ID A0A1U7RSZ7_ALLSI Unreviewed; 1617 AA.
AC A0A1U7RSZ7;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Transcription activator BRG1 isoform X5 {ECO:0000313|RefSeq:XP_006023448.1};
GN Name=SMARCA4 {ECO:0000313|RefSeq:XP_006023448.1};
OS Alligator sinensis (Chinese alligator).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae;
OC Alligator.
OX NCBI_TaxID=38654 {ECO:0000313|Proteomes:UP000189705, ECO:0000313|RefSeq:XP_006023448.1};
RN [1] {ECO:0000313|RefSeq:XP_006023448.1}
RP IDENTIFICATION.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_006023448.1; XM_006023386.3.
DR GeneID; 102369819; -.
DR CTD; 6597; -.
DR OrthoDB; 5482994at2759; -.
DR Proteomes; UP000189705; 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: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; 1.
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; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000189705}.
FT DOMAIN 171..206
FT /note="QLQ"
FT /evidence="ECO:0000259|PROSITE:PS51666"
FT DOMAIN 458..530
FT /note="HSA"
FT /evidence="ECO:0000259|PROSITE:PS51204"
FT DOMAIN 764..929
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1085..1247
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 1448..1518
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT REGION 1..342
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 575..615
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 636..696
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1379..1433
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1535..1617
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 73..88
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 133..147
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 159..181
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 215..286
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 298..333
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 657..672
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1399..1419
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1540..1557
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1558..1583
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1599..1617
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1617 AA; 182036 MW; B119DDCAD5393B8D CRC64;
MSTPDPPMGG TPRPGPSPGP GPSPGAMLGP SPGPSPGSAH SMMGPSPGPP SAGHPMPPQG
PGGYAQDNMH QMHKPMDSMH EKGLSDDPRY SQMKGMGMRP GGHAGMGPPP SPMDQHSQGY
PSPLGGSEHA SSPVPANGPS SGPQMSSGPG GVPLDGTDPQ ALGQQNRGPT PFNQNQLHQL
RAQIMAYKML ARGQPLPDHL QMAVQGKRPM PGMQQQMPTL PPPSVSGTGP VQGPGPGPGP
GPTPPNYNRP HGIGGPNMPP PGPSGVPPGM PGQPPGGPPK PWPEGPMANA AAPTSTPQKL
IPPQPTGRPS PAPPAVPPAA SPVMPPQTQS PGQPAQPAPM VQLHQKQNRI TPIQKPRGLD
PVEILQEREY RLQARIAHRI QELENLPGSL AGDLRTKATI ELKALRLLNF QRQLRQEVVV
CMRRDTALET ALNAKAYKRS KRQSLREARI TEKLEKQQKI EQERKRRQKH QEYLNSILQH
AKDFKEYHRS VTGKIQKLTK AVATYHANTE REQKKENERI EKERMRRLMA EDEEGYRKLI
DQKKDKRLAY LLQQTDEYVA NLTELVRQHK AAQVAKEKKK KKKKKKAENA EGQTPAIGPD
GEPLDETSQM SDLPVKVIHV ESGKILTGTD APKAGQLDAW LEMNPGYEVA PRSDSEESGS
EEEEEEEEEE QPQPAQPALP VVEEKKKIPD PDSDDVSEVD ARHIIENAKQ DVDDEYGVSQ
ALARGLQSYY AVAHAVTERV DKQSTLMVNG VLKQYQIKGL EWLVSLYNNN LNGILADEMG
LGKTIQTIAL ITYLMEHKRI NGPFLIIVPL STLSNWAYEF DKWAPSVVKV SYKGSPAARR
AFVPQLRSGK FNVLLTTYEY IIKDKHILAK IRWKYMIVDE GHRMKNHHCK LTQVLNTHYV
APRRLLLTGT PLQNKLPELW ALLNFLLPTI FKSCSTFEQW FNAPFAMTGE KVDLNEEETI
LIIRRLHKVX XXXXXXXLRR LKKEVEAQLP EKVEYVIKCD MSALQRVLYR HMQAKGVLLT
DGSEKDKKGK GGTKTLMNTI MQLRKICNHP YMFQHIEESF SEHLGFTGGI VQGLDLYRAS
GKFELLDRIL PKLRATNHKV LLFCQMTSLM TIMEDYFAYR GFKYLRLDGT TKAEDRGMLL
KTFNEPGSEY FIFLLSTRAG GLGLNLQSAD TVIIFDSDWN PHQDLQAQDR AHRIGQQNEV
RVLRLCTVNS VEEKILAAAK YKLNVDQKVI QAGMFDQKSS SHERRAFLQA ILEHEEQDEE
EDEVPDDETV NQMIARHEEE FDLFMRMDLD RRREEARNPK RKPRLMEEDE LPSWIIKDDA
EVERLTCEEE EEKMFGRGSR HRKEVDYSDS LTEKQWLKVY MAIEEGTLEE IEEEVRQKKS
SRKRKRDTDV GSATPTTSTR SRDKDDDSKK QKKRGRPPAE KLSPNPPNLT KKMKKIVDAV
IKYKDSSSGR QLSEVFIQLP SRKELPEYYE LIRKPVDFKK IKERIRNHKY RSLNDLEKDV
MLLCQNAQTF NLEGSLIYED SIVLQSVFTS VRQKIEKEED SEGEDSEEEE EGEEEGSESE
SRSVKVKIKL GRKEKAQDRL KGRRRTSRGS RAKPVVSDDD SEEEQEEDRS GSGTEED
//
