Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot A7H7J7 (SYP_ANADF)

Last modified November 3, 2009. Version 16. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Prolyl-tRNA synthetase
    EC=6.1.1.15
Alternative name(s):
    Proline--tRNA ligase
      Short name=ProRS
Gene names
Name: proS
Ordered Locus Names: Anae109_0478
OrganismAnaeromyxobacter sp. (strain Fw109-5) [Complete proteome] [HAMAP]
Taxonomic identifier404589 [NCBI]
Taxonomic lineageBacteriaProteobacteriaDeltaproteobacteriaMyxococcalesCystobacterineaeMyxococcaceaeAnaeromyxobacter

Protein attributes

Sequence length575 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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). As ProRS can inadvertently accommodate and process non-cognate amino acids such as alanine and cysteine, to avoid such errors it has two additional distinct editing activities against alanine. One activity is designated as 'pretransfer' editing and involves the tRNA(Pro)-independent hydrolysis of activated Ala-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Ala-tRNA(Pro). The misacylated Cys-tRNA(Pro) is not edited by ProRS By similarity.

Catalytic activity

ATP + L-proline + tRNA(Pro) = AMP + diphosphate + L-prolyl-tRNA(Pro). HAMAP MF_01569

Subunit structure

Homodimer By similarity.

Subcellular location

Cytoplasm By similarity.

Domain

Consists of three domains: the N-terminal catalytic domain, the editing domain and the C-terminal anticodon-binding domain By similarity.

Sequence similarities

Belongs to the class-II aminoacyl-tRNA synthetase family. ProS type 1 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: HAMAP

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: HAMAP

proline-tRNA ligase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 575575Prolyl-tRNA synthetase HAMAP MF_01569
PRO_1000069118

Sequences

Sequence LengthMass (Da)Tools
A7H7J7-1 [UniParc].

Last modified September 11, 2007. Version 1.
Checksum: 8899C540647D9ECD

FASTA57563,091
        10         20         30         40         50         60 
MPVVRLSQAF VPTLKEAPAD AQVASHKLLV RAGFIRQLGA GIYDYLPLAK RTLAKIEAIV 

        70         80         90        100        110        120 
REEMDAIGGQ EFYLPALHPA EIWKESGRWE VMGDNMFRLK DRKNGDYCLG MTHEEIFTAI 

       130        140        150        160        170        180 
ARDELRSYRQ LPQVWYQIQT KFRDEPRPKS GLLRVRQFTM KDAYSFDVDR AGLDKSYEDQ 

       190        200        210        220        230        240 
RRAYERIFTR CGLDFVAVQA HSGAMGGSES SEFMVRTDAG EDLVAACPRC RYAANTETAT 

       250        260        270        280        290        300 
SRLASEQDGA GLPKPEKFAT PGVVTIEALE QPPYGVAARR QLKTLVYVAD EKLVVAVVRG 

       310        320        330        340        350        360 
DQELNEAKLQ TATGAQVIRP AHPEEIPSLM GARAGSLGAV GFSRAKVFVD PSLADRKDMV 

       370        380        390        400        410        420 
TGANEDGFHL RGVEVRRDVL TGPHATVAEL RTVRAGEGCP RCDGTLDVFK ALEVGHIFKL 

       430        440        450        460        470        480 
GTKYSESMKA TVLDADGKAV PIVMGSYGIG VERIMAAAIE LHHDELGIRW PPAIAPFQAT 

       490        500        510        520        530        540 
VLTLGPEPEL KKAADELVKA LSDAGLEVLH DDREERAGVK FKDADLVGIP LRISVGKKGL 

       550        560        570 
AEGKVEWKLR GDKAVELVPL AEVARRAAEH VRAGR 

« Hide

References

[1]"Complete sequence of Anaeromyxobacter sp. Fw109-5."
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Sims D., Brettin T., Bruce D., Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N. expand/collapse author list , Lykidis A., Fields M., Richardson P.
Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000769 Genomic DNA. Translation: ABS24693.1.
RefSeqYP_001377677.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGA7H7J7.

Genome annotation databases

GeneID5377703.
GenomeReviewsGene locus Anae109_0478 in contig CP000769_GR.
KEGGafw:Anae109_0478.
NMPDRfig|404589.4.peg.427.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMAVVSHQLM.

Family and domain databases

HAMAPMF_01569.
[Tree]
InterProIPR002314. aa-tRNA-synt_IIb_cons-reg.
IPR006195. aa-tRNA-synth_II_cons-reg.
IPR004154. Anticodon_bd.
IPR004500. Pro-tRNA-synth_IIa_bac.
IPR002316. Pro-tRNA-synth_IIa_cons-reg.
IPR007214. YbaK/aa-tRNA-synth-assoc-reg.
[Graphical view]
Gene3DG3DSA:3.40.50.800. Anticodon_bd. 1 hit.
G3DSA:3.90.960.10. YbaK/aa-tRNA-synth-assoc-reg. 1 hit.
PfamPF03129. HGTP_anticodon. 1 hit.
PF00587. tRNA-synt_2b. 1 hit.
PF04073. YbaK. 1 hit.
[Graphical view]
PRINTSPR01046. TRNASYNTHPRO.
TIGRFAMsTIGR00409. proS_fam_II. 1 hit.
PROSITEPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYP_ANADF
AccessionPrimary (citable) accession number: A7H7J7
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: September 11, 2007
Last modified: November 3, 2009
This is version 16 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents