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Reviewed, UniProtKB/Swiss-Prot A4SJ23 (SYP_AERS4)

Last modified November 3, 2009. Version 18. 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: ASA_0733
OrganismAeromonas salmonicida (strain A449) [Complete proteome] [HAMAP]
Taxonomic identifier382245 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAeromonadalesAeromonadaceaeAeromonas

Protein attributes

Sequence length574 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 – 574574Prolyl-tRNA synthetase HAMAP MF_01569
PRO_1000069116

Sequences

Sequence LengthMass (Da)Tools
A4SJ23-1 [UniParc].

Last modified May 15, 2007. Version 1.
Checksum: 5A4C0C82733708B8

FASTA57462,723
        10         20         30         40         50         60 
MRTSQYLLST LKETPSDAEV VSHQLMLRAG MIRKLASGMY AWLPSGLRVL KKIENIVREE 

        70         80         90        100        110        120 
MNNAGAIEVS MPVVQPAELW QESGRWDDYG PELCRLTDRH NRPFVLGPTH EEVITSLVRY 

       130        140        150        160        170        180 
EVNSYKQLPL NLYQIQTKFR DEVRPRFGVM RGREFLMKDA YSFHIDKASL IETYERMHAA 

       190        200        210        220        230        240 
YCAAFTRMGL NFRPVQADTG SIGGTGSHEF QVLAESGEDL IAFSDTSDYA ANIEMAEALA 

       250        260        270        280        290        300 
PAGERPAATA ALTKVATPNV HTIDDVAAFL SVAPTAIAKT LLVLAEADEH GKQAVIALVL 

       310        320        330        340        350        360 
RGDHELNEIK AEKLPGVANP LTFANDEQIK AAAGCDAGSI GPVGFAGRII VDRSAAHLAD 

       370        380        390        400        410        420 
FVCGANETGF HLTGANWDRD IATYEVADLR NVVEGDPSPC GQGKLLLKRG IEVGHIFQLG 

       430        440        450        460        470        480 
TKYSEAMKAS VLNEGGKSVT MEMGCYGIGV SRLVAAAIEQ NNDQYGIIWP DAIAPFEVAI 

       490        500        510        520        530        540 
VPMNMHKSER VAEQAQQFYA ELKAAGVDVL FDDRKERPGV MFADMELLGV PHAIVIGDRG 

       550        560        570 
LDNGVVEYKC RRSGEKQEVA ITEIVAMLKA KLGR 

« Hide

References

[1]"The genome sequence of Aeromonas salmonicida subsp. salmonicida A449."
Reith M.E., Singh R.K., Curtis B., Boyd J., Bouevitch A., Kimball J., Munholland J., Murphy C., Sarty D., Williams J., Nash J., Johnson S., Brown L.
Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000644 Genomic DNA. Translation: ABO88895.1.
RefSeqYP_001140643.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGA4SJ23.

Genome annotation databases

GeneID4998457.
GenomeReviewsGene locus ASA_0733 in contig CP000644_GR.
KEGGasa:ASA_0733.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMAVVSHQLM.

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_AERS4
AccessionPrimary (citable) accession number: A4SJ23
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: May 15, 2007
Last modified: November 3, 2009
This is version 18 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