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B1Y963 (SYP_THENV) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 26. 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:Tneu_1366
OrganismThermoproteus neutrophilus (strain DSM 2338 / JCM 9278 / V24Sta) [Complete proteome] [HAMAP]
Taxonomic identifier444157 [NCBI]
Taxonomic lineageArchaeaCrenarchaeotaThermoproteiThermoprotealesThermoproteaceaeThermoproteus

Protein attributes

Sequence length487 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 – 487487Proline--tRNA ligase HAMAP MF_01571
PRO_1000215581

Sequences

Sequence LengthMass (Da)Tools
B1Y963 [UniParc].

Last modified May 20, 2008. Version 1.
Checksum: C181341BBA32F10F

FASTA48756,465
        10         20         30         40         50         60 
MELLRSARPH PKEKLKNVIE WFHWLLREAE LYDVRYPVKG AYVWRPYGMK LRRNVEELIR 

        70         80         90        100        110        120 
RVHDETGHEE VLFPVFIPYE FFGKESQHIR GFEKEVFWVS KGGEGGERLV LRPTSETAIM 

       130        140        150        160        170        180 
PMVKLWIQDY KDLPLRLYQI VSVFRAETKM THPMIRLREI SMFKEAHTVH VDREDAERQV 

       190        200        210        220        230        240 
REAVEIYKRI FDEMCLAYMI NKRPDWDKFA GAEYTIAFDT VLPDGRTLQI GTAHYLGTNF 

       250        260        270        280        290        300 
TRVFEVTYLD ADGTRKLAHT TSYGISERSI AAMLITHGDD GGTTLPPKLA PIQIAVVPIY 

       310        320        330        340        350        360 
YSDEEMPLVM KFVEEVVAAL KGAGLRLHVD DRRDKTPGWK FYYWELKGVP LRLEVGKRDV 

       370        380        390        400        410        420 
EKRQVVVTRR DTLEKYAVAL GELVDAVREL MKAVEDNLRR RAWEELRSKI VKVQSLEEAK 

       430        440        450        460        470        480 
KAIKEGKVVE VPWSGDNQCG MKIQELLGAD ALGIPMDSEA SIGGYDARDL ACGERRAELW 


LRLSERY 

« Hide

References

[1]"Complete sequence of Thermoproteus neutrophilus V24Sta."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L. expand/collapse author list , Kyrpides N., Mikhailova N., Biddle J.F., Zhang Z., Fitz-Gibbon S.T., Lowe T.M., Saltikov C., House C.H., Richardson P.
Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 2338 / JCM 9278 / V24Sta.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001014 Genomic DNA. Translation: ACB40292.1.
RefSeqYP_001794738.1. NC_010525.1.

3D structure databases

ProteinModelPortalB1Y963.
ModBaseSearch...

Protein-protein interaction databases

STRINGB1Y963.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID6164516.
GenomeReviewsGene locus Tneu_1366 in contig CP001014_GR.
KEGGtne:Tneu_1366.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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_THENV
AccessionPrimary (citable) accession number: B1Y963
Entry history
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: May 20, 2008
Last modified: January 25, 2012
This is version 26 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