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D8NNP8 (D8NNP8_RALSL) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 21. Feed History...

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

Protein namesRecommended name:
Proline--tRNA ligase HAMAP-Rule MF_01569
EC=6.1.1.15 HAMAP-Rule MF_01569
Alternative name(s):
Prolyl-tRNA synthetase HAMAP-Rule MF_01569
Gene names
Name:proS HAMAP-Rule MF_01569 EMBL CBJ41948.1
ORF Names:RCFBP_10644 EMBL CBJ41948.1
OrganismRalstonia solanacearum CFBP2957 EMBL CBJ41948.1
Taxonomic identifier859656 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Ralstonia ›

Protein attributes

Sequence length574 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the attachment of proline to tRNA(Pro) in a two-step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro). As ProRS can inadvertently accommodate and process non-cognate amino acids such as alanine and cysteine, to avoid such errors it has two additional distinct editing activities against alanine. One activity is designated as 'pretransfer' editing and involves the tRNA(Pro)-independent hydrolysis of activated Ala-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Ala-tRNA(Pro). The misacylated Cys-tRNA(Pro) is not edited by ProRS By similarity. HAMAP-Rule MF_01569 SAAS SAAS023717

Catalytic activity

ATP + L-proline + tRNA(Pro) = AMP + diphosphate + L-prolyl-tRNA(Pro). HAMAP-Rule MF_01569 SAAS SAAS023717

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_01569 SAAS SAAS023717

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_01569 SAAS SAAS023717.

Domain

Consists of three domains: the N-terminal catalytic domain, the editing domain and the C-terminal anticodon-binding domain By similarity. HAMAP-Rule MF_01569

Sequence similarities

Belongs to the class-II aminoacyl-tRNA synthetase family. ProS type 1 subfamily. HAMAP-Rule MF_01569

Sequences

Sequence LengthMass (Da)Tools
D8NNP8 [UniParc].

Last modified October 5, 2010. Version 1.
Checksum: ABF0E59A6D2135E3

FASTA57463,060
        10         20         30         40         50         60 
MKASQFFIST LKEAPADAEI VSHKLMMRAG MIKKLGAGIY TYMPVGLRAI RKVEQIVREE 

        70         80         90        100        110        120 
MNAAGAVEML MPVVQPGELW QETGRWDKMG EELMRVKDRH ERDLVIQPTS EEVVTDIART 

       130        140        150        160        170        180 
EIRSYKQMPV NFYQIQTKFR DERRPRFGIM RGREFTMKDA YSFDRDVEGM KVSYQKMFDA 

       190        200        210        220        230        240 
YTRIFQRFGL AFRAVAADNG AIGGSGSHEF HVIAETGEDA IVYSPESDYA ANIEAAEALA 

       250        260        270        280        290        300 
PSAPRGPAAE PLAKTSTPGR AKCEAVAEQL GIPLQRTVKS IVLAKEVDGG EPQIWLLLLR 

       310        320        330        340        350        360 
GDHELNEIKA SKVPGLADFR FATEGEILRA FGTPPGYLGP IGTKLPVKVV ADRTVAAMSD 

       370        380        390        400        410        420 
FVCGANEEDF HYTGVNWGRD LPEAEVADLR NVVEGDPSPD GKGTLAICRG IEVGHVFMLG 

       430        440        450        460        470        480 
TRYSESMSAT FLDENGKTQP MVMGCYGIGI TRILGAAIEQ NYDARGIIWP VSIAPFEVVI 

       490        500        510        520        530        540 
CPVGYDRSEA VRAEADRLHA ELAAAGIDVI LDDRGERPGV MFADWELIGV PFRVVVGERG 

       550        560        570 
LKEGKLELQG RRDEAATAVA PADVLATLKS RLAQ

« Hide

References

[1]"Genomes of three tomato pathogens within the Ralstonia solanacearum species complex reveal significant evolutionary divergence."
Remenant B., Coupat-Goutaland B., Guidot A., Cellier G., Wicker E., Allen C., Fegan M., Pruvost O., Elbaz M., Calteau A., Salvignol G., Mornico D., Mangenot S., Barbe V., Medigue C., Prior P.
BMC Genomics 11:379-379(2010)
Cited for: NUCLEOTIDE SEQUENCE.
Strain: CFBP2957 EMBL CBJ41948.1.
[2]Genoscope - CEA
Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
Strain: CFBP2957 EMBL CBJ41948.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		FP885897 Genomic DNA. Translation: CBJ41948.1.
RefSeqYP_003744592.1. NC_014307.1.

3D structure databases

ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCBJ41948; CBJ41948; RCFBP_10644.
GeneID9417277.
KEGGrsc:RCFBP_10644.
PATRIC42544138. VBIRalSol166517_0610.

Phylogenomic databases

HOGENOMHOG000076893.
KOK01881.

Family and domain databases

Gene3D3.40.50.800. 1 hit.
3.90.960.10. 1 hit.
HAMAPMF_01569. Pro_tRNA_synth_type1.
InterProIPR002314. aa-tRNA-synt_IIb_cons-dom.
IPR006195. aa-tRNA-synth_II.
IPR004154. Anticodon-bd.
IPR002316. Pro-tRNA-ligase_IIa.
IPR004500. Pro-tRNA-synth_IIa_bac-type.
IPR023717. Pro-tRNA-Synthase_IIa_type1.
IPR007214. YbaK/aa-tRNA-synth-assoc-dom.
[Graphical view]
PANTHERPTHR11451:SF3. PTHR11451:SF3. 1 hit.
PfamPF03129. HGTP_anticodon. 1 hit.
PF00587. tRNA-synt_2b. 1 hit.
PF04073. YbaK. 1 hit.
[Graphical view]
PRINTSPR01046. TRNASYNTHPRO.
SUPFAMSSF52954. Anticodon_bd. 1 hit.
SSF55826. YbaK/aa-tRNA-synth-assoc-reg. 1 hit.
TIGRFAMsTIGR00409. proS_fam_II. 1 hit.
PROSITEPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameD8NNP8_RALSL
AccessionPrimary (citable) accession number: D8NNP8
Entry history
Integrated into UniProtKB/TrEMBL: October 5, 2010
Last sequence update: October 5, 2010
Last modified: May 1, 2013
This is version 21 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
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