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Q9VFL5 (SYMM_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 86. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

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

Protein attributes

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

General annotation (Comments)

Catalytic activity

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

Subcellular location

Mitochondrion matrix By similarity.

Sequence similarities

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

Ontologies

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

Inferred from electronic annotation. Source: UniProtKB-KW

methionine-tRNA ligase activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

CG7048Q9VCZ81EBI-182711,EBI-100243

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 9595Mitochondrion Potential
Chain96 – 582487Methionine--tRNA ligase, mitochondrial
PRO_0000045497

Regions

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

Sites

Binding site3201ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9VFL5 [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

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.
Strain: Berkeley.
[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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE014297 Genomic DNA. Translation: AAF55037.2.
AY069128 mRNA. Translation: AAL39273.1.
RefSeqNP_650348.1. NM_142091.4.
UniGeneDm.1570.

3D structure databases

ProteinModelPortalQ9VFL5.
SMRQ9VFL5. Positions 16-552.
ModBaseSearch...

Protein-protein interaction databases

IntActQ9VFL5. 1 interaction.
MINTMINT-1023892.
STRINGQ9VFL5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0082895; FBpp0082356; FBgn0027083.
GeneID41733.
KEGGdme:Dmel_CG31322.
NMPDRfig|7227.3.peg.12732.

Organism-specific databases

CTD41733.
FlyBaseFBgn0027083. Aats-met.

Phylogenomic databases

eggNOGinNOG06281.
GeneTreeEMGT00050000004677.
InParanoidQ9VFL5.
OMAGTYPVFC.
OrthoDBEOG4V15G1.
PhylomeDBQ9VFL5.

Gene expression databases

BgeeQ9VFL5.
GermOnlineCG31322. Drosophila melanogaster.

Family and domain databases

InterProIPR015413. aa-tRNA-synt_I.
IPR014758. Met-tRNA_synth.
IPR014729. Rossmann-like_a/b/a_fold.
IPR009080. tRNAsynth_1a_anticodon-bd.
[Graphical view]
Gene3DG3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 2 hits.
KOK01874.
PfamPF09334. tRNA-synt_1g. 1 hit.
[Graphical view]
PRINTSPR01041. TRNASYNTHMET.
SUPFAMSSF47323. tRNAsyn_1a_bind. 1 hit.
TIGRFAMsTIGR00398. MetG. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. False negative.
[Graphical view]
ProtoNetSearch...

Other

NextBio825286.

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: January 25, 2012
This is version 86 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

Drosophila

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

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents