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Protein

Phenylalanine--tRNA ligase beta subunit

Gene

pheT

Organism
Shigella flexneri
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Catalytic activityi

ATP + L-phenylalanine + tRNA(Phe) = AMP + diphosphate + L-phenylalanyl-tRNA(Phe).UniRule annotation

Cofactori

Mg2+UniRule annotationNote: Binds 2 magnesium ions per tetramer.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi454 – 4541MagnesiumUniRule annotation
Metal bindingi460 – 4601Magnesium; via carbonyl oxygenUniRule annotation
Metal bindingi463 – 4631MagnesiumUniRule annotation
Metal bindingi464 – 4641MagnesiumUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Aminoacyl-tRNA synthetase, Ligase

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding, RNA-binding, tRNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Phenylalanine--tRNA ligase beta subunitUniRule annotation (EC:6.1.1.20UniRule annotation)
Alternative name(s):
Phenylalanyl-tRNA synthetase beta subunitUniRule annotation
Short name:
PheRSUniRule annotation
Gene namesi
Name:pheTUniRule annotation
Ordered Locus Names:SF1518, S1635
OrganismiShigella flexneri
Taxonomic identifieri623 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeShigella

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 795795Phenylalanine--tRNA ligase beta subunitPRO_0000126946Add
BLAST

Proteomic databases

PaxDbiQ83L36.
PRIDEiQ83L36.

Interactioni

Subunit structurei

Tetramer of two alpha and two beta subunits.UniRule annotation

Protein-protein interaction databases

STRINGi198214.SF1518.

Structurei

3D structure databases

ProteinModelPortaliQ83L36.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini39 – 148110tRNA-bindingUniRule annotationAdd
BLAST
Domaini401 – 47676B5UniRule annotationAdd
BLAST
Domaini701 – 79494FDX-ACBUniRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily.UniRule annotation
Contains 1 B5 domain.UniRule annotation
Contains 1 FDX-ACB domain.UniRule annotation
Contains 1 tRNA-binding domain.UniRule annotation

Phylogenomic databases

eggNOGiCOG0073.
HOGENOMiHOG000292085.
KOiK01890.
OMAiRQYGLHT.
OrthoDBiEOG6CCH1J.

Family and domain databases

Gene3Di2.40.50.140. 1 hit.
3.30.56.20. 1 hit.
3.30.70.380. 1 hit.
3.50.40.10. 1 hit.
HAMAPiMF_00283. Phe_tRNA_synth_beta1.
InterProiIPR005146. 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]
PfamiPF03483. B3_4. 1 hit.
PF03484. B5. 1 hit.
PF03147. FDX-ACB. 1 hit.
PF01588. tRNA_bind. 1 hit.
[Graphical view]
SMARTiSM00873. B3_4. 1 hit.
SM00874. B5. 1 hit.
SM00896. FDX-ACB. 1 hit.
[Graphical view]
SUPFAMiSSF46955. SSF46955. 1 hit.
SSF50249. SSF50249. 1 hit.
SSF54991. SSF54991. 1 hit.
SSF56037. SSF56037. 1 hit.
TIGRFAMsiTIGR00472. pheT_bact. 1 hit.
PROSITEiPS51483. B5. 1 hit.
PS51447. FDX_ACB. 1 hit.
PS50886. TRBD. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q83L36-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKFSELWLRE WVNPAIDSDT LANQITMAGL EVDGVEPVAG SFHGVVVGEV
60 70 80 90 100
VECAQHPNAD KLRVTKVNVG GDRLLDIVCG APNCRQGLRV AVATIGAVLP
110 120 130 140 150
GDFKIKAAKL RGEPSEGMLC SFSELGISDD HSGIIELPAD APIGTDIREY
160 170 180 190 200
LKLDDNTIEI SVTPNRADCL GIIGVARDVA VLNQLPLVEP EIVPVGATID
210 220 230 240 250
DTLPITVEAP EACPRYLGRV VKGINVKAPT PLWMKEKLRR CGIRSIDAVV
260 270 280 290 300
DVTNYVLLEL GQPMHAFDKD RIEGGIVVRM AKEGETLVLL DGTEAKLNAD
310 320 330 340 350
TLVIADHNKA LAMGGIFGGE HSGVNDETQN VLLECAFFSP LSITGRARRH
360 370 380 390 400
GLHTDASHRY ERGVDPVLQH KAMERATRLL IDICGGEAGP VIDITNEATL
410 420 430 440 450
PKRATITLRR SKLDRLIGHH IADEQVTDIL RRLGCEVTEG KDEWQAVAPS
460 470 480 490 500
WRFDMEIEED LVEEVARVYG YNNIPDEPVQ ASLIMGTHRE ADLSLKRVKT
510 520 530 540 550
LLNDKGYQEV ITYSFVDPKV QQMIHPGVEA LLLASPISVE MSAMRLSLWT
560 570 580 590 600
GLLATVVYNQ NRQQNRVRIF ESGLRFVPDT QAPLGIRQDL MLAGVICGNR
610 620 630 640 650
YEEHWNLAKE TVDFYDLKGD LESVLDLTGK LNEVEFRAEA NPALHPGQSA
660 670 680 690 700
AIYLKGERIG FVGVVHPELE RKLDLNGRTL VFELEWNKLA DRVVPQAREI
710 720 730 740 750
SRFPANRRDI AVVVAENVPA ADILSECKKV GVNQVVGVNL FDVYRGKGVA
760 770 780 790
EGYKSLAISL ILQDTSRTLE EEEIAATVAK CVEALKERFQ ASLRD
Length:795
Mass (Da):87,411
Last modified:June 1, 2003 - v1
Checksum:i7F59E6BE805AB0A2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE005674 Genomic DNA. Translation: AAN43108.1.
AE014073 Genomic DNA. Translation: AAP16998.1.
RefSeqiNP_707401.1. NC_004337.2.
WP_000672419.1. NZ_JMRK01000097.1.

Genome annotation databases

EnsemblBacteriaiAAN43108; AAN43108; SF1518.
AAP16998; AAP16998; S1635.
GeneIDi1024717.
KEGGisfl:SF1518.
sfx:S1635.
PATRICi18704628. VBIShiFle31049_1816.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE005674 Genomic DNA. Translation: AAN43108.1.
AE014073 Genomic DNA. Translation: AAP16998.1.
RefSeqiNP_707401.1. NC_004337.2.
WP_000672419.1. NZ_JMRK01000097.1.

3D structure databases

ProteinModelPortaliQ83L36.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi198214.SF1518.

Proteomic databases

PaxDbiQ83L36.
PRIDEiQ83L36.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAN43108; AAN43108; SF1518.
AAP16998; AAP16998; S1635.
GeneIDi1024717.
KEGGisfl:SF1518.
sfx:S1635.
PATRICi18704628. VBIShiFle31049_1816.

Phylogenomic databases

eggNOGiCOG0073.
HOGENOMiHOG000292085.
KOiK01890.
OMAiRQYGLHT.
OrthoDBiEOG6CCH1J.

Family and domain databases

Gene3Di2.40.50.140. 1 hit.
3.30.56.20. 1 hit.
3.30.70.380. 1 hit.
3.50.40.10. 1 hit.
HAMAPiMF_00283. Phe_tRNA_synth_beta1.
InterProiIPR005146. 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]
PfamiPF03483. B3_4. 1 hit.
PF03484. B5. 1 hit.
PF03147. FDX-ACB. 1 hit.
PF01588. tRNA_bind. 1 hit.
[Graphical view]
SMARTiSM00873. B3_4. 1 hit.
SM00874. B5. 1 hit.
SM00896. FDX-ACB. 1 hit.
[Graphical view]
SUPFAMiSSF46955. SSF46955. 1 hit.
SSF50249. SSF50249. 1 hit.
SSF54991. SSF54991. 1 hit.
SSF56037. SSF56037. 1 hit.
TIGRFAMsiTIGR00472. pheT_bact. 1 hit.
PROSITEiPS51483. B5. 1 hit.
PS51447. FDX_ACB. 1 hit.
PS50886. TRBD. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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.
    , 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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 700930 / 2457T / Serotype 2a.

Entry informationi

Entry nameiSYFB_SHIFL
AccessioniPrimary (citable) accession number: Q83L36
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 16, 2004
Last sequence update: June 1, 2003
Last modified: June 24, 2015
This is version 87 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Documents

  1. Aminoacyl-tRNA synthetases
    List of aminoacyl-tRNA synthetase entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.