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Q6G330 (SYD_BARHE) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 57. 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:
Aspartate--tRNA ligase

EC=6.1.1.12
Alternative name(s):
Aspartyl-tRNA synthetase
Short name=AspRS
Gene names
Name:aspS
Ordered Locus Names:BH09790
OrganismBartonella henselae (strain ATCC 49882 / Houston 1) (Rochalimaea henselae) [Complete proteome] [HAMAP]
Taxonomic identifier283166 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBartonellaceaeBartonella

Protein attributes

Sequence length596 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 processtRNA aminoacylation for protein translation

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 – 596596Aspartate--tRNA ligase HAMAP MF_00044_B
PRO_0000110831

Sequences

Sequence LengthMass (Da)Tools
Q6G330 [UniParc].

Last modified July 19, 2004. Version 1.
Checksum: BEFD90DE89257CED

FASTA59667,626
        10         20         30         40         50         60 
MHRYRSHHCA ALRKCDVGIK ARLSGWVHRV RDHGGILFVD LRDHFGITQI VADPASPAFK 

        70         80         90        100        110        120 
IIEKVRSEWV IRVDGEVRAR SDEVINTSLP TGEIEIFAKE VEILSKSDEL PLPVFGEPDY 

       130        140        150        160        170        180 
PEDIRLKYRF LDLRRETMHR NIMRRTEIIA AIRRSMQENG FTEFTTPLLT ASSPEGARDF 

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

       250        260        270        280        290        300 
MSFVEQEDVL VTMEPIMRSL FEEFADGKPV TQSFPRLSYE EAMRKYGSDK PDLRNPIIME 

       310        320        330        340        350        360 
DVSQHFYDSG FKVFAQILAN DENARVWAIP AKTGGSRAFC DRMNGWAQSE GQPGLGYIFW 

       370        380        390        400        410        420 
REEQGKFEGA GPIAKNIGEQ RTEALRMQLG LENGDACFFV AGDPKKFLPF AGAARTRVGE 

       430        440        450        460        470        480 
ELDLVDRDCF SLAWIVDFPF FEWNEEEKKL DFAHNPFSMP QGGKDALECQ DPLTLKAFQY 

       490        500        510        520        530        540 
DLVCNGYEIA SGGIRNHSPE MMLKVFNLAG LSKEVVEDRF GGLYRAFHYG APPHGGMAAG 

       550        560        570        580        590 
VDRIIMLLQG VKNLREVALF PMNQQALDLL MSAPSDVSPV QLRDLGIRIA PAAKND 

« 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: ATCC 49882 / Houston 1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX897699 Genomic DNA. Translation: CAF27772.1.
RefSeqYP_033770.1. NC_005956.1.

3D structure databases

ProteinModelPortalQ6G330.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2866084.
GenomeReviewsGene locus BH09790 in contig BX897699_GR.
KEGGbhe:BH09790.
NMPDRfig|283166.1.peg.898.
PATRIC20545779. VBIBarHen29080_1026.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG396032.
OMAYQLDVEM.
PhylomeDBQ6G330.
ProtClustDBPRK00476.

Enzyme and pathway databases

BioCycBHEN283166:BH09790-MONOMER.

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.
IPR004524. Asp-tRNA-synth_IIb_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:3.30.1360.30. GAD_dom. 1 hit.
G3DSA:2.40.50.140. OB_NA_bd_sub. 1 hit.
KOK01876.
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.
SSF55261. SSF55261. 1 hit.
TIGRFAMsTIGR00459. AspS_bact. 1 hit.
PROSITEPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYD_BARHE
AccessionPrimary (citable) accession number: Q6G330
Entry history
Integrated into UniProtKB/Swiss-Prot: March 29, 2005
Last sequence update: July 19, 2004
Last modified: January 25, 2012
This is version 57 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