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H2GQ53 (H2GQ53_CORDB) Unreviewed, UniProtKB/TrEMBL

Last modified May 29, 2013. Version 12. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Serine--tRNA ligase HAMAP-Rule MF_00176
EC=6.1.1.11 HAMAP-Rule MF_00176
Alternative name(s):
Seryl-tRNA synthetase HAMAP-Rule MF_00176
Seryl-tRNA(Ser/Sec) synthetase HAMAP-Rule MF_00176
Gene names
Name:serS HAMAP-Rule MF_00176 EMBL AEX49737.1
Ordered Locus Names:CDBH8_2223 EMBL AEX49737.1
OrganismCorynebacterium diphtheriae (strain BH8) [Complete proteome] [HAMAP] EMBL AEX49737.1
Taxonomic identifier698973 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Corynebacteriaceae › Corynebacterium ›

Protein attributes

Sequence length419 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(Sec) = AMP + diphosphate + L-seryl-tRNA(Sec). HAMAP-Rule MF_00176

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

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. HAMAP-Rule MF_00176

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Nucleotide binding257 – 2593ATP By similarity HAMAP-Rule MF_00176
Nucleotide binding344 – 3474ATP By similarity HAMAP-Rule MF_00176
Region226 – 2283Serine binding By similarity HAMAP-Rule MF_00176

Sites

Binding site2731ATP; via amide nitrogen and carbonyl oxygen By similarity HAMAP-Rule MF_00176
Binding site2801Serine By similarity HAMAP-Rule MF_00176
Binding site3791Serine By similarity HAMAP-Rule MF_00176

Sequences

Sequence LengthMass (Da)Tools
H2GQ53 [UniParc].

Last modified March 21, 2012. Version 1.
Checksum: EE8A9A9AA3C4DCCC

FASTA41946,566
        10         20         30         40         50         60 
MIDLKFLREN PDVVRESQRI RGEDPALVDQ LLEADEKRRE AIKSADDLRA EHKAFGKKIS 

        70         80         90        100        110        120 
QASPEERPAL LEGSNELKSR VKAAEEAEAE ALAKVNEIQM LFGNVVTDAP AGGEDDYIVL 

       130        140        150        160        170        180 
EHVGTPRTFD FEPKDHLDLG ESLGLIDVKR GTKVGGARFY YLTGDGAFLQ LGMLNLAAQK 

       190        200        210        220        230        240 
ARENGFQLMI PPVLVRPEVM SGTGFLGAHS DEIYYLERDD LYLVGTSEVA LAGYHQDEII 

       250        260        270        280        290        300 
DLSDGPIKYA GWSSCFRREA GSYGKDTRGI LRVHQFDKLE MFVYCKPEEA VAQHQALLNM 

       310        320        330        340        350        360 
EREMLAAVEV PYRIIDVAGG DLGSSAARKF DTEAWVPTQN TYRELTSTSN CTTFQARRLR 

       370        380        390        400        410 
TRYRDESGKA HTAATLNGTL ATTRWLVAIL ENNQQADGSV IVPEALRPFV GKEVLEPKK

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References

[1]"Pangenomic Study of Corynebacterium diphtheriae That Provides Insights into the Genomic Diversity of Pathogenic Isolates from Cases of Classical Diphtheria, Endocarditis, and Pneumonia."
Trost E., Blom J., de Castro Soares S., Huang I.H., Al-Dilaimi A., Schroder J., Jaenicke S., Dorella F.A., Rocha F.S., Miyoshi A., Azevedo V., Schneider M.P., Silva A., Camello T.C., Sabbadini P.S., Santos C.S., Santos L.S., Hirata R.Jr. expand/collapse author list , Mattos-Guaraldi A.L., Efstratiou A., Schmitt M.P., Ton-That H., Tauch A.
J. Bacteriol. 194:3199-3215(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: BH8 EMBL AEX49737.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP003209 Genomic DNA. Translation: AEX49737.1.
RefSeqYP_005161304.1. NC_016800.1.

3D structure databases

ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAEX49737; AEX49737; CDBH8_2223.
GeneID11734668.
KEGGcdb:CDBH8_2223.

Organism-specific databases

CMRSearch...

Phylogenomic databases

KOK01875.

Enzyme and pathway databases

BioCycCDIP698973:GHAI-2281-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. tRNA_binding_arm. 1 hit.
TIGRFAMsTIGR00414. serS. 1 hit.
PROSITEPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameH2GQ53_CORDB
AccessionPrimary (citable) accession number: H2GQ53
Entry history
Integrated into UniProtKB/TrEMBL: March 21, 2012
Last sequence update: March 21, 2012
Last modified: May 29, 2013
This is version 12 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info