ID A0A090LRX2_STRRB Unreviewed; 1372 AA.
AC A0A090LRX2;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE SubName: Full=ATP-dependent helicase brm {ECO:0000313|EMBL:CEF70336.1, ECO:0000313|WBParaSite:SRAE_2000496900.1};
GN ORFNames=SRAE_2000496900 {ECO:0000313|EMBL:CEF70336.1,
GN ECO:0000313|WBParaSite:SRAE_2000496900.1,
GN ECO:0000313|WormBase:SRAE_2000496900};
OS Strongyloides ratti (Parasitic roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC Strongyloides.
OX NCBI_TaxID=34506 {ECO:0000313|EMBL:CEF70336.1};
RN [1] {ECO:0000313|EMBL:CEF70336.1, ECO:0000313|Proteomes:UP000035682}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ED321 {ECO:0000313|Proteomes:UP000035682,
RC ECO:0000313|WBParaSite:SRAE_2000496900.1}, and ED321 Heterogonic
RC {ECO:0000313|EMBL:CEF70336.1};
RA Martin A.A.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|WBParaSite:SRAE_2000496900.1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (DEC-2020) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; LN609529; CEF70336.1; -; Genomic_DNA.
DR STRING; 34506.A0A090LRX2; -.
DR EnsemblMetazoa; SRAE_2000496900.1; SRAE_2000496900.1; WBGene00265216.
DR WBParaSite; SRAE_2000496900.1; SRAE_2000496900.1; WBGene00265216.
DR WormBase; SRAE_2000496900; SRP00146; WBGene00265216; -.
DR eggNOG; KOG0386; Eukaryota.
DR OMA; VNYISHT; -.
DR OrthoDB; 5482994at2759; -.
DR Proteomes; UP000035682; Chromosome X.
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; 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; 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; 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; 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}; Coiled coil {ECO:0000256|SAM:Coils};
KW Helicase {ECO:0000313|EMBL:CEF70336.1};
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:UP000035682}.
FT DOMAIN 160..195
FT /note="QLQ"
FT /evidence="ECO:0000259|PROSITE:PS51666"
FT DOMAIN 341..413
FT /note="HSA"
FT /evidence="ECO:0000259|PROSITE:PS51204"
FT DOMAIN 616..781
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 923..1074
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 1279..1349
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT REGION 1..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 450..473
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 517..553
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1174..1193
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1208..1263
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 391..418
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 35..51
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 526..547
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1232..1263
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1372 AA; 160703 MW; B4358AD698E2EAEF CRC64;
MQHQMHIQHP MHQGPPPQMH PGTMPPPGSH MQMHPGTMHP SQMQQPPQMM APHPQQMMHP
QGPQQQMMHP QHMQSMAYGN QQPPPMQMQR VGNPVPINQI PNKESAIQYI DNTMAGLEES
NLQQDPRYYQ MGQLRQRITG SATAPPKQIV DNNKKYEIKK MTPSQIEILR NQISVYRRLA
RNLPIASYMR ELVNRHLDIL PRPFQFGSDD QNAKLPYDLS KIYPLVSQKR DRGSLCPLPK
GIDPNLILKE KQNRVQNRIG HRIKELQQLS VTLPPQLRIK AEIELRALRL TSLQQSVRHD
VMMQLKRDTF MEHSINPNLY RRNKYICLRE ARQTEKLEKQ MKLEREKKRR QKHNDLLSAI
CTAAKEFREF HKNFQAKGHK LRKAISTYHT NNEKLKKKDE IKNEKERLMK LMQEDEEGYR
QMLDEKKDKR LVILLQQTDE YMESLTNLVR QHQRSEKQKK KDERKKQRAI ELSKISPDAK
CKVRHTTTGE IIEGDKAPTV AELDTWLQTH SGYEVLEKNG IPVESDSSDE SEEEEQTPTE
KEDDLAGLDE EERNRKILEK ARNEEDEYDA KSKSRMDSYY RIAHKIKEKV VKQHSSLGSD
KLQLKPYQLK GLEWMVSLYN NNLNGILADE MGLGKTIQTI SLITYLIEIK KVTGPYLVIV
PLSTISNWNL EFEKWAPHVN KIVYKGTKEV RKQLESYVKK GGFNVLLTTF DYVLKEKALL
GKINWKYMII DEGHRMKNSN CKLTLTLNAY FRAQHRLLLT GTPLQNKLPE LWALLNFLLP
SIFSSCSTFD SWFNAPFAHT GEKLELNQEE TMLIIRRLHK VLRPFLLRRL KKEVESQLPD
KVEYVIRCDM SAIQKILYEH MKEGMLLDSR NGQNRALMNT IIHLRKLCNH PFLFENVEDE
CRAYWGRECT GRDLFRVSGK FEFMDRVLPK FKATNHRVLI FCQMTSAMTL LEDYFTYREW
KYLRLDGSTK PDERGELLKV FNAPNSEYFL FILSTRAGGL GLNLQTADTV IIFDSDWNPH
QDLQAQDRAH RIGQKNEVRV LRLITANSVE EKILAAARYK LNVDEKVIQA GKFNQRSTGA
ERREMLEALI KADNDEAEEE SVPDDETINQ MIARTEEEFE IFQKMDIERR RAEAESDDRK
PRLIEESEIP TTIYEAAERS AKMKEQALLN SNDNSLLENL ETPGRRSRKN VNYSSDLISD
RDFFKAYEDD DDEQEEETRS RSKKERKNGN GRRKRVHLEE DDEDTEDSRS SRKKRRPSPE
SEKLFMEAVD GLCSITKQDG TTLADPFIQL PSRKELPHYY ETIKNPMDIN KIRKRIREGR
YTEFDELNAD MALVWQNAQE YNLENSEIYN DSVLLREYWL RITGQQTNIN QE
//
