ID A0A673BQB8_9TELE Unreviewed; 1476 AA.
AC A0A673BQB8;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 1.
DT 28-JAN-2026, entry version 28.
DE RecName: Full=SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 4 {ECO:0008006|Google:ProtNLM};
GN Name=smarca4a {ECO:0000313|Ensembl:ENSSORP00005042408.1};
OS Sphaeramia orbicularis (orbiculate cardinalfish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Gobiaria; Kurtiformes; Apogonoidei; Apogonidae; Apogoninae; Sphaeramia.
OX NCBI_TaxID=375764 {ECO:0000313|Ensembl:ENSSORP00005042408.1, ECO:0000313|Proteomes:UP000472271};
RN [1] {ECO:0000313|Ensembl:ENSSORP00005042408.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Wellcome Sanger Institute Data Sharing;
RL Submitted (JUN-2019) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSORP00005042408.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [3] {ECO:0000313|Ensembl:ENSSORP00005042408.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2025) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family.
CC {ECO:0000256|ARBA:ARBA00007025}.
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DR Ensembl; ENSSORT00005043486.1; ENSSORP00005042408.1; ENSSORG00005019638.1.
DR Proteomes; UP000472271; Chromosome 8.
DR GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-ARBA.
DR GO; GO:0016514; C:SWI/SNF complex; IEA:UniProtKB-ARBA.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0042393; F:histone binding; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0048513; P:animal organ development; IEA:UniProtKB-ARBA.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR GO; GO:0048731; P:system development; IEA:UniProtKB-ARBA.
DR CDD; cd05516; Bromo_SNF2L2; 1.
DR CDD; cd18062; DEXHc_SMARCA4; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR FunFam; 3.40.50.10810:FF:000008; Chromatin structure-remodeling complex subunit snf21; 1.
DR FunFam; 1.20.5.170:FF:000008; probable global transcription activator SNF2L2 isoform X1; 1.
DR FunFam; 1.20.920.10:FF:000004; probable global transcription activator SNF2L2 isoform X1; 1.
DR FunFam; 3.40.50.300:FF:003020; SNF2-related domain-containing protein; 1.
DR Gene3D; 1.20.5.170; -; 1.
DR Gene3D; 3.40.5.120; -; 1.
DR Gene3D; 1.20.920.10; Bromodomain-like; 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; IPR030100; BRG1_ATP-bd.
DR InterPro; IPR006576; BRK_domain.
DR InterPro; IPR037259; BRK_sf.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR018359; Bromodomain_CS.
DR InterPro; IPR014978; Gln-Leu-Gln_QLQ.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C-like.
DR InterPro; IPR014012; HSA_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR029295; SnAC.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR049730; SNF2/RAD54-like_C.
DR InterPro; IPR000330; SNF2_N.
DR PANTHER; PTHR10799; SNF2/RAD54 HELICASE FAMILY; 1.
DR Pfam; PF07533; BRK; 1.
DR Pfam; PF00439; Bromodomain; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF07529; HSA; 1.
DR Pfam; PF08880; QLQ; 1.
DR Pfam; PF14619; SnAC; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR PRINTS; PR00503; BROMODOMAIN.
DR SMART; SM00592; BRK; 1.
DR SMART; SM00297; BROMO; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00573; HSA; 1.
DR SMART; SM00951; QLQ; 1.
DR SMART; SM01314; SnAC; 1.
DR SUPFAM; SSF160481; BRK domain-like; 1.
DR SUPFAM; SSF47370; Bromodomain; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS00633; BROMODOMAIN_1; 1.
DR PROSITE; PS50014; BROMODOMAIN_2; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51204; HSA; 1.
DR PROSITE; PS51666; QLQ; 1.
PE 3: Inferred from homology;
KW Activator {ECO:0000256|ARBA:ARBA00023159};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Bromodomain {ECO:0000256|ARBA:ARBA00023117, ECO:0000256|PROSITE-
KW ProRule:PRU00035}; Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000472271};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT DOMAIN 155..190
FT /note="QLQ"
FT /evidence="ECO:0000259|PROSITE:PS51666"
FT DOMAIN 396..468
FT /note="HSA"
FT /evidence="ECO:0000259|PROSITE:PS51204"
FT DOMAIN 679..844
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 997..1158
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 1347..1417
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT REGION 1..153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 193..281
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 513..546
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1239..1260
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1283..1322
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1434..1463
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..23
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..45
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..60
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 74..89
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 132..153
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 193..203
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 233..264
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 515..524
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 528..539
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1437..1458
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1476 AA; 167719 MW; AA26E2EF23AF708E CRC64;
MSTPDPPMGG TPRPGPSPGP GPSPGGMMGP SPGPSPGSTH SMMGPSPGPP GSGHPHPPQG
PSGYPQDNMH QMHKPMEAMH DKGMPDDPRY GQMKSMGMRP GGHSGMGPPP SPMDQHSQGY
PSPLGGSEHA PSPVPANGPP SGPMIPGGPP GGPTPFNQNQ LHQLRAQIMA YKMLARSQPL
PEHLQMAVQG KRPMPGMQQQ PMPNICPGQA DPKQLICLPS SPSGPMVNAA APSNPPQKLI
PPQPTGRPSP APPSVPPAAS PVMPPQTQSP GQPAQPPPMM LHQKQSRITP IQKPRGLDPV
EILQEREYRL QARIAHRIQE LENLPGSLAG DLRTKATIEL KALRLLNFQR QLRQEVVVCM
RRDTALETAL NAKAYKRSKR QSLREARITE KLEKQQKIEQ ERKRRQKHQE YLNSILQHAK
DFKEYHRSIT AKIQKATKAV ATYHANTERE QKKENERIEK ERMRRLMAED EEGYRKLIDQ
KKDKRLAYLL QQTDEYVANL TELVRAHKAA QALKEKKKKK KKKKPEPAEA GAPALGPDGE
PLDETSQMSD LPVKVIHVDS GKILTGVDAP KAGQLEAWLE MNPGLVPYLS GNVNLKLSLP
EDEIFAVFHP SKVCVFVFFS TRHAKQDVDD EYSSASFNRG LQSYYAVAHA VTEKVEKQSS
LLVNGQLKQY QIKGLEWLVS LYNNNLNGIL ADEMGLGKTI QTIALITYLM EYKRLNGPFL
VIVPLSTLSN WVYEFDKWAP SVVKVSYKGS PAARRSFVPI LRSGKFNVLL TTYEYIIKDK
QVLAKLRWKY MIVDEGHRMK NHHCKLTQVL NTHYLAPRRL LLTGTPLQNK LPELWALLNF
LLPTIFKSCS TFEQWFNAPF AMTGEKVDLN EEETILIIRR LHKVLRPFLL RRLKKEVEAQ
LPEKVEYVIK CDMSALQRVL YRHMQAKGVL LTDGSEKDKK GKGGTKTLMN TIMQLRKICN
HPFMFQHIEE SFSEHLGYSN GIVSGPDLYR SSGKFELLDR ILPKLRATNH KVLLFCQMTS
LMNIMEDYFA YRNFKYLRLD GTTKAEDRGM LLKTFNDPAS EYFVFLLSTR AGGLGLNLQS
ADTVIIFDSD WNPHQDLQAQ DRAHRIGQQN EVRVLRLCTV NSVEEKILAA AKYKLNVDQK
VIQAGMFDQK SSGFERRAFL QAILEHEEQD EEEDEVPDDE TVNQMIARSE EEFEQFMRMD
LDRRREEARN PKRKPRLMEE DDLPSWILKD DAEVERLTCE EEEEKMFGRG SRQRKEVDYS
DSLTEKQWLK AIEEGNLEDI EEEVRHKKTT RKRRDKDDDV KKAKKRGRPP AEKLSPNPPS
LTKKMKKIVD AVIKYKDGVH ACFVCSNGRQ LSEVFIQLPS RKELPEYYEL IRKPVDFRKI
KERIRSHKYR SLNDLEKDVM LLCQNAQTFN LEGSLIYEDS IVLQSVFTSV RQKIEKEEDS
EGEDSEEEEE EIDEGSESEC EHHKQTVNLH KYLLCK
//
