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B2HXU5 (SYS_ACIBC) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 39. 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:
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:ACICU_02979
OrganismAcinetobacter baumannii (strain ACICU) [Complete proteome] [HAMAP]
Taxonomic identifier405416 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesMoraxellaceaeAcinetobacterAcinetobacter calcoaceticus/baumannii complex

Protein attributes

Sequence length423 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 – 423423Serine--tRNA ligase HAMAP-Rule MF_00176
PRO_1000098024

Regions

Nucleotide binding262 – 2643ATP By similarity
Nucleotide binding349 – 3524ATP By similarity
Region231 – 2333Serine binding By similarity

Sites

Binding site2851Serine By similarity
Binding site3841Serine By similarity

Sequences

Sequence LengthMass (Da)Tools
B2HXU5 [UniParc].

Last modified June 10, 2008. Version 1.
Checksum: C3F49924A84A622C

FASTA42347,411
        10         20         30         40         50         60 
MIDPKLLRNN IEVVNAALAK RGVQLDVQEW ASLETRRKDL QSKTEKLQAE RNAGAKQVGQ 

        70         80         90        100        110        120 
IKKSGGDASE IMARMQAIGD EIKAAEVALS ELQNEIEQKA LSIPNLPDES VPAGKDENDN 

       130        140        150        160        170        180 
VEISKWGTPR QFDFEIKDHT DLGEWMGGLE FETATKLTGS RFSVLKGPLA RLQRALTQFM 

       190        200        210        220        230        240 
LDTHTLKNGY TEAYVPYLVN ADSLRGTGQL PKFEEDLFKL QGEKEYYLIP TAEVPVTNFV 

       250        260        270        280        290        300 
RDEIIDADRL PLKYAAHTPC FRSEAGSYGR DTRGLIRQHQ FDKVEMVQIV KPETSMQALE 

       310        320        330        340        350        360 
ELTAHAEGIL QALGLPYRKI LLCGGDMGFG ATKTYDLEVW VPSQNTYREI SSCSNMGDFQ 

       370        380        390        400        410        420 
ARRMKARYRM DQKKTELVHT LNGSGLAVGR TLLAVMENYQ RKDGSIEIPE VLRPYMGGAT 


FID 

« Hide

References

[1]"Whole-genome pyrosequencing of an epidemic multidrug-resistant Acinetobacter baumannii strain belonging to the European clone II group."
Iacono M., Villa L., Fortini D., Bordoni R., Imperi F., Bonnal R.J., Sicheritz-Ponten T., De Bellis G., Visca P., Cassone A., Carattoli A.
Antimicrob. Agents Chemother. 52:2616-2625(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ACICU.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000863 Genomic DNA. Translation: ACC58291.1.
RefSeqYP_001847638.1. NC_010611.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING405416.ACICU_02979.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACC58291; ACC58291; ACICU_02979.
GeneID6235201.
KEGGabc:ACICU_02979.
PATRIC20714668. VBIAciBau103538_3008.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0172.
HOGENOMHOG000035938.
KOK01875.
OMAMGTDVIK.
OrthoDBEOG61KBH9.

Enzyme and pathway databases

BioCycABAU405416:GI27-3031-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_ACIBC
AccessionPrimary (citable) accession number: B2HXU5
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: June 10, 2008
Last modified: May 14, 2014
This is version 39 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

PATHWAY comments

Index of metabolic and biosynthesis pathways

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries