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Reviewed, UniProtKB/Swiss-Prot Q82JV8 (SYP2_STRAW)

Last modified November 3, 2009. Version 47. 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 2
    EC=6.1.1.15
Alternative name(s):
    Proline--tRNA ligase 2
      Short name=ProRS 2
Gene names
Name: proS2
Ordered Locus Names: SAV_2646
OrganismStreptomyces avermitilis [Complete proteome] [HAMAP]
Taxonomic identifier33903 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomyces

Protein attributes

Sequence length471 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 – 471471Prolyl-tRNA synthetase 2 HAMAP MF_01571
PRO_0000249151

Sequences

Sequence LengthMass (Da)Tools
Q82JV8-1 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 5061F2E9DB52E331

FASTA47152,164
        10         20         30         40         50         60 
MAKAPVLTPR ADDFPRWYQD LINKAELADN GPVRGTMVIR PYGYGLWERM QQEMDARIKE 

        70         80         90        100        110        120 
TGTQNAYFPL LIPQSYLTKE ADHVEGFAPE LAVVTHGGGK ELEEPAVVRP TSEMIINDYF 

       130        140        150        160        170        180 
SKWVQSYRDL PLLINQWANV VRWELRPRLF LRTTEFLWQE GHTAHATYEE ARDFAAHIHR 

       190        200        210        220        230        240 
HVYADFMENV LAMDVVLGRK TAKERFAGAV NTLTLEGMMG DGKALQMGTS HELGQNFARA 

       250        260        270        280        290        300 
FHTQYLSKEG KQELVWQTSW GSTTRMIGAL VMMHGDDNGL RVPPRLAQTQ VVVLAIKGDE 

       310        320        330        340        350        360 
AVLAKVRETG DRLKAAGLRV QVDDRTDVPF GRRAVDWELK GVPVRVEVGP RDLENGTAMV 

       370        380        390        400        410        420 
ARRIPGGKEP VALDALAALL PTALEEDQAL LLRQARERRA SRTSDVSTIE EAVEAAAGGG 

       430        440        450        460        470 
WARIPWATLG ERGEAELAEH AASVRCLVAE DGSVPGADDA PGNVAVVARA Y 

« Hide

References

[1]"Genome sequence of an industrial microorganism Streptomyces avermitilis: deducing the ability of producing secondary metabolites."
Omura S., Ikeda H., Ishikawa J., Hanamoto A., Takahashi C., Shinose M., Takahashi Y., Horikawa H., Nakazawa H., Osonoe T., Kikuchi H., Shiba T., Sakaki Y., Hattori M.
Proc. Natl. Acad. Sci. U.S.A. 98:12215-12220(2001) [PubMed: 11572948] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 31267 / DSM 46492 / JCM 5070 / NCIMB 12804 / NRRL 8165.
[2]"Complete genome sequence and comparative analysis of the industrial microorganism Streptomyces avermitilis."
Ikeda H., Ishikawa J., Hanamoto A., Shinose M., Kikuchi H., Shiba T., Sakaki Y., Hattori M., Omura S.
Nat. Biotechnol. 21:526-531(2003) [PubMed: 12692562] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 31267 / DSM 46492 / JCM 5070 / NCIMB 12804 / NRRL 8165.

Cross-references

Sequence databases

BA000030 Genomic DNA. Translation: BAC70357.1.
RefSeqNP_823822.1.

3D structure databases

HSSPHSSP built from PDB template 1HC7 based on UniProtKB Q93N97.
ModBaseSearch...

Genome annotation databases

GeneID1210491.
GenomeReviewsGene locus SAV_2646 in contig BA000030_GR.
KEGGsma:SAV_2646.
NMPDRfig|227882.1.peg.2648.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ82JV8.
OMACIEAMMQ.

Enzyme and pathway databases

BioCycSAVE227882:SAV2646-MON.
BRENDA6.1.1.15. 140873.

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.
[Graphical view]
Gene3DG3DSA:3.40.50.800. Anticodon_bd. 1 hit.
PANTHERPTHR11451:SF6. ProS_fam_I. 1 hit.
PfamPF03129. HGTP_anticodon. 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 nameSYP2_STRAW
AccessionPrimary (citable) accession number: Q82JV8
Entry history
Integrated into UniProtKB/Swiss-Prot: September 5, 2006
Last sequence update: June 1, 2003
Last modified: November 3, 2009
This is version 47 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