ID A0A1S3L562_SALSA Unreviewed; 1791 AA.
AC A0A1S3L562;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Transcription activator BRG1-like {ECO:0000313|RefSeq:XP_013986111.1};
GN Name=LOC106564512 {ECO:0000313|RefSeq:XP_013986111.1};
OS Salmo salar (Atlantic salmon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8030 {ECO:0000313|Proteomes:UP000087266, ECO:0000313|RefSeq:XP_013986111.1};
RN [1] {ECO:0000313|RefSeq:XP_013986111.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_013986111.1};
RG RefSeq;
RL Submitted (NOV-2023) 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 RefSeq; XP_013986111.1; XM_014130636.1.
DR STRING; 8030.ENSSSAP00000029155; -.
DR PaxDb; 8030-ENSSSAP00000029155; -.
DR KEGG; sasa:106564512; -.
DR OrthoDB; 5482994at2759; -.
DR Proteomes; UP000087266; Chromosome ssa12.
DR GO; GO:0070603; C:SWI/SNF superfamily-type complex; IEA:UniProt.
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: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:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd05516; Bromo_SNF2L2; 1.
DR CDD; cd18793; SF2_C_SNF; 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; 3.
DR Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1.
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.
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 PANTHER; PTHR10799:SF76; TRANSCRIPTION ACTIVATOR BRG1; 1.
DR Pfam; PF07533; BRK; 1.
DR Pfam; PF00439; Bromodomain; 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; 3.
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 ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Bromodomain {ECO:0000256|ARBA:ARBA00023117, ECO:0000256|PROSITE-
KW ProRule:PRU00035}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000087266}.
FT DOMAIN 342..377
FT /note="QLQ"
FT /evidence="ECO:0000259|PROSITE:PS51666"
FT DOMAIN 636..708
FT /note="HSA"
FT /evidence="ECO:0000259|PROSITE:PS51204"
FT DOMAIN 948..1113
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1158..1323
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 1622..1692
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT REGION 1..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 233..345
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 377..523
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 755..786
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 824..853
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1419..1440
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1504..1605
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1709..1791
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..31
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 252..271
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 284..320
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 321..337
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 476..519
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 835..849
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1504..1549
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1572..1593
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1714..1731
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1732..1755
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1772..1791
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1791 AA; 201038 MW; 36AD50C06425525B CRC64;
MSTPDPPIGG TPRQGPSPGP GPSPGAMLGP SPGPSPGGSS HSMMGPSPGP PSLPQPGPSG
YSEENMHPLH KPLEGMERTT MERTAMERTA MERTGIERTT MERTGMERTG MERTGMERSG
MERTGMERTG MERTGMERTG MERTGMERTG MERTGMERTA MERTAMERTA MERTAMERTA
MERTAMERTS MERTAMERTA MERTVMERTA MERTGMHEKG MSEESRFAQM KGMPMRQGGH
SGMGPPPSPM DQHSQGYHSP LGGSDHSSPV PSNGPPSGPL QPSSAGPNPS DTSSNPDSQT
LGGQNQQQNR PGGPQQSGSG PGPHGPSPGP TTPGGPGGGP TPFNQNQLHQ LRAQIMAYKM
LARGQPLPDH LQMAVQGKRP MGCSPGMQGP GPGQGGLGQP MPSLAPGGPG GVGPGQGPGG
PMGQGYSRAH GMMGPNMPPP GPSGPTGMQG QNPNGPPKSW SEGPMVNAAA PSNAPQKLIP
PQPTGRPSPA PPSIPPAASP VMPPQTQSPG QPVQPPPMVP HHAKQNRITP IQKPHGLDPV
EILQEREYRL QARITHRIAE LENLPGSLAG DLRTKATIEL KALQLLNFQR QLRQEVVVCM
RRDTALETAL DAKAYKRSKR QSLREARITE KLEKQQKIEQ ERKRRQKHQE YLSIILAHAK
DFKEYHRSIT AKIQKATKAV ATYHANTERE QKKENERIEK ERMRRLMAED EEGYRKLIDQ
KKDKRLAYLL QQTDEYVANL TELVRAHKLV QALKEKKKKR KKKKLENAEG QTPVLGPDGE
PLDETSQMSD LPVKVIHVDS GNILTGADAP KAGQLDTWLE MNPGYEVAPR SDSEDSGSEE
EEEEEEEPQP AVPPVVVLPG LVGLEEKKKK IPDPDSEEVS EVDVRHIIEH AKQDVDDEYN
SAEAAFARGL QSYYAVAHAV TERVEKQSTI LINGQLKQYQ IKGLEWLVSL YNNNLNGILA
DEMGLGKTIQ TIALITYLME NKRVNGPFLI IVPLSTLSNW VYEFDKWAPS VVKVSYKGSP
QARRAFIPQL RSGKFNVLLT TYEYIIKDKQ VLAKIRWKYM IVDEGHRMKN HHCKLTQVLN
THYLAPRRVL LTGTPLQNKL PELWALLNFL LPTIFKSCST FEQWFNAPFA MTGEKVDLNE
EETILIIRRL HKVLRPFLLR RLKKEVEAQL PEKVEYVIKC DMSALQRVLY RHMQAKGVLL
TDGSEKDKKV RRNNSSTTKA EDRGMLLKAF NDPASQYFIF LLSTRAGGLG LNLQSADTVV
IFDSDWNPHQ ESFSEHLGFS GGIVSGLDLY RASGKFEVLD RILPKLRATN HKVLLFCQMT
SLMTIMEDYF AYRNFKHLRL DGTDLQAQDR AHRIGQQNEV RVLRLCTVNS VEEKILAAAK
YKLNVDQKVI QAGMFDQKSS SHERRAFLQA ILEHEEQDEV GAPGGVWKSG GSWEEDEVPD
DETVNQMIAR SEEEFDHFMR MDLDRRREDA RNPRRKPRLM EEDELPTWIV KDDAEVERLT
CEEEEEKMFG RGSRQRKEVD YSDSLTEKQW LKAIEEGTLE EIEEEVRHKK TTRKRKRDRD
DLPGPSSSSS GGRRSRDKDE DGKRQKKRGR PPAEKLSPNP PALTKKMKKI VDAVIKYKDS
SNGRQLSEVF IQLPSRKELP EYYELIRKPV DFRKIKERIR SHRYRSLGDL ERDVMLLFQN
AQTFNLEGSL IYEDSIVLQS VFTSLRQKIE KEEDSEGEDS EEEEEDLDEG SESESRSVKV
KIRLGRREKS SDRGKGRRRM GRTRAKPVVS DDDTEEEQEE ERSPSGTDEE S
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