Q04Q66 (SYM_LEPBJ) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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:	LBJ_2519

Organism

Leptospira borgpetersenii serovar Hardjo-bovis (strain JB197) [Complete proteome] [HAMAP]

Taxonomic identifier

355277 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Spirochaetes › Spirochaetia › Spirochaetales › Leptospiraceae › Leptospira › Leptospira borgpetersenii › Leptospira borgpetersenii serovar Hardjo-bovis

Protein attributes

Sequence length	704 AA.
Sequence status	Complete.
Protein existence	Inferred 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	Homodimer 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. Contains 1 tRNA-binding domain.

Ontologies

Keywords
Biological process	Protein biosynthesis
Cellular component	Cytoplasm
Ligand	ATP-binding Metal-binding Nucleotide-binding RNA-binding Zinc tRNA-binding
Molecular function	Aminoacyl-tRNA synthetase Ligase
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	methionyl-tRNA aminoacylation Inferred from electronic annotation. Source: HAMAP
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP 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 tRNA binding Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 704	704	Methionine--tRNA ligase HAMAP-Rule MF_00098		PRO_0000331845
Regions
	Domain	603 – 704	102	tRNA-binding
	Motif	17 – 27	11	"HIGH" region HAMAP-Rule MF_00098
	Motif	348 – 352	5	"KMSKS" region HAMAP-Rule MF_00098
Sites
	Metal binding	148	1	Zinc By similarity
	Metal binding	151	1	Zinc By similarity
	Metal binding	161	1	Zinc By similarity
	Metal binding	164	1	Zinc By similarity
	Binding site	351	1	ATP By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q04Q66 [UniParc]. Last modified November 14, 2006. Version 1. Checksum: 2D59CFD57EA68102	FASTA	704	79,881
	10 20 30 40 50 60 MNSSSIQRKI LVTSALPYAN GPIHLGHVLE GIQTDIWVRF QKAIGNECYF FCADDTHGTP 70 80 90 100 110 120 VMLAARKEKI TPEQLIERVG QEHYTDLTSF GINYDNYDST HSKANQEISK DIYLKLKEKG 130 140 150 160 170 180 HISKRSIEQA YCEKDRMFLP DRFIKGTCPN CNSKNQYGDN CEVCGATYNP KDLIDSHCTL 190 200 210 220 230 240 CGTPPVVKNS DHIFFKLGNF HKKTEQSNVD FDLQSWIETS EAVSESEGVK KKLKEWFDAG 250 260 270 280 290 300 LQDWDISRDG PYFGFEIPSE KNKYFYVWLD APVGYMASSK NFFEKNFPNE PNKFDSFWKD 310 320 330 340 350 360 KNSEIVHFIG KDILYFHTLF WPAMLEGSGY RSPSKIHVHG FIGVNGEKMS KSRGTFIKAK 370 380 390 400 410 420 TFAKFLDAEH LRFYLAAKLG PGMDDIDLSF DDFVNKVNAD LVGNLINSVS RVSTTILDTL 430 440 450 460 470 480 DRTLGTVSEE GLALLEEILT QPVKTGTRDD SIQNIIKTAY EQRNYAKVMR EITRLGDRVN 490 500 510 520 530 540 RYVNDNAPWK LIKENPEKAR EIVTAVLNAS RFLAIYLYPV VPKISEQIYK LLNLKGSPEF 550 560 570 580 590 600 KDLDKSRILE KTKINPYEMI TKRVDEKAIK VMLEENKQSE HPKKEEIPKS SNKEEGIEIS 610 620 630 640 650 660 IEELSKVELR VGEIVEAKPV EGADKLVNVK VDLGELGIKN VFAGIKIAYQ PENLKGLKVV 670 680 690 700 VVANLKPRKM KFGISEAMLL ASGEGESLSL FVPHKDAKPG DRLK

References

[1]

"Genome reduction in Leptospira borgpetersenii reflects limited transmission potential." Bulach D.M., Zuerner R.L., Wilson P., Seemann T., McGrath A., Cullen P.A., Davis J., Johnson M., Kuczek E., Alt D.P., Peterson-Burch B., Coppel R.L., Rood J.I., Davies J.K., Adler B. Proc. Natl. Acad. Sci. U.S.A. 103:14560-14565(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: JB197.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000350 Genomic DNA. Translation: ABJ76954.1.
RefSeq	YP_801712.1. NC_008510.1.
3D structure databases
ProteinModelPortal	Q04Q66.
SMR	Q04Q66. Positions 141-166.
ModBase	Search...
Protein-protein interaction databases
STRING	355277.LBJ_2519.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ABJ76954; ABJ76954; LBJ_2519.
GeneID	4411632.
KEGG	lbj:LBJ_2519.
PATRIC	22361125. VBILepBor13265_3256.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0143.
HOGENOM	HOG000200400.
KO	K01874.
OMA	RMHGHEV.
ProtClustDB	PRK00133.
Enzyme and pathway databases
BioCyc	LBOR355277:GHYM-2488-MONOMER.
Family and domain databases
Gene3D	2.40.50.140. 1 hit. 3.40.50.620. 2 hits.
HAMAP	MF_00098. Met_tRNA_synth_type1.
InterPro	IPR001412. aa-tRNA-synth_I_CS. IPR023458. Met-tRNA_ligase_1. IPR014758. Met-tRNA_synth. 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. [Graphical view]
Pfam	PF09334. tRNA-synt_1g. 1 hit. PF01588. tRNA_bind. 1 hit. [Graphical view]
PRINTS	PR01041. TRNASYNTHMET.
SUPFAM	SSF50249. Nucleic_acid_OB. 1 hit. SSF47323. tRNAsyn_1a_bind. 1 hit.
TIGRFAMs	TIGR00398. metG. 1 hit.
PROSITE	PS00178. AA_TRNA_LIGASE_I. 1 hit. PS50886. TRBD. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SYM_LEPBJ

Accession

Primary (citable) accession number: Q04Q66

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 29, 2008
Last sequence update:	November 14, 2006
Last modified:	May 29, 2013
This is version 51 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program