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Reviewed, UniProtKB/Swiss-Prot Q5P7T1 (SYP_AZOSE)

Last modified June 16, 2009. Version 40. 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: AZOSEA05080
ORF Names: ebA950
OrganismAzoarcus sp. (strain EbN1) (Aromatoleum aromaticum (strain EbN1)) [Complete proteome] [HAMAP]
Taxonomic identifier76114 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaRhodocyclalesRhodocyclaceaeAromatoleum

Protein attributes

Sequence length583 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 – 583583Prolyl-tRNA synthetase HAMAP MF_01569
PRO_0000248641

Sequences

Sequence LengthMass (Da)Tools
Q5P7T1-1 [UniParc].

Last modified January 4, 2005. Version 1.
Checksum: 09D5032A103728A9

FASTA58364,296
        10         20         30         40         50         60 
MRASQYFIST LKEAPSDAEV VSQKLMLRAG FIRKVAAGIY SYLPIGLRVI RKVEDIVRDE 

        70         80         90        100        110        120 
MNRAGALELT MPLVQPAELW DETGRWEQMG AEMLRFKDRH QRDFALQPTS EEVVTDIARQ 

       130        140        150        160        170        180 
ELKSYRQLPK NFYQIQTKFR DERRPRFGVM RGREFTMKDA YSFDRDVAAA GRSYDAMYAA 

       190        200        210        220        230        240 
YCRIFDRLGL TYRAVAADTG AIGGDRSHEF QVIADTGEDA IVYCPGSDYA ANIELAEALP 

       250        260        270        280        290        300 
LLATRAAPAQ ALEKTPTPGR TTCEEVAKLL GVPLETTVKS LVLATDDVDD TNKPAGVTVW 

       310        320        330        340        350        360 
LLLVRGDHEL NEVKAGKIPG LKAGFRFATE TEIAERFGCQ PGYLGPVGVN KAVKIVADRT 

       370        380        390        400        410        420 
VANMADFICG ANEADFHLTG TNWGRDLPEP DLVADLRNII EGDPSPDGRG RLAIQRGIEV 

       430        440        450        460        470        480 
GHVFYLGTKY SQSMNATFLD ENGKPKHFEM GCYGIGVTRI LGAAIEQNHD ARGIIWPDAI 

       490        500        510        520        530        540 
APFRVVVCPV GWGKSDAVRT EATKLYETLC AGGIDVILDD RDERPGVMFA DWELIGVPHR 

       550        560        570        580 
VVIGDRGLKD GMAEYQGRRD AEAAKIPLAE LAAFVGSKLR PTA 

« Hide

References

[1]"The genome sequence of an anaerobic aromatic-degrading denitrifying bacterium, strain EbN1."
Rabus R., Kube M., Heider J., Beck A., Heitmann K., Widdel F., Reinhardt R.
Arch. Microbiol. 183:27-36(2005) [PubMed: 15551059] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CR555306 Genomic DNA. Translation: CAI06630.1.
RefSeqYP_157531.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID3181861.
GenomeReviewsGene locus AZOSEA05080 in contig CR555306_GR.
KEGGeba:ebA950.
NMPDRfig|76114.4.peg.1441.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ5P7T1.
OMAQ5P7T1. VVSHQLM.

Enzyme and pathway databases

BioCycASP76114:EBA950-MON.

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_AZOSE
AccessionPrimary (citable) accession number: Q5P7T1
Entry history
Integrated into UniProtKB/Swiss-Prot: September 5, 2006
Last sequence update: January 4, 2005
Last modified: June 16, 2009
This is version 40 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