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A9A787 (SYP_METM6) 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:MmarC6_0188
OrganismMethanococcus maripaludis (strain C6 / ATCC BAA-1332) [Complete proteome] [HAMAP]
Taxonomic identifier444158 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanococciMethanococcalesMethanococcaceaeMethanococcus

Protein attributes

Sequence length460 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 – 460460Proline--tRNA ligase HAMAP MF_01571
PRO_1000215566

Sequences

Sequence LengthMass (Da)Tools
A9A787 [UniParc].

Last modified January 15, 2008. Version 1.
Checksum: 0A6EC9A349250276

FASTA46053,323
        10         20         30         40         50         60 
MEFSEWYSDI LEKAGIYDLR YPIKGCGVYL PYGFKIRRYS FEILRKLLDE TNHDETLFPM 

        70         80         90        100        110        120 
LIPENLLAKE GEHIKGFEDE VFWVTHGGKT PLEVKLALRP TSETTMYYMM KQWIKVHTDL 

       130        140        150        160        170        180 
PMKLYQVVNT FRYETKHTRP LIRLREIMSF KEAHTAHATK EDCDAQITEA LNLYGEFFDE 

       190        200        210        220        230        240 
ICVPYIISKR PEWDKFPGAD YTMAFDTIYP DGKTMQIGTV HNLGQNFAKT FELEFETPDG 

       250        260        270        280        290        300 
EKDFVYQTCY GISDRAIASL ISVHGDEKGL VIPVDVAPIQ IVLIPLLFKG KEEIVMDKIK 

       310        320        330        340        350        360 
ELNRTLKSEF RVLLDDRDIR PGRKYNDWEI KGVPLRIELG PRDIENGQAL IVRRDTGEKI 

       370        380        390        400        410        420 
TVEYSNILEE VEKIVSMYKE NLKIKADEKI KNFLTVVDFE SDVNALSEKV KAALLENKGI 

       430        440        450        460 
ILIPFDESVY NEEFEELIDA SVLGQTTYEG KDYISVARTY 

« Hide

References

[1]"Complete sequence of Methanococcus maripaludis C6."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Clum A., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Sieprawska-Lupa M., Whitman W.B., Richardson P.
Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C6 / ATCC BAA-1332.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000867 Genomic DNA. Translation: ABX01011.1.
RefSeqYP_001548243.1. NC_009975.1.

3D structure databases

ProteinModelPortalA9A787.
SMRA9A787. Positions 1-460.
ModBaseSearch...

Protein-protein interaction databases

STRINGA9A787.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5737991.
GenomeReviewsGene locus MmarC6_0188 in contig CP000867_GR.
KEGGmmx:MmarC6_0188.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG334108.
OMAKFAEYEL.
ProtClustDBPRK08661.

Enzyme and pathway databases

BioCycMMAR444158:MMARC6_0188-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.
IPR015264. Pro-tRNA_synth_II_arc.
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.
PF09181. ProRS-C_2. 1 hit.
PF00587. tRNA-synt_2b. 1 hit.
[Graphical view]
PRINTSPR01046. TRNASYNTHPRO.
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_METM6
AccessionPrimary (citable) accession number: A9A787
Entry history
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: January 15, 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