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A4WJ22 (SYP_PYRAR) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 36. 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:Pars_0803
OrganismPyrobaculum arsenaticum (strain DSM 13514 / JCM 11321) [Complete proteome] [HAMAP]
Taxonomic identifier340102 [NCBI]
Taxonomic lineageArchaeaCrenarchaeotaThermoproteiThermoprotealesThermoproteaceaePyrobaculum

Protein attributes

Sequence length488 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 – 488488Proline--tRNA ligase HAMAP MF_01571
PRO_1000069194

Sequences

Sequence LengthMass (Da)Tools
A4WJ22 [UniParc].

Last modified May 29, 2007. Version 1.
Checksum: 9003248F746044CE

FASTA48856,562
        10         20         30         40         50         60 
MELIREARPH GREKLRANLI EWFHWLLREA ELYDVRYPVK GAYVWRPYGM RLRRHVEELI 

        70         80         90        100        110        120 
RRSHDETGHQ EVLFPVFIPY EFFGKESQHI RGFEKEVFWV SKGGEEGERL VLRPTSETAI 

       130        140        150        160        170        180 
MPMVKLWVHD YKDLPLRLYQ IVSVFRAETK MTHPMIRLRE ISMFKEAHTV HVDREDAERQ 

       190        200        210        220        230        240 
VREAVEIYKK IFDEMCLAYM INKRPDWDKF AGAEYTIAFD TVLPDGRTLQ IGTVHYLGTN 

       250        260        270        280        290        300 
FTRVFEVTYL AADGTRRLAH TTSYGISERS IAAMLITHGD DAGTVLPPRL APIQVVIVPI 

       310        320        330        340        350        360 
FYGEEEAASV ISYAREVEKA LREAGMRVHI DDRPDKTPGW KFYFWELKGV PLRVEVGKRD 

       370        380        390        400        410        420 
LEKRQVVITR RDTLEKYAVG LGELVDAVRG LMRTVEENLR RRAWEELRSR IVRAETVEAA 

       430        440        450        460        470        480 
KAAIREGKVV EVPWSGDNDC GIKLKDLVGA DALGVPLDSD ASVGGFDLRD LACGEKRAEF 


WLRLSERY 

« Hide

References

[1]"Complete sequence of Pyrobaculum arsenaticum DSM 13514."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N. expand/collapse author list , Cozen A.E., Fitz-Gibbon S.T., House C.H., Saltikov C., Lowe T.M., Richardson P.
Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 13514 / JCM 11321.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000660 Genomic DNA. Translation: ABP50389.1.
RefSeqYP_001153041.1. NC_009376.1.

3D structure databases

ProteinModelPortalA4WJ22.
ModBaseSearch...

Protein-protein interaction databases

STRINGA4WJ22.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5055342.
GenomeReviewsGene locus Pars_0803 in contig CP000660_GR.
KEGGpas:Pars_0803.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGarNOG04466.
HOGENOMHBG334108.
OMAKFAEYEL.
PhylomeDBA4WJ22.
ProtClustDBPRK08661.

Enzyme and pathway databases

BioCycPARS340102:PARS_0803-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_PYRAR
AccessionPrimary (citable) accession number: A4WJ22
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: May 29, 2007
Last modified: January 25, 2012
This is version 36 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