Type-2 seryl-tRNA synthetase - Methanopyrus kandleri

Contribute

Send feedback

Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot Q8TVD2 (SYS2_METKA)

Last modified November 3, 2009. Version 48. 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

Hide | Top

Names and origin

Protein names

Recommended name:
    Type-2 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:	MK1460

Organism

Methanopyrus kandleri [Complete proteome] [HAMAP]

Taxonomic identifier

2320 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Methanopyri › Methanopyrales › Methanopyraceae › Methanopyrus

Hide | Top

Protein attributes

Sequence length	527 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

Hide | Top

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.
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.
Subcellular location	Cytoplasm By similarity.
Domain	Consists of two distinct domains, a catalytic core and a N-terminal extension that is presumably involved in tRNA binding By similarity.
Sequence similarities	Belongs to the class-II aminoacyl-tRNA synthetase family. Type-2 seryl-tRNA synthetase subfamily.

Hide | Top

Ontologies

Keywords
Biological process	Protein biosynthesis
Cellular component	Cytoplasm
Ligand	ATP-binding Metal-binding Nucleotide-binding Zinc
Molecular function	Aminoacyl-tRNA synthetase Ligase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	selenocysteine biosynthetic process Inferred from electronic annotation. Source: HAMAP seryl-tRNA aminoacylation Inferred from electronic annotation. Source: HAMAP
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: HAMAP serine-tRNA ligase activity Inferred from electronic annotation. Source: HAMAP zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Hide | Top

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 527

527

Type-2 seryl-tRNA synthetase HAMAP MF_01278

PRO_0000286169

Regions

Nucleotide binding

349 – 351

ATP By similarity

Nucleotide binding

360 – 361

ATP By similarity

Region

366 – 368

Serine binding By similarity

Sites

Metal binding

319

Zinc; catalytic By similarity

Metal binding

368

Zinc; catalytic By similarity

Metal binding

478

Zinc; catalytic By similarity

Binding site

317

Serine; via carbonyl oxygen By similarity

Binding site

349

Serine By similarity

Binding site

485

ATP By similarity

Hide | Top

Sequences

Sequence

Length

Mass (Da)

Tools

Q8TVD2-1 [UniParc].

Last modified June 1, 2002. Version 1.
Checksum: 7526147D81EFC5CD
Show »

FASTA

527

61,368

        10         20         30         40         50         60 
MELKFSAEVE LTLSREVDPA EIEPTVEEFV KEANEDLLQR GVPTGKEGAK IESYRVLEDT 

        70         80         90        100        110        120 
IEMEITGTRY LRPHEAAMRV RKRLAERLGR KHRVGVRDLK IPRYEVVLRF DREVTRDDVG 

       130        140        150        160        170        180 
YVPVADDVVV EDGTVRLTFQ DVDEEMLRRH VIDRVIRLVA WAVEERSELV ERVTKVEPGT 

       190        200        210        220        230        240 
VVDESGPREI RFDGDVTEEA RRRGWVKEFP GRGQWIYTPP MAALFEVLRD FLLERVTRKL 

       250        260        270        280        290        300 
GFEPALFPKL IPLETMFRMR YLHGLPDGMY YVCPPKRDPE LFDDFKRELY VWGELNERTL 

       310        320        330        340        350        360 
GSLKEKLRDP GYVLAPAQCE PFYELLRDEV VDPERLPIKL YDCSGWTYRW EGGAAKGLER 

       370        380        390        400        410        420 
VNEFQRIEHV WIAEPEEAER IREELLEATK RVAEELELEW KVVVSDDPFY LEGRLLEDRD 

       430        440        450        460        470        480 
IELPDVPSYE FEVYLPFKGE RSSEEAWISV GSFNVHGEHF VDGFNVKEKS GRTLFTGCAG 

       490        500        510        520 
LGVTRWVVGL LAQHGFEPEE WPEPILERID EKFGGLPEVP KTLTWPE

« Hide

Hide | Top

References

[1]

"The complete genome of hyperthermophile Methanopyrus kandleri AV19 and monophyly of archaeal methanogens."
Slesarev A.I., Mezhevaya K.V., Makarova K.S., Polushin N.N., Shcherbinina O.V., Shakhova V.V., Belova G.I., Aravind L., Natale D.A., Rogozin I.B., Tatusov R.L., Wolf Y.I., Stetter K.O., Malykh A.G., Koonin E.V., Kozyavkin S.A.
Proc. Natl. Acad. Sci. U.S.A. 99:4644-4649(2002) [PubMed: 11930014] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: AV19 / DSM 6324 / JCM 9639 / NBRC 100938.

Hide | Top

Cross-references

Sequence databases
	AE009439 Genomic DNA. Translation: AAM02673.1.
RefSeq	NP_614743.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	1478055.
GenomeReviews	Gene locus MK1460 in contig AE009439_GR.
KEGG	mka:MK1460.
NMPDR	fig\|190192.1.peg.1456.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q8TVD2.
OMA	PAQCEPF.
Enzyme and pathway databases
BioCyc	MKAN190192:MK1460-MON.
BRENDA	6.1.1.11. 7577.
Family and domain databases
HAMAP	MF_01278. [Tree]
InterPro	IPR002314. aa-tRNA-synt_IIb_cons-reg. IPR006195. aa-tRNA-synth_II_cons-reg. IPR004503. Ser-tRNA-synth_IIa_arc. IPR018156. Ser-tRNA-synth_IIa_C. [Graphical view]
PANTHER	PTHR11778. tRNA-synt_ser. 1 hit.
Pfam	PF00587. tRNA-synt_2b. 1 hit. [Graphical view]
TIGRFAMs	TIGR00415. serS_MJ. 1 hit.
PROSITE	PS50862. AA_TRNA_LIGASE_II. 1 hit. [Graphical view]
ProtoNet	Search...

Hide | Top

Entry information

Entry name

SYS2_METKA

Accession

Primary (citable) accession number: Q8TVD2

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 2007
Last sequence update:	June 1, 2002
Last modified:	November 3, 2009
This is version 48 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Hide | Top

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)

Molecule processing

Regions

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents