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A5UJW4 (SYP_METS3) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 35. 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:Msm_0287
OrganismMethanobrevibacter smithii (strain PS / ATCC 35061 / DSM 861) [Complete proteome] [HAMAP]
Taxonomic identifier420247 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanobacteriaMethanobacterialesMethanobacteriaceaeMethanobrevibacter

Protein attributes

Sequence length469 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 – 469469Proline--tRNA ligase HAMAP MF_01571
PRO_0000318774

Sequences

Sequence LengthMass (Da)Tools
A5UJW4 [UniParc].

Last modified July 10, 2007. Version 1.
Checksum: 8768D9B633C82B0F

FASTA46954,052
        10         20         30         40         50         60 
MVENFSEWFH DILEEANITD SRYPIKGMAV WMPYGFQIRK YTTNLIKEVY DRDHEEVLFP 

        70         80         90        100        110        120 
LLVPEAELAK EGLHVKGFED EVYWVTHGGK TQLNEKLALR PTSETSIYPM YSLWIRSHID 

       130        140        150        160        170        180 
LPLKYYQIVN TFRYETKHTR PLIRVREITT FKEAHTAHAS KEEADIQVQE HIENYKEIFD 

       190        200        210        220        230        240 
TLGIPYTLTK RPEWDKFPGA DYTMAFDAIM PDGKTLQIGT IHNLGQTFAK TFDITFEDKD 

       250        260        270        280        290        300 
GEHKLVYQTC AGLSDRVIAS AIGIHGDEKG LRLPPEISPK QITIIPILFK KGKEEVLAKC 

       310        320        330        340        350        360 
EELKKEFEAA GLRVNIDNRD IRPGKKFYDW ELKGTPIKLE LGPRDLENNK TIAMRRDQLE 

       370        380        390        400        410        420 
KIELDLDENL VSNVIRLIDE LNENLAESAK EFHTDHIKFA SDIDEVRKLI EEGNVVAVNW 

       430        440        450        460 
CGDTDCGEKI EEITGYSVLG IYEELEEAGK KCILSDEDAK YVALIAKTY 

« Hide

References

[1]"Genomic and metabolic adaptations of Methanobrevibacter smithii to the human gut."
Samuel B.S., Hansen E.E., Manchester J.K., Coutinho P.M., Henrissat B., Fulton R., Latreille P., Kim K., Wilson R.K., Gordon J.I.
Proc. Natl. Acad. Sci. U.S.A. 104:10643-10648(2007) [PubMed: 17563350] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PS / ATCC 35061 / DSM 861.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000678 Genomic DNA. Translation: ABQ86492.1.
RefSeqYP_001272860.1. NC_009515.1.

3D structure databases

ProteinModelPortalA5UJW4.
SMRA5UJW4. Positions 4-469.
ModBaseSearch...

Protein-protein interaction databases

STRINGA5UJW4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5216746.
GenomeReviewsGene locus Msm_0287 in contig CP000678_GR.
KEGGmsi:Msm_0287.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGarNOG04466.
HOGENOMHBG334108.
OMAKFAEYEL.
ProtClustDBPRK08661.

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.
IPR002316. Pro-tRNA-synth_IIa.
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]
PRINTSPR01046. TRNASYNTHPRO.
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_METS3
AccessionPrimary (citable) accession number: A5UJW4
Entry history
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: July 10, 2007
Last modified: January 25, 2012
This is version 35 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