ID A0A0D9S164_CHLSB Unreviewed; 969 AA.
AC A0A0D9S164;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 24-JAN-2024, entry version 53.
DE SubName: Full=SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 5 {ECO:0000313|Ensembl:ENSCSAP00000014603.1};
GN Name=SMARCA5 {ECO:0000313|Ensembl:ENSCSAP00000014603.1};
OS Chlorocebus sabaeus (Green monkey) (Cercopithecus sabaeus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Chlorocebus.
OX NCBI_TaxID=60711 {ECO:0000313|Ensembl:ENSCSAP00000014603.1, ECO:0000313|Proteomes:UP000029965};
RN [1] {ECO:0000313|Ensembl:ENSCSAP00000014603.1, ECO:0000313|Proteomes:UP000029965}
RP NUCLEOTIDE SEQUENCE.
RA Warren W., Wilson R.K.;
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCSAP00000014603.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (JUL-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 EMBL; AQIB01017447; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_007998076.1; XM_007999885.1.
DR AlphaFoldDB; A0A0D9S164; -.
DR STRING; 60711.ENSCSAP00000014603; -.
DR Ensembl; ENSCSAT00000001472.1; ENSCSAP00000014603.1; ENSCSAG00000003448.1.
DR GeneID; 103236313; -.
DR CTD; 8467; -.
DR eggNOG; KOG0385; Eukaryota.
DR GeneTree; ENSGT00940000156733; -.
DR OMA; PRMDEWQ; -.
DR OrthoDB; 5482994at2759; -.
DR BioGRID-ORCS; 103236313; 10 hits in 23 CRISPR screens.
DR Proteomes; UP000029965; Chromosome 7.
DR Bgee; ENSCSAG00000003448; Expressed in adrenal cortex and 7 other cell types or tissues.
DR GO; GO:0016590; C:ACF complex; IEA:Ensembl.
DR GO; GO:0110016; C:B-WICH complex; IEA:Ensembl.
DR GO; GO:0005677; C:chromatin silencing complex; IEA:Ensembl.
DR GO; GO:0000793; C:condensed chromosome; IEA:Ensembl.
DR GO; GO:0001650; C:fibrillar center; IEA:Ensembl.
DR GO; GO:0090536; C:NoRC complex; IEA:Ensembl.
DR GO; GO:0043596; C:nuclear replication fork; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0016589; C:NURF complex; IEA:Ensembl.
DR GO; GO:0005721; C:pericentric heterochromatin; IEA:Ensembl.
DR GO; GO:0031213; C:RSF complex; IEA:Ensembl.
DR GO; GO:0035861; C:site of double-strand break; IEA:Ensembl.
DR GO; GO:0090535; C:WICH complex; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:Ensembl.
DR GO; GO:0003677; F:DNA binding; IEA:Ensembl.
DR GO; GO:0042393; F:histone binding; IEA:Ensembl.
DR GO; GO:0140751; F:histone octamer slider activity; IEA:Ensembl.
DR GO; GO:0031491; F:nucleosome binding; IEA:InterPro.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEA:Ensembl.
DR GO; GO:0006281; P:DNA repair; IEA:Ensembl.
DR GO; GO:0006352; P:DNA-templated transcription initiation; IEA:Ensembl.
DR GO; GO:1905213; P:negative regulation of mitotic chromosome condensation; IEA:Ensembl.
DR GO; GO:0016479; P:negative regulation of transcription by RNA polymerase I; IEA:Ensembl.
DR GO; GO:0006334; P:nucleosome assembly; IEA:Ensembl.
DR GO; GO:0045740; P:positive regulation of DNA replication; IEA:Ensembl.
DR GO; GO:0031065; P:positive regulation of histone deacetylation; IEA:Ensembl.
DR GO; GO:0031062; P:positive regulation of histone methylation; IEA:Ensembl.
DR GO; GO:0045945; P:positive regulation of transcription by RNA polymerase III; IEA:Ensembl.
DR GO; GO:0000183; P:rDNA heterochromatin formation; IEA:Ensembl.
DR GO; GO:0044030; P:regulation of DNA methylation; IEA:Ensembl.
DR CDD; cd18064; DEXHc_SMARCA5; 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; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000029965}.
FT DOMAIN 109..274
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 404..555
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 757..809
FT /note="SANT"
FT /evidence="ECO:0000259|PROSITE:PS51293"
FT REGION 29..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 932..969
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 726..757
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 932..962
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 969 AA; 113748 MW; 2086277580931F39 CRC64;
MQTDRANRFE YLLKQTELFA HFIQPAAQKT PTSPLKMKPG RPRIKKDEKQ NLLSVGDYRH
RRTEQEEDEE LLTESSKATN VCTRFEDSPS YVKWGKLRDY QVRGLNWLIS LYENGINGIL
ADEMGLGKTL QTISLLGYMK HYRNIPGPHM VLVPKSTLHN WMSEFKRWVP TLRSVCLIGD
KEQRAAFVRD VLLPGEWDVC VTSYEMLIKE KSVFKKFNWR YLVIDEAHRI KNEKSKLSEI
VREFKTTNRL LLTGTPLQNN LHELWSLLNF LLPDVFNSAD DFDSWFDTNN CLGDQKLVER
LHMVLRPFLL RRIKADVEKS LPPKKEVKIY VGLSKMQREW YTRILMKDID ILNSAGKMDK
MRLLNILMQL RKCCNHPYLF DGAEPGPPYT TDMHLVTNSG KMVVLDKLLP KLKEQGSRVL
IFSQMTRVLD ILEDYCMWRN YEYCRLDGQT PHDERQDSIN AYNEPNSTKF VFMLSTRAGG
LGINLATADV VILYDSDWNP QVDLQAMDRA HRIGQTKTVR VFRFITDNTV EERIVERAEM
KLRLDSIVIQ QGRLVDQNLN KIGKDEMLQM IRHGATHVFA SKESEITDED IDGILERGAK
KTAEMNEKLS KMGESSLRNF TMDTESSVYN FEGEDYREKQ KIAFTEWIEP PKRERKANYA
VDAYFREALR VSEPKAPKAP RPPKQPNVQD FQFFPPRLFE LLEKEILFYR KTIGYKVPRN
PELPNAAQAQ KEEQLKIDEA ESLNDEELEE KEKLLTQGFT NWNKRDFNQF IKANEKWGRD
DIENIAREVE GKTPEEVIEY SAVFWERCNE LQDIEKIMAQ IERGEARIQR RISIKKALDT
KIGRYKAPFH QLRISYGTNK GKNYTEEEDR FLICMLHKLG FDKENVYDEL RQCIRNSPQF
RFDWFLKSRT AMELQRRCNT LITLIERENM ELEEKEKAEK KKRGPKPSTQ KRKMDGAPDG
RGRKKKLKL
//