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Reviewed, UniProtKB/Swiss-Prot Q1LSM8 (SYP_BAUCH)

Last modified June 16, 2009. Version 22. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Prolyl-tRNA synthetase
    EC=6.1.1.15
Alternative name(s):
    Proline--tRNA ligase
      Short name=ProRS
Gene names
Name: proS
Ordered Locus Names: BCI_0609
OrganismBaumannia cicadellinicola subsp. Homalodisca coagulata [Complete proteome] [HAMAP]
Taxonomic identifier374463 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaCandidatus Baumannia

Protein attributes

Sequence length557 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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.

Catalytic activity

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

Subunit structure

Homodimer By similarity.

Subcellular location

Cytoplasm By similarity.

Domain

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

Sequence similarities

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

Ontologies

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

Inferred from electronic annotation. Source: HAMAP

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: HAMAP

proline-tRNA ligase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 557557Prolyl-tRNA synthetase HAMAP MF_01569
PRO_0000248650

Sequences

Sequence LengthMass (Da)Tools
Q1LSM8-1 [UniParc].

Last modified May 30, 2006. Version 1.
Checksum: 88DC7212658341D5

FASTA55762,864
        10         20         30         40         50         60 
MRTSQYLLST IKEIPLDAEV ISHQLMLRAG IIRQLASGLY TWLPTGLRIL RKVENIVREE 

        70         80         90        100        110        120 
MNNIGAIEVS MPIVQPANLW LESGRWGQYG PELLRFTDRS TRQFLLGPTH EEVITDLIRN 

       130        140        150        160        170        180 
EVKSYKQLPL NLFQIKTKFR DEVRPRYGVM RSREFIMKDA YSFHTSQQSL QATYDLMYYT 

       190        200        210        220        230        240 
YNTIFNRIGL DVRTVQADPG SIGGHLSHEF LALVSNYEDQ MLLIDASHKA TERNLPSENL 

       250        260        270        280        290        300 
QLVDAPGIYT LTELVKLFNL PIEKIAQIII VHAQQNALYP LVALMVRGDH SINYAQVEKL 

       310        320        330        340        350        360 
PQVASPLVFA TEDEIRLAIG VGSSSLGPIN LPLPLIIDHS VAVMSDFVAG ANIDGKYFFG 

       370        380        390        400        410        420 
INWERDLSLP EVANLTNQNI SVSQPQRLHR TNWIEVGHIF QLGSKYSKVM KATVQGEDGN 

       430        440        450        460        470        480 
NMIMTMGCYG IGITRVVAAA IDKYNDKQGL LLPVSIAPFQ VAIIPINLHK SLLVQTVAEQ 

       490        500        510        520        530        540 
LYNQLSIRKI DVLLDDRKER PGVMFADIEL IGIPHIIIIG DRNLAVQKIE YKNRSNGEKK 

       550 
LMNLSIIVDW IVAKLNS 

« Hide

References

[1]"Metabolic complementarity and genomics of the dual bacterial symbiosis of sharpshooters."
Wu D., Daugherty S.C., Van Aken S.E., Pai G.H., Watkins K.L., Khouri H., Tallon L.J., Zaborsky J.M., Dunbar H.E., Tran P.L., Moran N.A., Eisen J.A.
PLoS Biol. 4:1079-1092(2006) [PubMed: 16729848] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000238 Genomic DNA. Translation: ABF13821.1.
RefSeqYP_589036.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID4056150.
GenomeReviewsGene locus BCI_0609 in contig CP000238_GR.
KEGGbci:BCI_0609.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ1LSM8.
OMAQ1LSM8. VVSHQLM.

Family and domain databases

HAMAPMF_01569.
[Tree]
InterProIPR002314. aa-tRNA-synt_IIb_cons-reg.
IPR006195. aa-tRNA-synth_II_cons-reg.
IPR004154. Anticodon_bd.
IPR004500. Pro-tRNA-synth_IIa_bac.
IPR002316. Pro-tRNA-synth_IIa_cons-reg.
IPR007214. YbaK/aa-tRNA-synth-assoc-reg.
[Graphical view]
Gene3DG3DSA:3.40.50.800. Anticodon_bd. 1 hit.
PfamPF03129. HGTP_anticodon. 1 hit.
PF00587. tRNA-synt_2b. 1 hit.
PF04073. YbaK. 1 hit.
[Graphical view]
PRINTSPR01046. TRNASYNTHPRO.
TIGRFAMsTIGR00409. proS_fam_II. 1 hit.
PROSITEPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYP_BAUCH
AccessionPrimary (citable) accession number: Q1LSM8
Entry history
Integrated into UniProtKB/Swiss-Prot: September 5, 2006
Last sequence update: May 30, 2006
Last modified: June 16, 2009
This is version 22 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents