ID A0AAD8E0T6_MYTSE Unreviewed; 1674 AA.
AC A0AAD8E0T6;
DT 29-MAY-2024, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2024, sequence version 1.
DT 28-JAN-2026, entry version 9.
DE RecName: Full=ATP-dependent helicase brm {ECO:0008006|Google:ProtNLM};
GN ORFNames=PYW07_014750 {ECO:0000313|EMBL:KAJ8734199.1};
OS Mythimna separata (Oriental armyworm) (Pseudaletia separata).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Noctuoidea;
OC Noctuidae; Noctuinae; Hadenini; Mythimna.
OX NCBI_TaxID=271217 {ECO:0000313|EMBL:KAJ8734199.1, ECO:0000313|Proteomes:UP001231518};
RN [1] {ECO:0000313|EMBL:KAJ8734199.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=BeijingLab {ECO:0000313|EMBL:KAJ8734199.1};
RC TISSUE=Pupa {ECO:0000313|EMBL:KAJ8734199.1};
RA Zhao H.;
RT "Chromosome-level genomes of two armyworms, Mythimna separata and Mythimna
RT loreyi, provide insights into the biosynthesis and reception of sex
RT pheromones.";
RL Submitted (MAR-2023) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KAJ8734199.1}.
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DR EMBL; JARGEI010000003; KAJ8734199.1; -; Genomic_DNA.
DR Proteomes; UP001231518; Chromosome 5.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:0048513; P:animal organ development; IEA:UniProtKB-ARBA.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR GO; GO:0048731; P:system development; IEA:UniProtKB-ARBA.
DR CDD; cd17996; DEXHc_SMARCA2_SMARCA4; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR FunFam; 3.40.50.10810:FF:000008; Chromatin structure-remodeling complex subunit snf21; 1.
DR FunFam; 1.20.5.170:FF:000008; probable global transcription activator SNF2L2 isoform X1; 1.
DR FunFam; 3.40.50.300:FF:003020; SNF2-related domain-containing protein; 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-like.
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 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 4: Predicted;
KW Activator {ECO:0000256|ARBA:ARBA00023159};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Bromodomain {ECO:0000256|ARBA:ARBA00023117, ECO:0000256|PROSITE-
KW ProRule:PRU00035}; Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP001231518};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT DOMAIN 325..360
FT /note="QLQ"
FT /evidence="ECO:0000259|PROSITE:PS51666"
FT DOMAIN 583..655
FT /note="HSA"
FT /evidence="ECO:0000259|PROSITE:PS51204"
FT DOMAIN 863..1028
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1181..1342
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 1527..1597
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT REGION 1..304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 359..480
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 694..752
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 770..812
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1459..1509
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1617..1674
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 617..656
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 7..33
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 92..103
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 104..123
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 149..159
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 162..177
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 179..192
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 219..233
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 234..259
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 260..272
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 293..304
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 368..377
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 383..412
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 694..707
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 743..752
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 773..785
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 786..812
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1459..1472
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1475..1484
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1621..1635
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1641..1663
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1674 AA; 187307 MW; 75F22AEAE70A3441 CRC64;
MASPSPQSSP MPPPQAPSPM GPPTQSPAPP QSPHSPYNQQ HVNGPPPSHP SGGGQPPMPN
HMSPSGPAHP IAANSNGPPG VPQQHPGMPP SGHQMPPHMV GPHMPGPPGH PLGPGGAHPP
GPNGHPGAPQ HPNMPGQGPP HGYMQHQIGH MPPGQAPMPM GGGPPPGNGP QGPPGAPGGP
LQLAGPPHGH PQGMPPSAPA HHAPHHAMMG GQGPPPHAAS PGYGAATSPA GAPSAPPQPG
APPHPPAAQT PPHGQPPPST SSANGAPPAS SPMQGSLPAP GPDNLHAIQR TIDSMEEKGL
QEDPRFSQLL ALRARSNPQD PGKGLFSNNQ LCQLKAQITA YRSLARNQAL SQQIAMMAAG
KRTGETPPEC PTPPAQPPYE VAGSGGAPPG ATGGKAGAGG AAGDAARGGG GAPPTPLPMT
GQMAPPTQLT PPLVNPPMSG GPPMRGPAPL RPQAPGSQPQ HQPGVPIPGA KQNRITSMPK
PVGIDPLQIL NERENRIAAR IAHRIEMLSN LPANMPDDLR LQAQIELRAL RVLNFQKQLR
SEILGQVRRD TTLETAVNIK AYKRTKRQGL REARATEKLE KQQKLEAERK RRQKHQEFLQ
TVLQHAKDFK EYHRNNVAKL SRMNKAIMNH HANAEREQKK EQERIEKERM RRLMAEDEEG
YRKLIDQKKD KRLAFLLSQT DEYIASLTEM VKQHKQEQRK KQQEEERRKR KSRKKKLLEG
GEIDAMDDSS QTSDSRVNVM DPKTGEILRG EEAPLLSQLK DWMETHPGWE VLSDSEDSGD
DSQDDDEKRR GHRDERSDKE KTDEEKAREM IKKAKVEDDE YKTEEQTYYS IAHTVHESVT
EQSSILVNGK LKEYQIKGLE WLVSLFNNNL NGILADEMGL GKTIQTIALV TYLMEKKKVN
GPFLIIVPLS TLSNWVLEFE KWAPTVSVVS YKGSPQSRRL VQAQMRSTKF NVLLTTYEYV
IKDKAVLAKV QWKYMIIDEG HRMKNHHCKL TQVLNTHYIA PHRLLLTGTP LQNKLPELWA
LLNFLLPSIF KSCSTFEQWF NAPFATTGEK VELNEEETIL IIRRLHKVLR PFLLRRLKKE
VESQLPDKVE YIIKCDMSGL QRVLYKHMQS KGVLLTDGSE KGNKGKGGAK ALMNTIVQLR
KLCNHPFMFQ HIEEKFCDHI GTGGGVVSGP DLYRASGKFE LLDRILPKLK QTGHRVLVFC
QMTQCMTIIE DYLSWRAFQY LRLDGMTKAE DRGELLKKFN DVGSEYFIFL LSTRAGGLGL
NLQSADTVII FDSDWNPHQD LQAQDRAHRI GQRNEVRVLR LMTVNSVEER ILAAARYKLN
MDEKVIQAGM FDQKSTGSER QQFLQSILHQ DGDDEEEENE LPDDDLINEM IARSEEELEI
FKQIDIERKK TETQSRLIEE SELPDWLVKH EDEVVCNKGH GWNYLDEDET LGRGSRQRKE
VDYTDSLTEK EWLKAIDDEF EEEEEEDDDD EVLDKKRKKG RKRRRQEESE EEEAPSSSKK
KSKTEINQQK KRWKNIMKKV IDYADEAGRV LSEPFMKLPS RRELPDYYDV IKKPLDIKKI
MNRIEDGKYT DISDLERDFF TLCANAQTYN EEQSLIYEDS VRLRNVFIEV RRRYETGQNS
DDSDDNEKDD DDSDGESSRS VKMKIKLKGK SKSTPSRKRK QRKYVSDDED YEED
//
