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Q9Y105

- SYQ_DROME

UniProt

Q9Y105 - SYQ_DROME

Protein

Probable glutamine--tRNA ligase

Gene

Aats-gln

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 117 (01 Oct 2014)
      Sequence version 1 (01 Nov 1999)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    ATP + L-glutamine + tRNA(Gln) = AMP + diphosphate + L-glutaminyl-tRNA(Gln).

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei499 – 4991ATPBy similarity

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. glutamine-tRNA ligase activity Source: FlyBase

    GO - Biological processi

    1. dendrite morphogenesis Source: FlyBase
    2. glutaminyl-tRNA aminoacylation Source: InterPro

    Keywords - Molecular functioni

    Aminoacyl-tRNA synthetase, Ligase

    Keywords - Biological processi

    Protein biosynthesis

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_214144. Cytosolic tRNA aminoacylation.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Probable glutamine--tRNA ligase (EC:6.1.1.18)
    Alternative name(s):
    Glutaminyl-tRNA synthetase
    Short name:
    GlnRS
    Gene namesi
    Name:Aats-gln
    ORF Names:CG10506
    OrganismiDrosophila melanogaster (Fruit fly)
    Taxonomic identifieri7227 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
    ProteomesiUP000000803: Chromosome 3R

    Organism-specific databases

    FlyBaseiFBgn0027090. Aats-gln.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: InterPro
    2. microtubule associated complex Source: FlyBase

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 778778Probable glutamine--tRNA ligasePRO_0000195863Add
    BLAST

    Proteomic databases

    PaxDbiQ9Y105.
    PRIDEiQ9Y105.

    Expressioni

    Gene expression databases

    BgeeiQ9Y105.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    SpdSQ9VHA11EBI-109039,EBI-154429

    Protein-protein interaction databases

    BioGridi69882. 8 interactions.
    DIPiDIP-18324N.
    IntActiQ9Y105. 1 interaction.
    MINTiMINT-307310.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9Y105.
    SMRiQ9Y105. Positions 4-188, 239-777.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi273 – 28311"HIGH" regionAdd
    BLAST
    Motifi496 – 5005"KMSKS" region

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0008.
    GeneTreeiENSGT00550000074972.
    InParanoidiQ9Y105.
    KOiK01886.
    OMAiRMQKRAK.
    OrthoDBiEOG75XGK9.
    PhylomeDBiQ9Y105.

    Family and domain databases

    Gene3Di1.10.1160.10. 1 hit.
    2.40.240.10. 2 hits.
    3.40.50.620. 2 hits.
    InterProiIPR001412. aa-tRNA-synth_I_CS.
    IPR004514. Gln-tRNA-synth.
    IPR007638. Gln-tRNA-synth_Ib_RNA-bd_2.
    IPR007639. Gln-tRNA-synth_Ib_RNA-bd_N.
    IPR000924. Glu/Gln-tRNA-synth.
    IPR020061. Glu/Gln-tRNA-synth_Ib_a-bdl.
    IPR020058. Glu/Gln-tRNA-synth_Ib_cat-dom.
    IPR020059. Glu/Gln-tRNA-synth_Ib_codon-bd.
    IPR020056. Rbsml_L25/Gln-tRNA_synth_b-brl.
    IPR011035. Ribosomal_L25/Gln-tRNA_synth.
    IPR014729. Rossmann-like_a/b/a_fold.
    [Graphical view]
    PANTHERiPTHR10119. PTHR10119. 1 hit.
    PfamiPF00749. tRNA-synt_1c. 1 hit.
    PF03950. tRNA-synt_1c_C. 1 hit.
    PF04558. tRNA_synt_1c_R1. 1 hit.
    PF04557. tRNA_synt_1c_R2. 1 hit.
    [Graphical view]
    PRINTSiPR00987. TRNASYNTHGLU.
    SUPFAMiSSF50715. SSF50715. 1 hit.
    TIGRFAMsiTIGR00440. glnS. 1 hit.
    PROSITEiPS00178. AA_TRNA_LIGASE_I. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9Y105-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAGDDLIAKF QALGMSEQKA KETLKNANVT KNLQLSLAAA GSATLSDGTG    50
    MLIYHMATKL KPQTADHLPL LVRYIVEHKL DNTQRVDAAL EYLLKCGQSL 100
    NANIDLQALE KECGVGVVVT PEQIERTVQA KIKASYKEAL LEQRYHFNSF 150
    KILQDVRGEL KWADAKSVKA AIDVEIFDLL GPKTEADLKP QTKANDKPKA 200
    AKPKAEVTPA AQTAEAASDG ATTISELMKT KVHFHAPGEN FKADGYVVTE 250
    HTERLLKEHL ARTGGKVHTR FPPEPNGILH IGHAKAININ FGYAAAHDGV 300
    CYLRYDDTNP EKEEEKFFLA IKEMVEWLGY KPFKITYSSD NFQQLYEWAV 350
    VLINKGLAYV CHQKAEELKG FNPKPSPWRE RPIEESLRLF EDMKRGKIDE 400
    GAATLRMKVT LEEGKMDPVA YRIKFISHHR TGSDWCIYPT YDYTHCLCDS 450
    LEDITHSLCT KEFQSRRSSY YWLCNALGIY CPVQWEYGRL NMNYALVSKR 500
    KIAKLITEQI VHDWDDPRLF TLTALRRRGF PAEAINNFCA QMGVTGAQIA 550
    VDPAMLEAAV RDVLNVTAPR RLVVLEPLKV TIKNFPHAAP VQLEVPDFPQ 600
    NPQQGTHKIT LDKVIYIEQG DFKLEPEKGY RRLAPKQSVG LRHAGLVISV 650
    DEIVKDPATG QVVELICTSQ PAEQAEKPKA FVQWVSQPIQ LEVRLYEQLF 700
    KHKNPEDPNE VPGGFLSDIS EQSMSVVVAF ADRALNQAKV YDKFQFERIG 750
    FFSVDPDTSA NHLVFNRTVG LKEDAGKK 778
    Length:778
    Mass (Da):87,508
    Last modified:November 1, 1999 - v1
    Checksum:i748509EC93E5E43A
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE014297 Genomic DNA. Translation: AAF56434.2.
    AF145668 mRNA. Translation: AAD38643.1.
    RefSeqiNP_524841.1. NM_080102.5.
    UniGeneiDm.1790.

    Genome annotation databases

    EnsemblMetazoaiFBtr0084866; FBpp0084240; FBgn0027090.
    GeneIDi45786.
    KEGGidme:Dmel_CG10506.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE014297 Genomic DNA. Translation: AAF56434.2 .
    AF145668 mRNA. Translation: AAD38643.1 .
    RefSeqi NP_524841.1. NM_080102.5.
    UniGenei Dm.1790.

    3D structure databases

    ProteinModelPortali Q9Y105.
    SMRi Q9Y105. Positions 4-188, 239-777.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 69882. 8 interactions.
    DIPi DIP-18324N.
    IntActi Q9Y105. 1 interaction.
    MINTi MINT-307310.

    Proteomic databases

    PaxDbi Q9Y105.
    PRIDEi Q9Y105.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai FBtr0084866 ; FBpp0084240 ; FBgn0027090 .
    GeneIDi 45786.
    KEGGi dme:Dmel_CG10506.

    Organism-specific databases

    CTDi 45786.
    FlyBasei FBgn0027090. Aats-gln.

    Phylogenomic databases

    eggNOGi COG0008.
    GeneTreei ENSGT00550000074972.
    InParanoidi Q9Y105.
    KOi K01886.
    OMAi RMQKRAK.
    OrthoDBi EOG75XGK9.
    PhylomeDBi Q9Y105.

    Enzyme and pathway databases

    Reactomei REACT_214144. Cytosolic tRNA aminoacylation.

    Miscellaneous databases

    GenomeRNAii 45786.
    NextBioi 838357.
    PROi Q9Y105.

    Gene expression databases

    Bgeei Q9Y105.

    Family and domain databases

    Gene3Di 1.10.1160.10. 1 hit.
    2.40.240.10. 2 hits.
    3.40.50.620. 2 hits.
    InterProi IPR001412. aa-tRNA-synth_I_CS.
    IPR004514. Gln-tRNA-synth.
    IPR007638. Gln-tRNA-synth_Ib_RNA-bd_2.
    IPR007639. Gln-tRNA-synth_Ib_RNA-bd_N.
    IPR000924. Glu/Gln-tRNA-synth.
    IPR020061. Glu/Gln-tRNA-synth_Ib_a-bdl.
    IPR020058. Glu/Gln-tRNA-synth_Ib_cat-dom.
    IPR020059. Glu/Gln-tRNA-synth_Ib_codon-bd.
    IPR020056. Rbsml_L25/Gln-tRNA_synth_b-brl.
    IPR011035. Ribosomal_L25/Gln-tRNA_synth.
    IPR014729. Rossmann-like_a/b/a_fold.
    [Graphical view ]
    PANTHERi PTHR10119. PTHR10119. 1 hit.
    Pfami PF00749. tRNA-synt_1c. 1 hit.
    PF03950. tRNA-synt_1c_C. 1 hit.
    PF04558. tRNA_synt_1c_R1. 1 hit.
    PF04557. tRNA_synt_1c_R2. 1 hit.
    [Graphical view ]
    PRINTSi PR00987. TRNASYNTHGLU.
    SUPFAMi SSF50715. SSF50715. 1 hit.
    TIGRFAMsi TIGR00440. glnS. 1 hit.
    PROSITEi PS00178. AA_TRNA_LIGASE_I. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The genome sequence of Drosophila melanogaster."
      Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
      , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
      Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Berkeley.
    2. Cited for: GENOME REANNOTATION.
      Strain: Berkeley.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: Berkeley.
      Tissue: Head.

    Entry informationi

    Entry nameiSYQ_DROME
    AccessioniPrimary (citable) accession number: Q9Y105
    Secondary accession number(s): Q9VBU3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: November 1, 1999
    Last modified: October 1, 2014
    This is version 117 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programDrosophila annotation project

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Aminoacyl-tRNA synthetases
      List of aminoacyl-tRNA synthetase entries
    2. Drosophila
      Drosophila: entries, gene names and cross-references to FlyBase
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3