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Q83L36 (SYFB_SHIFL) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 80. 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

Names and origin

Protein namesRecommended name:
Phenylalanine--tRNA ligase beta subunit

EC=6.1.1.20
Alternative name(s):
Phenylalanyl-tRNA synthetase beta subunit
Short name=PheRS
Gene names
Name:pheT
Ordered Locus Names:SF1518, S1635
OrganismShigella flexneri [Complete proteome] [HAMAP]
Taxonomic identifier623 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeShigella

Protein attributes

Sequence length795 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

ATP + L-phenylalanine + tRNA(Phe) = AMP + diphosphate + L-phenylalanyl-tRNA(Phe). HAMAP-Rule MF_00283

Cofactor

Binds 2 magnesium ions per tetramer By similarity. HAMAP-Rule MF_00283

Subunit structure

Tetramer of two alpha and two beta subunits By similarity.

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00283.

Sequence similarities

Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily.

Contains 1 B5 domain.

Contains 1 FDX-ACB domain.

Contains 1 tRNA-binding domain.

Ontologies

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

Inferred from electronic annotation. Source: UniProtKB-HAMAP

tRNA processing

Inferred from electronic annotation. Source: InterPro

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

magnesium ion binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

phenylalanine-tRNA ligase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

tRNA binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 795795Phenylalanine--tRNA ligase beta subunit HAMAP-Rule MF_00283
PRO_0000126946

Regions

Domain39 – 148110tRNA-binding
Domain401 – 47676B5
Domain701 – 79494FDX-ACB

Sites

Metal binding4541Magnesium By similarity
Metal binding4601Magnesium; via carbonyl oxygen By similarity
Metal binding4631Magnesium By similarity
Metal binding4641Magnesium By similarity

Sequences

Sequence LengthMass (Da)Tools
Q83L36 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 7F59E6BE805AB0A2

FASTA79587,411
        10         20         30         40         50         60 
MKFSELWLRE WVNPAIDSDT LANQITMAGL EVDGVEPVAG SFHGVVVGEV VECAQHPNAD 

        70         80         90        100        110        120 
KLRVTKVNVG GDRLLDIVCG APNCRQGLRV AVATIGAVLP GDFKIKAAKL RGEPSEGMLC 

       130        140        150        160        170        180 
SFSELGISDD HSGIIELPAD APIGTDIREY LKLDDNTIEI SVTPNRADCL GIIGVARDVA 

       190        200        210        220        230        240 
VLNQLPLVEP EIVPVGATID DTLPITVEAP EACPRYLGRV VKGINVKAPT PLWMKEKLRR 

       250        260        270        280        290        300 
CGIRSIDAVV DVTNYVLLEL GQPMHAFDKD RIEGGIVVRM AKEGETLVLL DGTEAKLNAD 

       310        320        330        340        350        360 
TLVIADHNKA LAMGGIFGGE HSGVNDETQN VLLECAFFSP LSITGRARRH GLHTDASHRY 

       370        380        390        400        410        420 
ERGVDPVLQH KAMERATRLL IDICGGEAGP VIDITNEATL PKRATITLRR SKLDRLIGHH 

       430        440        450        460        470        480 
IADEQVTDIL RRLGCEVTEG KDEWQAVAPS WRFDMEIEED LVEEVARVYG YNNIPDEPVQ 

       490        500        510        520        530        540 
ASLIMGTHRE ADLSLKRVKT LLNDKGYQEV ITYSFVDPKV QQMIHPGVEA LLLASPISVE 

       550        560        570        580        590        600 
MSAMRLSLWT GLLATVVYNQ NRQQNRVRIF ESGLRFVPDT QAPLGIRQDL MLAGVICGNR 

       610        620        630        640        650        660 
YEEHWNLAKE TVDFYDLKGD LESVLDLTGK LNEVEFRAEA NPALHPGQSA AIYLKGERIG 

       670        680        690        700        710        720 
FVGVVHPELE RKLDLNGRTL VFELEWNKLA DRVVPQAREI SRFPANRRDI AVVVAENVPA 

       730        740        750        760        770        780 
ADILSECKKV GVNQVVGVNL FDVYRGKGVA EGYKSLAISL ILQDTSRTLE EEEIAATVAK 

       790 
CVEALKERFQ ASLRD 

« Hide

References

[1]"Genome sequence of Shigella flexneri 2a: insights into pathogenicity through comparison with genomes of Escherichia coli K12 and O157."
Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J., Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L., Xue Y. expand/collapse author list , Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H., Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.
Nucleic Acids Res. 30:4432-4441(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 301 / Serotype 2a.
[2]"Complete genome sequence and comparative genomics of Shigella flexneri serotype 2a strain 2457T."
Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G., Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T., Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.
Infect. Immun. 71:2775-2786(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700930 / 2457T / Serotype 2a.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE005674 Genomic DNA. Translation: AAN43108.1.
AE014073 Genomic DNA. Translation: AAP16998.1.
RefSeqNP_707401.1. NC_004337.2.
NP_837191.1. NC_004741.1.

3D structure databases

ProteinModelPortalQ83L36.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING198214.SF1518.

Proteomic databases

PaxDbQ83L36.
PRIDEQ83L36.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAN43108; AAN43108; SF1518.
AAP16998; AAP16998; S1635.
GeneID1024717.
1079642.
KEGGsfl:SF1518.
sfx:S1635.
PATRIC18704628. VBIShiFle31049_1816.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0073.
HOGENOMHOG000292085.
KOK01890.
OMAMKFSEQW.
OrthoDBEOG6CCH1J.
ProtClustDBPRK00629.

Family and domain databases

Gene3D2.40.50.140. 1 hit.
3.30.56.20. 1 hit.
3.30.70.380. 1 hit.
3.50.40.10. 1 hit.
HAMAPMF_00283. Phe_tRNA_synth_beta1.
InterProIPR005146. B3/B4_tRNA-bd.
IPR009061. DNA-bd_dom_put.
IPR012340. NA-bd_OB-fold.
IPR004532. Phe-tRNA-ligase_IIc_bsu.
IPR020825. Phe-tRNA_synthase_B3/B4.
IPR005121. PheS_beta_Fdx_antiC-bd.
IPR002547. tRNA-bd_dom.
IPR005147. tRNA_synthase_B5-dom.
[Graphical view]
PfamPF03483. B3_4. 1 hit.
PF03484. B5. 1 hit.
PF03147. FDX-ACB. 1 hit.
PF01588. tRNA_bind. 1 hit.
[Graphical view]
SMARTSM00873. B3_4. 1 hit.
SM00874. B5. 1 hit.
SM00896. FDX-ACB. 1 hit.
[Graphical view]
SUPFAMSSF46955. SSF46955. 1 hit.
SSF50249. SSF50249. 1 hit.
SSF54991. SSF54991. 1 hit.
SSF56037. SSF56037. 1 hit.
TIGRFAMsTIGR00472. pheT_bact. 1 hit.
PROSITEPS51483. B5. 1 hit.
PS51447. FDX_ACB. 1 hit.
PS50886. TRBD. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYFB_SHIFL
AccessionPrimary (citable) accession number: Q83L36
Entry history
Integrated into UniProtKB/Swiss-Prot: January 16, 2004
Last sequence update: June 1, 2003
Last modified: February 19, 2014
This is version 80 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries