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A4J7D0 (SYGA_DESRM) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 32. 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:
Glycine--tRNA ligase alpha subunit

EC=6.1.1.14
Alternative name(s):
Glycyl-tRNA synthetase alpha subunit
Short name=GlyRS
Gene names
Name:glyQ
Ordered Locus Names:Dred_2473
OrganismDesulfotomaculum reducens (strain MI-1) [Complete proteome] [HAMAP]
Taxonomic identifier349161 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesPeptococcaceaeDesulfotomaculum

Protein attributes

Sequence length295 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

ATP + glycine + tRNA(Gly) = AMP + diphosphate + glycyl-tRNA(Gly). HAMAP MF_00254

Subunit structure

Tetramer of two alpha and two beta subunits By similarity.

Subcellular location

Cytoplasm HAMAP MF_00254.

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 processglycyl-tRNA aminoacylation

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

glycine-tRNA ligase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 295295Glycine--tRNA ligase alpha subunit HAMAP MF_00254
PRO_1000071876

Sequences

Sequence LengthMass (Da)Tools
A4J7D0 [UniParc].

Last modified May 1, 2007. Version 1.
Checksum: 5372682A9D910936

FASTA29533,838
        10         20         30         40         50         60 
MNFQELILTL NKFWAEQNCI IQQPYDIEKG AGTMNPATFL RALGPEPWRV AYVEPSRRPT 

        70         80         90        100        110        120 
DGRYGENPNR LQHYFQYQVI LKPSPDDVIP VYLDSLRAIG IDPDKHDIRF VEDNWESPTL 

       130        140        150        160        170        180 
GAWGLGWEVW LDGMEVTQFT YFQQCGGIDC HPVSAEITYG LERLAMFIQQ KDSVYDITWV 

       190        200        210        220        230        240 
GDITYGDVYH QNEVEQSGYN FEVANTEMLF DLFDMYEAEA NHILEKGLVL PAYDYVLKCS 

       250        260        270        280        290 
HTFNLLDARG AISVSERQGF IARVRQMARA CAHAYVEQRE KLGFPLLKKG GNING 

« Hide

References

[1]"Complete sequence of Desulfotomaculum reducens MI-1."
US DOE Joint Genome Institute
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., Sims D., Brettin T., Bruce D., Han C., Tapia R., Schmutz J., Larimer F. expand/collapse author list , Land M., Hauser L., Kyrpides N., Kim E., Tebo B.M., Richardson P.
Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MI-1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000612 Genomic DNA. Translation: ABO50983.1.
RefSeqYP_001113808.1. NC_009253.1.

3D structure databases

ProteinModelPortalA4J7D0.
SMRA4J7D0. Positions 1-277.
ModBaseSearch...

Protein-protein interaction databases

STRINGA4J7D0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4957152.
GenomeReviewsGene locus Dred_2473 in contig CP000612_GR.
KEGGdrm:Dred_2473.
PATRIC21731301. VBIDesRed82656_2707.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0752.
HOGENOMHBG285316.
OMACRRPTDG.
PhylomeDBA4J7D0.
ProtClustDBPRK09348.

Enzyme and pathway databases

BioCycDRED349161:DRED_2473-MONOMER.

Family and domain databases

HAMAPMF_00254. Gly_tRNA_synth_alpha.
[Tree]
InterProIPR006194. Gly-tRNA-synth_II_heterodimer.
IPR002310. Gly-tRNA_synth_IIc_asu.
[Graphical view]
KOK01878.
PfamPF02091. tRNA-synt_2e. 1 hit.
[Graphical view]
PRINTSPR01044. TRNASYNTHGA.
TIGRFAMsTIGR00388. GlyQ. 1 hit.
PROSITEPS50861. AA_TRNA_LIGASE_II_GLYAB. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYGA_DESRM
AccessionPrimary (citable) accession number: A4J7D0
Entry history
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: May 1, 2007
Last modified: January 25, 2012
This is version 32 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