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Q049U9 (SYP_LACDB) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 52. 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:LBUL_1247
OrganismLactobacillus delbrueckii subsp. bulgaricus (strain ATCC BAA-365) [Complete proteome] [HAMAP]
Taxonomic identifier321956 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesLactobacillaceaeLactobacillus

Protein attributes

Sequence length565 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
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 – 565565Proline--tRNA ligase HAMAP-Rule MF_01569
PRO_0000288337

Sequences

Sequence LengthMass (Da)Tools
Q049U9 [UniParc].

Last modified November 14, 2006. Version 1.
Checksum: A2EC890DB3777C0A

FASTA56562,731
        10         20         30         40         50         60 
MRQSIFFMPT LKETPADAVA KSHQVMLRGG YIRQVTAGVY SYLPLGYKVL RKTEKIIEEE 

        70         80         90        100        110        120 
MANAGVVEMI MPHMLPASMW EESGRLPKYG PEMFRLKDRH GREMLLGPTH EETFTDVVAK 

       130        140        150        160        170        180 
SLKSYKQMPL QLYQIQTKFR DENRPRFGLL RGREFVMLDG YSFAASQEQL DKQFDDEKAA 

       190        200        210        220        230        240 
YLKIFKRTGV EVRPVIADSG TMGGKNSIEF QAPAAVGEDT IATNASGTYA ANLEMAVSVD 

       250        260        270        280        290        300 
TFKQEPEELK AMEKVATPGC DSIDKLAEFL QVPATRIVKS VLYIVDEKKK VLVLIRADKE 

       310        320        330        340        350        360 
VNEVKLTHLL DCDSLRVAET SDLEELTGAG KGGVGPVNAD WADEIVADKT VKGLYNVVVG 

       370        380        390        400        410        420 
AGESDAQFIN ANLDRDFKAD RFADLRVANE GEPDPVDHEP LKFTTSIEVG HIFKLGTYYT 

       430        440        450        460        470        480 
ETMGAKFLDQ NGKSQPVIMG SYGIGVTRLL SAVVEQHATE NGVAWPKEIA PFGIHIIQMK 

       490        500        510        520        530        540 
MKDEIQSKLA EDLEAKFAKY DVLYDDRNER PGVKFNDADL VGAPIRITVG RDAADGIVEV 

       550        560 
KRPGDDQAQK LAVADLEDFI ANELD 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000412 Genomic DNA. Translation: ABJ58773.1.
RefSeqYP_813211.1. NC_008529.1.

3D structure databases

ProteinModelPortalQ049U9.
SMRQ049U9. Positions 1-564.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING321956.LBUL_1247.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABJ58773; ABJ58773; LBUL_1247.
GeneID4436321.
KEGGlbu:LBUL_1247.
PATRIC22222335. VBILacDel70259_1217.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycLDEL321956:GI15-1242-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_LACDB
AccessionPrimary (citable) accession number: Q049U9
Entry history
Integrated into UniProtKB/Swiss-Prot: May 29, 2007
Last sequence update: November 14, 2006
Last modified: April 16, 2014
This is version 52 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

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries