GenomeNet

Database: UniProt
Entry: Q9VNV3
LinkDB: Q9VNV3
Original site: Q9VNV3 
ID   DDX1_DROME              Reviewed;         727 AA.
AC   Q9VNV3; O61663; Q24131;
DT   15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   16-OCT-2019, entry version 149.
DE   RecName: Full=ATP-dependent RNA helicase Ddx1;
DE            Short=DEAD box protein 1;
DE            EC=3.6.4.13;
GN   Name=Ddx1; ORFNames=CG9054;
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] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND DEVELOPMENTAL STAGE.
RC   TISSUE=Embryo;
RX   PubMed=8666277; DOI=10.1016/0378-1119(96)00034-0;
RA   Rafti F., Scarvelis D., Lasko P.F.;
RT   "A Drosophila melanogaster homologue of the human DEAD-box gene
RT   DDX1.";
RL   Gene 171:225-229(1996).
RN   [2] {ECO:0000305}
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   [3]
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Berkeley; TISSUE=Embryo;
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   [5] {ECO:0000305, ECO:0000312|EMBL:AAM50315.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 458-727.
RC   STRAIN=Berlin;
RA   Zinsmaier K.E., Eberle K.K., Buchner E.;
RL   Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Acts as an ATP-dependent RNA helicase, able to unwind
CC       both RNA-RNA and RNA-DNA duplexes. Possesses 5' single-stranded
CC       RNA overhang nuclease activity (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=3.6.4.13;
CC   -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically
CC       throughout development. Expression is highest in early embryos.
CC       {ECO:0000269|PubMed:8666277}.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX1
CC       subfamily. {ECO:0000305}.
DR   EMBL; U34773; AAC47309.1; -; mRNA.
DR   EMBL; AE014296; AAF51814.1; -; Genomic_DNA.
DR   EMBL; AY119661; AAM50315.1; -; mRNA.
DR   EMBL; AF057167; AAD09429.1; -; Genomic_DNA.
DR   RefSeq; NP_524212.2; NM_079488.4.
DR   SMR; Q9VNV3; -.
DR   BioGrid; 65694; 4.
DR   IntAct; Q9VNV3; 1.
DR   STRING; 7227.FBpp0078144; -.
DR   PaxDb; Q9VNV3; -.
DR   PRIDE; Q9VNV3; -.
DR   EnsemblMetazoa; FBtr0078492; FBpp0078144; FBgn0015075.
DR   GeneID; 40457; -.
DR   KEGG; dme:Dmel_CG9054; -.
DR   UCSC; CG9054-RA; d. melanogaster.
DR   CTD; 1653; -.
DR   FlyBase; FBgn0015075; Ddx1.
DR   eggNOG; KOG0349; Eukaryota.
DR   eggNOG; COG0513; LUCA.
DR   GeneTree; ENSGT00940000155678; -.
DR   InParanoid; Q9VNV3; -.
DR   KO; K13177; -.
DR   OMA; DGVHDRD; -.
DR   OrthoDB; 973872at2759; -.
DR   PhylomeDB; Q9VNV3; -.
DR   GenomeRNAi; 40457; -.
DR   PRO; PR:Q9VNV3; -.
DR   Proteomes; UP000000803; Chromosome 3L.
DR   Bgee; FBgn0015075; Expressed in 4 organ(s), highest expression level in larva.
DR   Genevisible; Q9VNV3; DM.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR   GO; GO:0033677; F:DNA/RNA helicase activity; ISS:UniProtKB.
DR   GO; GO:0004527; F:exonuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0004386; F:helicase activity; ISS:UniProtKB.
DR   GO; GO:0004518; F:nuclease activity; ISS:UniProtKB.
DR   GO; GO:0008143; F:poly(A) binding; ISS:UniProtKB.
DR   GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0003712; F:transcription coregulator activity; ISS:UniProtKB.
DR   GO; GO:0032508; P:DNA duplex unwinding; ISS:UniProtKB.
DR   GO; GO:0006302; P:double-strand break repair; ISS:UniProtKB.
DR   GO; GO:0001700; P:embryonic development via the syncytial blastoderm; IEP:UniProtKB.
DR   GO; GO:0048477; P:oogenesis; IMP:FlyBase.
DR   GO; GO:0042254; P:ribosome biogenesis; ISS:FlyBase.
DR   GO; GO:0007283; P:spermatogenesis; IMP:FlyBase.
DR   InterPro; IPR001870; B30.2/SPRY.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
DR   InterPro; IPR003877; SPRY_dom.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF00622; SPRY; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SMART; SM00449; SPRY; 1.
DR   SUPFAM; SSF49899; SSF49899; 1.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   PROSITE; PS50188; B302_SPRY; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 2.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS51195; Q_MOTIF; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Complete proteome; Exonuclease; Helicase; Hydrolase;
KW   Nuclease; Nucleotide-binding; Reference proteome; RNA-binding.
FT   CHAIN         1    727       ATP-dependent RNA helicase Ddx1.
FT                                /FTId=PRO_0000054989.
FT   DOMAIN        2    428       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN       69    246       B30.2/SPRY. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00548}.
FT   DOMAIN      483    676       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   NP_BIND      46     53       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   MOTIF       370    373       DEAD box.
FT   CONFLICT     78     89       KGGAIGGAVTPW -> QGRCNWRSCDSV (in Ref. 1;
FT                                AAC47309). {ECO:0000305}.
FT   CONFLICT    217    217       L -> S (in Ref. 1; AAC47309).
FT                                {ECO:0000305}.
FT   CONFLICT    274    279       AAGAPS -> DSWST (in Ref. 1; AAC47309).
FT                                {ECO:0000305}.
FT   CONFLICT    365    365       R -> G (in Ref. 1; AAC47309).
FT                                {ECO:0000305}.
FT   CONFLICT    429    429       V -> G (in Ref. 1; AAC47309).
FT                                {ECO:0000305}.
FT   CONFLICT    458    458       S -> C (in Ref. 4; AAD09429).
FT                                {ECO:0000305}.
FT   CONFLICT    529    530       GG -> D (in Ref. 1; AAC47309).
FT                                {ECO:0000305}.
FT   CONFLICT    580    589       MINVTLPDDK -> SKFSNFETIT (in Ref. 4;
FT                                AAD09429). {ECO:0000305}.
FT   CONFLICT    682    682       K -> P (in Ref. 1; AAC47309).
FT                                {ECO:0000305}.
FT   CONFLICT    704    704       V -> E (in Ref. 1; AAC47309).
FT                                {ECO:0000305}.
SQ   SEQUENCE   727 AA;  80869 MW;  52B7BE91A33599DB CRC64;
     MTAFEEFGVL PELGMATDEL DWTLPTDVQA EAIPLILGGG DVLMAAETGS GKTGAFCLPI
     LQIVWETLRD LEEGKAGKGG AIGGAVTPWT MSFFDRGNAL AVTPDGLRCQ SREFKEWHGC
     RATTGVRGKG KFYFEATVTD EGLCRVGWST QQANLDLGTC RMGFGFGGTG KKSNNRQFDD
     YGEAFGKADV IGCLLDLKNQ EVSFTKNGQN LGVAFRLPDN LAKETFYPAV VLKNAEMQFN
     FGKTDFKYAP GNGFVGACQA GPEHSKANPI TGPAAGAPSA KPAPNAPQAI IMEPSRELAE
     QTYNQIEKFK YHLSNPEVRS LLLIGGVRLE EQKAQLMQGT HIVVGTPGRL EEMINSGLVL
     LTHCRFFVLD EADALLKQGY TELIDRLHKQ IPKITSDGRR LQMVVCSATL HAFEVKKMAE
     RLMHFPTWVD LKGEDAVPET VHHVVCLVDP QMDTTWQSLR QPIGTDGVHD RDNVHPGNHS
     KETLSQAVKL LKGEYCVHAI DKHNMDRAII FCRTKQDCDN LERFLRQRGG KHYSCVCLHG
     DRKPQERKEN LEMFKRQQVK FLICTDVAAR GLDITGLPFM INVTLPDDKT NYVHRIGRVG
     RAERMGLAIS LVATVPEKVW YHGEWCKSRG RSCNNTNLTE VRGCCIWYNE PNLLAEVEDH
     LNITIQQVDK TMDVPVNDFD GKVVYGQKNL RTGSGYEDHV EQLVPTVRKL TELELQSQSL
     FLKRLKV
//
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