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F2L4G5 (F2L4G5_THEU7) Unreviewed, UniProtKB/TrEMBL

Last modified May 29, 2013. Version 17. 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
Ordered Locus Names:TUZN_1938 EMBL AEA13397.1
OrganismThermoproteus uzoniensis (strain 768-20) [Complete proteome] [HAMAP] EMBL AEA13397.1
Taxonomic identifier999630 [NCBI]
Taxonomic lineageArchaeaCrenarchaeotaThermoproteiThermoprotealesThermoproteaceaeThermoproteus

Protein attributes

Sequence length453 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 binding281 – 2833ATP By similarity HAMAP-Rule MF_00176
Nucleotide binding368 – 3714ATP By similarity HAMAP-Rule MF_00176
Region250 – 2523Serine binding By similarity HAMAP-Rule MF_00176

Sites

Binding site2971ATP; via amide nitrogen and carbonyl oxygen By similarity HAMAP-Rule MF_00176
Binding site3041Serine By similarity HAMAP-Rule MF_00176
Binding site4031Serine By similarity HAMAP-Rule MF_00176

Sequences

Sequence LengthMass (Da)Tools
F2L4G5 [UniParc].

Last modified May 31, 2011. Version 1.
Checksum: 1BFE8FB51F920FA4

FASTA45352,380
        10         20         30         40         50         60 
MSWSVLEALR NSPDVVRKTL VARRMDVTLV DRFLDLDSKW RELKREIDEL RHQHNVLSRE 

        70         80         90        100        110        120 
ASKAPPQDRK TIAEKAKELI EKIKGLEDQL KAVEMERERL LFSFPNLIHE SVPVCPEGVD 

       130        140        150        160        170        180 
SIPVRYWGTI KVAREDLEKV LRLDPRPEYV VVDKAPVGHA DEAENVLKMV DTLKAGEVAG 

       190        200        210        220        230        240 
SRFYYMLDDL VWLDFALSLY ALEHLTSKGF RPIVPPYMLK YDVIRRVIDL DTFKDAIYKL 

       250        260        270        280        290        300 
ENEDLYLIAT AEHGIAAYLY GRDLLEEELP QLYVGWSPCF RREAGAGSRD IKGIFRVHIF 

       310        320        330        340        350        360 
HKVEQFVFSL AEESWTWHEE ITKNTEELMQ GLGLPYRVVN ICAHDLGAPA AKKYDVEVWY 

       370        380        390        400        410        420 
PAQGTYRELA SCSNVTDWQS YRLGIRVTRR GMKREYVHTL NCTGLATTRT ITAILENYQR 

       430        440        450 
EDGAVEIPKV LRKYLEPIAT APKDYIVPKN VRR 

« Hide

References

« Hide 'large scale' references
[1]"Complete genome sequence of the thermoacidophilic crenarchaeon Thermoproteus uzoniensis 768-20."
Mardanov A.V., Gumerov V.M., Beletsky A.V., Prokofeva M.I., Bonch-Osmolovskaya E.A., Ravin N.V., Skryabin K.G.
J. Bacteriol. 193:3156-3157(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 768-20 EMBL AEA13397.1.
[2]"Complete genome sequence of the thermoacidophilic crenarchaeon Thermoproteus uzoniensis 768-20."
Mardanov A.V., Gumerov V.M., Beletsky A.V., Prokofeva M.I., Bonch-Osmolovskaya E.A., Ravin N.V., Skryabin K.G.
Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
Strain: 768-20.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP002590 Genomic DNA. Translation: AEA13397.1.
RefSeqYP_004338709.1. NC_015315.1.

3D structure databases

ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAEA13397; AEA13397; TUZN_1938.
GeneID10361450.
KEGGtuz:TUZN_1938.

Organism-specific databases

CMRSearch...

Phylogenomic databases

KOK01875.

Enzyme and pathway databases

BioCycTUZO999630:GJC9-1925-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 nameF2L4G5_THEU7
AccessionPrimary (citable) accession number: F2L4G5
Entry history
Integrated into UniProtKB/TrEMBL: May 31, 2011
Last sequence update: May 31, 2011
Last modified: May 29, 2013
This is version 17 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)