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Database: UniProt
Entry: Q9VL72
LinkDB: Q9VL72
Original site: Q9VL72 
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   16-OCT-2019, entry version 140.
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;
OC   Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
OC   Ephydroidea; 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.,
RA   Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
RA   Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
RA   Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
RA   Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
RA   Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
RA   Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
RA   Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
RA   Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
RA   de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
RA   Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
RA   Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
RA   Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
RA   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.,
RA   Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
RA   Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
RA   Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
RA   Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
RA   Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
RA   Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
RA   Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
RA   Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
RA   Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
RA   Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
RA   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.,
RA   Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
RA   Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
RA   Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
RA   Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
RA   Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
RA   Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., 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.,
RA   Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
RA   Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a
RT   systematic 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.,
RA   George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H.,
RA   Rubin G.M., 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
RP   SER-841, AND 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
CC       and heterochromatin organization. Promotes DNA end resection of
CC       double-strand breaks (DSBs) following DNA damage: probably acts by
CC       weakening histone DNA interactions in nucleosomes flanking DSBs
CC       (By similarity). {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.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAL28145.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
DR   EMBL; AE014134; AAF52824.1; -; Genomic_DNA.
DR   EMBL; AY060597; AAL28145.1; ALT_SEQ; mRNA.
DR   RefSeq; NP_609320.2; NM_135476.4.
DR   SMR; Q9VL72; -.
DR   BioGrid; 60405; 5.
DR   IntAct; Q9VL72; 2.
DR   STRING; 7227.FBpp0079496; -.
DR   iPTMnet; Q9VL72; -.
DR   PaxDb; Q9VL72; -.
DR   PRIDE; Q9VL72; -.
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   CTD; 34311; -.
DR   FlyBase; FBgn0032157; Etl1.
DR   eggNOG; KOG0389; Eukaryota.
DR   eggNOG; ENOG410XNUT; LUCA.
DR   GeneTree; ENSGT00910000144252; -.
DR   InParanoid; Q9VL72; -.
DR   KO; K14439; -.
DR   OMA; TIENWIG; -.
DR   OrthoDB; 61251at2759; -.
DR   PhylomeDB; Q9VL72; -.
DR   GenomeRNAi; 34311; -.
DR   PRO; PR:Q9VL72; -.
DR   Proteomes; UP000000803; Chromosome 2L.
DR   Bgee; FBgn0032157; Expressed in 46 organ(s), highest expression level in female gonad.
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:0003682; F:chromatin binding; IBA:GO_Central.
DR   GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR   GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008094; F:DNA-dependent ATPase activity; IBA:GO_Central.
DR   GO; GO:0043044; P:ATP-dependent chromatin remodeling; IBA:GO_Central.
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   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR000330; SNF2_N.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF00176; SNF2_N; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; SSF52540; 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; Complete proteome; DNA damage;
KW   DNA repair; DNA-binding; Helicase; Hydrolase; Nucleotide-binding;
KW   Nucleus; Phosphoprotein; Reference proteome.
FT   CHAIN         1    844       SWI/SNF-related matrix-associated actin-
FT                                dependent regulator of chromatin
FT                                subfamily A containing DEAD/H box 1
FT                                homolog.
FT                                /FTId=PRO_0000420488.
FT   DOMAIN      301    471       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      656    818       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   NP_BIND     314    321       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   MOTIF       422    425       DEGH box.
FT   MOD_RES     834    834       Phosphoserine.
FT                                {ECO:0000269|PubMed:18327897}.
FT   MOD_RES     838    838       Phosphoserine.
FT                                {ECO:0000269|PubMed:18327897}.
FT   MOD_RES     841    841       Phosphoserine.
FT                                {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
//
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