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Reviewed, UniProtKB/Swiss-Prot Q8A988 (SYP_BACTN)

Last modified November 3, 2009. Version 48. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Prolyl-tRNA synthetase
    EC=6.1.1.15
Alternative name(s):
    Proline--tRNA ligase
      Short name=ProRS
Gene names
Name: proS
Ordered Locus Names: BT_0929
OrganismBacteroides thetaiotaomicron [Complete proteome] [HAMAP]
Taxonomic identifier818 [NCBI]
Taxonomic lineageBacteriaBacteroidetesBacteroidiaBacteroidalesBacteroidaceaeBacteroides

Protein attributes

Sequence length497 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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) By similarity.

Catalytic activity

ATP + L-proline + tRNA(Pro) = AMP + diphosphate + L-prolyl-tRNA(Pro). HAMAP MF_01571

Subunit structure

Homodimer By similarity.

Subcellular location

Cytoplasm By similarity.

Domain

Consists of three domains: the N-terminal catalytic domain, the anticodon-binding domain and the C-terminal extension By similarity.

Sequence similarities

Belongs to the class-II aminoacyl-tRNA synthetase family. ProS type 3 subfamily.

Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionAminoacyl-tRNA synthetase
Ligase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processprolyl-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

proline-tRNA ligase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 497497Prolyl-tRNA synthetase HAMAP MF_01571
PRO_0000249123

Sequences

Sequence LengthMass (Da)Tools
Q8A988-1 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 5960D3C9344E11FA

FASTA49756,848
        10         20         30         40         50         60 
MAKELKDLTK RSENYSQWYN DLVVKADLAE QSAVRGCMVI KPYGYAIWEK MQRQLDDMFK 

        70         80         90        100        110        120 
ETGHVNAYFP LLIPKSFLSR EAEHVEGFAK ECAVVTHYRL KNAEDGSGVV VDPAAKLEEE 

       130        140        150        160        170        180 
LIIRPTSETI IWNTYKNWIQ SYRDLPILCN QWANVFRWEM RTRLFLRTAE FLWQEGHTAH 

       190        200        210        220        230        240 
ATREEAEEEA IRMLNVYGEF AEKYMAVPVV KGVKSANERF AGALDTYTIE AMMQDGKALQ 

       250        260        270        280        290        300 
SGTSHFLGQN FAKAFDVQFV NKENKMEYVW ATSWGVSTRL MGALIMTHSD DNGLVLPPHL 

       310        320        330        340        350        360 
APIQVVIVPI YKNDEQLKQI DAKVEGIVAK LKALGISVKY DNADNKRPGF KFADYELKGV 

       370        380        390        400        410        420 
PVRLVMGGRD LENNTMEVMR RDTLEKETVT CDGIETYVQK LLEEIQANIY KKALDYRNSK 

       430        440        450        460        470        480 
ITTVDTYEEF KEKIEEGGFI LAHWDGTTET EEKIKEDTKA TIRCIPFDSY VEGDKEPGKC 

       490 
MVTGKPSACR VVFARSY 

« Hide

References

[1]"A genomic view of the human-Bacteroides thetaiotaomicron symbiosis."
Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K., Chiang H.C., Hooper L.V., Gordon J.I.
Science 299:2074-2076(2003) [PubMed: 12663928] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482.

Cross-references

Sequence databases

AE015928 Genomic DNA. Translation: AAO76036.1.
RefSeqNP_809842.1.

3D structure databases

HSSPHSSP built from PDB template 1HC7 based on UniProtKB Q93N97.
ModBaseSearch...

Genome annotation databases

GeneID1073381.
GenomeReviewsGene locus BT_0929 in contig AE015928_GR.
KEGGbth:BT_0929.
NMPDRfig|226186.1.peg.929.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ8A988.
OMACIEAMMQ.

Enzyme and pathway databases

BioCycBTHE226186:BT_0929-MON.
BRENDA6.1.1.15. 21018.

Family and domain databases

HAMAPMF_01571.
[Tree]
InterProIPR002314. aa-tRNA-synt_IIb_cons-reg.
IPR006195. aa-tRNA-synth_II_cons-reg.
IPR004154. Anticodon_bd.
IPR004499. Pro-tRNA-synth_IIa_pro-type.
IPR016061. Pro-tRNA_synth_II_C.
[Graphical view]
Gene3DG3DSA:3.40.50.800. Anticodon_bd. 1 hit.
G3DSA:3.30.110.30. Pro-tRNA-synth_II_C_arc/euk. 1 hit.
PANTHERPTHR11451:SF6. ProS_fam_I. 1 hit.
PfamPF03129. HGTP_anticodon. 1 hit.
PF09180. ProRS-C_1. 1 hit.
PF00587. tRNA-synt_2b. 1 hit.
[Graphical view]
TIGRFAMsTIGR00408. proS_fam_I. 1 hit.
PROSITEPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYP_BACTN
AccessionPrimary (citable) accession number: Q8A988
Entry history
Integrated into UniProtKB/Swiss-Prot: September 5, 2006
Last sequence update: June 1, 2003
Last modified: November 3, 2009
This is version 48 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents