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Q64TJ6 (SYP_BACFR) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 52. 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:
Proline--tRNA ligase

EC=6.1.1.15
Alternative name(s):
Prolyl-tRNA synthetase
Short name=ProRS
Gene names
Name:proS
Ordered Locus Names:BF2434
OrganismBacteroides fragilis (strain YCH46) [Complete proteome] [HAMAP]
Taxonomic identifier295405 [NCBI]
Taxonomic lineageBacteriaBacteroidetesBacteroidiaBacteroidalesBacteroidaceaeBacteroides

Protein attributes

Sequence length497 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) By similarity. HAMAP MF_01571

Catalytic activity

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

Subunit structure

Homodimer By similarity. HAMAP MF_01571

Subcellular location

Cytoplasm By similarity HAMAP MF_01571.

Domain

Consists of three domains: the N-terminal catalytic domain, the anticodon-binding domain and the C-terminal extension By similarity. HAMAP MF_01571

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: InterPro

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

proline-tRNA ligase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 497497Proline--tRNA ligase HAMAP MF_01571
PRO_0000249121

Sequences

Sequence LengthMass (Da)Tools
Q64TJ6 [UniParc].

Last modified October 25, 2004. Version 1.
Checksum: DEAD2CB76F1284E0

FASTA49756,954
        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 IRMLNVYAEF AEKYMAVPVV KGVKSANERF AGALDTYTIE AMMQDGKALQ 

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

       310        320        330        340        350        360 
APIQVVIVPI YKNDEQLKLI DAKVEGIVAR LKQLGISVKY DNADNKRPGF KFADYELKGV 

       370        380        390        400        410        420 
PVRLVMGGRD LENNTMEVMR RDTLEKETVT CDGIETYVQN LLEEIQANIY KKARTYRDSR 

       430        440        450        460        470        480 
ITTVDSYDEF KEKIEEGGFI LAHWDGTVET EEKIKEETKA TIRCIPFESF VEGDKEPGKC 

       490 
MVTGKPSACR VIFARSY 

« Hide

References

[1]"Genomic analysis of Bacteroides fragilis reveals extensive DNA inversions regulating cell surface adaptation."
Kuwahara T., Yamashita A., Hirakawa H., Nakayama H., Toh H., Okada N., Kuhara S., Hattori M., Hayashi T., Ohnishi Y.
Proc. Natl. Acad. Sci. U.S.A. 101:14919-14924(2004) [PubMed: 15466707] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: YCH46.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP006841 Genomic DNA. Translation: BAD49183.1.
RefSeqYP_099717.1. NC_006347.1.

3D structure databases

HSSPHSSP built from PDB template 1NJ1 based on UniProtKB O26708.
ProteinModelPortalQ64TJ6.
SMRQ64TJ6. Positions 6-497.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3083839.
GenomeReviewsGene locus BF2434 in contig AP006841_GR.
KEGGbfr:BF2434.
PATRIC21050497. VBIBacFra17906_2352.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG334108.
OMAKFAEYEL.
PhylomeDBQ64TJ6.
ProtClustDBPRK08661.

Enzyme and pathway databases

BioCycBFRA295405:BF2434-MONOMER.

Family and domain databases

HAMAPMF_01571. Pro_tRNA_synth_type3.
[Tree]
InterProIPR002314. aa-tRNA-synt_IIb_cons-dom.
IPR006195. aa-tRNA-synth_II.
IPR004154. Anticodon-bd.
IPR004499. Pro-tRNA-synth_IIa_arc-type.
IPR017449. Pro-tRNA_synth_II.
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.
KOK01881.
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]
SMARTSM00946. ProRS-C_1. 1 hit.
[Graphical view]
SUPFAMSSF52954. Anticodon_bd. 1 hit.
SSF64586. Pro-tRNA_synth_II_C. 1 hit.
TIGRFAMsTIGR00408. ProS_fam_I. 1 hit.
PROSITEPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYP_BACFR
AccessionPrimary (citable) accession number: Q64TJ6
Entry history
Integrated into UniProtKB/Swiss-Prot: September 5, 2006
Last sequence update: October 25, 2004
Last modified: January 25, 2012
This is version 52 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