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A0B5E9 (SYS2_METTP) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 38. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Type-2 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:Mthe_0123
OrganismMethanosaeta thermophila (strain DSM 6194 / PT) (Methanothrix thermophila (strain DSM 6194 / PT)) [Complete proteome] [HAMAP]
Taxonomic identifier349307 [NCBI]
Taxonomic lineageArchaea › Euryarchaeota › Methanomicrobia › Methanosarcinales › Methanosaetaceae › Methanosaeta

Protein attributes

Sequence length500 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_01278

Catalytic activity

ATP + L-serine + tRNA(Ser) = AMP + diphosphate + L-seryl-tRNA(Ser). HAMAP MF_01278

ATP + L-serine + tRNA(Sec) = AMP + diphosphate + L-seryl-tRNA(Sec). HAMAP MF_01278

Cofactor

Binds 1 Zn2+ ion per subunit. This ion is coordinated with 2 cysteines, 1 glutamate and a water molecule that dissociates from the zinc ion to allow the coordination of the amino group of the serine substrate, which is essential for catalysis By similarity.

Pathway

Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec) biosynthesis; L-seryl-tRNA(Sec) from L-serine and tRNA(Sec): step 1/1. HAMAP MF_01278

Subunit structure

Homodimer By similarity. HAMAP MF_01278

Subcellular location

Cytoplasm By similarity HAMAP MF_01278.

Domain

Consists of two distinct domains, a catalytic core and a N-terminal extension that is presumably involved in tRNA binding By similarity. HAMAP MF_01278

Sequence similarities

Belongs to the class-II aminoacyl-tRNA synthetase family. Type-2 seryl-tRNA synthetase subfamily.

Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Metal-binding
Nucleotide-binding
Zinc
   Molecular functionAminoacyl-tRNA synthetase
Ligase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processseryl-tRNA aminoacylation

Inferred from electronic annotation. Source: InterPro

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

serine-tRNA ligase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 500500Type-2 serine--tRNA ligase HAMAP MF_01278
PRO_0000286170

Regions

Nucleotide binding337 – 3393ATP By similarity
Nucleotide binding348 – 3492ATP By similarity
Region354 – 3563Serine binding By similarity

Sites

Metal binding3071Zinc; catalytic By similarity
Metal binding3561Zinc; catalytic By similarity
Metal binding4591Zinc; catalytic By similarity
Binding site3051Serine; via carbonyl oxygen By similarity
Binding site3371Serine By similarity
Binding site4011Serine By similarity
Binding site4301ATP By similarity
Binding site4331Serine By similarity
Binding site4661ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
A0B5E9 [UniParc].

Last modified November 28, 2006. Version 1.
Checksum: 2F27B81E766AFD4B

FASTA50058,083
        10         20         30         40         50         60 
MKFHLEVSLK LSGDAANAEG DLAEFFEKQA VDLLKKGAPE GMGAKVAGWR ITGDQLEIKI 

        70         80         90        100        110        120 
ESDRYVRAHD ALLRLRKPLA NLLGRKHRLG IRGINVSRFE IQIESNRQIT HRIPYVRESR 

       130        140        150        160        170        180 
YEDGLLTLIL GVEDPKRGWT WMLENRIPDR IVNLLEEKLQ SYGGKAEHWE LLWESPPREF 

       190        200        210        220        230        240 
KFSGDPTQEM VKRGWIKHGS ARGQWIHGPQ STHLFRTFER IVLEEILVPL GYREMIFPKL 

       250        260        270        280        290        300 
DTWDVWKRSG HAQGVYPEIY YVCPPKSRDP AFWEEVIDYY KVTHEIPLDL IKEKIDYPIG 

       310        320        330        340        350        360 
GMCYAQCPTF WVFLQGATLP NDELPIKVFD RSGTSHRYES GGIHGIERVD EFHRIEIVWL 

       370        380        390        400        410        420 
GTKQQVMEEA ERLKERYKHI FEEILELRWR MAWVTPWFMA QEGRTGLAEM EGAGTIDYEA 

       430        440        450        460        470        480 
LLPYSGNWIE FQNLSVNGEK YPKGFSVKAQ SGESLWSGCS GVGLERWTSV FLGQKGLDPD 

       490        500 
NWPDEFRKRF GEMPRGIRFL

« Hide

References

[1]"Complete sequence of Methanosaeta thermophila PT."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N. expand/collapse author list , Kim E., Smith K.S., Ingram-Smith C., Richardson P.
Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 6194 / PT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000477 Genomic DNA. Translation: ABK13923.1.
RefSeqYP_842563.1. NC_008553.1.

3D structure databases

ProteinModelPortalA0B5E9.
SMRA0B5E9. Positions 1-500.
ModBaseSearch...

Protein-protein interaction databases

STRINGA0B5E9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4462297.
GenomeReviewsGene locus Mthe_0123 in contig CP000477_GR.
KEGGmtp:Mthe_0123.
NMPDRfig|349307.7.peg.128.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGarNOG04799.
HOGENOMHBG542255.
OMAAQCEPFY.
ProtClustDBPRK00960.

Enzyme and pathway databases

BioCycMTHE349307:MTHE_0123-MONOMER.

Family and domain databases

HAMAPMF_01278. Ser_tRNA_synth_type2.
[Tree]
InterProIPR002314. aa-tRNA-synt_IIb_cons-dom.
IPR006195. aa-tRNA-synth_II.
IPR004503. Ser-tRNA-synth_IIa_arc.
[Graphical view]
KOK01875.
PfamPF00587. tRNA-synt_2b. 1 hit.
[Graphical view]
PROSITEPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYS2_METTP
AccessionPrimary (citable) accession number: A0B5E9
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 2007
Last sequence update: November 28, 2006
Last modified: January 25, 2012
This is version 38 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

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

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