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Q9ZDB4 (SYFB_RICPR) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 76. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Phenylalanine--tRNA ligase beta chain

EC=6.1.1.20
Alternative name(s):
Phenylalanyl-tRNA synthetase beta chain
Short name=PheRS
Gene names
Name:pheT
Ordered Locus Names:RP418
OrganismRickettsia prowazekii (strain Madrid E)
Taxonomic identifier272947 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRickettsialesRickettsiaceaeRickettsieaeRickettsiatyphus group

Protein attributes

Sequence length815 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

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

Cofactor

Binds 2 magnesium ions per tetramer By similarity. HAMAP MF_00283

Subunit structure

Tetramer of two alpha and two beta chains By similarity.

Subcellular location

Cytoplasm HAMAP MF_00283.

Sequence similarities

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

Contains 1 B5 domain.

Contains 1 FDX-ACB domain.

Contains 1 tRNA-binding domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 815815Phenylalanine--tRNA ligase beta chain HAMAP MF_00283
PRO_0000126940

Regions

Domain39 – 148110tRNA-binding
Domain421 – 49676B5
Domain721 – 81494FDX-ACB

Sites

Metal binding4741Magnesium By similarity
Metal binding4801Magnesium; via carbonyl oxygen By similarity
Metal binding4831Magnesium By similarity
Metal binding4841Magnesium By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9ZDB4 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: F508E95333FCAE43

FASTA81591,585
        10         20         30         40         50         60 
MKFTLSWLKQ FLEISASVTE IAEALTDIGL EVEEVIDKSK ELQKFEVAYI RNIKPHPSAD 

        70         80         90        100        110        120 
KLKLCDVETK NGILQIVCGA SNVRADIKVV LANIGIEIPK GNLKIKESVI RGQKSYGMLC 

       130        140        150        160        170        180 
SEEELLLSSN SDGIIELPKD AVVGDNFTKY YGLDDPIFVI NVTPNRGDVL GVYGIARDLS 

       190        200        210        220        230        240 
AKGLGTLKEL ELSEIKSTFF SKIKLNVHDK EACPLFTFRE IRNLKNKPSP NWLQQLLKNV 

       250        260        270        280        290        300 
GIKTISSLVD VTNYISHSFG QPIHAYDADK IYGGISVDCY IRSDKVISCK NHEMATAVLQ 

       310        320        330        340        350        360 
FSNDSANFYA INGKGYLLTE NDLAIKDESG IQGLAGIIGG AKSSCNDSTT NVILEAACFN 

       370        380        390        400        410        420 
AKMVAASGRR LKIDTDARYR NERNIDRNFT EKALNIATNL ILSICGNCEV SEVVKVGEQE 

       430        440        450        460        470        480 
PQKKPLDFSV YFLEKITGIK LSIQEIEDIL NKLGFITDVK GDIIKVIAPS WRHDINILED 

       490        500        510        520        530        540 
IAEEIVRIYG YDKIESIKLP ELYQNNNLRE YKRISSFKRI LASKGYDEVV TNSFMSSEDA 

       550        560        570        580        590        600 
KLFAELKEGL FLLNPMSIEE NYMRPTVLPN LISIVSKNLA RDVKDMAFFE VGPSFVNLNI 

       610        620        630        640        650        660 
ESTYLTAIIS GAFNNKNPHS FGRNYDIFDI KGDLEQVIEY AGLSLDKCIV IDETVLPQYY 

       670        680        690        700        710        720 
HPTRAINIRL GKNLLGHFGQ IHPKILKYYD INQEIFAFEL NITNLPLIKA KFGKRDEFTV 

       730        740        750        760        770        780 
SDYQANFRDY SFIVDQDHKV GEIISYIKNF NKKLVKSVML FDIYSGDKLP EGKKSIAIKI 

       790        800        810 
KLQADDRTLS ETDLNSFSED LVASISQKFQ GILRE 

« Hide

References

[1]"The genome sequence of Rickettsia prowazekii and the origin of mitochondria."
Andersson S.G.E., Zomorodipour A., Andersson J.O., Sicheritz-Ponten T., Alsmark U.C.M., Podowski R.M., Naeslund A.K., Eriksson A.-S., Winkler H.H., Kurland C.G.
Nature 396:133-140(1998) [PubMed: 9823893] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Madrid E.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ235271 Genomic DNA. Translation: CAA14875.1.
PIRA71700.
RefSeqNP_220799.1. NC_000963.1.

3D structure databases

ProteinModelPortalQ9ZDB4.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID883323.
GenomeReviewsGene locus RP418 in contig AJ235269_GR.
KEGGrpr:RP418.
PATRIC17901617. VBIRicPro72556_0431.

Phylogenomic databases

HOGENOMHBG399638.
OMAADKLRVC.
ProtClustDBPRK00629.

Enzyme and pathway databases

BioCycRPRO272947:RP418-MONOMER.

Family and domain databases

HAMAPMF_00283. Phe_tRNA_synth_beta1.
[Tree]
InterProIPR005146. B3/B4_tRNA-bd.
IPR009061. DNA-bd_dom_put.
IPR012340. NA-bd_OB-fold.
IPR016027. NA-bd_OB-fold-like.
IPR004532. Phe-tRNA-synth_IIc_bsu_bac.
IPR020825. Phe-tRNA_synthase_B3/B4.
IPR005121. PheS_beta_Fdx_antiC-bd.
IPR002547. tRNA-bd_dom.
IPR005147. tRNA_synthase_B5-dom.
[Graphical view]
Gene3DG3DSA:3.50.40.10. B3_4. 1 hit.
G3DSA:3.30.56.20. B5. 1 hit.
G3DSA:3.30.70.380. Fdx_AntiC_bd. 1 hit.
G3DSA:2.40.50.140. OB_NA_bd_sub. 1 hit.
KOK01890.
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]
SUPFAMSSF56037. B3_4. 1 hit.
SSF54991. Fdx_AntiC_bd. 1 hit.
SSF50249. Nucleic_acid_OB. 1 hit.
SSF46955. Putativ_DNA_bind. 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_RICPR
AccessionPrimary (citable) accession number: Q9ZDB4
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 1, 1999
Last modified: January 25, 2012
This is version 76 of the entry and version 1 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

Rickettsia prowazekii

Rickettsia prowazekii (strain Madrid E): entries and gene names

SIMILARITY comments

Index of protein domains and families