ID A0A2K6AEA3_MANLE Unreviewed; 1070 AA.
AC A0A2K6AEA3;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE SubName: Full=SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 1 {ECO:0000313|Ensembl:ENSMLEP00000038396.1};
GN Name=SMARCA1 {ECO:0000313|Ensembl:ENSMLEP00000038396.1};
OS Mandrillus leucophaeus (Drill) (Papio leucophaeus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Mandrillus.
OX NCBI_TaxID=9568 {ECO:0000313|Ensembl:ENSMLEP00000038396.1, ECO:0000313|Proteomes:UP000233140};
RN [1] {ECO:0000313|Ensembl:ENSMLEP00000038396.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. ISWI subfamily.
CC {ECO:0000256|ARBA:ARBA00009687}.
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DR RefSeq; XP_011844241.1; XM_011988851.1.
DR AlphaFoldDB; A0A2K6AEA3; -.
DR STRING; 9568.ENSMLEP00000038396; -.
DR Ensembl; ENSMLET00000062007.1; ENSMLEP00000038396.1; ENSMLEG00000043198.1.
DR GeneID; 105545810; -.
DR KEGG; mleu:105545810; -.
DR CTD; 6594; -.
DR GeneTree; ENSGT00940000157297; -.
DR OMA; VHDYQFF; -.
DR OrthoDB; 5482994at2759; -.
DR Proteomes; UP000233140; Unplaced.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
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; IPR000330; SNF2_N.
DR PANTHER; PTHR45623; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 3-RELATED-RELATED; 1.
DR PANTHER; PTHR45623:SF49; ISW-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:UP000233140}.
FT DOMAIN 195..360
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 490..653
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 855..907
FT /note="SANT"
FT /evidence="ECO:0000259|PROSITE:PS51293"
FT REGION 25..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1030..1070
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1055..1070
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1070 AA; 124343 MW; 48C04BDDE6470173 CRC64;
MEQDTAAVAA TVAAADATAT IVVIEDEQPG PSTSQEEGAA AAATEATAAT EKGEKKKEKN
VSSFQLKLAA KAPKSEKEMD PEYEEKMKAD RAKRFEFLLK QTELFAHFIQ PSAQKSPTSP
LNMKLGRPRI KKDEKQSLIS AGDYRHRRTE QEEDEELLSE SRKTSNVCIR FEVSPSYVKG
GPLRDYQIRG LNWLISLYEN GVNGILADEM GLGKTLQTIA LLGYLKHYRN IPGPHMVLVP
KSTLHNWMNE FKRWVPSLRV ICFVGDKDAR AAFIRDEMMP GEWDVCVTSY EMVIKEKSVF
KKFHWRYLVI DEAHRIKNEK SKLSEIVREF KSTNRLLLTG TPLQNNLHEL WALLNFLLPD
VFNSADDFDS WFDTKNCLGD QKLVERLHAV LKPFLLRRIK TDVEKSLPPK KEIKIYLGLS
KMQREWYTKI LMKDIDVLNS SGKMDKMRLL NILMQLRKCC NHPYLFDGAE PGPPYTTDEH
IVSNSGKMVV LDKLLAKLKE QGSRVLIFSQ MTRLLDILED YCMWRGYEYC RLDGQTPHEE
REDKFLEVEF LGQREAIEAF NAPNSSKFIF MLSTRAGGLG INLASADVVI LYDSDWNPQV
DLQAMDRAHR IGQKKPVRVF RLITDNTVEE RIVERAEIKL RLDSIVIQQG RLIDQQSNKL
AKEEMLQMIR HGATHVFASK ESELTDEDIT TILERGEKKT AEMNERLQKM GESSLRNFRM
DIEQSLYKFE GEDYREKQKL GMVEWIEPPK RERKANYAVD AYFREALRVS EPKIPKAPRP
PKQPNVQDFQ FFPPRLFELL EKEILYYRKT IGYKVPRNPD IPNPALAQRE EQKKIDGAEP
LTLEETEEKE KLLTQGFTNW TKRDFNQFIK ANEKYGRDDI DNIAREVEGK SPEEVMEYSA
VFWERCNELQ DIEKIMAQIE RGEARIQRRI SIKKALDAKI ARYKAPFHQL RIQYGTSKGK
NYTEEEDRFL ICMLHKMGFD RENVYEELRQ CVRNAPQFRF DWFIKSRTAM EFQRRCNTLI
SLIEKENMEI EERERAEKKK RATKTPMSQK RKAESATESS GKKDVKKVKS
//