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B0R3A3 (SYP_HALS3) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 30. 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:OE1595F
OrganismHalobacterium salinarum (strain ATCC 29341 / DSM 671 / R1) [Complete proteome] [HAMAP]
Taxonomic identifier478009 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaHalobacteriaHalobacterialesHalobacteriaceaeHalobacterium

Protein attributes

Sequence length501 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 – 501501Proline--tRNA ligase HAMAP MF_01571
PRO_1000215565

Sequences

Sequence LengthMass (Da)Tools
B0R3A3 [UniParc].

Last modified April 8, 2008. Version 1.
Checksum: 6ECAB1AB82DF1D03

FASTA50156,123
        10         20         30         40         50         60 
MSDDDQELGI TESKEHSPGD WYAEVVQKAG LADYAPMGGF IVTRPRGYAL WEAIQDNLDG 

        70         80         90        100        110        120 
WFKDTGVENA YFPMFIPEDY LEREKDIVEG FDPEVAWVTQ GGHDDLDQRL AVRPTSESII 

       130        140        150        160        170        180 
APYLSQWVRS HRDLPLRVNQ WNSVVRWEAT ETKPFFRTKE FLWQEGHTAH ATDEAAWAET 

       190        200        210        220        230        240 
TLRLDQYHRL YEDVLGIPVL RGRKPDHDKF PGADTTMSVE ALMPDGKSVQ GGTSHHLGQS 

       250        260        270        280        290        300 
FADAFDITFA DEDEAERTAY TTSWGLSWRA IGALVMSHSD DQGLVLPPTV APKQVVIVPI 

       310        320        330        340        350        360 
WQEDTKDDVE QYGAEIAAEL EAQGVRVHFD DRDGRNPGFK FNEWELNGVP VRFEIGPNEV 

       370        380        390        400        410        420 
EDDEVTVVHR PDGESTVEDR AAIADRVHDH LDEVYDKLYD AAADRLAENV READNRADIL 

       430        440        450        460        470        480 
GTIGQHGGYV KAPWCGDQDC EAEIKDQIAA EIVMVPLGED SAARAASELE GERVPEPDHD 

       490        500 
GEDCAICGDE ATRTAYFAKS Y 

« Hide

References

[1]"Evolution in the laboratory: the genome of Halobacterium salinarum strain R1 compared to that of strain NRC-1."
Pfeiffer F., Schuster S.C., Broicher A., Falb M., Palm P., Rodewald K., Ruepp A., Soppa J., Tittor J., Oesterhelt D.
Genomics 91:335-346(2008) [PubMed: 18313895] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 29341 / DSM 671 / R1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM774415 Genomic DNA. Translation: CAP13217.1.
RefSeqYP_001688566.1. NC_010364.1.

3D structure databases

ProteinModelPortalB0R3A3.
ModBaseSearch...

Protein-protein interaction databases

STRINGB0R3A3.

Proteomic databases

PRIDEB0R3A3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5952517.
GenomeReviewsGene locus OE1595F in contig AM774415_GR.
KEGGhsl:OE1595F.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG334108.
OMAKFAEYEL.
PhylomeDBB0R3A3.
ProtClustDBPRK08661.

Enzyme and pathway databases

BioCycHSAL478009:OE1595F-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.
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_HALS3
AccessionPrimary (citable) accession number: B0R3A3
Entry history
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: April 8, 2008
Last modified: January 25, 2012
This is version 30 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