Skip Header

Contribute Send feedback
Read comments (0) or add your own

Q6FZI4 (SYD_BARQU) Reviewed, UniProtKB/Swiss-Prot

Last modified August 10, 2010. Version 49. Feed History...

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

Names and origin

Protein namesRecommended name:
Aspartyl-tRNA synthetase

EC=6.1.1.12
Alternative name(s):
Aspartate--tRNA ligase
Short name=AspRS
Gene names
Name:aspS
Ordered Locus Names:BQ07550
OrganismBartonella quintana (Rochalimaea quintana) [Complete proteome] [HAMAP]
Taxonomic identifier803 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBartonellaceaeBartonella

Protein attributes

Sequence length597 AA.
Sequence statusComplete.
Protein existenceInferred from homology.

General annotation (Comments)

Catalytic activity

ATP + L-aspartate + tRNA(Asp) = AMP + diphosphate + L-aspartyl-tRNA(Asp). HAMAP MF_00044_B

Subunit structure

Homodimer By similarity. HAMAP MF_00044_B

Subcellular location

Cytoplasm HAMAP MF_00044_B.

Sequence similarities

Belongs to the class-II aminoacyl-tRNA synthetase family.

Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionAminoacyl-tRNA synthetase
Ligase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processaspartyl-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

aspartate-tRNA ligase activity

Inferred from electronic annotation. Source: EC

nucleic acid binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 597597Aspartyl-tRNA synthetase HAMAP MF_00044_B
PRO_0000110832

Sequences

Sequence LengthMass (Da)Tools
Q6FZI4-1 [UniParc].

Last modified July 19, 2004. Version 1.
Checksum: 1EC39A18BF353CA1

FASTA59767,815
        10         20         30         40         50         60 
MHRYRSHNCA ALRKHDVGKH VRLSGWVHRV RDHGGILFVD LRDHFGITQI VANPASPAFE 

        70         80         90        100        110        120 
IIEKVRSEWV IRVDGEVCAR SDEVINTVLP TGEIEIFVKE VEILSKSDEL PLPVFGEPDY 

       130        140        150        160        170        180 
PEDIRLKYRF LDLRRETMHK NIMRRTEIIT AIRRSMQNNG FTEFTTPLLT ASSPEGARDF 

       190        200        210        220        230        240 
LVPSRIHQGK FYALPQAPQQ YKQLLMMSGF DRYFQIAPCF RDEDPRADRL PGEFYQLDVE 

       250        260        270        280        290        300 
MSFVEQEDVF VTMEPIMRSI FEEFANGKPV TQNFPRISYD EAIKKYGSDK PDLRNPIIMQ 

       310        320        330        340        350        360 
DVSQHFYDSC FKIFAQILTN DENAQVWAIP AKTGGSRAFC DRMNLWAQSE GQPGLGYIFW 

       370        380        390        400        410        420 
REEEGKFEGA GPIAKNIGEQ RTEALRIQLG LESGDACFFI AGNPKKFSTF AGAVRTRIGE 

       430        440        450        460        470        480 
ELDLIDRECF SLAWIVDFPF FEWNEDEKKL DFAHNPFSMP QGGKNALECQ DPLTLKAFQY 

       490        500        510        520        530        540 
DLVCNGYEIA SGGIRNHSPE MMLKVFNLAG LSREVVEDRF GALYRAFHYG APPHGGMAAG 

       550        560        570        580        590 
VDRIIMLLQG VKNLREIALF PMNQQALDLL MSAPSDVSSA QLRDLGIRVA PAAKNGS 

« Hide

References

[1]"The louse-borne human pathogen Bartonella quintana is a genomic derivative of the zoonotic agent Bartonella henselae."
Alsmark U.C.M., Frank A.C., Karlberg E.O., Legault B.-A., Ardell D.H., Canbaeck B., Eriksson A.-S., Naeslund A.K., Handley S.A., Huvet M., La Scola B., Holmberg M., Andersson S.G.E.
Proc. Natl. Acad. Sci. U.S.A. 101:9716-9721(2004) [PubMed: 15210978] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Toulouse.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX897700 Genomic DNA. Translation: CAF26239.1.
RefSeqYP_032384.1.

3D structure databases

ProteinModelPortalQ6FZI4.
SMRQ6FZI4. Positions 4-590.
ModBaseSearch...

Genome annotation databases

GeneID2866839.
GenomeReviewsGene locus BQ07550 in contig BX897700_GR.
KEGGbqu:BQ07550.
NMPDRfig|283165.1.peg.654.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG396032.
OMAYQLDVEM.
ProtClustDBPRK00476.

Enzyme and pathway databases

BioCycBQUI283165:BQ07550-MONOMER.
BRENDA6.1.1.12. 292235.

Family and domain databases

HAMAPMF_00044_B. Asp_tRNA_synth_B.
[Tree]
InterProIPR004364. aa-tRNA-synt_II.
IPR018150. aa-tRNA-synt_II-like.
IPR006195. aa-tRNA-synth_II_cons-dom.
IPR020564. Asp-tRNA-synth_IIb_bac-type.
IPR004524. Asp-tRNA-synth_IIb_bac/mt.
IPR018153. Asp-tRNA-synth_IIb_C_bac/mt.
IPR002312. Asp/Asn-tRNA-synth_IIb.
IPR004115. GAD_dom.
IPR012340. NA-bd_OB-fold.
IPR016027. NA-bd_OB-fold-like.
IPR004365. NA-bd_OB_tRNA-helicase.
[Graphical view]
Gene3DG3DSA:2.40.50.140. OB_NA_bd_sub. 1 hit.
PANTHERPTHR22594. aa-tRNA-synt_II. 1 hit.
PTHR22594:SF5. AspS_bac. 1 hit.
PfamPF02938. GAD. 1 hit.
PF00152. tRNA-synt_2. 1 hit.
PF01336. tRNA_anti. 1 hit.
[Graphical view]
PRINTSPR01042. TRNASYNTHASP.
SUPFAMSSF50249. Nucleic_acid_OB. 1 hit.
TIGRFAMsTIGR00459. aspS_bact. 1 hit.
PROSITEPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYD_BARQU
AccessionPrimary (citable) accession number: Q6FZI4
Entry history
Integrated into UniProtKB/Swiss-Prot: March 29, 2005
Last sequence update: July 19, 2004
Last modified: August 10, 2010
This is version 49 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