DDX51_DROME
ID DDX51_DROME Reviewed; 687 AA.
AC P26802; Q9XZ18;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 3.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Probable ATP-dependent RNA helicase Dbp73D;
DE Short=DEAD box protein 73D;
DE EC=3.6.4.13;
GN Name=Dbp73D; ORFNames=CG9680;
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 [GENOMIC DNA], AND TISSUE SPECIFICITY.
RC STRAIN=Canton-S;
RX PubMed=1620603; DOI=10.1093/nar/20.12.3063;
RA Patterson L.F., Harvey M., Lasko P.F.;
RT "Dbp73D, a Drosophila gene expressed in ovary, encodes a novel D-E-A-D box
RT protein.";
RL Nucleic Acids Res. 20:3063-3067(1992).
RN [2]
RP SEQUENCE REVISION.
RA Lasko P.F.;
RL Submitted (JUN-1994) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
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 [5]
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., 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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M.,
RA Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A.,
RA Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A.,
RA Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S.,
RA Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.;
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: ATP-binding RNA helicase involved in the biogenesis of 60S
CC ribosomal subunits. {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 -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in the germline tissue of the ovary.
CC {ECO:0000269|PubMed:1620603}.
CC -!- DOMAIN: The Q motif is unique to and characteristic of the DEAD box
CC family of RNA helicases and controls ATP binding and hydrolysis.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX51/DBP6
CC subfamily. {ECO:0000305}.
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DR EMBL; M74824; AAC14192.1; -; Genomic_DNA.
DR EMBL; AE014296; AAF49419.1; -; Genomic_DNA.
DR EMBL; AF132173; AAD34761.1; -; mRNA.
DR EMBL; BT010045; AAQ22514.1; -; mRNA.
DR PIR; S28762; S28762.
DR RefSeq; NP_476833.1; NM_057485.4.
DR AlphaFoldDB; P26802; -.
DR SMR; P26802; -.
DR BioGRID; 65170; 1.
DR IntAct; P26802; 6.
DR STRING; 7227.FBpp0075106; -.
DR PaxDb; P26802; -.
DR PRIDE; P26802; -.
DR EnsemblMetazoa; FBtr0075347; FBpp0075106; FBgn0004556.
DR GeneID; 39871; -.
DR KEGG; dme:Dmel_CG9680; -.
DR CTD; 39871; -.
DR FlyBase; FBgn0004556; Dbp73D.
DR VEuPathDB; VectorBase:FBgn0004556; -.
DR eggNOG; KOG0350; Eukaryota.
DR GeneTree; ENSGT00550000075141; -.
DR HOGENOM; CLU_003041_15_3_1; -.
DR InParanoid; P26802; -.
DR OMA; TEQYCVT; -.
DR OrthoDB; 973872at2759; -.
DR PhylomeDB; P26802; -.
DR SignaLink; P26802; -.
DR BioGRID-ORCS; 39871; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 39871; -.
DR PRO; PR:P26802; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0004556; Expressed in ovary and 27 other tissues.
DR Genevisible; P26802; DM.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; -; 2.
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; IPR000629; RNA-helicase_DEAD-box_CS.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00039; DEAD_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Helicase; Hydrolase; Nucleotide-binding; Nucleus;
KW Reference proteome; Ribosome biogenesis; RNA-binding; rRNA processing.
FT CHAIN 1..687
FT /note="Probable ATP-dependent RNA helicase Dbp73D"
FT /id="PRO_0000055005"
FT DOMAIN 177..381
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 434..583
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 52..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 646..675
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 160..168
FT /note="Q motif"
FT MOTIF 305..308
FT /note="DEAD box"
FT COMPBIAS 7..22
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 52..84
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 655..675
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 190..197
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT CONFLICT 55
FT /note="L -> P (in Ref. 1; AAC14192)"
FT /evidence="ECO:0000305"
FT CONFLICT 86
FT /note="D -> V (in Ref. 1; AAC14192)"
FT /evidence="ECO:0000305"
FT CONFLICT 594..595
FT /note="AG -> PR (in Ref. 1; AAC14192)"
FT /evidence="ECO:0000305"
FT CONFLICT 617..687
FT /note="KALIHKKQEETATVRPLTLMEKLQIKANEIVQSSKKSSETKNSKTKADKTKY
FT QPKETKKQIIAKQLKAIEN -> QGIDPQETGGNGHSSSTDVDGKVANQSE (in
FT Ref. 1; AAC14192)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 687 AA; 77590 MW; 252D39D8BB948639 CRC64;
MELFTVNRYT EDLKEQKDGA QGTNNEDEIL QKLLKKAAKR KRKHEAIEVV ETPILEKETS
DVKESESKEE QVEEPEKPLE VVQEEDVPSN EFQVLGGDDS AAKKKKVQMQ LPNWLAHPTI
IEGGSLQPEE EVPASEAIDQ LDYLEKYTCQ ALKQMKIKRL FPVQKQVIPW ILEAHAKPPP
FRPRDICVSA PTGSGKTLAF AIPIVQLLSQ RVDCKVRALV VLPVAELALQ VYRVISELCS
KTELEVCLLS KQHKLEDEQE KLVEQYKGKY YSKADIVVTT PGRLVDHLHA TKGFCLKSLK
FLVIDEADRI MDAVFQNWLY HLDSHVKETT DQLLAGTQAP LCYAELQASF GKQPHKLLFS
ATLSQDPEKL QDLRLFQPRL FATVLTMPVL KDATEEGADT EALTDPGQFV GRYTTPAELT
EQYCVTELRL KPLTVFALVE KYKWKRFLCF TNSSDQATRL TFVLKVLFQK YSTKVSELSG
NLSAKVRNER LRDFAAGKIN GLICSDALAR GIDVADVDVV LSYETPRHIT TYIHRVGRTA
RAGRKGTAVT VLTEQDMTLF KKILSDANKG LGEEIHVSPD IEIQHAVEYK EALAGLRSEK
VKNKNQKMAE KNRVATKALI HKKQEETATV RPLTLMEKLQ IKANEIVQSS KKSSETKNSK
TKADKTKYQP KETKKQIIAK QLKAIEN
