ID A0A2D0S5D6_ICTPU Unreviewed; 1613 AA.
AC A0A2D0S5D6;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2023, sequence version 2.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Transcription activator BRG1 isoform X2 {ECO:0000313|RefSeq:XP_017337953.2};
GN Name=LOC108273301 {ECO:0000313|RefSeq:XP_017337953.2};
OS Ictalurus punctatus (Channel catfish) (Silurus punctatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Siluriformes;
OC Ictaluridae; Ictalurus.
OX NCBI_TaxID=7998 {ECO:0000313|RefSeq:XP_017337953.2};
RN [1] {ECO:0000313|RefSeq:XP_017337953.2}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_017337953.2};
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_017337953.2; XM_017482464.3.
DR OrthoDB; 5482994at2759; -.
DR Proteomes; UP000221080; Chromosome 12.
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; 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 175..210
FT /note="QLQ"
FT /evidence="ECO:0000259|PROSITE:PS51666"
FT DOMAIN 453..525
FT /note="HSA"
FT /evidence="ECO:0000259|PROSITE:PS51204"
FT DOMAIN 755..920
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1073..1235
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 1443..1513
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT REGION 1..183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 202..338
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 571..606
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 633..700
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1369..1429
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1530..1613
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..25
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..65
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 67..82
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 136..183
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 258..273
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 290..321
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 653..669
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 670..700
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1395..1415
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1535..1552
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1553..1576
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1613 AA; 181887 MW; 27CE7AC708AC4F6C CRC64;
MSTPDPPLGP SPGPGPSPGP MMGPGPSPGS SHGMMGPSPG PSTTSGHAVP QQGAAGYTQQ
DSMHPMHKSL EGLHEKNVGE DSRFGQMKGV SMRAGGHAGM GPPPSPMDQH SQGYPSPLGS
SDHVSSPLPA GAPPTSGPLL SSSCTSSSPL EGTDSQPSRS GAQSNTPGSS ANPTPFNQNQ
LHQLRAQIMA YKMLARGQPL PDHLQMAVQG KRPMPGMQQG QAMPSLPPGG GGGPGTGPGP
LGPNYSRGHV LSGPSVPPSG PNAVPPANGP PKTWPEGPMV NAATPSNAPQ KLIPPQPTGR
PSPVPPSVPP AASPVMPPQT QSPGHPGHSA QPAPTIPLHQ KHNRITPMQK PCGLDPVEIL
QEREYRLEAR ITHRIQELEN LPGSLAGDLR TKATIELKAL RLLNFQRQLR QEVVVCMRRD
AALETALDAK AYKRSKRQSL REARITEKLE KQQKIEQERK RRQKHQEYLN SILQHAKDFK
EYHRSITGKI QKLTKAVATY HANTEREQKK ENERIEKERM RRLMAEDEEG YRKLIDQKKD
KRLAYLLQQT DEYVANLTEL VRAHKAAQAL KEKKKKKKKK KKLENAEGQP LALGPDGEPL
DETSQMSDLP VKVIHVDSGK ILSGVDAPKA GQLDTWLEMN PGYEVAPRSD SEDTGSEEDE
EEEEDQPQPS QAPLEEKKKI PDPDSEDVSE VDARHIIEHA KQDVDDEYGG AAFARGLQSY
YAVAHAVTEK VDRQSSLLVN GQLKQYQIKG LEWLVSLYNN NLNGILADEM GLGKTIQTIA
LITYLMEYKR LNGPYLIIVP LSTLSNWVYE FDKWAPSVVK VSYKGSPAAR RAFVPQLRSG
KFNVLLTTYE YIIKDKQVLA KIRWKYMIVD EGHRMKNHHC KLTQVLNTHY LAPRRVLLTG
TPLQNKLPEL WALLNFLLPT IFKSCSTFEQ WFNAPFAMTG EKVDLNEEET ILIIRRLHKV
LRPFLLRRLK KEVEAQLPEK VEYVIKCDMS ALQRVLYRHM QAKGVLLTDG SEKDKKGKGG
TKTLMNTIMQ LRKICNHPYM FQQIEESFSE HLGFSGGIVQ GPDLYRASGK FEVLDRILPK
LRATNHKVLL FCQMTSLMTI MEDYFAYRNF KYLRLDGTTK AEDRGMLLKT FNDPESQYFI
FLLSTRAGGL GLNLQSADTV VIFDSDWNPH QDLQAQDRAH RIGQQNEVRV LRLCTVNSVE
EKILAAAKYK LNVDQKVIQA GMFDQKSSSH ERRAFLQAIL EHEEQDEVSD IYMPYILEED
EVPDDETVNQ MIARSEEEFD HFMRMDLDRR REEARNPKRR PRLMEEDELP TWIMKDDAEV
ERLTCEEEAE KMFGRGSRQR KEVDYSDSLT EKQWLKAIEE GTLDEIEEEV RHKKTTRKRK
RDRDLDAGPS TSGTRGARDK DEDSKRQKKR GRPPAEKITP NPPSLTKKMK KIVEAVIKYK
ESNGRQLSEV FIQLPSRKEL PEYYELIRRP VDFRKIKERI RSHRYRSLND LERDVMLLCQ
NAQTFNLEGS LIYEDSIVLQ SVFTSLRQKI EKEEESDGDE SEEEEEEQDE GSESESRSVK
VKIKLGRKER SAERGKGRRR GGRTRAKPVV SDDDTEDERE EERSNTASDE DQG
//
