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Y8611_DROME
ID   Y8611_DROME             Reviewed;         975 AA.
AC   Q86B47; Q9VX53; Q9Y159;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 152.
DE   RecName: Full=Probable ATP-dependent RNA helicase CG8611;
DE            EC=3.6.4.13;
GN   ORFNames=CG8611;
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, AND ALTERNATIVE SPLICING.
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] (ISOFORM A).
RC   STRAIN=Berkeley; TISSUE=Head;
RX   PubMed=10731138; DOI=10.1126/science.287.5461.2222;
RA   Rubin G.M., Hong L., Brokstein P., Evans-Holm M., Frise E., Stapleton M.,
RA   Harvey D.A.;
RT   "A Drosophila complementary DNA resource.";
RL   Science 287:2222-2224(2000).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-667, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY.
RX   PubMed=17372656; DOI=10.1039/b617545g;
RA   Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D., Juenger M.A.,
RA   Eng J.K., Aebersold R., Tao W.A.;
RT   "An integrated chemical, mass spectrometric and computational strategy for
RT   (quantitative) phosphoproteomics: application to Drosophila melanogaster
RT   Kc167 cells.";
RL   Mol. Biosyst. 3:275-286(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75; SER-99; SER-210; SER-220
RP   AND SER-224, 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: Probable ATP-dependent RNA helicase. {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   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=B;
CC         IsoId=Q86B47-1; Sequence=Displayed;
CC       Name=A;
CC         IsoId=Q86B47-2; Sequence=VSP_037205;
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX31/DBP7
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AE014298; AAF48727.2; -; Genomic_DNA.
DR   EMBL; AE014298; AAO41693.1; -; Genomic_DNA.
DR   EMBL; AF145609; AAD38584.1; -; mRNA.
DR   RefSeq; NP_573214.1; NM_132986.5. [Q86B47-2]
DR   RefSeq; NP_788922.1; NM_176749.2. [Q86B47-1]
DR   AlphaFoldDB; Q86B47; -.
DR   SMR; Q86B47; -.
DR   BioGRID; 59053; 4.
DR   IntAct; Q86B47; 6.
DR   STRING; 7227.FBpp0074214; -.
DR   iPTMnet; Q86B47; -.
DR   PaxDb; Q86B47; -.
DR   PRIDE; Q86B47; -.
DR   DNASU; 32725; -.
DR   EnsemblMetazoa; FBtr0074439; FBpp0074213; FBgn0027602. [Q86B47-2]
DR   EnsemblMetazoa; FBtr0074440; FBpp0074214; FBgn0027602. [Q86B47-1]
DR   GeneID; 32725; -.
DR   KEGG; dme:Dmel_CG8611; -.
DR   UCSC; CG8611-RA; d. melanogaster.
DR   UCSC; CG8611-RB; d. melanogaster. [Q86B47-1]
DR   FlyBase; FBgn0027602; CG8611.
DR   VEuPathDB; VectorBase:FBgn0027602; -.
DR   eggNOG; KOG0348; Eukaryota.
DR   GeneTree; ENSGT00550000075041; -.
DR   InParanoid; Q86B47; -.
DR   PhylomeDB; Q86B47; -.
DR   BioGRID-ORCS; 32725; 0 hits in 1 CRISPR screen.
DR   GenomeRNAi; 32725; -.
DR   PRO; PR:Q86B47; -.
DR   Proteomes; UP000000803; Chromosome X.
DR   Bgee; FBgn0027602; Expressed in embryonic/larval visceral muscle (Drosophila) and 33 other tissues.
DR   ExpressionAtlas; Q86B47; baseline and differential.
DR   Genevisible; Q86B47; DM.
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; ISS:FlyBase.
DR   GO; GO:0042254; P:ribosome biogenesis; IBA:GO_Central.
DR   Gene3D; 3.40.50.300; -; 2.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR025313; DUF4217.
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; PF13959; DUF4217; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM01178; DUF4217; 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.
DR   PROSITE; PS51195; Q_MOTIF; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; ATP-binding; Helicase; Hydrolase; Nucleotide-binding;
KW   Phosphoprotein; Reference proteome; RNA-binding.
FT   CHAIN           1..975
FT                   /note="Probable ATP-dependent RNA helicase CG8611"
FT                   /id="PRO_0000372851"
FT   DOMAIN          359..548
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          616..789
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          1..38
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          50..104
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          127..295
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          915..942
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          955..975
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           327..356
FT                   /note="Q motif"
FT   MOTIF           485..488
FT                   /note="DEAD box"
FT   COMPBIAS        1..29
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        61..104
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        138..156
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        188..215
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        231..245
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        264..295
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         372..379
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   MOD_RES         75
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   MOD_RES         99
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   MOD_RES         210
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   MOD_RES         220
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   MOD_RES         224
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   MOD_RES         667
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:17372656"
FT   VAR_SEQ         19
FT                   /note="Missing (in isoform A)"
FT                   /evidence="ECO:0000303|PubMed:10731138"
FT                   /id="VSP_037205"
SQ   SEQUENCE   975 AA;  107968 MW;  2B7FCCA1C83DE00B CRC64;
     MVENISLNVT VKSSARKNQQ QSPALSVKKR AQKSQDFDFQ FNVDKPKVKA IVVRRRAPPS
     KVEPTNSSVP NTTKSPTPSV SSSKSAISTL SASPKANASN DDLMFNVSPT KPPVKSVLGD
     DFMLNVTTKP VVAQKAKPKI TRAERLGKKQ RQGKPLTKLS EEQITRALKS NKKPKNPNQL
     PTPGDLFRAQ LEEERRQKRR EEGGGDQEAS ADEEDAKNNS GGGSPRVKPS SAVKESKKSS
     DIEDSGESGE ESATSDEEPD ESSAQSPGQE KEPKQTAKKP PKAEETSSTN RFRTKKIGLF
     DQSDVEALKQ LGQRAVKPVK ETIFTGSKIS TLGLHPHAVK NLEDLLSIRE LTSVQQKTIP
     EVLQGKDVLV RSQTGSGKTL AYALPLVELL QKQQPRIQRK DGVLALVIVP TRELVMQTYE
     LIQKLVKPYT WIVPGSLLGG ESRKSEKARL RKGINILIGT PGRLVDHLLH TASFKLTKLQ
     FLILDEADRL LELGYERDVK QLVEAIDKQR AECEDKELPQ LQRMLLSATL TSQVQQLAGL
     TLKNPLYIDN SDEAASAALK SKDGYQKETI EALLEVDDGL GEYQEDVTGV LSIPENLQLS
     YVVVPPKLRL VALSSLLAKE VDASPKQFKA IVFMSTTEMV NFHHDMLNEA LTRRVLDEED
     EQEKGDSDDD GDIPLLQGLR FFKLHGSMTQ TERQGVFRGF RDCASCVLLA TDVVGRGIDV
     PDIKLVVQYT PPQTTADFVH RVGRTARAGR KGRAVLFLTP SEAQFVRHLE KKRIRIQQGD
     MYAYLQTLLP KDDEARTVQE AASNLQHKFQ TLLEDDRELH DKSCKAFVSW MKFYSTFPKE
     LKPIFNVRIA HMGHFAKSFA LKEAPSKFAA KHAAPKAAPP TNRLTYTERD PEKIQAQKRA
     KRRFTTTVSG EVRQLQQRDV GAQKPGAPPP KGGFIGGGVG RSSFMKSLGK SRALNMSEFD
     SGLPPEGAAK RRKQA
 
 
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