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Q215P7 (SYD_RHOPB) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 46. 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:RPC_2336
OrganismRhodopseudomonas palustris (strain BisB18) [Complete proteome] [HAMAP]
Taxonomic identifier316056 [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_1000006740

Sequences

Sequence LengthMass (Da)Tools
Q215P7 [UniParc].

Last modified April 18, 2006. Version 1.
Checksum: 6EFA306B59BB5E06

FASTA59066,795
        10         20         30         40         50         60 
MHRYRSHTCG ALRESDIDQT VRVSGWCHRI RDHGGLLFID LRDHYGLTQC VADPDSPAFK 

        70         80         90        100        110        120 
DAEKLRAEWV VRIDGKVRRR PEGTDNNDLP TGQVEIFITE IEVLGPAGEL PLPVFGEQEY 

       130        140        150        160        170        180 
PEDIRLKYRF LDLRREKLHQ NIMTRGAIVD SMRKRMKEQG FFEFQTPILT ASSPEGARDF 

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

       250        260        270        280        290        300 
MSFITQDDVF AAMEPVITGV FEDFAKGKPV TKSWPRIAYA DSLKKYGTDK PDLRNPIEMQ 

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

       370        380        390        400        410        420 
EGGEGAGPLA NNIGPERTAA IREQLGLKAG DAAFFVAGDP SKFVRFAGLA RTRLGEELNL 

       430        440        450        460        470        480 
VDKERFELAW IVDFPMYEYN EDDKKVDFSH NPFSMPQGGM DALLNQDPLT IKAFQYDITC 

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

       550        560        570        580        590 
VMLLCGTNNL REISLFPMNQ RAEDLLMGAP SDVTPKQLRE LHIRLNLPEN 

« Hide

References

[1]"Complete sequence of Rhodopseudomonas palustris BisB18."
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., Anderson I., 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: BisB18.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000301 Genomic DNA. Translation: ABD87889.1.
RefSeqYP_532208.1. NC_007925.1.

3D structure databases

ProteinModelPortalQ215P7.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ215P7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3972177.
GenomeReviewsGene locus RPC_2336 in contig CP000301_GR.
KEGGrpc:RPC_2336.
PATRIC23269398. VBIRhoPal29154_2398.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0173.
HOGENOMHBG396032.
OMAYQLDVEM.
PhylomeDBQ215P7.
ProtClustDBPRK00476.

Enzyme and pathway databases

BioCycRPAL316056:RPC_2336-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_RHOPB
AccessionPrimary (citable) accession number: Q215P7
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: April 18, 2006
Last modified: January 25, 2012
This is version 46 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