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A7FQA4 (A7FQA4_CLOB1) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 51. 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_01228
EC=6.1.1.10 HAMAP-Rule MF_01228
Alternative name(s):
Methionyl-tRNA synthetase HAMAP-Rule MF_01228
Gene names
Name:metG HAMAP-Rule MF_01228 EMBL ABS32964.1
Ordered Locus Names:CLB_0111
OrganismClostridium botulinum (strain ATCC 19397 / Type A) [Complete proteome] [HAMAP]
Taxonomic identifier441770 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Clostridia › Clostridiales › Clostridiaceae › Clostridium ›

Protein attributes

Sequence length645 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_01228 SAAS SAAS002547

Catalytic activity

ATP + L-methionine + tRNA(Met) = AMP + diphosphate + L-methionyl-tRNA(Met). HAMAP-Rule MF_01228 SAAS SAAS002547

Cofactor

Binds 1 zinc ion per subunit By similarity. HAMAP-Rule MF_01228

Subunit structure

Homodimer By similarity. SAAS SAAS002547

Monomer By similarity. HAMAP-Rule MF_01228

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_01228 SAAS SAAS014758.

Sequence similarities

Belongs to the class-I aminoacyl-tRNA synthetase family. MetG type 2A subfamily. HAMAP-Rule MF_01228

Contains 1 tRNA-binding domain. HAMAP-Rule MF_01228 SAAS SAAS002547

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Domain543 – 645103tRNA-binding By similarity HAMAP-Rule MF_01228
Motif13 – 2311"HIGH" region By similarity HAMAP-Rule MF_01228
Motif298 – 3025"KMSKS" region By similarity HAMAP-Rule MF_01228

Sites

Metal binding1281Zinc By similarity HAMAP-Rule MF_01228
Metal binding1311Zinc By similarity HAMAP-Rule MF_01228
Metal binding1451Zinc By similarity HAMAP-Rule MF_01228
Metal binding1481Zinc By similarity HAMAP-Rule MF_01228

Sequences

Sequence LengthMass (Da)Tools
A7FQA4 [UniParc].

Last modified September 11, 2007. Version 1.
Checksum: 10E2C0E797C82C02

FASTA64573,675
        10         20         30         40         50         60 
MSKGTYYVTT PIYYPSAKLH IGNTYTTVAA DTLARFKRLT GYDVMFLTGT DEHGQKIQRL 

        70         80         90        100        110        120 
AEAKKVTPKV YVDEIVAGIK ELWKMMNIDY DKFIRTTDEY HVELVQKIFK TLYDKGDIYK 

       130        140        150        160        170        180 
SEYSGWYCTP CESFWTETQL EDGKCPDCGR SVEKAKEEAY FFKMSKYAPK LIEYIESHPE 

       190        200        210        220        230        240 
FIQPESRKNE MLNNFLKPGL QDLCVSRTSF DWGIPVTFDE KHVIYVWIDA LANYITALGY 

       250        260        270        280        290        300 
STEKDELYKK YWPADVHLVG KDILRFHTIY WPIMLMALDI PLPKQVFGHG WLLVDGGKMS 

       310        320        330        340        350        360 
KSKGNVVDPV VLVNHFGTDP VRYYLLREIP FGADGIFNNE IFIKKINSDL ANDLGNLLSR 

       370        380        390        400        410        420 
TVAMIEKYFD GEIPAGNCKE DIDEELIKLA LETPKKVEEN MEKLRIPEAL EEIWTFIGRA 

       430        440        450        460        470        480 
NKYIDETTPW ILAKDESKKE RLGTVLYNLA ESLRIISVCI SAFIPETSIK INEQINADVL 

       490        500        510        520        530        540 
NWDSLSKFNG TKVGTKVKKG EAIFPRIDVE KKIEELNKLK EEQLKQNKAK NIAPIKEEIT 

       550        560        570        580        590        600 
IDDFEKIDLR VAKVLECEPI KGAKKLLKLK VSLGGEERQV VSGIAKYYKP EDLIGKKVVL 

       610        620        630        640 
VANLKPVKLR GELSQGMILA ASTEDDSELF VASIDGDIEE GNIVR

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References

[1]"Analysis of the Neurotoxin Complex Genes in Clostridium botulinum A1-A4 and B1 Strains: BoNT/A3, /Ba4 and /B1 Clusters Are Located within Plasmids."
Smith T.J., Hill K.K., Foley B.T., Detter J.C., Munk A.C., Bruce D.C., Doggett N.A., Smith L.A., Marks J.D., Xie G., Brettin T.S.
PLoS ONE 2:E1271-E1271(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 19397 / Type A.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000726 Genomic DNA. Translation: ABS32964.1.
RefSeqYP_001382482.1. NC_009697.1.

3D structure databases

ProteinModelPortalA7FQA4.
SMRA7FQA4. Positions 539-641.
ModBaseSearch...

Protein-protein interaction databases

STRING441770.CLB_0111.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABS32964; ABS32964; CLB_0111.
GeneID5395346.
KEGGcba:CLB_0111.
PATRIC19354849. VBICloBot110701_0073.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0143.
HOGENOMHOG000200401.
KOK01874.
OMARINYDLA.
ProtClustDBPRK12267.

Enzyme and pathway databases

BioCycCBOT441770:GH1E-171-MONOMER.

Family and domain databases

Gene3D2.40.50.140. 1 hit.
3.40.50.620. 2 hits.
HAMAPMF_01228. Met_tRNA_synth_type2.
InterProIPR001412. aa-tRNA-synth_I_CS.
IPR004495. Met-tRNA-synth_Ia_bsu_C.
IPR014758. Met-tRNA_synth.
IPR023457. Met-tRNA_synth_2.
IPR015413. Methionyl/Leucyl_tRNA_Synth.
IPR012340. NA-bd_OB-fold.
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]
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 nameA7FQA4_CLOB1
AccessionPrimary (citable) accession number: A7FQA4
Entry history
Integrated into UniProtKB/TrEMBL: September 11, 2007
Last sequence update: September 11, 2007
Last modified: May 1, 2013
This is version 51 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