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C6AFX7 (C6AFX7_BIFAS) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 30. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Methionine--tRNA ligase HAMAP-Rule MF_00098
EC=6.1.1.10 HAMAP-Rule MF_00098
Alternative name(s):
Methionyl-tRNA synthetase HAMAP-Rule MF_00098
Gene names
Name:metG HAMAP-Rule MF_00098
Ordered Locus Names:Balat_1542
OrganismBifidobacterium animalis subsp. lactis (strain DSM 10140 / JCM 10602 / LMG 18314) [Complete proteome] [HAMAP] EMBL ACS48450.1
Taxonomic identifier555970 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Bifidobacteriales › Bifidobacteriaceae › Bifidobacterium ›

Protein attributes

Sequence length619 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation By similarity. HAMAP-Rule MF_00098

Catalytic activity

ATP + L-methionine + tRNA(Met) = AMP + diphosphate + L-methionyl-tRNA(Met). HAMAP-Rule MF_00098 SAAS SAAS023458

Cofactor

Binds 1 zinc ion per subunit By similarity. HAMAP-Rule MF_00098

Subunit structure

Monomer By similarity. HAMAP-Rule MF_00098

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00098.

Sequence similarities

Belongs to the class-I aminoacyl-tRNA synthetase family. MetG type 1 subfamily. HAMAP-Rule MF_00098

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Motif7 – 1711"HIGH" region By similarity HAMAP-Rule MF_00098
Motif343 – 3475"KMSKS" region By similarity HAMAP-Rule MF_00098

Sites

Metal binding1391Zinc By similarity HAMAP-Rule MF_00098
Metal binding1421Zinc By similarity HAMAP-Rule MF_00098
Metal binding1521Zinc By similarity HAMAP-Rule MF_00098
Metal binding1551Zinc By similarity HAMAP-Rule MF_00098
Binding site3461ATP By similarity HAMAP-Rule MF_00098

Sequences

Sequence LengthMass (Da)Tools
C6AFX7 [UniParc].

Last modified September 1, 2009. Version 1.
Checksum: 1413198B79609508

FASTA61968,849
        10         20         30         40         50         60 
MVNVAWPYAN GPRHIGHVAG FGVPSDVYAR YQRMKGNDVL MVSGTDEHGT PILVEADKEG 

        70         80         90        100        110        120 
VTPQELANRY NRVIANDLCN LGLSYDLFTR TTTKNHEHVV QEMFRQCLAN GYIYKGTQKV 

       130        140        150        160        170        180 
AISPSTGRTL PDRYIEGECP ICHAQGARGD QCDNCGNELD PDELINPVSK INGETPIFEE 

       190        200        210        220        230        240 
TEHYFLDLPA LAEANLAWLK TRKGWRPNVL NFSIGLFKEV KPRAITRDID WGIPVPVPGW 

       250        260        270        280        290        300 
IDNPNKRLYV WFDAVIGYLS ASIEWARRSG DPEAWRAWWN DPATPGYYFM GKDNITFHSQ 

       310        320        330        340        350        360 
IWPSEMLAYN GEGSKGGEPG ELGRLDLPEQ VVASEFMTME GKKFSSSRGI VIYVKDILSR 

       370        380        390        400        410        420 
YPVDAVRYYI SAAGPESSDS DFTWAEFVRQ NNEVLAASWG NLVNRVANLI AKNFGQIPPI 

       430        440        450        460        470        480 
VEEKMTDEDR ALLAQSSAAF DTVGALIEQH RQKSALNDAM SLVGDINKYI SATEPWKIKD 

       490        500        510        520        530        540 
DPERLGTVLH VAAQAVSDAN HLLAPFLPHS SQKVWEALGG EGTFSPLPHI EEVNDLDDPE 

       550        560        570        580        590        600 
FTYPVITGKY VLGENVHPWK SEPIVVGAPV VKPTPIFAKI PPEAVDEELA RFDADLKARR 

       610 
EAEQARLDAE KAKLAAGEE

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References

[1]"Comparison of the complete genome sequences of Bifidobacterium animalis subsp. lactis DSM 10140 and Bl-04."
Barrangou R., Briczinski E.P., Traeger L.L., Loquasto J.R., Richards M., Horvath P., Coute-Monvoisin A.-C., Leyer G., Rendulic S., Steele J.L., Broadbent J.R., Oberg T., Dudley E.G., Schuster S., Romero D.A., Roberts R.F.
J. Bacteriol. 191:4144-4151(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 10140 / JCM 10602 / LMG 18314.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP001606 Genomic DNA. Translation: ACS48450.1.
RefSeqYP_002970512.1. NC_012815.1.

3D structure databases

ProteinModelPortalC6AFX7.
ModBaseSearch...

Protein-protein interaction databases

STRING555970.Balat_1542.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACS48450; ACS48450; Balat_1542.
GeneID8011162.
KEGGblt:Balat_1542.
PATRIC21112674. VBIBifAni93544_1527.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0143.
HOGENOMHOG000200402.
KOK01874.
OMASYYFMGK.
ProtClustDBPRK12268.

Enzyme and pathway databases

BioCycBANI555970:GJ22-1540-MONOMER.

Family and domain databases

Gene3D3.40.50.620. 2 hits.
HAMAPMF_00098. Met_tRNA_synth_type1.
InterProIPR023458. Met-tRNA_ligase_1.
IPR014758. Met-tRNA_synth.
IPR015413. Methionyl/Leucyl_tRNA_Synth.
IPR014729. Rossmann-like_a/b/a_fold.
IPR009080. tRNAsynth_1a_anticodon-bd.
IPR013155. V/L/I-tRNA-synth_anticodon-bd.
[Graphical view]
PfamPF08264. Anticodon_1. 1 hit.
PF09334. tRNA-synt_1g. 1 hit.
[Graphical view]
PRINTSPR01041. TRNASYNTHMET.
SUPFAMSSF47323. tRNAsyn_1a_bind. 1 hit.
TIGRFAMsTIGR00398. metG. 1 hit.
ProtoNetSearch...

Entry information

Entry nameC6AFX7_BIFAS
AccessionPrimary (citable) accession number: C6AFX7
Entry history
Integrated into UniProtKB/TrEMBL: September 1, 2009
Last sequence update: September 1, 2009
Last modified: May 1, 2013
This is version 30 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info