Phenylalanine--tRNA ligase beta subunit - Rhizobium loti (strain MAFF303099)

Preferred order of sections

Names and origin

Protein names

Recommended 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:	mll5053

Organism

Rhizobium loti (strain MAFF303099) (Mesorhizobium loti) [Complete proteome] [HAMAP]

Taxonomic identifier

266835 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Phyllobacteriaceae › Mesorhizobium ›

Protein attributes

Sequence length	802 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-Rule MF_00283
Cofactor	Binds 2 magnesium ions per tetramer By similarity.
Subunit structure	Tetramer of two alpha and two beta subunits By similarity.
Subcellular location	Cytoplasm By similarity.
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 process	Protein biosynthesis
Cellular component	Cytoplasm
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding RNA-binding tRNA-binding
Molecular function	Aminoacyl-tRNA synthetase Ligase
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	phenylalanyl-tRNA aminoacylation Inferred from electronic annotation. Source: HAMAP tRNA processing Inferred from electronic annotation. Source: InterPro
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: HAMAP magnesium ion binding Inferred from electronic annotation. Source: HAMAP phenylalanine-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 – 802

802

Phenylalanine--tRNA ligase beta subunit HAMAP-Rule MF_00283

PRO_0000126936

Regions

Domain

38 – 149

112

tRNA-binding

Domain

399 – 474

76

B5

Domain

708 – 801

94

FDX-ACB

Sites

Metal binding

452

1

Magnesium By similarity

Metal binding

458

1

Magnesium; via carbonyl oxygen By similarity

Metal binding

461

1

Magnesium By similarity

Metal binding

462

1

Magnesium By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

Q98CQ1 [UniParc].

Last modified October 1, 2001. Version 1.
Checksum: 32C01501A34D5241
Show »

FASTA

802

85,169

        10         20         30         40         50         60 
MKFTLSWLKD HLETDASLDE IVERLTSIGL EVEHVDDKSS LKPFVIAKVL TAVQHPDADR 

        70         80         90        100        110        120 
LRVLTVDTGD GKSPVQVVCG APNARAGLIG AFAAPGTYVP GIDVTLTVGK IRGVESHGMM 

       130        140        150        160        170        180 
CSERELELSD EHNGIIDLPA DAPVGTSFAS YAHLDDPVIE INLTPNRPDA TSVYGIARDL 

       190        200        210        220        230        240 
AASGLGTLKS AAVEKIPGKG ETPVKVVIEA PELCPGFALR LVRGVKNGPS PKWLQQRLIA 

       250        260        270        280        290        300 
IGLRPISALV DITNYVTFDR GRPLHVFDAR KVAGNLVVRR AHDGEKVMAL DGREYTLTPD 

       310        320        330        340        350        360 
MCAIADDNGV ESIAGVMGGE HSGCDENTTD VLIESALWDP ITTARTGRTL GIITDARYRF 

       370        380        390        400        410        420 
ERGVDPEFMV PGVELATRLV LDLCGGEPAE TEVVGYAGHK PKIVSFPISE VTRLTGIEVP 

       430        440        450        460        470        480 
KEESLDILSR LGFKPQGSSE VVDVALPSWR PDVDGKADLV EEVMRIHGVD NIAPQPLGAH 

       490        500        510        520        530        540 
DAVNSKILTT LQVRTRTAKR ALAVRGMMEA VTWSFIPAKH AELFGGGQTA LKLANPIAAD 

       550        560        570        580        590        600 
MSDMRPSLLP GLIAAAQRNA DKGIGDVALF EVSGTYEGDG ADQQRRVAAG VRRGTAKLDG 

       610        620        630        640        650        660 
SGRSWAGNSG PVGVFDAKAD AIAALEACGA PVERLQIEAG GPAWYHPGRS GTIKLGPKTV 

       670        680        690        700        710        720 
LGTFGEFHPK TMEGLDVSGP LCGFEVFVDA VPEPKAKPTK TKPKLELSAF QAVKRDFAFV 

       730        740        750        760        770        780 
VDKAVEAGTL VRAALAADKK LITAVSVFDI FEGASLGADK KSIAIEVSIQ PVEKTLTDED 

       790        800 
FEALAKRVVE NVGKQTGGVL RG

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References

[1]

"Complete genome structure of the nitrogen-fixing symbiotic bacterium Mesorhizobium loti."
Kaneko T., Nakamura Y., Sato S., Asamizu E., Kato T., Sasamoto S., Watanabe A., Idesawa K., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Mochizuki Y., Nakayama S.

Tabata S.
DNA Res. 7:331-338(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MAFF303099.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BA000012 Genomic DNA. Translation: BAB51570.1.
RefSeq	NP_105784.1. NC_002678.2.
3D structure databases
ProteinModelPortal	Q98CQ1.
ModBase	Search...
Protein-protein interaction databases
STRING	266835.mll5053.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	BAB51570; BAB51570; BAB51570.
GeneID	1228445.
KEGG	mlo:mll5053.
PATRIC	22482220. VBIMesLot2464_3992.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0072.
HOGENOM	HOG000292085.
KO	K01890.
OMA	MKFSEQW.
ProtClustDB	PRK00629.
Enzyme and pathway databases
BioCyc	MLOT266835:GJ9L-3932-MONOMER.
Family and domain databases
Gene3D	2.40.50.140. 1 hit. 3.30.56.20. 1 hit. 3.30.70.380. 1 hit. 3.50.40.10. 1 hit.
HAMAP	MF_00283. Phe_tRNA_synth_beta1.
InterPro	IPR005146. B3/B4_tRNA-bd. IPR009061. DNA-bd_dom_put. IPR012340. NA-bd_OB-fold. IPR004532. Phe-tRNA-ligase_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]
Pfam	PF03483. B3_4. 1 hit. PF03484. B5. 1 hit. PF03147. FDX-ACB. 1 hit. PF01588. tRNA_bind. 1 hit. [Graphical view]
SMART	SM00873. B3_4. 1 hit. SM00874. B5. 1 hit. SM00896. FDX-ACB. 1 hit. [Graphical view]
SUPFAM	SSF56037. B3_4. 1 hit. SSF54991. Fdx_AntiC_bd. 1 hit. SSF50249. Nucleic_acid_OB. 1 hit. SSF46955. Putativ_DNA_bind. 1 hit.
TIGRFAMs	TIGR00472. pheT_bact. 1 hit.
PROSITE	PS51483. B5. 1 hit. PS51447. FDX_ACB. 1 hit. PS50886. TRBD. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SYFB_RHILO

Accession

Primary (citable) accession number: Q98CQ1

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 30, 2003
Last sequence update:	October 1, 2001
Last modified:	May 1, 2013
This is version 64 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

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents