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Reviewed, UniProtKB/Swiss-Prot O16129 (SYFM_DROME)

Last modified July 22, 2008. Version 59. 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:
    Probable phenylalanyl-tRNA synthetase, mitochondrial
    EC=6.1.1.20
Alternative name(s):
    Phenylalanine--tRNA ligase
      Short name=PheRS
Gene names
Name: Aats-phe
Synonyms: Pts
ORF Names: CG13348
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 length453 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-phenylalanine + tRNA(Phe) = AMP + diphosphate + L-phenylalanyl-tRNA(Phe).

Subcellular location

Mitochondrion matrixPotential.

Sequence similarities

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

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Binary interactions

With

Entry

#Exp.

IntAct

Notes

Q9W0M11EBI-111246,EBI-92679

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical view

Molecule processing

Transit peptide1 – 2727Mitochondrion Potential
Chain28 – 453426Probable phenylalanyl-tRNA synthetase, mitochondrial

Experimental info

Sequence conflict217 – 23216SSKFM…CHTLE → HPSSWTKPNSPATRR in AAB65750. Ref.1

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Sequences

Sequence LengthMass (Da)Tools
O16129-1 [UniParc].

Last modified October 1, 2000. Version 3.
Checksum: 4540742E54D1AE24

FASTA45351,996
        10         20         30         40         50         60 
MLLTLRVQGA RHWLKSTRCL ASSAAPAKSP SSPPQLEVSG STYATDGWTN VTPKILSYVG 

        70         80         90        100        110        120 
ANKHLQTDHP LSIIRQRIVN YFYGAYRNQR GNPLFSVYDQ MNPVVTVQQN FDNLLIPADH 

       130        140        150        160        170        180 
VSRQKSDCYY INQQHLLRAH TTAHQVELIS GGLDNFLVVG EVYRRDEIDS THYPVFHQAD 

       190        200        210        220        230        240 
AVRLVTKDKL FERNPGLELF EETWSGTLAD PKLILPSSKF MDQTKQPCHT LEAVKLMEHE 

       250        260        270        280        290        300 
MKHVLVGLTK DLFGPRIKYR WVDTYFPFTQ PSWELEIYFK DNWLEVLGCG IMRHEILQRS 

       310        320        330        340        350        360 
GVHQSIGYAF GVGLERLAMV LFDIPDIRLF WSNDSGFLSQ FSEKDLHNLP KYKPISHYPQ 

       370        380        390        400        410        420 
CTNDLSFWLP QDIEVDAGFS PNDFYDLVRS VAGDMVEQIS LVDKFKHPKT GKSSVCFRIV 

       430        440        450 
YRHMERTLTQ AEVNEIHKQI ASASVDSFNV QIR

« Hide

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References

« Hide 'large scale' references
[1]"Structure and associated mutational effects of the cysteine proteinase (CP1) gene of Drosophila melanogaster."
Gray Y.H.M., Sved J.A., Preston C.R., Engels W.R.
Insect Mol. Biol. 7:291-293(1998) [PubMed: 9662479] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"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.
[3]"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.
[4]"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: Embryo.

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Cross-references

Sequence databases

AF012089 Genomic DNA. Translation: AAB65750.2.
AE013599 Genomic DNA. Translation: AAF58310.1.
AY058580 mRNA. Translation: AAL13809.1.
RefSeqNP_477283.1.
UniGeneDm.4156

3D structure databases

HSSPHSSP built from PDB template 1JJC based on UniProtKB P27001.
ModBaseSearch...

Protein-protein interaction databases

IntActO16129.

Genome annotation databases

EnsemblCG13348. Drosophila melanogaster. [Contig view]
GeneID36547.
KEGGdme:Dmel_CG13348.
NMPDRfig|7227.3.peg.5148.

Organism-specific databases

FlyBaseFBgn0020766. Aats-phe.

Phylogenomic databases

HOGENOMO16129.

Enzyme and pathway databases

BioCycDMEL-XXX-02:DMEL-XXX-02-004529-MON.

Gene expression databases

GermOnlineCG13348. Drosophila melanogaster.

Family and domain databases

InterProIPR006195. aa-tRNA-synth_II.
IPR002319. Phe-tRNA-synth_IIc.
IPR004530. Phe-tRNA-synth_IIc_mito.
IPR005121. PheS_beta_Fdx_antiC_bd.
[Graphical view]
Gene3DG3DSA:3.30.70.380. Fdx_AntiC_bd. 1 hit.
PANTHERPTHR11538. tRNA-synt_2d. 1 hit.
PfamPF03147. FDX-ACB. 1 hit.
PF01409. tRNA-synt_2d. 2 hits.
[Graphical view]
TIGRFAMsTIGR00469. pheS_mito. 1 hit.
PROSITEPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]
ProDomO16129.
[Graphical view] [Entries sharing at least one domain]
BLOCKSSearch...

Other Resources

ProtoNetSearch...

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Entry information

Entry nameSYFM_DROME
AccessionPrimary (citable) accession number: O16129
Secondary accession number(s): Q9V6V8
Entry history
Integrated into UniProtKB/Swiss-Prot: May 10, 2004
Last sequence update: October 1, 2000
Last modified: July 22, 2008
This is version 59 of the entry and version 3 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