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Reviewed, UniProtKB/Swiss-Prot Q0AB94 (SYP_ALHEH)

Last modified June 16, 2009. Version 21. 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: Mlg_0539
OrganismAlkalilimnicola ehrlichei (strain MLHE-1) [Complete proteome] [HAMAP]
Taxonomic identifier187272 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaChromatialesEctothiorhodospiraceaeAlkalilimnicola

Protein attributes

Sequence length568 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 – 568568Prolyl-tRNA synthetase HAMAP MF_01569
PRO_0000288308

Sequences

Sequence LengthMass (Da)Tools
Q0AB94-1 [UniParc].

Last modified October 17, 2006. Version 1.
Checksum: 49D836E1F1B5FF48

FASTA56862,591
        10         20         30         40         50         60 
MRASLFPLST SKETPADAEI VSHQLMLRAG MIRKLAAGLY TWTPLGLRVL RKVEQIVREE 

        70         80         90        100        110        120 
MDRAGAHELL MPAVQPAELW QESTRWDKYG PELLRLKDRH ERDFCFGPTH EEVITDYVRR 

       130        140        150        160        170        180 
EVKSYRQLPL NLYQIQTKFR DEIRPRFGVM RAREFLMKDA YSFHLDDDCL ARTYQVMYET 

       190        200        210        220        230        240 
YTRIFERTGL VFRAVAADSG NIGGSVSHEF HVLAESGEDA VAFSDESDYA ANVELAEAVA 

       250        260        270        280        290        300 
PAGEAPPPAE TMRRVDTPGA RTIDDLVRDY GLPIEKTVKT LVVHGADGGL VALLVRGDHS 

       310        320        330        340        350        360 
LNDVKATTLP QVAEPLVMAG EEEIRAAVGA GPGSLGPVEL PLPCVVDRSV AVMSDFAAGA 

       370        380        390        400        410        420 
NQDDAHYFGI NWGRDVALPE VADLREVVAG DPSPDGRGTL EIARGIEVGH IFQLGREYSE 

       430        440        450        460        470        480 
KMKATVLNEA GDAQTVTMGC YGIGVSRVVA AAIEQNHDDN GIIWPAPIAP FQLALVPIGM 

       490        500        510        520        530        540 
NRSEAVTEQA EKLYAELQAE GVEVFFDDRD ARPGVKFADM ELIGIPHRLV IGDRGLKNGV 

       550        560 
VEYRGRRDSE STDVPLAELS AFLRERLG 

« Hide

References

[1]"Complete sequence of Alkalilimnicola ehrilichei MLHE-1."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Sims D., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J. expand/collapse author list , Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Oremland R.S., Hoeft S.E., Switzer-Blum J., Kulp T., King G., Tabita R., Witte B., Santini J.M., Basu P., Hollibaugh J.T., Xie G., Stolz J.F., Richardson P.
Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000453 Genomic DNA. Translation: ABI55893.1.
RefSeqYP_741383.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID4268068.
GenomeReviewsGene locus Mlg_0539 in contig CP000453_GR.
KEGGaeh:Mlg_0539.
NMPDRfig|187272.6.peg.512.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ0AB94.
OMAQ0AB94. VVSHQLM.

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.
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_ALHEH
AccessionPrimary (citable) accession number: Q0AB94
Entry history
Integrated into UniProtKB/Swiss-Prot: May 29, 2007
Last sequence update: October 17, 2006
Last modified: June 16, 2009
This is version 21 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