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A8AZA7 (SYP_STRGC) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 42. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Proline--tRNA ligase

EC=6.1.1.15
Alternative name(s):
Prolyl-tRNA synthetase
Short name=ProRS
Gene names
Name:proS
Ordered Locus Names:SGO_1851
OrganismStreptococcus gordonii (strain Challis / ATCC 35105 / CH1 / DL1 / V288) [Complete proteome] [HAMAP]
Taxonomic identifier29390 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus

Protein attributes

Sequence length616 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the attachment of proline to tRNA(Pro) in a two-step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro). As ProRS can inadvertently accommodate and process non-cognate amino acids such as alanine and cysteine, to avoid such errors it has two additional distinct editing activities against alanine. One activity is designated as 'pretransfer' editing and involves the tRNA(Pro)-independent hydrolysis of activated Ala-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Ala-tRNA(Pro). The misacylated Cys-tRNA(Pro) is not edited by ProRS By similarity. HAMAP-Rule MF_01569

Catalytic activity

ATP + L-proline + tRNA(Pro) = AMP + diphosphate + L-prolyl-tRNA(Pro). HAMAP-Rule MF_01569

Subunit structure

Homodimer By similarity.

Subcellular location

Cytoplasm By similarity.

Domain

Consists of three domains: the N-terminal catalytic domain, the editing domain and the C-terminal anticodon-binding domain By similarity. HAMAP-Rule MF_01569

Sequence similarities

Belongs to the class-II aminoacyl-tRNA synthetase family. ProS type 1 subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 616616Proline--tRNA ligase HAMAP-Rule MF_01569
PRO_1000087859

Sequences

Sequence LengthMass (Da)Tools
A8AZA7 [UniParc].

Last modified October 23, 2007. Version 1.
Checksum: 1CE99E45D366006B

FASTA61668,509
        10         20         30         40         50         60 
MKQSKMLIPT LREMPSDAQV ISHALLLRAG YVRQVSAGVY SYLPLANRVI EKAKNIMRQE 

        70         80         90        100        110        120 
FEKIGAVEML APALLSADLW RESGRYETYG DDLFKLKNRE GSDFILGPTH EETFTALVRD 

       130        140        150        160        170        180 
SVKSYKQLPL NLYQIQPKYR DEKRPRNGLL RTREFIMKDA YSFHANYDSL DVTYDEYKSA 

       190        200        210        220        230        240 
YEKIFTRSEI DFKAIIGDGG AMGGKDSQEF MAITPDRTDL DRWLVLDKSV ASLDEIPADV 

       250        260        270        280        290        300 
LEAIKAELSN WMVSGEDTIA YSSESSYAAN LEMATNEYKP SNRVVAETEL VRVETPNCKT 

       310        320        330        340        350        360 
IDEVAAFLQV SEEQTIKTLV YIADEKPVVA LLVGNDQLNE VKLKNHLGAD FFEAATEAEV 

       370        380        390        400        410        420 
QELFGANFGS LGPVNLPEEV TIIADRKVQD LSNAVAGANE DGYHLTGVNP GRDFTAEYVD 

       430        440        450        460        470        480 
IREVREGEIS PDGNGVLKFA RGIEIGHIFK LGTRYSDSMN ATVLDENGRA VPLVMGCYGI 

       490        500        510        520        530        540 
GVSRLLSAVM EQHARLFVNK TPKGEYRYAW GINFPKELAP FDVHLIPVNV KDEESLALTD 

       550        560        570        580        590        600 
KIEESLVGAG YEVLVDDRNE RVGVKFSDSD LIGLPIRVTV GKKAAEGIVE VKIKASGDTI 

       610 
EVHADNLIET LSILTK 

« Hide

References

[1]"Genome-wide transcriptional changes in Streptococcus gordonii in response to competence signaling peptide."
Vickerman M.M., Iobst S., Jesionowski A.M., Gill S.R.
J. Bacteriol. 189:7799-7807(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Challis / ATCC 35105 / CH1 / DL1 / V288.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000725 Genomic DNA. Translation: ABV10446.1.
RefSeqYP_001451117.1. NC_009785.1.

3D structure databases

ProteinModelPortalA8AZA7.
SMRA8AZA7. Positions 1-614.
ModBaseSearch...

Protein-protein interaction databases

STRING467705.SGO_1851.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABV10446; ABV10446; SGO_1851.
GeneID5599745.
KEGGsgo:SGO_1851.
PATRIC19661650. VBIStrGor124371_1818.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0442.
HOGENOMHOG000076893.
KOK01881.
OMAIQPAELW.
ProtClustDBPRK09194.

Enzyme and pathway databases

BioCycSGOR467705:GH3R-1893-MONOMER.

Family and domain databases

Gene3D3.40.50.800. 1 hit.
3.90.960.10. 1 hit.
HAMAPMF_01569. Pro_tRNA_synth_type1.
InterProIPR002314. aa-tRNA-synt_IIb_cons-dom.
IPR006195. aa-tRNA-synth_II.
IPR004154. Anticodon-bd.
IPR002316. Pro-tRNA-ligase_IIa.
IPR004500. Pro-tRNA-synth_IIa_bac-type.
IPR023717. Pro-tRNA-Synthase_IIa_type1.
IPR007214. YbaK/aa-tRNA-synth-assoc-dom.
[Graphical view]
PANTHERPTHR11451:SF3. PTHR11451:SF3. 1 hit.
PfamPF03129. HGTP_anticodon. 1 hit.
PF00587. tRNA-synt_2b. 1 hit.
PF04073. YbaK. 1 hit.
[Graphical view]
PRINTSPR01046. TRNASYNTHPRO.
SUPFAMSSF52954. Anticodon_bd. 1 hit.
SSF55826. YbaK/aa-tRNA-synth-assoc-reg. 1 hit.
TIGRFAMsTIGR00409. proS_fam_II. 2 hits.
PROSITEPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYP_STRGC
AccessionPrimary (citable) accession number: A8AZA7
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: October 23, 2007
Last modified: May 1, 2013
This is version 42 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