ID A0A287CVX9_ICTTR Unreviewed; 1029 AA.
AC A0A287CVX9;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 1 {ECO:0000313|Ensembl:ENSSTOP00000025424.1};
GN Name=SMARCA1 {ECO:0000313|Ensembl:ENSSTOP00000025424.1};
OS Ictidomys tridecemlineatus (Thirteen-lined ground squirrel) (Spermophilus
OS tridecemlineatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha; Sciuridae;
OC Xerinae; Marmotini; Ictidomys.
OX NCBI_TaxID=43179 {ECO:0000313|Ensembl:ENSSTOP00000025424.1, ECO:0000313|Proteomes:UP000005215};
RN [1] {ECO:0000313|Proteomes:UP000005215}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG The Broad Institute Genome Assembly & Analysis Group;
RG Computational R&D Group;
RG and Sequencing Platform;
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lindblad-Toh K.;
RT "The Draft Genome of Spermophilus tridecemlineatus.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSTOP00000025424.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. ISWI subfamily.
CC {ECO:0000256|ARBA:ARBA00009687}.
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DR EMBL; AGTP01013084; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01013085; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01013086; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_013211515.1; XM_013356061.1.
DR AlphaFoldDB; A0A287CVX9; -.
DR Ensembl; ENSSTOT00000034330.1; ENSSTOP00000025424.1; ENSSTOG00000014524.3.
DR GeneID; 101970417; -.
DR CTD; 6594; -.
DR GeneTree; ENSGT00940000157297; -.
DR OrthoDB; 5482994at2759; -.
DR Proteomes; UP000005215; Unassembled WGS sequence.
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; 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; 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; 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; 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 Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000005215}.
FT DOMAIN 166..331
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 461..612
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 814..866
FT /note="SANT"
FT /evidence="ECO:0000259|PROSITE:PS51293"
FT REGION 25..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 778..808
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 989..1029
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 786..808
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1014..1029
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1029 AA; 119636 MW; 6D7025655EB2774F CRC64;
MEPDTAAVAA TVAAADETAT IVVLEDEQPG PSTSKEEGAA AAATEATATT EKGEKKREKA
DRAKRFEFLL KQTELFAHFI QPSAQKSPTS PLNMKLGRPR IKKDEKQNLI SAGDYRHRRT
EQEEDEELLS ESRKTSNVCV RFEVSPSYVK GGPLRDYQIR GLNWLISLYE NGVNGILADE
MGLGKTLQTI ALLGYLKHYR NIPGPHMVLV PKSTLHNWMN EFKRWVPSLR VICFVGDKDA
RAAFIRDEMM PGEWDVCVTS YEMVIKEKSV FKKFHWRYLV IDEAHRIKNE KSKLSEIVRE
FKSTNRLLLT GTPLQNNLHE LWALLNFLLP DVFNSADDFD SWFDTKNCLG DQKLVERLHA
VLKPFLLRRI KTDVEKSLPP KKEIKIYLGL SKMQREWYTK ILMKDIDVLN SAGKMDKMRL
LNILMQLRKC CNHPYLFDGA EPGPPYTTDE HIVSNSGKMV VLDKLLAKLK EQGSRVLIFS
QMTRLLDILE DYCMWRSYEY CRLDGQTPHE EREEAIEAFN ATNSSKFIFM LSTRAGGLGI
NLASADVVIL YDSDWNPQVD LQAMDRAHRI GQKKPVRVFR LITDNTVEER IVERAEIKLR
LDSIVIQQGR LIDQQSNKLA KEEMLQMIRH GATHVFASKE SELTEEDITT ILERGEKKTA
EMNERLQKMG ESSLRNFRMD IEQSLYKFEG EDYREKQKLG MVEWIEPPKR ERKANYAVDA
YFREALRVSE PKIPKAPRPP KQPNVQDFQF FPPHLFELLE KEILYYRKTI GYKVPRNPDI
PNPALAQREE QKKIDGAEPL TPEETEEKEK LLTQGFTNWT KRDFNQFIKA NEKYGRDDID
NIAREVEGKS PEEVMEYSAV FWERCNELQD IEKIMAQIER GEARIQRRIS IKKALDAKIA
RYKAPFHQLR IQYGTSKGKN YTEEEDRFLI CMLHKMGFDR ENVYEELRQC VRNAPQFRFD
WFIKSRTAME FQRRCNTLIS LIEKENMEIE ERERAEKKKR ATKTPMSQKR KAESATESSG
KKDVKKVKS
//
