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Q83F67 (SYP_COXBU) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 77. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:CBU_0081
OrganismCoxiella burnetii (strain RSA 493 / Nine Mile phase I) [Reference proteome] [HAMAP]
Taxonomic identifier227377 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaLegionellalesCoxiellaceaeCoxiella

Protein attributes

Sequence length566 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). 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. HAMAP-Rule MF_01569

Catalytic activity

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

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_01569

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_01569.

Domain

Consists of three domains: the N-terminal catalytic domain, the editing domain and the C-terminal anticodon-binding domain By similarity. HAMAP-Rule MF_01569

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
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

aminoacyl-tRNA editing activity

Inferred from electronic annotation. Source: InterPro

proline-tRNA ligase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 566566Proline--tRNA ligase HAMAP-Rule MF_01569
PRO_0000248680

Sequences

Sequence LengthMass (Da)Tools
Q83F67 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 46EAB65336DC0383

FASTA56663,589
        10         20         30         40         50         60 
MLMKVSQFFL ATVKETPADA VLASHQLMIR AGMLRKLASG LYTWLPLGLR VLQKVADVVR 

        70         80         90        100        110        120 
EEMNRAGALE LLMPIVQPAS LWQESGRWEA YGAELLRIMD RHQNGFCFGP THEEVITDIA 

       130        140        150        160        170        180 
RQELKSYKQL PLNFYQIQTK FRDEIRPRFG VMRSREFLMK DAYSFDLDEK GMQAAYEKMF 

       190        200        210        220        230        240 
DAYRRIFTRL GLNFRAVLAD TGAIGGDYSH EFQVLADVGE DTVVYSDESD YAANIEKAAA 

       250        260        270        280        290        300 
QAPQGERVKP VAEMKKIATP GVRTIKQLAD KANILPEKGV KTLIVKGDES SLIALILRGD 

       310        320        330        340        350        360 
HELNDVKAQH LPGVAFPLQF ADEKEIREAI GCGPGSLGPV NLPIPFIVDR DAAQLVDFSC 

       370        380        390        400        410        420 
GANEDDFHWI NVNWERDVPL GSVADIRKVV EGDISPDGKG RLRFARGIEV GQVFQLGDKY 

       430        440        450        460        470        480 
SRKMNATVVD ELGKSRYLQM GCYGIGVSRT VAAAIEQNHD ERGIIWPMPM APFFIALVPV 

       490        500        510        520        530        540 
NMHKSYRVRE ACEKLYNELI DAGYEVLWDD RKERPGVMFA DMDLIGIPHR LVISESGLDR 

       550        560 
GIVEYKARKS KEAENVSLEN VLSVFR 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE016828 Genomic DNA. Translation: AAO89648.1.
RefSeqNP_819134.1. NC_002971.3.

3D structure databases

ProteinModelPortalQ83F67.
SMRQ83F67. Positions 3-223.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING227377.CBU_0081.

Proteomic databases

PRIDEQ83F67.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAO89648; AAO89648; CBU_0081.
GeneID1207951.
KEGGcbu:CBU_0081.
PATRIC17928841. VBICoxBur82552_0083.

Phylogenomic databases

eggNOGCOG0442.
HOGENOMHOG000076893.
KOK01881.
OMAIQPAELW.
OrthoDBEOG6TTVMR.
ProtClustDBPRK09194.

Enzyme and pathway databases

BioCycCBUR227377:GJ7S-81-MONOMER.

Family and domain databases

Gene3D3.40.50.800. 1 hit.
3.90.960.10. 1 hit.
HAMAPMF_01569. Pro_tRNA_synth_type1.
InterProIPR002314. aa-tRNA-synt_IIb_cons-dom.
IPR006195. aa-tRNA-synth_II.
IPR004154. Anticodon-bd.
IPR002316. Pro-tRNA-ligase_IIa.
IPR004500. Pro-tRNA-synth_IIa_bac-type.
IPR023717. Pro-tRNA-Synthase_IIa_type1.
IPR007214. YbaK/aa-tRNA-synth-assoc-dom.
[Graphical view]
PANTHERPTHR11451:SF3. PTHR11451:SF3. 1 hit.
PfamPF03129. HGTP_anticodon. 1 hit.
PF00587. tRNA-synt_2b. 1 hit.
PF04073. tRNA_edit. 1 hit.
[Graphical view]
PRINTSPR01046. TRNASYNTHPRO.
SUPFAMSSF52954. SSF52954. 1 hit.
SSF55826. SSF55826. 1 hit.
TIGRFAMsTIGR00409. proS_fam_II. 1 hit.
PROSITEPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYP_COXBU
AccessionPrimary (citable) accession number: Q83F67
Entry history
Integrated into UniProtKB/Swiss-Prot: September 5, 2006
Last sequence update: June 1, 2003
Last modified: April 16, 2014
This is version 77 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Coxiella burnetii

Coxiella burnetii (strain RSA 493): entries and gene names

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries