Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q92I92 (SYP_RICCN) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 75. 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:RC0528
OrganismRickettsia conorii (strain ATCC VR-613 / Malish 7) [Complete proteome] [HAMAP]
Taxonomic identifier272944 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRickettsialesRickettsiaceaeRickettsieaeRickettsiaspotted fever group

Protein attributes

Sequence length426 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.

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 – 426426Proline--tRNA ligase HAMAP-Rule MF_01570
PRO_0000248915

Sequences

Sequence LengthMass (Da)Tools
Q92I92 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: F9393F3CB7A261B6

FASTA42648,472
        10         20         30         40         50         60 
MLLSKYFLPV LKEEPSEAQV TSHKLMLRSG MIRQQAAGIY TWLPLGLKVL KNIENIVRLN 

        70         80         90        100        110        120 
MNKAGALEVL MPCIQPAHLW MESGRFDNYG KEMLKFQDRH DNTLLFGPTN EDMITDIFRH 

       130        140        150        160        170        180 
NIKSYKDLPK NLYHIQWKFR DEIRPRFGVM RGREFLMKDA YSFDINEENA VKTYNQMYKA 

       190        200        210        220        230        240 
YINAFRDLGV FVIPVIADNG PIGGNLSHEF HIIAETGEST IYYDKKFKTL KDNPDIDVEE 

       250        260        270        280        290        300 
IKSWYAAAEE KYEVNKLPIS EQEITSSKGI EVGHIFYIGS KYSVNMNALI NDEYGKLTPI 

       310        320        330        340        350        360 
EMSSYGIGIS RLVAAIIEAN CDEKGIIWPS SVAPFKVSLI NLNIHDSKCV ELAEMAYKEL 

       370        380        390        400        410        420 
SDKNIEVLYD DTEARPGSKF ATHDLIGSPH QIIIGPKKAA NNIVELKDRK SGVIEDIEVG 


SLMSVL 

« Hide

References

[1]"Mechanisms of evolution in Rickettsia conorii and R. prowazekii."
Ogata H., Audic S., Renesto-Audiffren P., Fournier P.-E., Barbe V., Samson D., Roux V., Cossart P., Weissenbach J., Claverie J.-M., Raoult D.
Science 293:2093-2098(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC VR-613 / Malish 7.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE006914 Genomic DNA. Translation: AAL03066.1.
PIRH97765.
RefSeqNP_360165.1. NC_003103.1.

3D structure databases

ProteinModelPortalQ92I92.
SMRQ92I92. Positions 1-423.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272944.RC0528.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAL03066; AAL03066; RC0528.
GeneID927646.
KEGGrco:RC0528.
PATRIC17888306. VBIRicCon45613_0604.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0442.
HOGENOMHOG000076894.
KOK01881.
OMAMISRIRP.
OrthoDBEOG6TTVMR.
ProtClustDBPRK12325.

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_RICCN
AccessionPrimary (citable) accession number: Q92I92
Entry history
Integrated into UniProtKB/Swiss-Prot: September 5, 2006
Last sequence update: December 1, 2001
Last modified: February 19, 2014
This is version 75 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

Rickettsia conorii

(strain Malish 7): entries and gene names

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries