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Reviewed, UniProtKB/Swiss-Prot Q9VFL5 (SYMM_DROME)

Last modified July 22, 2008. Version 57. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Methionyl-tRNA synthetase, mitochondrial
    EC=6.1.1.10
Alternative name(s):
    Mitochondrial methionine--tRNA ligase
      Short name(s)=MtMetRS
Gene names
Name: Aats-met
ORF Names: CG31322, CG8684
OrganismDrosophila melanogaster (Fruit fly) [Complete proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

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Protein attributes

Sequence length582 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Catalytic activity

ATP + L-methionine + tRNA(Met) = AMP + diphosphate + L-methionyl-tRNA(Met).

Subcellular location

Mitochondrion matrixBy similarity.

Sequence similarities

Belongs to the class-I aminoacyl-tRNA synthetase family.

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Ontologies

Keywords

   Biological processProtein biosynthesis
   Cellular componentMitochondrion
   DomainTransit peptide
   LigandATP-binding
Nucleotide-binding
   Molecular functionAminoacyl-tRNA synthetase
Ligase
   Technical termComplete proteome

Gene Ontology (GO)

   Biological processmethionyl-tRNA aminoacylation

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular componentmitochondrial matrix

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular functionmethionine-tRNA ligase activity

Inferred from sequence or structural similarity. Source: UniProtKB

protein binding

Inferred from physical interaction. Source: IntAct

Complete GO annotation...

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Binary interactions

With

Entry

#Exp.

IntAct

Notes

Q9VCZ81EBI-182711,EBI-100243

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical view

Molecule processing

Transit peptide1 – 9595Mitochondrion Potential
Chain96 – 582487Methionyl-tRNA synthetase, mitochondrial

Regions

Motif27 – 3711"HIGH" region
Motif317 – 3215"KMSKS" region

Sites

Binding site3201ATP By similarity

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Sequences

Sequence LengthMass (Da)Tools
Q9VFL5-1 [UniParc].

Last modified October 1, 2002. Version 2.
Checksum: 581A3D42A746F9AC

FASTA58265,998
        10         20         30         40         50         60 
MLIRRIKCLR YLGTRYNSSH YVTTPIFYVN AAPHIGHLYS AVIADAHCRY QRLRYPEQDV 

        70         80         90        100        110        120 
RLCTGTDEHG TKIQQAASLH GVPVAKYCDD ISQRYREVFR SASIQQDDFI RTTEDRHKRA 

       130        140        150        160        170        180 
VANFWRTLHT RGHIYSAAYS GWYCVSDETF LTDSQLRLDE ATGTRYSLES GHPVEWTEET 

       190        200        210        220        230        240 
NYMFRLSQFQ DDVRHWVKTE ARVRPAKFEK ILLDTLSEPL PDVSVSRPSN RVHWAIPVPD 

       250        260        270        280        290        300 
DDSQTVYVWL DALVNYLSSV GYPDEKFSAH WPPAQQVIGK DILKFHGIYW TAFLLAAGLE 

       310        320        330        340        350        360 
PPGQLYVHSH WTVDGQKMSK SKHNVVDPLQ AAQQYTMEGL RYFLLREGVA HSDGNYSHVK 

       370        380        390        400        410        420 
AQRILNSELA DTLGNLLSRA SAKSLNPGQI YPSPSAEHLA DLLRSLDVAK RLQDSLLQLS 

       430        440        450        460        470        480 
ERCESHYECN HFHLVADTTM AALHAANNFF ESSKPWTLKA GAPDGNQARL ETIIAMTMDA 

       490        500        510        520        530        540 
LRLSGIVLQP IIPQLANRLL DKLSVPTAQR GWNYLAESFA TSPNSSNSPA GLGESRQLDG 

       550        560        570        580 
QTSALLFQRI LEETSAKEVK EQKPQPAKRS KSKKKERRET MS

« Hide

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References

« Hide 'large scale' references
[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. expand/collapse author list , 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: 10731132] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Berkeley.
[2]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. expand/collapse author list , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed: 12537572] [Abstract]
Cited for: GENOME REANNOTATION.
[3]"A Drosophila full-length cDNA resource."
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed: 12537569] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Berkeley.
Tissue: Head.

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Cross-references

Sequence databases

AE014297 Genomic DNA. Translation: AAF55037.2.
AY069128 mRNA. Translation: AAL39273.1.
RefSeqNP_650348.1.
UniGeneDm.1570

3D structure databases

HSSPHSSP built from PDB template 1A8H based on UniProtKB P23395.
ModBaseSearch...

Protein-protein interaction databases

IntActQ9VFL5.

Genome annotation databases

EnsemblCG31322. Drosophila melanogaster. [Contig view]
GeneID41733.
KEGGdme:Dmel_CG31322.
NMPDRfig|7227.3.peg.12732.

Organism-specific databases

FlyBaseFBgn0027083. Aats-met.

Phylogenomic databases

HOGENOMQ9VFL5.

Gene expression databases

ArrayExpressQ9VFL5.
GermOnlineCG31322. Drosophila melanogaster.

Family and domain databases

InterProIPR015413. aa-tRNA-synt_I.
IPR001412. aa-tRNA-synth_I_CS.
IPR014729. Rossmann-like_a/b/a_fold.
IPR014758. tRNA-synt_met_N.
[Graphical view]
Gene3DG3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 1 hit.
PfamPF09334. tRNA-synt_1g. 1 hit.
[Graphical view]
PRINTSPR01041. TRNASYNTHMET.
PROSITEPS00178. AA_TRNA_LIGASE_I. False negative.
[Graphical view]
ProDomQ9VFL5.
[Graphical view] [Entries sharing at least one domain]
BLOCKSSearch...

Other Resources

ProtoNetSearch...

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Entry information

Entry nameSYMM_DROME
AccessionPrimary (citable) accession number: Q9VFL5
Secondary accession number(s): Q8T0Q6
Entry history
Integrated into UniProtKB/Swiss-Prot: January 10, 2006
Last sequence update: October 1, 2002
Last modified: July 22, 2008
This is version 57 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectDrosophila annotation project

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Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase

UniProtKB secondary accession numbers

Index of UniProtKB secondary accession numbers

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents