ID A0A3B3UCU6_9TELE Unreviewed; 1636 AA.
AC A0A3B3UCU6;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Transcription activator BRG1 {ECO:0000313|Ensembl:ENSPLAP00000011150.1};
OS Poecilia latipinna (sailfin molly).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=48699 {ECO:0000313|Ensembl:ENSPLAP00000011150.1, ECO:0000313|Proteomes:UP000261500};
RN [1] {ECO:0000313|Ensembl:ENSPLAP00000011150.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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_014900080.1; XM_015044594.1.
DR STRING; 48699.ENSPLAP00000011150; -.
DR Ensembl; ENSPLAT00000029087.1; ENSPLAP00000011150.1; ENSPLAG00000014294.1.
DR GeneID; 106954812; -.
DR KEGG; plai:106954812; -.
DR CTD; 353295; -.
DR GeneTree; ENSGT00940000156887; -.
DR OrthoDB; 5482994at2759; -.
DR Proteomes; UP000261500; Unplaced.
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:0060038; P:cardiac muscle cell proliferation; IEA:Ensembl.
DR GO; GO:0060973; P:cell migration involved in heart development; IEA:Ensembl.
DR GO; GO:0007417; P:central nervous system development; IEA:Ensembl.
DR GO; GO:0048596; P:embryonic camera-type eye morphogenesis; IEA:Ensembl.
DR GO; GO:0060059; P:embryonic retina morphogenesis in camera-type eye; IEA:Ensembl.
DR GO; GO:0048703; P:embryonic viscerocranium morphogenesis; IEA:Ensembl.
DR GO; GO:0031101; P:fin regeneration; IEA:Ensembl.
DR GO; GO:0001947; P:heart looping; IEA:Ensembl.
DR GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IEA:Ensembl.
DR GO; GO:0014032; P:neural crest cell development; IEA:Ensembl.
DR GO; GO:0030182; P:neuron differentiation; IEA:Ensembl.
DR GO; GO:0021634; P:optic nerve formation; IEA:Ensembl.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; IEA:Ensembl.
DR GO; GO:0010750; P:positive regulation of nitric oxide mediated signal transduction; IEA:Ensembl.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR GO; GO:0010842; P:retina layer formation; IEA:Ensembl.
DR GO; GO:0003406; P:retinal pigment epithelium development; IEA:Ensembl.
DR CDD; cd05516; Bromo_SNF2L2; 1.
DR CDD; cd18062; DEXHc_SMARCA4; 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; 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.
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; 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 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}.
FT DOMAIN 187..222
FT /note="QLQ"
FT /evidence="ECO:0000259|PROSITE:PS51666"
FT DOMAIN 482..554
FT /note="HSA"
FT /evidence="ECO:0000259|PROSITE:PS51204"
FT DOMAIN 787..952
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1105..1266
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 1466..1536
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT REGION 1..195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 214..362
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 600..632
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 670..722
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1348..1452
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1553..1636
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 48..62
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 73..88
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 165..180
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 231..246
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 281..299
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 321..358
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 681..698
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 703..722
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1348..1395
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1403..1438
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1558..1576
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1577..1602
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1618..1636
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1636 AA; 183331 MW; E1B8C22292EB0955 CRC64;
MSTPDPPMGG TPRPGPSPGP GPSPGGMMGP SPGPSPGSAH SMMGPSPGPP SSGHPHPPQG
PSGYPQDNMH QMHKPMDPMH DKGMPDDPRY GQMKGMGMRP GGHSGMGPPP SPMDQHSQGY
PSPLGGSEHA PSPVPANGPP SGPGASPMEG GGDPAQSMGQ PNRAGPPGPG GPPGPGVGPG
AAGGPTPFNQ NQLHQLRAQI MAYKMLARNH PIPEHLQLAV QGKRPMPGMQ QQQQQPPPPM
PNMPPSAGPG GGQAAGPGPG PGPGPGPAQT NYNRPHGMVG PNMAPPGPAG VPPAMQGQPA
NGPPKSWPEG PMVNAAAPSN PPQKLIPPQP TGRPSPAPPS VPPAASPVMP PQTQSPGQPA
QLPPMMLHQK QNRITPIQKP HGLDPVEILQ EREYRLQARI VHRIQELEHL PGSLAGDLRT
KATIELKALR LLTFQRQLRQ EVVACMRRDT ALETALNAKA YKRSKRQSLR EARITEKLEK
QQKIEQERKR RQKHQEYLNS ILQHAKDFKE YHRSITAKIQ KATKAVATYH ANTEREQKKE
NERIEKERMR RLMAEDEEGY RKLIDQKKDK RLAYLLQQTD EYVANLTELV RAHKAAQALK
EKKKKKKKKK PDAVEGGAPA MGPDGEPLDE TSQMSDLPVK VIHVDSGNIL TGVDAPKAGQ
LEAWLEMNPG YEVAPRSDSE DSGSEDEDEE DEDDAEDQPQ PTTAPTEEKK KIPDPDSEDV
SEVDVQHIIE HAKQDVDDEY GSASFNRGLQ SYYAVAHAVT EKVDKQSSLM VNGTLKQYQI
KGLEWLVSLY NNNLNGILAD EMGLGKTIQT IALITYLMEL KRINGPFLII VPLSTLSNWV
YEFDKWAPSV VKVSYKGSPQ ARRSFVPILR SGKFNVLLTT YEYIIKDKQV LAKIRWKYMI
VDEGHRMKNH HCKLTQVLNT HYLAPRRLLL TGTPLQNKLP ELWALLNFLL PTIFKSCSTF
EQWFNAPFAM TGEKVDLNEE ETILIIRRLH KVLRPFLLRR LKKEVEAQLP EKVEYVIKCD
MSALQRVLYR HMQAKGVLLT DGSEKDKKGK GGTKTLMNTI MQLRKICNHP YMFQHIEESF
SEHLGFSGGI VTGPDLYRAS GKFELLDRIL PKLRATKHKV LLFCQMTSLM TIMEDYFAYR
NFKYLRLDGT TKAEDRGMLL KTFNDPASEY FVFLLSTRAG GLGLNLQSAD TVIIFDSDWN
PHQDLQAQDR AHRIGQQNEV RVLRLCTVNS VEEKILAAAK YKLNVDQKVI QAGMFDQKSS
GYERRAFLQA ILEHEEQDEE EDEVPDDETV NQMIARSEEE FELFMRMDLD RRREDARNPK
RKPRLMEEDD MPGWILKDDA EVERLTCEEE EEKMFGRGSR QRKEVDYSDS LTEKQWLKAI
EEGNLEDIEE EVRHKKTTRK RKRERDHDGS PATPSSSHRG RDKDDSGKKA KKRGRPPAEK
LSPNPPTLTK KMKKIVDAVV KYKDGNGRQL SEVFIQLPSR KELPEYYELI RKPVDFKKIK
ERIRSHKYRN LNDLEKDVML LCQNAQTFNL EGSLIYEDSI VLQSVFTSVR QKIEKDDESE
GEESEEEEEE EMDEGSESES RSVKVKIKLS RKEKGDRGGK SQRRRGRGSR AKPVVSDDDS
EDEQEEERSA SGSEDD
//
