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Reviewed, UniProtKB/Swiss-Prot Q8YQ59 (SYS_ANASP)

Last modified February 9, 2010. Version 44. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Seryl-tRNA synthetase
    EC=6.1.1.11
Alternative name(s):
    Seryl-tRNA(Ser/Sec) synthetase
    Serine--tRNA ligase
      Short name=SerRS
Gene names
Name: serS
Ordered Locus Names: all3976
OrganismAnabaena sp. (strain PCC 7120) [Complete proteome] [HAMAP]
Taxonomic identifier103690 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaNostocalesNostocaceaeNostoc

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 MF_00176

Catalytic activity

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

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

Pathway

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

Subunit structure

Homodimer. The tRNA molecule binds across the dimer By similarity. HAMAP MF_00176

Subcellular location

Cytoplasm By similarity HAMAP 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 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: HAMAP

seryl-tRNA aminoacylation

Inferred from electronic annotation. Source: HAMAP

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: HAMAP

serine-tRNA ligase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 426426Seryl-tRNA synthetase HAMAP MF_00176
PRO_0000121994

Regions

Nucleotide binding266 – 2683ATP By similarity
Nucleotide binding353 – 3564ATP By similarity
Region235 – 2373Serine binding By similarity

Sites

Binding site2891Serine By similarity
Binding site3891Serine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8YQ59-1 [UniParc].

Last modified March 1, 2002. Version 1.
Checksum: E3EB9E94894E9DBB

FASTA42647,676
        10         20         30         40         50         60 
MLDIKQIREN PQLIQERLNS RNGTYDIQPI LQLDKQQREL EATRSQIQAR SNEIGKIVGQ 

        70         80         90        100        110        120 
KIKSGINPQD PEIQALRDEG NAIKAQLSEL EPREKELKAE IEQLILALPN LPSDSTPIGK 

       130        140        150        160        170        180 
GEEENVEVRL WGDEYLPQNP NIIPHWEIGE KLGILNFERA VKVAQSRFVN LIGAGAALER 

       190        200        210        220        230        240 
ALINFMLKMQ TAAGYIEVSP PLLVNTDSLT GTGQLPKFAE ESFKCADDEL WLIPTAEVPV 

       250        260        270        280        290        300 
TNLYRGEILA AENLPIYHCA YTPCFRREAG SYGRDMRGLI RLHQFNKVEL VKVVHPSTSF 

       310        320        330        340        350        360 
DELEKLVGNA EAILQALKLP YRVINLCTGD LGFGATKTYD LEVWLPSSGK YREISSCSNC 

       370        380        390        400        410        420 
FDFQARRADI RFKEAGKKGT QFVHTLNGSG LAVGRTMAAI LENYQQPDGT ILIPEVLQPF 


LGREVL 

« Hide

References

[1]"Complete genomic sequence of the filamentous nitrogen-fixing cyanobacterium Anabaena sp. strain PCC 7120."
Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A., Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M. expand/collapse author list , Takazawa M., Yamada M., Yasuda M., Tabata S.
DNA Res. 8:205-213(2001) [PubMed: 11759840] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000019 Genomic DNA. Translation: BAB75675.1.
PIRAI2302.
RefSeqNP_488016.1.

3D structure databases

SMRQ8YQ59. Positions 1-426.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ8YQ59.

Genome annotation databases

GeneID1107574.
GenomeReviewsGene locus all3976 in contig BA000019_GR.
KEGGana:all3976.
NMPDRfig|103690.1.peg.4283.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0172.
HOGENOMHBG629391.
OMAWSSCYRR.
PhylomeDBQ8YQ59.

Enzyme and pathway databases

BioCycNSP103690:ALL3976-MONOMER.

Family and domain databases

HAMAPMF_00176. Ser_tRNA_synth_type1.
[Tree]
InterProIPR002314. aa-tRNA-synt_IIb_cons-dom.
IPR006195. aa-tRNA-synth_II_cons-dom.
IPR002317. Ser-tRNA-synth_IIa.
IPR018156. Ser-tRNA-synth_IIa_C.
IPR015866. Ser-tRNA-synth_IIa_N.
IPR010978. tRNA_bd_arm.
[Graphical view]
Gene3DG3DSA:1.10.287.40. Ser-tRNA-synth_IIa_N. 1 hit.
PANTHERPTHR11778. tRNA-synt_ser. 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.
TIGRFAMsTIGR00414. serS. 1 hit.
PROSITEPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYS_ANASP
AccessionPrimary (citable) accession number: Q8YQ59
Entry history
Integrated into UniProtKB/Swiss-Prot: April 23, 2003
Last sequence update: March 1, 2002
Last modified: February 9, 2010
This is version 44 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents