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B7J2F0 (SYM_BORBZ) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 27. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Methionine--tRNA ligase
EC=6.1.1.10
Alternative name(s):
Methionyl-tRNA synthetase
Short name=MetRS
Gene names
Name:metG
Ordered Locus Names:BbuZS7_0600
OrganismBorrelia burgdorferi (strain ZS7) [Complete proteome] [HAMAP]
Taxonomic identifier445985 [NCBI]
Taxonomic lineageBacteria › Spirochaetes › Spirochaetales › Spirochaetaceae › Borrelia › Borrelia burgdorferi group

Protein attributes

Sequence length734 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 MF_00098

Catalytic activity

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

Cofactor

Binds 1 zinc ion per subunit By similarity. HAMAP MF_00098

Subunit structure

Homodimer By similarity. HAMAP MF_00098

Subcellular location

Cytoplasm By similarity HAMAP MF_00098.

Sequence similarities

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

Contains 1 tRNA-binding domain.

Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Metal-binding
Nucleotide-binding
RNA-binding
Zinc
tRNA-binding
   Molecular functionAminoacyl-tRNA synthetase
Ligase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processmethionyl-tRNA aminoacylation

Inferred from electronic annotation. Source: InterPro

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

methionine-tRNA ligase activity

Inferred from electronic annotation. Source: EC

tRNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 734734Methionine--tRNA ligase HAMAP MF_00098
PRO_1000199280

Regions

Domain570 – 675106tRNA-binding
Motif12 – 2211"HIGH" region HAMAP MF_00098
Motif330 – 3345"KMSKS" region HAMAP MF_00098

Sites

Metal binding1431Zinc By similarity
Metal binding1461Zinc By similarity
Metal binding1551Zinc By similarity
Metal binding1581Zinc By similarity
Binding site3331ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
B7J2F0 [UniParc].

Last modified February 10, 2009. Version 1.
Checksum: 8A3EC6ED44755216

FASTA73485,198
        10         20         30         40         50         60 
MKKMNLVTAA LPYVNNIPHL GNLVQVLSAD AFARYSKMSG IKTLYVCGTD EYGTATETKA 

        70         80         90        100        110        120 
LIENTTPLEL CNKYYEIHKS IYKWFNIEFD IFGRTTNKNH QDIVQNFFLQ LEKNGYIKER 

       130        140        150        160        170        180 
ETEQFFCNKD SMFLADRYVI GECPECQSMA KGDQCDNCSK LLNPTDLINP KCIICKNKPI 

       190        200        210        220        230        240 
LKKTNHLYLD LPKIKTKLEK WIKNPDTSKN WNTNALKMTK AFLRDGLKER AITRDLKWGI 

       250        260        270        280        290        300 
PVPKKGFENK VFYVWFDAPI GYISITKNII KNWESWWKNN DQVNLVQFIG KDNILFHTII 

       310        320        330        340        350        360 
FPCIEIGSEE NWTILNQLSS SEYLNYENLK FSKSEGTGIF GNDAITTGIP SDIWRFYIYY 

       370        380        390        400        410        420 
NRPEKSDFQF MWQDLMERVN TELIDNFSNL VNRVLTFQRK FFGDVIETIE IQNKFWKQIT 

       430        440        450        460        470        480 
PKYNKILNLF KKTELKSALK EILKISSLGN KIFQDNEPWK RKNNSPQETK ELISNLIYLI 

       490        500        510        520        530        540 
RDLSILMMPF IPETSKKIQQ FFGNSYQFST KILGTKSGIK KIEFTEILFN KLEQKKINNL 

       550        560        570        580        590        600 
KLKYSGDKNM KENEQAENLP IAKEQPENLF REKVLLRVVK INKIERNPEA KNLFILKLDD 

       610        620        630        640        650        660 
GTNKDKQIVS GLEGYYTEEE LLGKHIIIVD NLKPAKFRGI KSEGMLIAAE DKNKNFKVII 

       670        680        690        700        710        720 
VEDSIQNPIA GERIILENDQ NKDLACPPKI DINKFLKANI VAENGELKIN GINLILENSK 

       730 
NKILSKDIPN GTVC

« Hide

References

[1]"Whole-genome sequences of thirteen isolates of Borrelia burgdorferi."
Schutzer S.E., Fraser-Liggett C.M., Casjens S.R., Qiu W.G., Dunn J.J., Mongodin E.F., Luft B.J.
J. Bacteriol. 193:1018-1020(2011) [PubMed: 20935092] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ZS7.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP001205 Genomic DNA. Translation: ACK74552.1.
RefSeqYP_002375095.1. NC_011728.1.

3D structure databases

ProteinModelPortalB7J2F0.
ModBaseSearch...

Protein-protein interaction databases

STRINGB7J2F0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBORT00000002987; EBBORP00000002726; EBBORG00000002987.
GeneID7106326.
GenomeReviewsGene locus BbuZS7_0600 in contig CP001205_GR.
KEGGbbz:BbuZS7_0600.
PATRIC20560627. VBIBorBur54821_0718.

Organism-specific databases

CMRSearch...

Phylogenomic databases

GeneTreeEBGT00050000007495.
HOGENOMHBG721667.
OMAEEKTRNV.
ProtClustDBPRK00133.

Family and domain databases

HAMAPMF_00098. Met_tRNA_synth_type1.
[Tree]
InterProIPR015413. aa-tRNA-synt_I.
IPR001412. aa-tRNA-synth_I_CS.
IPR004495. Met-tRNA-synth_Ia_bsu_C.
IPR014758. Met-tRNA_synth.
IPR023458. Met-tRNA_synth_1.
IPR012340. NA-bd_OB-fold.
IPR016027. NA-bd_OB-fold-like.
IPR014729. Rossmann-like_a/b/a_fold.
IPR002547. tRNA-bd_dom.
IPR009080. tRNAsynth_1a_anticodon-bd.
IPR013155. V/L/I-tRNA-synth_anticodon-bd.
[Graphical view]
Gene3DG3DSA:2.40.50.140. OB_NA_bd_sub. 1 hit.
G3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 2 hits.
KOK01874.
PfamPF08264. Anticodon_1. 1 hit.
PF09334. tRNA-synt_1g. 1 hit.
PF01588. tRNA_bind. 1 hit.
[Graphical view]
PRINTSPR01041. TRNASYNTHMET.
SUPFAMSSF50249. Nucleic_acid_OB. 1 hit.
SSF47323. tRNAsyn_1a_bind. 1 hit.
TIGRFAMsTIGR00398. MetG. 1 hit.
TIGR00399. MetG_C_term. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
PS50886. TRBD. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYM_BORBZ
AccessionPrimary (citable) accession number: B7J2F0
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: February 10, 2009
Last modified: January 25, 2012
This is version 27 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

SIMILARITY comments

Index of protein domains and families

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