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Reviewed, UniProtKB/Swiss-Prot Q5PAZ5 (SYP_ANAMM)

Last modified February 9, 2010. Version 40. 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: AM507
OrganismAnaplasma marginale (strain St. Maries) [Complete proteome] [HAMAP]
Taxonomic identifier234826 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRickettsialesAnaplasmataceaeAnaplasma

Protein attributes

Sequence length425 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_01570

Catalytic activity

ATP + L-proline + tRNA(Pro) = AMP + diphosphate + L-prolyl-tRNA(Pro). HAMAP MF_01570

Subunit structure

Homodimer By similarity. HAMAP MF_01570

Subcellular location

Cytoplasm By similarity HAMAP MF_01570.

Sequence similarities

Belongs to the class-II aminoacyl-tRNA synthetase family. ProS type 2 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 – 425425Prolyl-tRNA synthetase HAMAP MF_01570
PRO_0000248887

Sequences

Sequence LengthMass (Da)Tools
Q5PAZ5-1 [UniParc].

Last modified January 4, 2005. Version 1.
Checksum: C778F95246013B1D

FASTA42547,664
        10         20         30         40         50         60 
MRLSECYVPT MKDVSSDVVV ASHKYSLRAG LVRQNASGLY TWLPLGLKVL RTIERIVREE 

        70         80         90        100        110        120 
MDSSGFLEIL MPSVQPADLW RESLRYDSYG PEMLRMQDRS GREMVFGPTH EEAISDVVRS 

       130        140        150        160        170        180 
SLKSYRDLPI NLYQIQWKFR DELRPRHGIM RGREFLMKDA YSFDVDFEGV MRSYENVFSA 

       190        200        210        220        230        240 
YFRIFRRLGL VPIAAKADSG AIGGSISHEF HVLVPTGEST VYHDKKALDL SKNDYCTTEE 

       250        260        270        280        290        300 
IASVYAATED AHDPQNCGVD PNDLQVSKGI EVAHVFYLGD RYSAPMNVKF HDKDGNSAHA 

       310        320        330        340        350        360 
LMGCYGIGIS RLVAAIIEVF HDDVGIRWPE SIAPFKVGIV NLLTTNEDCK TTAETIYAAL 

       370        380        390        400        410        420 
ADSSLYDDST DSPGVKLARM DLLGMPWQVI IGNSFVKDKV VELKNRANGA TERCTVDALI 


ARMQA 

« Hide

References

[1]"Complete genome sequencing of Anaplasma marginale reveals that the surface is skewed to two superfamilies of outer membrane proteins."
Brayton K.A., Kappmeyer L.S., Herndon D.R., Dark M.J., Tibbals D.L., Palmer G.H., McGuire T.C., Knowles D.P. Jr.
Proc. Natl. Acad. Sci. U.S.A. 102:844-849(2005) [PubMed: 15618402] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000030 Genomic DNA. Translation: AAV86535.1.
RefSeqYP_153790.1.

3D structure databases

SMRQ5PAZ5. Positions 1-422.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ5PAZ5.

Genome annotation databases

GeneID3171578.
GenomeReviewsGene locus AM507 in contig CP000030_GR.
KEGGama:AM507.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0442.
HOGENOMHBG403504.
OMADFVLGPT.
PhylomeDBQ5PAZ5.

Enzyme and pathway databases

BioCycAMAR234826:AM507-MONOMER.

Family and domain databases

HAMAPMF_01570. Pro_tRNA_synth_type2.
[Tree]
InterProIPR002314. aa-tRNA-synt_IIb_cons-dom.
IPR006195. aa-tRNA-synth_II_cons-dom.
IPR004154. Anticodon_bd.
IPR004500. Pro-tRNA-synth_IIa_bac.
IPR002316. Pro-tRNA-synth_IIa_cons-reg.
[Graphical view]
Gene3DG3DSA:3.40.50.800. Anticodon_bd. 1 hit.
PfamPF03129. HGTP_anticodon. 1 hit.
PF00587. tRNA-synt_2b. 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_ANAMM
AccessionPrimary (citable) accession number: Q5PAZ5
Entry history
Integrated into UniProtKB/Swiss-Prot: September 5, 2006
Last sequence update: January 4, 2005
Last modified: February 9, 2010
This is version 40 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