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Q0SNA5 (SYP_BORAP) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 41. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Proline--tRNA ligase

EC=6.1.1.15
Alternative name(s):
Prolyl-tRNA synthetase
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.
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. HAMAP MF_01571

Catalytic activity

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

Subunit structure

Homodimer By similarity. HAMAP MF_01571

Subcellular location

Cytoplasm By similarity HAMAP MF_01571.

Domain

Consists of three domains: the N-terminal catalytic domain, the anticodon-binding domain and the C-terminal extension By similarity. HAMAP MF_01571

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: InterPro

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

proline-tRNA ligase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 488488Proline--tRNA ligase HAMAP MF_01571
PRO_0000288404

Sequences

Sequence LengthMass (Da)Tools
Q0SNA5 [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].
Strain: PKo.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000395 Genomic DNA. Translation: ABH01673.1.
RefSeqYP_709849.1. NC_008277.1.

3D structure databases

ProteinModelPortalQ0SNA5.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ0SNA5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBORT00000004287; EBBORP00000003905; EBBORG00000004287.
GeneID4227615.
GenomeReviewsGene locus BAPKO_0419 in contig CP000395_GR.
KEGGbaf:BAPKO_0419.
NMPDRfig|390236.5.peg.466.
PATRIC37189122. VBIBorAfz3878_0471.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0442.
GeneTreeEBGT00050000007260.
HOGENOMHBG334108.
OMAKFAEYEL.
ProtClustDBPRK08661.

Enzyme and pathway databases

BioCycBAFZ390236:BAPKO_0419-MONOMER.

Family and domain databases

HAMAPMF_01571. Pro_tRNA_synth_type3.
[Tree]
InterProIPR002314. aa-tRNA-synt_IIb_cons-dom.
IPR006195. aa-tRNA-synth_II.
IPR004154. Anticodon-bd.
IPR002316. Pro-tRNA-synth_IIa.
IPR004499. Pro-tRNA-synth_IIa_arc-type.
IPR017449. Pro-tRNA_synth_II.
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.
KOK01881.
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.
SMARTSM00946. ProRS-C_1. 1 hit.
[Graphical view]
SUPFAMSSF52954. Anticodon_bd. 1 hit.
SSF64586. Pro-tRNA_synth_II_C. 1 hit.
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: January 25, 2012
This is version 41 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

SIMILARITY comments

Index of protein domains and families