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Q1RKF4 (SYS_RICBR) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 56. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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:
Serine--tRNA ligase

EC=6.1.1.11
Alternative name(s):
Seryl-tRNA synthetase
Short name=SerRS
Seryl-tRNA(Ser/Sec) synthetase
Gene names
Name:serS
Ordered Locus Names:RBE_0079
OrganismRickettsia bellii (strain RML369-C) [Complete proteome] [HAMAP]
Taxonomic identifier336407 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRickettsialesRickettsiaceaeRickettsieaeRickettsiabelli group

Protein attributes

Sequence length426 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the attachment of serine to tRNA(Ser). Is also able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L-seryl-tRNA(Sec), which will be further converted into selenocysteinyl-tRNA(Sec) By similarity. HAMAP-Rule MF_00176

Catalytic activity

ATP + L-serine + tRNA(Ser) = AMP + diphosphate + L-seryl-tRNA(Ser). HAMAP-Rule MF_00176

ATP + L-serine + tRNA(Sec) = AMP + diphosphate + L-seryl-tRNA(Sec). HAMAP-Rule MF_00176

Pathway

Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec) biosynthesis; L-seryl-tRNA(Sec) from L-serine and tRNA(Sec): step 1/1. HAMAP-Rule MF_00176

Subunit structure

Homodimer. The tRNA molecule binds across the dimer By similarity.

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00176.

Domain

Consists of two distinct domains, a catalytic core and a N-terminal extension that is involved in tRNA binding By similarity. HAMAP-Rule MF_00176

Sequence similarities

Belongs to the class-II aminoacyl-tRNA synthetase family. Type-1 seryl-tRNA synthetase subfamily.

Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionAminoacyl-tRNA synthetase
Ligase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processselenocysteine biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-HAMAP

selenocysteinyl-tRNA(Sec) biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

seryl-tRNA aminoacylation

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

serine-tRNA ligase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 426426Serine--tRNA ligase HAMAP-Rule MF_00176
PRO_0000278053

Regions

Nucleotide binding260 – 2623ATP By similarity
Nucleotide binding347 – 3504ATP By similarity
Region229 – 2313Serine binding By similarity

Sites

Binding site2831Serine By similarity
Binding site3831Serine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q1RKF4 [UniParc].

Last modified May 16, 2006. Version 1.
Checksum: 5F2DE56BB2F78081

FASTA42648,559
        10         20         30         40         50         60 
MLNIKWIREN QELFDDKLRQ RFIEPMAKRI EELDGKKRKI TNLIQEFQHA RKVKSKILGN 

        70         80         90        100        110        120 
INPKSGEEFE GLQRDVKDIN EKLEELEQDL NNNNELNELL NTLPNIPDEE VPYGIDESMN 

       130        140        150        160        170        180 
KLIRTHGEVD LNAQNKKQHF ELGVKLDLMD FEQTAKISGA RFVTLKGDLA KLERALANFM 

       190        200        210        220        230        240 
LDVHTGEFGF LEVSPPVLVR DNAMYNSGQL PKFADESFAT TNGYRLIPTA EVSLVNMVAD 

       250        260        270        280        290        300 
TIIPREKLPM RLVAYTPCFR SEAGSSGRDT RGMIRLHQFS KVELVSITTP EESKNEHEYM 

       310        320        330        340        350        360 
TNASETILQK LGLHYRTMLL CTGDMGFASQ KTYDIEVWLP GQKQYREIAS CSNCGDFQAR 

       370        380        390        400        410        420 
RMKARYKEFG SHDTTLVHTL NASGLPIGRT MVAILENYQN EDGSITVPDV LVNYMGGLQK 


ITAYKE 

« Hide

References

[1]"Genome sequence of Rickettsia bellii illuminates the role of amoebae in gene exchanges between intracellular pathogens."
Ogata H., La Scola B., Audic S., Renesto P., Blanc G., Robert C., Fournier P.-E., Claverie J.-M., Raoult D.
PLoS Genet. 2:733-744(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: RML369-C.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000087 Genomic DNA. Translation: ABE04160.1.
RefSeqYP_537249.1. NC_007940.1.

3D structure databases

ProteinModelPortalQ1RKF4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING336407.RBE_0079.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABE04160; ABE04160; RBE_0079.
GeneID3995070.
KEGGrbe:RBE_0079.
PATRIC17881403. VBIRicBel102610_0086.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0172.
HOGENOMHOG000035938.
KOK01875.
OMAYRPERHE.
OrthoDBEOG61KBH9.
ProtClustDBPRK05431.

Enzyme and pathway databases

BioCycRBEL336407:GJCY-81-MONOMER.
UniPathwayUPA00906; UER00895.

Family and domain databases

Gene3D1.10.287.40. 1 hit.
HAMAPMF_00176. Ser_tRNA_synth_type1.
InterProIPR002314. aa-tRNA-synt_IIb_cons-dom.
IPR006195. aa-tRNA-synth_II.
IPR002317. Ser-tRNA-ligase_type_1.
IPR015866. Ser-tRNA-synth_1_N.
IPR010978. tRNA-bd_arm.
[Graphical view]
PANTHERPTHR11778. PTHR11778. 1 hit.
PfamPF02403. Seryl_tRNA_N. 1 hit.
PF00587. tRNA-synt_2b. 1 hit.
[Graphical view]
PIRSFPIRSF001529. Ser-tRNA-synth_IIa. 1 hit.
PRINTSPR00981. TRNASYNTHSER.
SUPFAMSSF46589. SSF46589. 1 hit.
TIGRFAMsTIGR00414. serS. 1 hit.
PROSITEPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYS_RICBR
AccessionPrimary (citable) accession number: Q1RKF4
Entry history
Integrated into UniProtKB/Swiss-Prot: February 20, 2007
Last sequence update: May 16, 2006
Last modified: February 19, 2014
This is version 56 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 bellii strain RML369-C

Rickettsia bellii (strain RML369-C): entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries