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Q135R5 (SYD_RHOPS) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 44. 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:RPD_2947
OrganismRhodopseudomonas palustris (strain BisB5) [Complete proteome] [HAMAP]
Taxonomic identifier316057 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBradyrhizobiaceaeRhodopseudomonas

Protein attributes

Sequence length590 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 – 590590Aspartate--tRNA ligase HAMAP MF_00044_B
PRO_1000006741

Sequences

Sequence LengthMass (Da)Tools
Q135R5 [UniParc].

Last modified October 31, 2006. Version 1.
Checksum: 59BF63D0FD57E0DD

FASTA59066,581
        10         20         30         40         50         60 
MHRYRTHTCG ALRDSDIDQT VRLSGWCHRI RDHGGLLFID LRDHYGLTQC VADPDSPAFK 

        70         80         90        100        110        120 
DAEKLRAEWV VRIDGRVRRR PEGTDNDDLP TGKIELFITE IEVLGPAGEL PLPVFGEQEY 

       130        140        150        160        170        180 
PEDVRLRYRF LDLRREKLHQ NIMTRGAIVD AMRARMKQQG FFEFQTPILT ASSPEGARDF 

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

       250        260        270        280        290        300 
MSFVTQDDVF AAMEPVITGV FEDFAKGKRV TKGWPRIPYA DSMRKYGTDK PDLRNPIEMQ 

       310        320        330        340        350        360 
DVSEHFRGSG FKVFARMLEE ERNQVWAIPG PGGGSRAFCD RMNSWAQGEG QPGLGYIMWR 

       370        380        390        400        410        420 
EGGEGAGPLA NNIGPERTEA IRAALGLKAG DAAFFVAGDP SKFVKFAGLA RTKVGEELNL 

       430        440        450        460        470        480 
IDKDQFALAW VVDFPMYEYN EDDKKVDFSH NPFSMPQGGM DALLGQDPLT IKAFQYDITC 

       490        500        510        520        530        540 
NGFEIASGGI RNHRPEAMVK AFEIAGYGEQ EVVDRFGGMY RAFQYGAPPH GGMAAGVDRI 

       550        560        570        580        590 
VMLLCGTNNL REISLFPMNQ RAEDLLMGAP SQVTPKQLRE LHIRLNLPEN 

« Hide

References

[1]"Complete sequence of Rhodopseudomonas palustris BisB5."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Pelletier D.A., Kyrpides N., Lykidis A., Oda Y., Harwood C.S., Richardson P.
Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: BisB5.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000283 Genomic DNA. Translation: ABE40174.1.
RefSeqYP_570075.1. NC_007958.1.

3D structure databases

ProteinModelPortalQ135R5.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ135R5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4023450.
GenomeReviewsGene locus RPD_2947 in contig CP000283_GR.
KEGGrpd:RPD_2947.
PATRIC23280949. VBIRhoPal120395_3037.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0173.
HOGENOMHBG396032.
OMAYQLDVEM.
ProtClustDBPRK00476.

Enzyme and pathway databases

BioCycRPAL316057:RPD_2947-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_RHOPS
AccessionPrimary (citable) accession number: Q135R5
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: October 31, 2006
Last modified: January 25, 2012
This is version 44 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