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Q5L7I8 (SYM_BACFN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 53. 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:BF4297
OrganismBacteroides fragilis (strain ATCC 25285 / NCTC 9343) [Complete proteome] [HAMAP]
Taxonomic identifier272559 [NCBI]
Taxonomic lineageBacteria › Bacteroidetes › Bacteroidia › Bacteroidales › Bacteroidaceae › Bacteroides

Protein attributes

Sequence length679 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 – 679679Methionine--tRNA ligase HAMAP MF_00098
PRO_0000331781

Regions

Domain578 – 679102tRNA-binding
Motif15 – 2511"HIGH" region HAMAP MF_00098
Motif332 – 3365"KMSKS" region HAMAP MF_00098

Sites

Metal binding1471Zinc By similarity
Metal binding1501Zinc By similarity
Metal binding1601Zinc By similarity
Metal binding1631Zinc By similarity
Binding site3351ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5L7I8 [UniParc].

Last modified June 21, 2005. Version 1.
Checksum: 41C069E08C59799B

FASTA67977,608
        10         20         30         40         50         60 
MEKNFKRTTV TSALPYANGP VHIGHLAGVY VPADIYVRYL RLKKEDVLFI GGSDEHGVPI 

        70         80         90        100        110        120 
TIRAKKEGIT PQDVVDRYHF LIKKSFEEFG ISFDVYSRTS SKTHHELASD FFKKLYEKGE 

       130        140        150        160        170        180 
FIEKTSEQYY DEEAHQFLAD RYITGECPHC HSEGAYGDQC EKCGTSLSPT DLINPKSAIS 

       190        200        210        220        230        240 
GSKPVMKETK HWYLPLDKHE TWLRQWILEE HKEWRPNVYG QCKSWLDMGL QPRAVSRDLD 

       250        260        270        280        290        300 
WGIPVPVEGA EGKVLYVWFD APIGYISNTK ELLPDSWETW WKDPETRLVH FIGKDNIVFH 

       310        320        330        340        350        360 
CIVFPAMLKA EGSYILPDNV PSNEFLNLEG DKISTSRNWA VWLHEYLEDF PGKQDVLRYV 

       370        380        390        400        410        420 
LTANAPETKD NDFTWKDFQA RNNNELVAVY GNFVNRAMVL TQKYFEGKVP AAGELIDYDK 

       430        440        450        460        470        480 
ETLKEFSDVK AEVEKLLNVF KFRDAQKEAM NLARIGNKYL ADTEPWKLAK TDMERVGTIL 

       490        500        510        520        530        540 
NISLQLVANL AIAFEPFLPF SSERLRQMLN MDSFDWAELG RNDLLPAGHQ LNKPELLFEK 

       550        560        570        580        590        600 
IEDATIEAQV QKLLDTKKAN EEANYKAKPI RANIEFDDFM KLDIRVGTVL ECQKVPKADK 

       610        620        630        640        650        660 
LLQFKIDDGL ETRTIVSGIA QHYKPEELVG KQVCFIANLA PRKLKGIVSE GMILSAENND 

       670 
GSLAVVMPGR EVKPGSEVK

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CR626927 Genomic DNA. Translation: CAH09964.1.
RefSeqYP_213853.1. NC_003228.3.

3D structure databases

HSSPHSSP built from PDB template 1MEA based on UniProtKB P00959.
ProteinModelPortalQ5L7I8.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ5L7I8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3289247.
GenomeReviewsGene locus BF4297 in contig CR626927_GR.
KEGGbfs:BF4297.
PATRIC21045469. VBIBacFra29119_4415.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0143.
HOGENOMHBG721667.
OMACGNQLDP.
ProtClustDBPRK00133.

Enzyme and pathway databases

BioCycBFRA272559:BF4297-MONOMER.

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_BACFN
AccessionPrimary (citable) accession number: Q5L7I8
Entry history
Integrated into UniProtKB/Swiss-Prot: April 29, 2008
Last sequence update: June 21, 2005
Last modified: January 25, 2012
This is version 53 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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