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B4RCT1 (SYD_PHEZH) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 25. 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:PHZ_c1857
OrganismPhenylobacterium zucineum (strain HLK1) [Complete proteome] [HAMAP]
Taxonomic identifier450851 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaCaulobacteralesCaulobacteraceaePhenylobacterium

Protein attributes

Sequence length592 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 By similarity 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 – 592592Aspartate--tRNA ligase HAMAP MF_00044_B
PRO_1000091024

Sequences

Sequence LengthMass (Da)Tools
B4RCT1 [UniParc].

Last modified September 23, 2008. Version 1.
Checksum: B3B8A971B3EB977E

FASTA59266,337
        10         20         30         40         50         60 
MHLYRTHTCG QLRASDTGSK VRLSGWVHRK RDHGGLIFID LRDHYGLTQL VVSPSTPGFD 

        70         80         90        100        110        120 
LVEHVRAESV IRVDGEVVAR SAETVNPNLP TGEIEVVVRQ VEVLSEAAEL PLPVFGEPEY 

       130        140        150        160        170        180 
PEDIRLKYRY LDLRRETLHR NIVLRSQVIQ SIRRRMIDQG FLEFQTPILT ASSPEGARDF 

       190        200        210        220        230        240 
LVPSRLHPTK FYALPQAPQQ FKQLLMVSGF DRYFQIAPCF RDEDLRADRS LEFYQLDVEM 

       250        260        270        280        290        300 
SFVTQDDVFA AIEPVMHGVF TEFGEGKPVT PYPFPRIPYR EAIAKYGSDK PDLRNPIEMQ 

       310        320        330        340        350        360 
DVSEHFRGGG FGLFARILED AKNAVWAIPG PKGGSRAFCD RMNSWAQGEG QPGLGYIFWS 

       370        380        390        400        410        420 
DDQGGWGGPI AKNLGPEKTD GLMKALGLGQ GDAAFFVAGD PKVFYKFAGA ARTKVGTDLK 

       430        440        450        460        470        480 
LIDEGRFEFC WIVDFPMFEW SDEEKKYDFS HNPFSMPQGE LDALLNKEPG EIVAYQYDIV 

       490        500        510        520        530        540 
CNGHELCSGA IRNHRPDVML KAFEIAGYGP EVVEEQFGGM LNAFRHGAPP HGGLAPGIDR 

       550        560        570        580        590 
IVMLLAGETA IREVIAFPLN QQGQDLLMNA PSEVSEKQLK ELHIRLAPPI KA 

« Hide

References

[1]"Complete genome of Phenylobacterium zucineum - a novel facultative intracellular bacterium isolated from human erythroleukemia cell line K562."
Luo Y., Xu X., Ding Z., Liu Z., Zhang B., Yan Z., Sun J., Hu S., Hu X.
BMC Genomics 9:386-386(2008) [PubMed: 18700039] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: HLK1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000747 Genomic DNA. Translation: ACG78268.1.
RefSeqYP_002130697.1. NC_011144.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGB4RCT1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID6791372.
GenomeReviewsGene locus PHZ_c1857 in contig CP000747_GR.
KEGGpzu:PHZ_c1857.
PATRIC22926676. VBIPheZuc44517_2408.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG396032.
OMAYQLDVEM.
ProtClustDBPRK00476.

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_PHEZH
AccessionPrimary (citable) accession number: B4RCT1
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: September 23, 2008
Last modified: January 25, 2012
This is version 25 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