ID SMRCD_DROME Reviewed; 844 AA.
AC Q9VL72; Q2PDU7; Q95ST4;
DT 28-NOV-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 27-MAR-2024, entry version 157.
DE RecName: Full=SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A containing DEAD/H box 1 homolog;
DE EC=3.6.4.12;
DE AltName: Full=Enhancer trap locus homolog 1;
DE Short=Etl-1;
GN Name=Etl1; ORFNames=CG5899;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-636.
RC STRAIN=Berkeley; TISSUE=Head;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-834; SER-838 AND SER-841, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
CC -!- FUNCTION: DNA helicase that possesses intrinsic ATP-dependent
CC nucleosome-remodeling activity and is both required for DNA repair and
CC heterochromatin organization. Promotes DNA end resection of double-
CC strand breaks (DSBs) following DNA damage: probably acts by weakening
CC histone DNA interactions in nucleosomes flanking DSBs (By similarity).
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL28145.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
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DR EMBL; AE014134; AAF52824.1; -; Genomic_DNA.
DR EMBL; AY060597; AAL28145.1; ALT_SEQ; mRNA.
DR RefSeq; NP_609320.2; NM_135476.4.
DR AlphaFoldDB; Q9VL72; -.
DR SMR; Q9VL72; -.
DR BioGRID; 60405; 5.
DR IntAct; Q9VL72; 2.
DR STRING; 7227.FBpp0079496; -.
DR iPTMnet; Q9VL72; -.
DR PaxDb; 7227-FBpp0079496; -.
DR EnsemblMetazoa; FBtr0079901; FBpp0079496; FBgn0032157.
DR GeneID; 34311; -.
DR KEGG; dme:Dmel_CG5899; -.
DR UCSC; CG5899-RA; d. melanogaster.
DR UCSC; CG5899-RB; d. melanogaster.
DR UCSC; CG5899-RC; d. melanogaster.
DR AGR; FB:FBgn0032157; -.
DR CTD; 34311; -.
DR FlyBase; FBgn0032157; Etl1.
DR VEuPathDB; VectorBase:FBgn0032157; -.
DR eggNOG; KOG0389; Eukaryota.
DR GeneTree; ENSGT00910000144252; -.
DR HOGENOM; CLU_000315_16_3_1; -.
DR InParanoid; Q9VL72; -.
DR OMA; NLACANM; -.
DR OrthoDB; 5482994at2759; -.
DR PhylomeDB; Q9VL72; -.
DR SignaLink; Q9VL72; -.
DR BioGRID-ORCS; 34311; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 34311; -.
DR PRO; PR:Q9VL72; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0032157; Expressed in ovary and 30 other cell types or tissues.
DR Genevisible; Q9VL72; DM.
DR GO; GO:0005634; C:nucleus; HDA:FlyBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0008094; F:ATP-dependent activity, acting on DNA; IBA:GO_Central.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; HMP:FlyBase.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0045089; P:positive regulation of innate immune response; HMP:FlyBase.
DR CDD; cd17998; DEXHc_SMARCAD1; 1.
DR CDD; cd18793; SF2_C_SNF; 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; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
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:SF964; SWI_SNF-RELATED MATRIX-ASSOCIATED ACTIN-DEPENDENT REGULATOR OF CHROMATIN SUBFAMILY A CONTAINING DEAD_H BOX 1; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Chromatin regulator; DNA damage; DNA repair; DNA-binding;
KW Helicase; Hydrolase; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..844
FT /note="SWI/SNF-related matrix-associated actin-dependent
FT regulator of chromatin subfamily A containing DEAD/H box 1
FT homolog"
FT /id="PRO_0000420488"
FT DOMAIN 301..471
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 656..818
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 121..180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 422..425
FT /note="DEGH box"
FT COMPBIAS 1..42
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..75
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 150..180
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 314..321
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 834
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 838
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 841
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
SQ SEQUENCE 844 AA; 95447 MW; A181F8017A88DA00 CRC64;
MSDSTVAASA SASASSSAKS SLSDLRQFRI NKNASSVVAS PSRTERVPGK KRIQVMADSD
SDGNDSQTPK KTKLELTVKE KEERYMAAAK ISPHFDTMAI QESLSRTNWD VAASVRYLRE
NCKPKGHNGP LAKSKLKPRS NGISGGNFSD NDHSDDDDVK QSKDQVYDSD DSDSEMSTKM
TGQRKKVFQF MNEASLIELQ SVKTLSEKKA LAIIDVRPFS DWSDLRQKLE SIRMSGDLLN
YAQELINKQN TVAAILSKCN NMVSRLEKAI SNGAGIVEQP KLLSSGLQLA DYQIIGLNWL
TVMHKQEMNG ILADEMGLGK TIQVIAFLAY LKENGLSQAA HLIVVPSSTL DNWEAEISRW
CPELVVEKYH GSQDERRRMR GRFAKDGFTG FDVLLTTYHI VGSTPEERKM FRVCKLDYVI
FDEAHMLKNM TTQRYANLIT INARMRILLT GTPLQNNLLE LISLLCFVMP KFFAKSIEDI
KSLFAKKGKS DGDQDEVSQF QETQIQRAKR IMKPFVLRRL KKDVLKNLPK KLSLVEKVPM
SSQQKIYYHE LVDYYSNNKG EVCSSSERAG IAIMMEMRRI ANHPLLMRHY FTDANLRGFS
KRLANASSFK KTNEQYIFEE LAVMSDFQVY QMMNKHEFYD VKIPDNLICD SGKFLYLDTL
LPKLKAEGHR VLLFSQFTMM LDIVEEYLRI RKFGFCRLDG ATAVNVRQDL ITDFNGDDSI
FVFLLSTKAG GVGINLTAAD TCVIHDIDFN PYNDKQAEDR CHRMGQQRPV TIYRLISEST
IEEGILMAAE EKLKLEKDIT SNEKGEVHEQ RCVVKLLTTA LGLDKDQEEQ LNNSLNNSIA
SPAK
//
