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Database: UniProt
Entry: A0A2K6AEA3_MANLE
LinkDB: A0A2K6AEA3_MANLE
Original site: A0A2K6AEA3_MANLE 
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
//
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