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Reviewed, UniProtKB/Swiss-Prot A1TTD0 (SYP_ACIAC)

Last modified November 3, 2009. Version 20. 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: Aave_3670
OrganismAcidovorax avenae subsp. citrulli (strain AAC00-1) [Complete proteome] [HAMAP]
Taxonomic identifier397945 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesComamonadaceaeAcidovorax

Protein attributes

Sequence length581 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 – 581581Prolyl-tRNA synthetase HAMAP MF_01569
PRO_0000288304

Sequences

Sequence LengthMass (Da)Tools
A1TTD0-1 [UniParc].

Last modified February 6, 2007. Version 1.
Checksum: 1D10276E9C5EAFB2

FASTA58164,156
        10         20         30         40         50         60 
MKASQFFVST LKEAPADAEV VSHKLMTRAG LIKKLGAGIY NYMPMGLRVI RKVEAIVREE 

        70         80         90        100        110        120 
MNRAGAVEVT MPVVQPAEYW QETGRFDKMG PELLRIRDRH GRDFVVQPTS EEVVTDIARQ 

       130        140        150        160        170        180 
ELRSYKQLPK NLYQIQTKFR DERRPRFGLM RGREFIMKDA YSFDRDQAAA KASYQVMAQA 

       190        200        210        220        230        240 
YRRIFDRFGL TYRAVAADSG AIGGDLSEEF QVIAATGEDA IVYCPQSDYA ANMEKAEALP 

       250        260        270        280        290        300 
PQGPRPAASQ ALARTATPGK STCADVAQLL GVPLQATVKS LVLATDETNE SGEIVRSQVW 

       310        320        330        340        350        360 
LLLLRGDHDM NEIKVGKVPG LDAGFRFATV GEIEDHFGCR PGYLGPLNLR QPVRLVVDRE 

       370        380        390        400        410        420 
VAVMADWICG ANEVDFHMTG VNWGRDLPEP DVVADLRNVV AGDPSPDGKG TLAIERGIEV 

       430        440        450        460        470        480 
GHVFYLGTKY SRAMNATFLG EDGKPAFFEM GCYGIGITRL PAAAIEQNHD ERGIIWPDAI 

       490        500        510        520        530        540 
APFTVVVCPI GMDRSDEVRA AAEKLHADLL TAGVDVILDD RGERPGAMFA DWELIGVPHR 

       550        560        570        580 
VVLSDRGLKE GQVEYQHRRD AAATKVASAD IFAFIKDRIK V 

« Hide

References

[1]"Complete sequence of Acidovorax avenae subsp. citrulli AAC00-1."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Kim E., Stahl D., Richardson P.
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000512 Genomic DNA. Translation: ABM34218.1.
RefSeqYP_971992.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGA1TTD0.

Genome annotation databases

GeneID4665262.
GenomeReviewsGene locus Aave_3670 in contig CP000512_GR.
KEGGaav:Aave_3670.
NMPDRfig|397945.5.peg.3134.

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_ACIAC
AccessionPrimary (citable) accession number: A1TTD0
Entry history
Integrated into UniProtKB/Swiss-Prot: May 29, 2007
Last sequence update: February 6, 2007
Last modified: November 3, 2009
This is version 20 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