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A1RYD8 (SYP_THEPD) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 33. 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:Tpen_0817
OrganismThermofilum pendens (strain Hrk 5)
Taxonomic identifier368408 [NCBI]
Taxonomic lineageArchaeaCrenarchaeotaThermoproteiThermoprotealesThermofilaceaeThermofilum

Protein attributes

Sequence length482 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
Reference 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 – 482482Proline--tRNA ligase HAMAP MF_01571
PRO_0000288424

Sequences

Sequence LengthMass (Da)Tools
A1RYD8 [UniParc].

Last modified February 6, 2007. Version 1.
Checksum: DE03235CC18F4C5E

FASTA48256,335
        10         20         30         40         50         60 
MSEQGITVSK SEDFSEWYSQ VLSKAGLVDL RYNVQGFVVH KPWLMRIIKA IYRFFEEELE 

        70         80         90        100        110        120 
KTGHEPVLFP LVIPEENFEK EKEHVEGFKP EVFWVTQAGD EKLERRLALR PTSETAFYYM 

       130        140        150        160        170        180 
YSYWIQSWRD LPLKLYQSVS VYRNEKNTRP LIRGREFLWI EAHDAFATHE EALNQIREDM 

       190        200        210        220        230        240 
ENSRKVIWEK LGIPFLFLRR PPWDKFSGAE DTYAADTIMP DGRVLQISST HDLGQRFAKA 

       250        260        270        280        290        300 
FNVTFLDKDG KRKYVWQTCY GPGIWRITAA LIAIHGDDKG LVLPMNVAPI QVVIVPIYYK 

       310        320        330        340        350        360 
ESDKERVLEK CRKLEAMIRE AGYRVYLDAR EEYTPGWKFN DWELKGVPVR LEVGVREVET 

       370        380        390        400        410        420 
GTVTVFRRDL RVKEKVADSE LISHIRKLEN DILEELKRRA KEFFESRIVT ATRREEVEEA 

       430        440        450        460        470        480 
LRSGKMVKMP FCGREECADD LKEATDGGKV RGTEIDFKEG DYGRCAWCGA PARLIVYVAK 


SY 

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References

[1]"Genome sequence of Thermofilum pendens reveals an exceptional loss of biosynthetic pathways without genome reduction."
Anderson I., Rodriguez J., Susanti D., Porat I., Reich C., Ulrich L.E., Elkins J.G., Mavromatis K., Lykidis A., Kim E., Thompson L.S., Nolan M., Land M., Copeland A., Lapidus A., Lucas S., Detter C., Zhulin I.B. expand/collapse author list , Olsen G.J., Whitman W., Mukhopadhyay B., Bristow J., Kyrpides N.
J. Bacteriol. 190:2957-2965(2008) [PubMed: 18263724] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Hrk 5.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000505 Genomic DNA. Translation: ABL78218.1.
RefSeqYP_920221.1. NC_008698.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGA1RYD8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4601988.
GenomeReviewsGene locus Tpen_0817 in contig CP000505_GR.
KEGGtpe:Tpen_0817.

Phylogenomic databases

eggNOGarNOG04466.
HOGENOMHBG334108.
OMAKFAEYEL.
PhylomeDBA1RYD8.

Enzyme and pathway databases

BioCycTPEN368408:TPEN_0817-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_THEPD
AccessionPrimary (citable) accession number: A1RYD8
Entry history
Integrated into UniProtKB/Swiss-Prot: May 29, 2007
Last sequence update: February 6, 2007
Last modified: January 25, 2012
This is version 33 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