ID A0A673BKT9_9TELE Unreviewed; 1599 AA.
AC A0A673BKT9;
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:ENSSORP00005042390.1};
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:ENSSORP00005042390.1, ECO:0000313|Proteomes:UP000472271};
RN [1] {ECO:0000313|Ensembl:ENSSORP00005042390.1}
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:ENSSORP00005042390.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [3] {ECO:0000313|Ensembl:ENSSORP00005042390.1}
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; ENSSORT00005043468.1; ENSSORP00005042390.1; 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; 3.40.5.120:FF:000001; 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 196..231
FT /note="QLQ"
FT /evidence="ECO:0000259|PROSITE:PS51666"
FT DOMAIN 477..549
FT /note="HSA"
FT /evidence="ECO:0000259|PROSITE:PS51204"
FT DOMAIN 776..941
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1094..1255
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 1456..1526
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT REGION 1..199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 234..371
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 594..627
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 665..711
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1336..1440
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1545..1599
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 155..173
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 174..193
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 234..243
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 251..260
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 261..277
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 314..345
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 596..605
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 609..620
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 675..686
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1350..1370
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1383..1393
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1409..1418
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1545..1562
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1563..1573
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1579..1589
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1599 AA; 179265 MW; 402D685C9BE966DD CRC64;
MSTPDPPMGG TPRPGPSPGP GPSPGGMMGP SPGPSPGSTH SMMGPSPGPP GSGHPHPPQG
PSGYPQDNMH QMHKPMEAMH DKGMPDDPRY GQMKSMGMRP GGHSGMGPPP SPMDQHSQGY
PSPLGGSEHA PSPVPANGPP SGPMIPGGPP GPGAGPMEGS GDPNQGMGQP NRGGPQGPGG
PGGAAGGPGG SGGPTPFNQN QLHQLRAQIM AYKMLARSQP LPEHLQMAVQ GKRPMPGMQQ
QPMPNMPPST GPGGGPGAGP GPTQANYNRP HGMVGPNMAP PGPAGVPPGM QGQPTNGPPK
SWPEGPMVNA AAPSNPPQKL IPPQPTGRPS PAPPSVPPAA SPVMPPQTQS PGQPAQPPPM
MLHQKQSRIT PIQKPRGLDP VEILQEREYR LQARIAHRIQ ELENLPGSLA GDLRTKATIE
LKALRLLNFQ RQLRQEVVVC MRRDTALETA LNAKAYKRSK RQSLREARIT EKLEKQQKIE
QERKRRQKHQ EYLNSILQHA KDFKEYHRSI TAKIQKATKA VATYHANTER EQKKENERIE
KERMRRLMAE DEEGYRKLID QKKDKRLAYL LQQTDEYVAN LTELVRAHKA AQALKEKKKK
KKKKKPEPAE AGAPALGPDG EPLDETSQMS DLPVKVIHVD SGKILTGVDA PKAGQLEAWL
EMNPGYEVAP RSDSEDSGSD DEDEEEQPQH SSAPSEEKKK IPDPDSEDVS EVDVRHIIEH
AKQDVDDEYS SASFNRGLQS YYAVAHAVTE KVEKQSSLLV NGQLKQYQIK GLEWLVSLYN
NNLNGILADE MGLGKTIQTI ALITYLMEYK RLNGPFLVIV PLSTLSNWVY EFDKWAPSVV
KVSYKGSPAA RRSFVPILRS GKFNVLLTTY EYIIKDKQVL AKLRWKYMIV DEGHRMKNHH
CKLTQVLNTH YLAPRRLLLT GTPLQNKLPE LWALLNFLLP TIFKSCSTFE QWFNAPFAMT
GEKVDLNEEE TILIIRRLHK VLRPFLLRRL KKEVEAQLPE KVEYVIKCDM SALQRVLYRH
MQAKGVLLTD GSEKDKKGKG GTKTLMNTIM QLRKICNHPF MFQHIEESFS EHLGYSNGIV
SGPDLYRSSG KFELLDRILP KLRATNHKVL LFCQMTSLMN IMEDYFAYRN FKYLRLDGTT
KAEDRGMLLK TFNDPASEYF VFLLSTRAGG LGLNLQSADT VIIFDSDWNP HQDLQAQDRA
HRIGQQNEVR VLRLCTVNSV EEKILAAAKY KLNVDQKVIQ AGMFDQKSSG FERRAFLQAI
LEHEEQDEEE DEVPDDETVN QMIARSEEEF EQFMRMDLDR RREEARNPKR KPRLMEEDDL
PSWILKDDAE VERLTCEEEE EKMFGRGSRQ RKEVDYSDSL TEKQWLKAIE EGNLEDIEEE
VRHKKTTRKR KRERDHDGGM ATPSSSSGRG RDKDDDVKKA KKRGRPPAEK LSPNPPSLTK
KMKKIVDAVI KYKDGNGRQL SEVFIQLPSR KELPEYYELI RKPVDFRKIK ERIRSHKYRS
LNDLEKDVML LCQNAQTFNL EGSLIYEDSI VLQSVFTSVR QKIEKEEDKS ECDRKEKGER
GGKGQRRRGR GSRAKPVVSD DDSEDEQEEE RSASGSDED
//
