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A0B9N3 (SYP_METTP) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 37. 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:Mthe_1640
OrganismMethanosaeta thermophila (strain DSM 6194 / PT) (Methanothrix thermophila (strain DSM 6194 / PT)) [Complete proteome] [HAMAP]
Taxonomic identifier349307 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanomicrobiaMethanosarcinalesMethanosaetaceaeMethanosaeta

Protein attributes

Sequence length478 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 – 478478Proline--tRNA ligase HAMAP MF_01571
PRO_0000288422

Sequences

Sequence LengthMass (Da)Tools
A0B9N3 [UniParc].

Last modified November 28, 2006. Version 1.
Checksum: 69A9EB7606BB8F77

FASTA47854,861
        10         20         30         40         50         60 
MTKKEERDAK LPPKSNFSEW YHELLRSAEI VDVRYPVKGM SVWYPFGFAL RSHVYQIIKE 

        70         80         90        100        110        120 
LLDVDHYETQ FPLLIPETEF MKEAEHIKGF EDEVYWVTHG GRDPLDIKLA LRPTSETAIY 

       130        140        150        160        170        180 
PMLKLWIRSH ADLPLRIYQI VNTFRYETKH TRPLIRLREI TSFKEAHTAH ATWEEAAMQV 

       190        200        210        220        230        240 
EIAIQRYIEF YRRLAIPCLV SKRPSWDKFP GADYSIALDV IMPDGRTLQV GTAHLLGTNF 

       250        260        270        280        290        300 
AKTYEITYED EHGEQRYVNQ TCYGISERCI AALIAVHGDD KGLVLPWRVA PVQVVIVPII 

       310        320        330        340        350        360 
FGEREPIIEV CRSIASTLAG RNIRVRLDDG DERPGAKFYK WEMRGVPVRI EIGPRDIKNG 

       370        380        390        400        410        420 
VVTIVRRDGV RKTLPMDERL VDAILIEAEE LQTVLYNRAK EFMDSKIKLV SSLDEARSQV 

       430        440        450        460        470 
QSGVARVPWC GSVECGHALE DQIGANLLGE PRGDELPPMR CLVCGRESTG STYMARQY 

« Hide

References

[1]"Complete sequence of Methanosaeta thermophila PT."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N. expand/collapse author list , Kim E., Smith K.S., Ingram-Smith C., Richardson P.
Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 6194 / PT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000477 Genomic DNA. Translation: ABK15407.1.
RefSeqYP_844047.1. NC_008553.1.

3D structure databases

ProteinModelPortalA0B9N3.
SMRA0B9N3. Positions 16-478.
ModBaseSearch...

Protein-protein interaction databases

STRINGA0B9N3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4462512.
GenomeReviewsGene locus Mthe_1640 in contig CP000477_GR.
KEGGmtp:Mthe_1640.
NMPDRfig|349307.7.peg.1708.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGarNOG04466.
HOGENOMHBG334108.
OMAKFAEYEL.
PhylomeDBA0B9N3.
ProtClustDBPRK08661.

Enzyme and pathway databases

BioCycMTHE349307:MTHE_1640-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_METTP
AccessionPrimary (citable) accession number: A0B9N3
Entry history
Integrated into UniProtKB/Swiss-Prot: May 29, 2007
Last sequence update: November 28, 2006
Last modified: January 25, 2012
This is version 37 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