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Q9Z959 (SYM_CHLPN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 101. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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:CPn_0122, CP_0651, CpB0123
OrganismChlamydia pneumoniae (Chlamydophila pneumoniae) [Complete proteome] [HAMAP]
Taxonomic identifier83558 [NCBI]
Taxonomic lineageBacteria › Chlamydiae › Chlamydiales › Chlamydiaceae › Chlamydia/Chlamydophila group › Chlamydia

Protein attributes

Sequence length551 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

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.

Ontologies

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

Inferred from electronic annotation. Source: HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: HAMAP

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

methionine-tRNA ligase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 551551Methionine--tRNA ligase HAMAP-Rule MF_00098
PRO_0000139121

Regions

Motif12 – 2211"HIGH" region HAMAP-Rule MF_00098
Motif330 – 3345"KMSKS" region HAMAP-Rule MF_00098

Sites

Metal binding1441Zinc By similarity
Metal binding1471Zinc By similarity
Metal binding1571Zinc By similarity
Metal binding1601Zinc By similarity
Binding site3331ATP By similarity

Natural variations

Natural variant4231V → A in strain: CWL029 and TW-183.

Experimental info

Sequence conflict1711D → G in AAD18275. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9Z959 [UniParc].

Last modified January 11, 2001. Version 2.
Checksum: CAB2E383314E2B19

FASTA55163,453
        10         20         30         40         50         60 
MPQKVLITSA LPYANGPLHF GHIAGVYLPA DVYARFRRLL GDDVLYICGS DEFGIAITLN 

        70         80         90        100        110        120 
ADREGLGYQE YVDMYHKLHK DTFEKLGFAL DFFSRTTNPF HAELVQDFYS QLKASGLIEN 

       130        140        150        160        170        180 
RISEQLYSEQ EQRFLADRYV EGTCPRCGFD HARGDECQSC GADYEAIDLI DPKSKISGVE 

       190        200        210        220        230        240 
LVKKETEHSY FLLDRMKDAL LSFIQGCYLP DHVRKFVVDY IEHVRSRAIT RDLSWGIPVP 

       250        260        270        280        290        300 
DFPGKVFYVW FDAPIGYISG TMEWAASQGN PDEWKRFWLE DGVEYVQFIG KDNLPFHSVV 

       310        320        330        340        350        360 
FPAMELGQKL DYKKVDALVV SEFYLLEGRQ FSKSEGNYVD MDKFLSSYSL DKLRYVLAAT 

       370        380        390        400        410        420 
APETSDSEFT FLDFKTRCNS ELVGKFGNFI NRVLAFAEKN HYDKLSYHSV VLEDSDRAFL 

       430        440        450        460        470        480 
EEVRQLVRDA EKCYREYSLR KATSVIMSLA ALGNVYFNQQ APWKLLKEGT RERVEAILFC 

       490        500        510        520        530        540 
ACYCQKLLAL ISYPIIPESA VAIWEMISPK SLENCNLDTM YARDLWKEEI LDVINEEFHL 

       550 
KSPRLLFTTV E

« Hide

References

[1]"Comparative genomes of Chlamydia pneumoniae and C. trachomatis."
Kalman S., Mitchell W.P., Marathe R., Lammel C.J., Fan J., Hyman R.W., Olinger L., Grimwood J., Davis R.W., Stephens R.S.
Nat. Genet. 21:385-389(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CWL029.
[2]"Genome sequences of Chlamydia trachomatis MoPn and Chlamydia pneumoniae AR39."
Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F., White O., Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J., Bass S., Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C., Dodson R.J., Gwinn M.L. expand/collapse author list , Nelson W.C., DeBoy R.T., Kolonay J.F., McClarty G., Salzberg S.L., Eisen J.A., Fraser C.M.
Nucleic Acids Res. 28:1397-1406(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: AR39.
[3]"Comparison of whole genome sequences of Chlamydia pneumoniae J138 from Japan and CWL029 from USA."
Shirai M., Hirakawa H., Kimoto M., Tabuchi M., Kishi F., Ouchi K., Shiba T., Ishii K., Hattori M., Kuhara S., Nakazawa T.
Nucleic Acids Res. 28:2311-2314(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: J138.
[4]"The genome sequence of Chlamydia pneumoniae TW183 and comparison with other Chlamydia strains based on whole genome sequence analysis."
Geng M.M., Schuhmacher A., Muehldorfer I., Bensch K.W., Schaefer K.P., Schneider S., Pohl T., Essig A., Marre R., Melchers K.
Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: TW-183.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE001363 Genomic DNA. Translation: AAD18275.1.
AE002161 Genomic DNA. Translation: AAF38466.1.
BA000008 Genomic DNA. Translation: BAA98333.1.
AE009440 Genomic DNA. Translation: AAP98056.1.
PIRC86506.
H72117.
H81552.
RefSeqNP_224330.1. NC_000922.1.
NP_300182.1. NC_002491.1.
NP_445193.1. NC_002179.2.
NP_876399.1. NC_005043.1.

3D structure databases

ProteinModelPortalQ9Z959.
ModBaseSearch...

Protein-protein interaction databases

STRING115713.CPn0122.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAD18275; AAD18275; CPn_0122.
AAF38466; AAF38466; CP_0651.
AAP98056; AAP98056; CpB0123.
BAA98333; BAA98333; BAA98333.
GeneID1466806.
894667.
918910.
963233.
KEGGcpa:CP0651.
cpj:CPj0122.
cpn:CPn0122.
cpt:CpB0123.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0143.
HOGENOMHOG000200402.
KOK01874.
OMAQFSKSEG.
ProtClustDBPRK12268.

Enzyme and pathway databases

BioCycCPNE115711:GI7B-673-MONOMER.
CPNE115713:GHEY-126-MONOMER.
CPNE138677:GH8N-125-MONOMER.
CPNE182082:GH4N-126-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.
PROSITEPS00178. AA_TRNA_LIGASE_I. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYM_CHLPN
AccessionPrimary (citable) accession number: Q9Z959
Secondary accession number(s): Q9JRW1
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: January 11, 2001
Last modified: May 29, 2013
This is version 101 of the entry and version 2 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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