Skip Header

Contribute Send feedback
Read comments (?) or add your own

O83678 (SYG_TREPA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 87. 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
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
EC=6.1.1.14
Alternative name(s):
Glycyl-tRNA synthetase
Short name=GlyRS
Gene names
Name:glyQS
Synonyms:glyS
Ordered Locus Names:TP_0672
OrganismTreponema pallidum (strain Nichols) [Complete proteome] [HAMAP]
Taxonomic identifier243276 [NCBI]
Taxonomic lineageBacteria › Spirochaetes › Spirochaetales › Spirochaetaceae › Treponema ›

Protein attributes

Sequence length462 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the attachment of glycine to tRNA(Gly) By similarity. HAMAP-Rule MF_00253

Catalytic activity

ATP + glycine + tRNA(Gly) = AMP + diphosphate + glycyl-tRNA(Gly). HAMAP-Rule MF_00253

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_00253

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00253.

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: HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: HAMAP

glycine-tRNA ligase activity

Inferred from sequence or structural similarity. Source: UniProtKB

protein dimerization activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 462462Glycine--tRNA ligase HAMAP-Rule MF_00253
PRO_0000072986

Regions

Nucleotide binding175 – 1773ATP By similarity
Nucleotide binding185 – 1906ATP By similarity
Nucleotide binding259 – 2602ATP By similarity
Nucleotide binding308 – 3114ATP By similarity
Region190 – 1945Substrate binding By similarity
Region304 – 3085Substrate binding By similarity

Sites

Binding site941Substrate By similarity
Binding site1431Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
O83678 [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: D2E52E16B9CA61BE

FASTA46252,677
        10         20         30         40         50         60 
MEKIVGLCKR RGFVFPSSEI YGGQGGVWDY GPMGIALKNN IAHAWWQDMT RLHDHIVGLD 

        70         80         90        100        110        120 
AAILMHPNVW RTSGHVDHFS DPLVDCTVCK SRFRADQVAV PSAGGPCPQC GGALTGVRNF 

       130        140        150        160        170        180 
NLMFSTHMGP TDERASLLYL RPETAQGIYV NYKNVLQTTR LKVPFGIAQI GKAFRNEIVT 

       190        200        210        220        230        240 
KNFIFRTCEF EQMEMQFFVR PAEDTHWFEY WCAQRWAFYQ KYGVRMNHMR WRTHAAHELA 

       250        260        270        280        290        300 
HYARAACDIE YAFPMGFREL EGVHNRGDFD LTRHAQHSGK DLCYVDPDPN LDAAARRYVP 

       310        320        330        340        350        360 
CVVETSAGLT RCVLMFLCDA YTEEYVQAPN VAFSETTQTA DQEGAARTGE MRIVLRLHPA 

       370        380        390        400        410        420 
LSPTTVAFLP LVKKDGLVDL ARAVRDELRE DFACDFDAAG AIGKRYRRQD EVGTPFCVTV 

       430        440        450        460 
DYQSKEDDTV TVRLRDSMAQ RRVSRAFLAE FLRTEIKHYR RP

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE000520 Genomic DNA. Translation: AAC26570.1.
PIRC71296.
RefSeqNP_219109.1. NC_000919.1.

3D structure databases

ProteinModelPortalO83678.
ModBaseSearch...

Protein-protein interaction databases

STRING243276.TP0672.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC26570; AAC26570; TP_0672.
GeneID2611575.
KEGGtpa:TP0672.
PATRIC20531419. VBITrePal57110_0712.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0423.
KOK01880.
OMADLSYFDQ.
ProtClustDBPRK04173.

Enzyme and pathway databases

BioCycTPAL243276:GC1H-715-MONOMER.

Family and domain databases

Gene3D3.40.50.800. 1 hit.
HAMAPMF_00253_B. Gly_tRNA_synth_B.
InterProIPR002314. aa-tRNA-synt_IIb_cons-dom.
IPR006195. aa-tRNA-synth_II.
IPR004154. Anticodon-bd.
IPR027031. Gly-tRNA_synthase/POLG2.
IPR022961. Gly_tRNA_ligase_bac.
IPR002315. tRNA-synt_gly.
[Graphical view]
PANTHERPTHR10745. PTHR10745. 1 hit.
PfamPF03129. HGTP_anticodon. 1 hit.
PF00587. tRNA-synt_2b. 1 hit.
[Graphical view]
PRINTSPR01043. TRNASYNTHGLY.
SUPFAMSSF52954. Anticodon_bd. 1 hit.
TIGRFAMsTIGR00389. glyS_dimeric. 1 hit.
PROSITEPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYG_TREPA
AccessionPrimary (citable) accession number: O83678
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: November 1, 1998
Last modified: May 29, 2013
This is version 87 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

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents