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Q58477 (SYS2_METJA) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 76. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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:MJ1077
OrganismMethanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii)
Taxonomic identifier243232 [NCBI]
Taxonomic lineageArchaea › Euryarchaeota › Methanococci › Methanococcales › Methanocaldococcaceae › Methanocaldococcus

Protein attributes

Sequence length521 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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). Ref.2

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. Ref.2

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.

Biophysicochemical properties

Temperature dependence:

Thermostable. Fully active at 80 degrees Celsius. HAMAP MF_01278

Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Metal-binding
Nucleotide-binding
Zinc
   Molecular functionAminoacyl-tRNA synthetase
Ligase
   Technical termComplete proteome
Reference 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 – 521521Type-2 serine--tRNA ligase HAMAP MF_01278
PRO_0000122174

Regions

Nucleotide binding347 – 3493ATP By similarity
Nucleotide binding358 – 3592ATP By similarity
Region364 – 3663Serine binding By similarity

Sites

Metal binding3181Zinc; catalytic By similarity
Metal binding3661Zinc; catalytic By similarity
Metal binding4731Zinc; catalytic By similarity
Binding site3161Serine; via carbonyl oxygen By similarity
Binding site3471Serine By similarity
Binding site4801ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q58477 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: E8D40DB16915B4FE

FASTA52160,632
        10         20         30         40         50         60 
MKLTFDLDGK IIFSKELSEE AKNAVEEVLK NADSIFLKGV PKGKENEASK IKSYEFEGNI 

        70         80         90        100        110        120 
LKLKIASGTY TRAHEGLIRL RKPLAEKLGR NFRIGVRGIE IDNYVITIET DEDKAKKLEG 

       130        140        150        160        170        180 
IKVPECEAKV EGNKIILTFK DIGESELKRN IIDRAIKFVK TELEKEEEDL TFKVCKIPPG 

       190        200        210        220        230        240 
TIVSEYKAKR KITFDKDPTD VAEKLGWVKK FPGRGQWFYT PPITALFRAL EELIVEEVVK 

       250        260        270        280        290        300 
KIGFQECLFP KLIPLEIMYK MRYLEGLPEG MYYVCPPKRE PELFKEFVNE MMIKKEIPIE 

       310        320        330        340        350        360 
KLKNLLRDPG YVLAPAQCEP FYQFFEGEVI DVDKPIMFFD RSGWTYRWEG GGARGLDRVN 

       370        380        390        400        410        420 
EFLRVECVWI GSPEFVEETR DKTLKYAEKL AEKLDLEYWV EVGDDPFYLE GRKKEDRGIE 

       430        440        450        460        470        480 
FPDVPKYEMR LWLPHIKDER KGVAVTSANV HGTHFVEGFR IKDYKGRRVW TGCTGYGITR 

       490        500        510        520 
WVVGYLAQYG FNFDDWHPII KKKIKKLPEV PQLITWPKKD E

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		L77117 Genomic DNA. Translation: AAB99075.1.
PIRD64434.
RefSeqNP_248070.1. NC_000909.1.

3D structure databases

ProteinModelPortalQ58477.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1451973.
GenomeReviewsGene locus MJ1077 in contig L77117_GR.
KEGGmja:MJ_1077.
NMPDRfig|243232.1.peg.1107.
TIGRMJ1077.

Phylogenomic databases

HOGENOMHBG542255.
OMAAQCEPFY.
ProtClustDBPRK00960.

Enzyme and pathway databases

BioCycMJAN243232:MJ_1077-MONOMER.

Family and domain databases

HAMAPMF_01278. Ser_tRNA_synth_type2.
[Tree]
InterProIPR002314. aa-tRNA-synt_IIb_cons-dom.
IPR004503. Ser-tRNA-synth_IIa_arc.
[Graphical view]
KOK01875.
PfamPF00587. tRNA-synt_2b. 1 hit.
[Graphical view]
TIGRFAMsTIGR00415. SerS_MJ. 1 hit.
PROSITEPS50862. AA_TRNA_LIGASE_II. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYS2_METJA
AccessionPrimary (citable) accession number: Q58477
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: November 1, 1996
Last modified: January 25, 2012
This is version 76 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

Methanococcus jannaschii

Methanococcus jannaschii: entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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