVPKST LHNWMNEFKR WVPSLRAVCL
IGDKDARAAF IRDVMMPGEW DVCVTSYEMV IKEKSVFKKF NWRYLVIDEA HRIKNEKSKL
SEIVREFKTT NRLLLTGTPL QNNLHELWAL LNFLLPDVFN SADDFDSWFD TKNCLGDQKL
VERLHAVLKP FLLRRIKAEV EKSLPPKKEV KIYLGLSKMQ REWYTRILMK DIDILNSAGK
MDKMRLLNIL MQLRKCCNHP YLFDGAEPGP PYTTDTHLIT NSGKMLVLDK LLAKLREQGS
RVLLFSQMTR LLDILEDYCM WRGYEYCRLD GQTPHEEREE AIDTFNAPNS SKFIFMLSTR
AGGLGINLAT ADVVILYDSD WNPQVDLQAM DRAHRIGQKK PVRVFRLITD NTVEERIVER
AEIKLRLDSI VIQQGRLIDQ QSNKLAKDEM LQMIRHGATH VFASKDSELT EEDITTILER
GEKKTAEMNE RLQKMGESSL RNFTMDTEMS LYNFEGEDYR EKQKLSMMEW IEPPKRERKA
NYAVDAYFRE ALRVSEPKVP KVPRNPDLPN AAQVQKEEQK KIDDSMPLTP EETEEKEKLL
TQGFTNWNKR DFNQFIKANE KYGRDDIDNI AREVEGKSPE EVIEYSAVFW ERCNELQDIE
RIMAQIERGE ARIQRRISIK KALDAKIARY KAPFHQLRIQ YGTNKGKNYT EEEDRFLICM
LHKMGFDKEN VYEELRQCVR NAPQFRFDWF IKSRTAMEFQ RRCNTLISLI EKENMEIEEK
ERAEKKKRGS KVTSSQKRKA DLATENSGKK DAKKVKS
//
