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Q8YGL8 (SYP_BRUME) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 79. 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:BMEI1140
OrganismBrucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094) [Complete proteome] [HAMAP]
Taxonomic identifier224914 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBrucellaceaeBrucella

Protein attributes

Sequence length442 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-Rule MF_01570

Catalytic activity

ATP + L-proline + tRNA(Pro) = AMP + diphosphate + L-prolyl-tRNA(Pro). HAMAP-Rule MF_01570

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_01570

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_01570.

Sequence similarities

Belongs to the class-II aminoacyl-tRNA synthetase family. ProS type 2 subfamily.

Sequence caution

The sequence AAL52321.1 differs from that shown. Reason: Erroneous initiation.

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: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 442442Proline--tRNA ligase HAMAP-Rule MF_01570
PRO_0000248894

Sequences

Sequence LengthMass (Da)Tools
Q8YGL8 [UniParc].

Last modified September 5, 2006. Version 2.
Checksum: 4E9AD5F6F4AD5AB8

FASTA44249,477
        10         20         30         40         50         60 
MRLSRYFLPI LKENPKEAEI VSHRLMLRSG MIRQQSAGIY SWLPIGLKVL NKVCTIIREE 

        70         80         90        100        110        120 
QNRAGANEIL MPTIQSADLW RESGRYDAYG KEMLRIQDRQ KREMLFGPTN EEMVTDIFRS 

       130        140        150        160        170        180 
YVRSYKDLPL NLYHIQWKFR DEVRPRFGVM RSREFLMKDA YSFDLDYEGA KMAYYRMFVS 

       190        200        210        220        230        240 
YLRTFARVGL QAIPMRADTG PIGGDLSHEF IILAETGESQ VYCDRAYLDL AVPGADTDFR 

       250        260        270        280        290        300 
NDAQLTDTVT RWTTPYAATD EMHDEADWAK VKPESQVSAR GIEVGHIFHF GTKYSEPMGA 

       310        320        330        340        350        360 
KVQGPDGKEH LVSMGSYGIG PSRLVAAAIE ASHDDAGIIW PKTIAPFGAG IVNMKPGDEG 

       370        380        390        400        410        420 
CDGVSEKLYE ALTNAGVDPL LDDKDERPGA KFATIDLIGL PTQVIVGPRG VAAGEVEVKD 

       430        440 
RKTGERQSLG IEAAINMLTA QA 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE008917 Genomic DNA. Translation: AAL52321.1. Different initiation.
PIRAF3394.
RefSeqNP_540057.1. NC_003317.1.

3D structure databases

ProteinModelPortalQ8YGL8.
SMRQ8YGL8. Positions 1-439.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING224914.BMEI1140.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAL52321; AAL52321; BMEI1140.
GeneID1196851.
KEGGbme:BMEI1140.
PATRIC17852561. VBIBruMel92729_1275.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000076894.
KOK01881.
OMAIQPAELW.
OrthoDBEOG6TTVMR.
ProtClustDBPRK12325.

Enzyme and pathway databases

BioCycBMEL224914:GCJ0-1175-MONOMER.

Family and domain databases

Gene3D3.40.50.800. 1 hit.
HAMAPMF_01570. Pro_tRNA_synth_type2.
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.
IPR023716. Prolyl-tRNA_ligase_IIa_type2.
[Graphical view]
PANTHERPTHR11451:SF3. PTHR11451:SF3. 1 hit.
PfamPF03129. HGTP_anticodon. 1 hit.
PF00587. tRNA-synt_2b. 1 hit.
[Graphical view]
PRINTSPR01046. TRNASYNTHPRO.
SUPFAMSSF52954. SSF52954. 1 hit.
TIGRFAMsTIGR00409. proS_fam_II. 1 hit.
PROSITEPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYP_BRUME
AccessionPrimary (citable) accession number: Q8YGL8
Entry history
Integrated into UniProtKB/Swiss-Prot: September 5, 2006
Last sequence update: September 5, 2006
Last modified: February 19, 2014
This is version 79 of the entry and version 2 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

Brucella melitensis

Brucella melitensis (strain 16M): entries and gene names

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries