ID A0A0R3SBC5_HYMDI Unreviewed; 1618 AA.
AC A0A0R3SBC5;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=Transcription activator BRG1 {ECO:0000313|WBParaSite:HDID_0000176001-mRNA-1};
GN ORFNames=HDID_LOCUS1761 {ECO:0000313|EMBL:VDL19222.1},
GN WMSIL1_LOCUS4252 {ECO:0000313|EMBL:VUZ44061.1};
OS Hymenolepis diminuta (Rat tapeworm).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Cestoda;
OC Eucestoda; Cyclophyllidea; Hymenolepididae; Hymenolepis.
OX NCBI_TaxID=6216 {ECO:0000313|Proteomes:UP000046397, ECO:0000313|WBParaSite:HDID_0000176001-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:HDID_0000176001-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDL19222.1, ECO:0000313|Proteomes:UP000274504}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Pathogen Informatics;
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:VUZ44061.1, ECO:0000313|Proteomes:UP000321570}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WMS-il1 {ECO:0000313|EMBL:VUZ44061.1,
RC ECO:0000313|Proteomes:UP000321570};
RA Jastrzebski P J., Paukszto L., Jastrzebski P J.;
RL Submitted (JUL-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; UYSG01000360; VDL19222.1; -; Genomic_DNA.
DR EMBL; CABIJS010000122; VUZ44061.1; -; Genomic_DNA.
DR STRING; 6216.A0A0R3SBC5; -.
DR WBParaSite; HDID_0000176001-mRNA-1; HDID_0000176001-mRNA-1; HDID_0000176001.
DR Proteomes; UP000046397; Unplaced.
DR Proteomes; UP000274504; Unassembled WGS sequence.
DR Proteomes; UP000321570; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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; cd17996; DEXHc_SMARCA2_SMARCA4; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 1.20.5.170; -; 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:SF973; ATP-DEPENDENT HELICASE BRM; 1.
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; 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 4: Predicted;
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:UP000274504}.
FT DOMAIN 143..178
FT /note="QLQ"
FT /evidence="ECO:0000259|PROSITE:PS51666"
FT DOMAIN 363..436
FT /note="HSA"
FT /evidence="ECO:0000259|PROSITE:PS51204"
FT DOMAIN 683..848
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1007..1174
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 1376..1446
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT REGION 1..86
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1286..1357
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1466..1618
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..25
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..54
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 55..83
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1339..1355
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1477..1499
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1511..1527
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1555..1577
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1601..1618
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1618 AA; 184013 MW; F8072CBA6AC0E6A9 CRC64;
MQQPPSQQMQ IAPPNGPSTP MNGQDAPNPI VAAPLPPQQQ QGFPPPPPLG PSGYVNPSAP
SQDSTTVHHQ PPLSSQMQCN APPNVIIGRQ PLPGQAYDSV QPPMYPPHPG PSYGSNPGGV
FPPPNTSIVG PVGGPSMLQQ SSTFVKSQLG QLRAQISVYK LLSKSQAVPE NILSVAEGRG
STVPVFHNFP QRPPATVSGH SQILQDVPNQ LYPQQHQPNR PPLPVRWGHT GYSGPPPNSA
FMAGSQGSQI GRSRIGSIQR PQGLDPVELL KEREQRIQSR IGQRIKQLSS LGVFSTPQQR
ISLEVELRSL RLLNFQRQLR QDMVASMHRD TSLETALNIK AYRRPKKQSL REARYNEKLE
RQLKHEQEKR RRQKHQEFLN AVLSHGREFR EYHRNCNVRM SKINKAILTA ERDRRRVQQR
IDRERMRRLM EEDDAGYRTL IDEKKNKRLH YLLTQTDQFI DNLAKLVKDH KKEQNKLRIK
DIRERGRQAQ ERCLLNAVNK YHAIAKNLII EGVAPPVWMN TLPPPGVFPD ELAQASRELA
AGKAPMLNTI PWPDIRLPVC NPSTKEFLEG ESAPFANEAH TWLQEHVGWE IAPTDENGVV
LVDLIEEDED ASSKKKNLGS AEDDDDAVID TVRGNEDDEY KSGGSQSYYA LAHAIREQVK
EQASILVNGK LKEYQMRGLE WLVSLYNNNL NGILADEMGL GKTIQTIGLI TYLMEKKRVN
GPYLIIVPLS VMANWAMEFE KWAPSVKKIL YKGSPQCRRA LQNQIKAAKF NVLLTTYEYI
IKDKSALSKV NWRYMIIDEG HRMKNHHCKL TQILNHHYNA PYRLLLTGTP LQNKLPELWA
LLNFLLPKIF DSCNTFEQWF NAPFAATGEK VELNHEETLL IIRRLHKVLR PFLLRRLKKE
VESQLPEKVE YVIRCEMSAL QRVLYSYMQS KGVILTDGSE RDKKGKGGTR TLMNTIMQLR
KICNHPFMFS HIEAAIAEFQ SPPPPGQPPP TQVEGKLLFR SSGKFELLDR ILPKLRATGH
RVLIFCQMTS LMTIMQDYFD YRGFRYLRLD GATRADDRGE MLKEFNDESQ EYFIFLLSTR
AGGLGLNLQT ADTVIIFDSD WNPHQDLQAQ DRAHRIGQQN EVRVLRLITI NSVEEKILAA
ARYKLNVDEK VIQAGMFDNK STGSERRQFL QNLLEADEEA DEDENEAPDD ETVNQMLARS
EKEFDIYQRM DVERQVAERQ QSKPEPRLME YSELPDWIVR DEEEVERSLN MDETALTSMR
RQRKEVDYSE VLTEREFLKA IDEGDDLEEA EEKSRQRRAK RKRKRNEPDY SGMDDMSSDA
GSSVKAAPVV KRRRGRPPQS NSAAGSTTNT RRPISPKLQE RMKRLLQLVI DYKDKDQRVL
SEPFMKLPTR KELPDYYEVI KRPVDFHRIK TRVKDGKYRS MDELEADVIL LCKNAQTYNI
DGSLIFEDSV VLQTVWTNAR QQLEAMEGVT PSEGDTSIYA EDETSSSRKM PSTSRHHNQS
MADESMDCDN TMDETTCNIT AGDANPGGGN ETSLMGDTID DDDDSRESFS TKSRKSSTSR
KPPSSLIPST SGGSATAAGE GGPQPRRKGS RSGRPPVYDN ESEEEDMEVN DDDDDEDY
//
