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Reviewed, UniProtKB/Swiss-Prot Q0SNA5 (SYP_BORAP)

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: BAPKO_0419
OrganismBorrelia afzelii (strain PKo) [Complete proteome] [HAMAP]
Taxonomic identifier390236 [NCBI]
Taxonomic lineageBacteriaSpirochaetesSpirochaetalesSpirochaetaceaeBorreliaBorrelia burgdorferi group

Protein attributes

Sequence length488 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) By similarity.

Catalytic activity

ATP + L-proline + tRNA(Pro) = AMP + diphosphate + L-prolyl-tRNA(Pro). HAMAP MF_01571

Subunit structure

Homodimer By similarity.

Subcellular location

Cytoplasm By similarity.

Domain

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

Sequence similarities

Belongs to the class-II aminoacyl-tRNA synthetase family. ProS type 3 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 – 488488Prolyl-tRNA synthetase HAMAP MF_01571
PRO_0000288404

Sequences

Sequence LengthMass (Da)Tools
Q0SNA5-1 [UniParc].

Last modified September 19, 2006. Version 1.
Checksum: EDD310D875662AE0

FASTA48856,265
        10         20         30         40         50         60 
MSDFIASKED DYSKWYLDIV QKAKLADYSP VKGCMVIMPY GYSIWSKIQS ILDKKFKETG 

        70         80         90        100        110        120 
HENAYFPMLI PYGFLEKEKD HIDGFSPEFA IIKDAGGESL VEPLVLRPTS ETIIWNMYSK 

       130        140        150        160        170        180 
WIKSYRDLPL KINQWANVIR WEKRTRPFLR TTEFLWQEGH TAHATEEEAL EETLLILDVY 

       190        200        210        220        230        240 
KRFMEDYLAI PVFCGKKSEN EKFAGAVSTY SVEALMQDKK ALQAATSHYL GLNFAKAFDV 

       250        260        270        280        290        300 
KFQDKDGKMK HVFASSWGVS TRLIGALIMV HSDEKGLILP PRIAPVEIIV IPIFKKEDEI 

       310        320        330        340        350        360 
NKKILDYSDC VVHTLKKAEF RVEIDKDVRS SPGFRFSSAE FKGIPIRIEV GINDILLNSV 

       370        380        390        400        410        420 
TIIRRDKDRK FKYQISLDSL VSKVRVELDS MQKDLFKKAL NFRTLNTKEI FRSGKDSYEL 

       430        440        450        460        470        480 
FKAYVNDYSG FVLSCWCGGL NCENIIKNET KATIRCIPDD FKARDLTGMT CIYCSSKAKY 


YVLFAKSY 

« Hide

References

[1]"Comparative genome analysis: selection pressure on the Borrelia vls cassettes is essential for infectivity."
Gloeckner G., Schulte-Spechtel U., Schilhabel M., Felder M., Suehnel J., Wilske B., Platzer M.
BMC Genomics 7:211-211(2006) [PubMed: 16914037] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000395 Genomic DNA. Translation: ABH01673.1.
RefSeqYP_709849.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID4227615.
GenomeReviewsGene locus BAPKO_0419 in contig CP000395_GR.
KEGGbaf:BAPKO_0419.
NMPDRfig|390236.5.peg.466.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ0SNA5.
OMAQ0SNA5. CIEAMMQ.

Enzyme and pathway databases

BioCycBAFZ390236:BAPKO_0419-MON.

Family and domain databases

HAMAPMF_01571.
[Tree]
InterProIPR002314. aa-tRNA-synt_IIb_cons-reg.
IPR006195. aa-tRNA-synth_II_cons-reg.
IPR004154. Anticodon_bd.
IPR002316. Pro-tRNA-synth_IIa_cons-reg.
IPR004499. Pro-tRNA-synth_IIa_pro-type.
IPR016061. Pro-tRNA_synth_II_C.
[Graphical view]
Gene3DG3DSA:3.40.50.800. Anticodon_bd. 1 hit.
G3DSA:3.30.110.30. Pro-tRNA-synth_II_C_arc/euk. 1 hit.
PANTHERPTHR11451:SF6. ProS_fam_I. 1 hit.
PfamPF03129. HGTP_anticodon. 1 hit.
PF09180. ProRS-C_1. 1 hit.
PF00587. tRNA-synt_2b. 1 hit.
[Graphical view]
PRINTSPR01046. TRNASYNTHPRO.
TIGRFAMsTIGR00408. proS_fam_I. 1 hit.
PROSITEPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYP_BORAP
AccessionPrimary (citable) accession number: Q0SNA5
Entry history
Integrated into UniProtKB/Swiss-Prot: May 29, 2007
Last sequence update: September 19, 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