Phenylalanine--tRNA ligase alpha chain - Mycobacterium tuberculosis

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P94984 (SYFA_MYCTU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 90. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Phenylalanine--tRNA ligase alpha chain
EC=6.1.1.20

Alternative name(s):
Phenylalanyl-tRNA synthetase alpha chain
Short name=PheRS

Gene names

Name:	pheS
Ordered Locus Names:	Rv1649, MT1687
ORF Names:	MTCY06H11.14

Organism

Mycobacterium tuberculosis

Taxonomic identifier

1773 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex

Protein attributes

Sequence length	341 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Catalytic activity	ATP + L-phenylalanine + tRNA(Phe) = AMP + diphosphate + L-phenylalanyl-tRNA(Phe). HAMAP MF_00281
Cofactor	Binds 2 magnesium ions per tetramer By similarity. HAMAP MF_00281
Subunit structure	Tetramer of two alpha and two beta chains By similarity.
Subcellular location	Cytoplasm HAMAP MF_00281.
Sequence similarities	Belongs to the class-II aminoacyl-tRNA synthetase family. Phe-tRNA synthetase alpha chain type 1 subfamily.

Ontologies

Keywords
Biological process	Protein biosynthesis
Cellular component	Cytoplasm
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Aminoacyl-tRNA synthetase Ligase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	growth Inferred from mutant phenotype. Source: MTBBASE phenylalanyl-tRNA aminoacylation Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from direct assay. Source: MTBBASE
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW phenylalanine-tRNA ligase activity Inferred from electronic annotation. Source: EC tRNA binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 341

341

Phenylalanine--tRNA ligase alpha chain HAMAP MF_00281

PRO_0000126733

Sites

Metal binding

259

Magnesium By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

P94984 [UniParc].

Last modified May 1, 1997. Version 1.
Checksum: C4C31DD8CAEE449B
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FASTA

341

37,371

        10         20         30         40         50         60 
MLSPEALTTA VDAAQQAIAL ADTLDVLARV KTEHLGDRSP LALARQALAV LPKEQRAEAG 

        70         80         90        100        110        120 
KRVNAARNAA QRSYDERLAT LRAERDAAVL VAEGIDVTLP STRVPAGARH PIIMLAEHVA 

       130        140        150        160        170        180 
DTFIAMGWEL AEGPEVETEQ FNFDALNFPA DHPARGEQDT FYIAPEDSRQ LLRTHTSPVQ 

       190        200        210        220        230        240 
IRTLLARELP VYIISIGRTF RTDELDATHT PIFHQVEGLA VDRGLSMAHL RGTLDAFARA 

       250        260        270        280        290        300 
EFGPSARTRI RPHFFPFTEP SAEVDVWFAN KIGGAAWVEW GGCGMVHPNV LRATGIDPDL 

       310        320        330        340 
YSGFAFGMGL ERTLQFRNGI PDMRDMVEGD VRFSLPFGVG A

« Hide

References

[1]	"Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence." Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K. Barrell B.G. Nature 393:537-544(1998) [PubMed: 9634230] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 25618 / H37Rv.
[2]	"Whole-genome comparison of Mycobacterium tuberculosis clinical and laboratory strains." Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O., Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K., Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L., Delcher A., Utterback T.R. Fraser C.M. J. Bacteriol. 184:5479-5490(2002) [PubMed: 12218036] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CDC 1551 / Oshkosh.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BX842577 Genomic DNA. Translation: CAB06643.1. AE000516 Genomic DNA. Translation: AAK45956.1.
PIR	D70620.
RefSeq	NP_336142.1. NC_002755.2.
3D structure databases
ProteinModelPortal	P94984.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBMYCT00000003442; EBMYCP00000003442; EBMYCG00000003440. EBMYCT00000072111; EBMYCP00000070170; EBMYCG00000072106.
GeneID	924351.
GenomeReviews	Gene locus MT1687 in contig AE000516_GR. Gene locus Rv1649 in contig AL123456_GR.
KEGG	mtc:MT1687. mtu:Rv1649.
PATRIC	18125472. VBIMycTub22151_1850.
TIGR	MT1687.
Organism-specific databases
TubercuList	Rv1649.
Phylogenomic databases
GeneTree	EBGT00050000016426.
HOGENOM	HBG284353.
OMA	FRASYFP.
PhylomeDB	P94984.
ProtClustDB	PRK00488.
Family and domain databases
HAMAP	MF_00281. Phe_tRNA_synth_alpha1. [Tree]
InterPro	IPR006195. aa-tRNA-synth_II. IPR004529. Phe-tRNA-synth_IIc_asu. IPR004188. Phe-tRNA_synth_II_N. IPR022911. Phe_tRNA_synth_alpha1_bac. IPR002319. Phenylalanyl-tRNA_Synthase. IPR010978. tRNA-bd_arm. [Graphical view]
KO	K01889.
Pfam	PF02912. Phe_tRNA-synt_N. 1 hit. PF01409. tRNA-synt_2d. 1 hit. [Graphical view]
SUPFAM	SSF46589. tRNA_binding_arm. 1 hit.
TIGRFAMs	TIGR00468. PheS. 1 hit.
PROSITE	PS50862. AA_TRNA_LIGASE_II. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SYFA_MYCTU

Accession

Primary (citable) accession number: P94984

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 8, 2000
Last sequence update:	May 1, 1997
Last modified:	January 25, 2012
This is version 90 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Family and domain databases

Entry information

Relevant documents