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A1BGZ4 (SYD_CHLPD) 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:Cpha266_1650
OrganismChlorobium phaeobacteroides (strain DSM 266) [Complete proteome] [HAMAP]
Taxonomic identifier290317 [NCBI]
Taxonomic lineageBacteriaChlorobiChlorobiaChlorobialesChlorobiaceaeChlorobium/Pelodictyon groupChlorobium

Protein attributes

Sequence length606 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 – 606606Aspartate--tRNA ligase HAMAP MF_00044_B
PRO_1000057300

Sequences

Sequence LengthMass (Da)Tools
A1BGZ4 [UniParc].

Last modified January 23, 2007. Version 1.
Checksum: 3259DAB6BB92CCFE

FASTA60668,832
        10         20         30         40         50         60 
MSRAAGSTET LKNRFRTDYC GLLNPEVEHQ SVKLGGWVHR KRDHGGLIFI DLRDHTGICQ 

        70         80         90        100        110        120 
IVIQPEEQQL FAKAEQLHLE SVICIEGTVV RRSPGAVNPR IPSGEIEVVA AGISVESSAH 

       130        140        150        160        170        180 
PLPFPVADEV QTSEELRLKY RFIDLRRDKI HENIIFRSRL TAAIRRYLEE KSFIEIQTPI 

       190        200        210        220        230        240 
LTSSSPEGAR DFLVPSRLHP GKFYALPQAP QQFKQLLMVS GFPRYFQIAP CFRDEDARAD 

       250        260        270        280        290        300 
RSPGEFYQLD MEMAFIEQDD LFEILEGMFS HLTGSMSTKR IREFPFPRIS FRDVMNRYGT 

       310        320        330        340        350        360 
DKPDLRIPLE ISDVTHLFLQ SSFKVFAANT KEGCCVKAML VKGRGNESRL FYDKAEKRAK 

       370        380        390        400        410        420 
ELGSGGLAYI QFREDGPKGP LVKFLSGEEL AALRELLGVE VGDVVFFGAG KWEQTCRIMG 

       430        440        450        460        470        480 
GMRTYFSDLF TLDRDELAFC WVVDFPMYEY NEDQKKIDFS HNPFSMPQGE MDALESMPPL 

       490        500        510        520        530        540 
NILAYQYDIV CNGIELSSGA IRNHRPDIMY KAFEIAGYTK EDVDSRFGHM IEAFKLGAPP 

       550        560        570        580        590        600 
HGGIAPGLDR LVMILRDEQN IREVIAFPMN QQAQDLMMGS PSEVTPIQLR ELHLQVELPK 


KAEAKP 

« Hide

References

[1]"Complete sequence of Chlorobium phaeobacteroides DSM 266."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Pitluck S., Goltsman E., Schmutz J., Larimer F., Land M., Hauser L., Mikhailova N., Li T., Overmann J., Bryant D.A., Richardson P.
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 266.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000492 Genomic DNA. Translation: ABL65671.1.
RefSeqYP_912095.1. NC_008639.1.

3D structure databases

ProteinModelPortalA1BGZ4.
ModBaseSearch...

Protein-protein interaction databases

STRINGA1BGZ4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4571030.
GenomeReviewsGene locus Cpha266_1650 in contig CP000492_GR.
KEGGcph:Cpha266_1650.
NMPDRfig|290317.7.peg.1731.
PATRIC21391568. VBIChlPha122104_1948.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0173.
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_CHLPD
AccessionPrimary (citable) accession number: A1BGZ4
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: January 23, 2007
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