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Reviewed, UniProtKB/Swiss-Prot B0C230 (SYP_ACAM1)

Last modified November 3, 2009. Version 12. 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: AM1_2321
OrganismAcaryochloris marina (strain MBIC 11017) [Complete proteome] [HAMAP]
Taxonomic identifier329726 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaAcaryochloris

Protein attributes

Sequence length600 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 – 600600Prolyl-tRNA synthetase HAMAP MF_01569
PRO_1000087832

Sequences

Sequence LengthMass (Da)Tools
B0C230-1 [UniParc].

Last modified February 26, 2008. Version 1.
Checksum: 66C483FCEC93C157

FASTA60066,372
        10         20         30         40         50         60 
MRLSQMLFVT LREDPAEAEI PSHKLLLRAG YIRRVGSGIY AYLPLMWRVL QKVSQIVREE 

        70         80         90        100        110        120 
MDAAGAQECL LPQIQPAELW QESGRWDTYT QAEGIMFALQ DRQDRELGLG PTHEEVITAV 

       130        140        150        160        170        180 
ARDMIRSYRQ LPLNLYQIQT KFRDEIRPRF GLMRGREFIM KDAYSFSTDE ADLKIIYSKM 

       190        200        210        220        230        240 
HDAYCNILQR SGLAYRAVDA DSGAIGGSGS QEFMVLAEAG EDEVLYTDDG KYAANVEKAV 

       250        260        270        280        290        300 
SRPADAQPSS FKSVEKKETP KTDTIAKLCD CLQCSPTQVV KTVLYEAVYD NGQTLLALVS 

       310        320        330        340        350        360 
LRGDQSVNEV KLQNELVQLG DVVKGKALIA LTVAEGGTKW ASQPLPLGYI APDLADSYIQ 

       370        380        390        400        410        420 
KSKQVHGKFV RLVDQTAVDL KNFVTGANEV GIHQVGVNWK TDIPLPKHVV DIRTAQVGDR 

       430        440        450        460        470        480 
AVHDPKQTLQ TARGIEIGHI FQLGTKYSQA LGATYTNEAG KEQPLVMGCY GVGVSRLAQA 

       490        500        510        520        530        540 
AVEQSYDKDG IVWPVAIAPY HAIIIIPNGK DSDQVEAAEK LYSELNAAGI ETLLDDRTER 

       550        560        570        580        590        600 
AGVKFKDADL IGIPYRIVTG RSLKEGNVEM VERATHDAHQ IALDQVLPTL KEYLAKAIST 

« Hide

References

Cross-references

Sequence databases

CP000828 Genomic DNA. Translation: ABW27331.1.
RefSeqYP_001516645.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID5681134.
GenomeReviewsGene locus AM1_2321 in contig CP000828_GR.
KEGGamr:AM1_2321.

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_ACAM1
AccessionPrimary (citable) accession number: B0C230
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: February 26, 2008
Last modified: November 3, 2009
This is version 12 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