ID A0A2K6AEC0_MANLE Unreviewed; 1058 AA.
AC A0A2K6AEC0;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, 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:ENSMLEP00000038390.1};
GN Name=SMARCA1 {ECO:0000313|Ensembl:ENSMLEP00000038390.1};
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:ENSMLEP00000038390.1, ECO:0000313|Proteomes:UP000233140};
RN [1] {ECO:0000313|Ensembl:ENSMLEP00000038390.1}
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 RefSeq; XP_011844242.1; XM_011988852.1.
DR AlphaFoldDB; A0A2K6AEC0; -.
DR Ensembl; ENSMLET00000062001.1; ENSMLEP00000038390.1; ENSMLEG00000043198.1.
DR GeneID; 105545810; -.
DR CTD; 6594; -.
DR GeneTree; ENSGT00940000157297; -.
DR OrthoDB; 5482994at2759; -.
DR Proteomes; UP000233140; Unplaced.
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:UP000233140}.
FT DOMAIN 195..360
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 490..641
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 843..895
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 1018..1058
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1043..1058
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1058 AA; 122880 MW; 6ECF36D0C2B336CA 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
REEAIEAFNA PNSSKFIFML STRAGGLGIN LASADVVILY DSDWNPQVDL QAMDRAHRIG
QKKPVRVFRL ITDNTVEERI VERAEIKLRL DSIVIQQGRL IDQQSNKLAK EEMLQMIRHG
ATHVFASKES ELTDEDITTI LERGEKKTAE MNERLQKMGE SSLRNFRMDI EQSLYKFEGE
DYREKQKLGM VEWIEPPKRE RKANYAVDAY FREALRVSEP KIPKAPRPPK QPNVQDFQFF
PPRLFELLEK EILYYRKTIG YKVPRNPDIP NPALAQREEQ KKIDGAEPLT LEETEEKEKL
LTQGFTNWTK RDFNQFIKAN EKYGRDDIDN IAREVEGKSP EEVMEYSAVF WERCNELQDI
EKIMAQIERG EARIQRRISI KKALDAKIAR YKAPFHQLRI QYGTSKGKNY TEEEDRFLIC
MLHKMGFDRE NVYEELRQCV RNAPQFRFDW FIKSRTAMEF QRRCNTLISL IEKENMEIEE
RERAEKKKRA TKTPMSQKRK AESATESSGK KDVKKVKS
//
