Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot Q9YFY3 (SYT2_AERPE)

Last modified July 28, 2009. Version 55. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:
    Probable threonyl-tRNA synthetase 2
    EC=6.1.1.3
Alternative name(s):
    Threonine--tRNA ligase 2
      Short name=ThrRS 2
Gene names
Name: thrS2
Ordered Locus Names: APE_0117.1
OrganismAeropyrum pernix [Complete proteome] [HAMAP]
Taxonomic identifier56636 [NCBI]
Taxonomic lineageArchaeaCrenarchaeotaThermoproteiDesulfurococcalesDesulfurococcaceaeAeropyrum

Protein attributes

Sequence length421 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Catalytic activity

ATP + L-threonine + tRNA(Thr) = AMP + diphosphate + L-threonyl-tRNA(Thr). HAMAP MF_00184

Subcellular location

Cytoplasm Potential.

Miscellaneous

There are two ThrRS in this archaea. The first one (APE_0809.1) is most similar to bacterial ThrRS but it lack the N-terminal domain. The second one (APE_0117.1) is most similar to archaeal ThrRS but lacks the central domain. HAMAP MF_00184

Sequence similarities

Belongs to the class-II aminoacyl-tRNA synthetase family.

Ontologies

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

threonine-tRNA ligase activity

Inferred from electronic annotation. Source: HAMAP

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 421421Probable threonyl-tRNA synthetase 2 HAMAP MF_00184
PRO_0000101118

Sequences

Sequence LengthMass (Da)Tools
Q9YFY3-1 [UniParc].

Last modified June 26, 2007. Version 2.
Checksum: 9B311637CE9FBC73

FASTA42145,003
        10         20         30         40         50         60 
MRLLYLHADR FEYKTVKPAL KNPPDPPGEA SFGEALVVFT TVEDGDGPQT VMYAASDIAS 

        70         80         90        100        110        120 
HSSRLKVTTV ILYPYAHLSS RLAKPMAAHK RLIELEGALR TKFPGHVHRA PFGWYKSFSI 

       130        140        150        160        170        180 
ACKGHPLAEL SRSFTEAGAL QPWPAVEDYK TGLSGEVLAR AGLLGGGSLS PASWALEVHR 

       190        200        210        220        230        240 
RLAEEVVGPA ESVGFGESLS EAYQACISSS VTTLLMGPYP PSIVFGPLED DPVEAVSRVL 

       250        260        270        280        290        300 
GLISPQLEGV KPLLSGGEGA LKASSPDGAE LPVAFLKEGR VCLGPTLSFF KLAVSMLVEK 

       310        320        330        340        350        360 
ARKEGLTPYL NPTLTPVQSA VIPVDSESEG YAQRIAEDLA ASGVRVSIVR GSGLGRRVRE 

       370        380        390        400        410        420 
AGRSWASLVI VVGKREEETG TVVVRRRWEP GKQEVLTLDE LSSEAKKLAS GSRGSLYSTT 


L 

« Hide

References

[1]"Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon, Aeropyrum pernix K1."
Kawarabayasi Y., Hino Y., Horikawa H., Yamazaki S., Haikawa Y., Jin-no K., Takahashi M., Sekine M., Baba S., Ankai A., Kosugi H., Hosoyama A., Fukui S., Nagai Y., Nishijima K., Nakazawa H., Takamiya M., Masuda S. expand/collapse author list , Funahashi T., Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Kubota K., Nakamura Y., Nomura N., Sako Y., Kikuchi H.
DNA Res. 6:83-101(1999) [PubMed: 10382966] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K1.

Cross-references

Sequence databases

BA000002 Genomic DNA. Translation: BAA79028.2.
PIRB72766.
RefSeqNP_146977.2.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID1445659.
GenomeReviewsGene locus APE_0117.1 in contig BA000002_GR.
KEGGape:APE_0117.1.
NMPDRfig|272557.1.peg.84.

Organism-specific databases

CMRSearch...

Enzyme and pathway databases

BRENDA6.1.1.3. 256344.

Family and domain databases

HAMAPMF_00184. Divergent sequence.
[Tree]
InterProIPR004154. Anticodon_bd.
IPR015011. Threonyl-tRNA_syntase_arc.
[Graphical view]
Gene3DG3DSA:3.40.50.800. Anticodon_bd. 1 hit.
PfamPF03129. HGTP_anticodon. 1 hit.
PF08915. tRNA-Thr_ED. 1 hit.
[Graphical view]
PROSITEPS50862. AA_TRNA_LIGASE_II. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYT2_AERPE
AccessionPrimary (citable) accession number: Q9YFY3
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: June 26, 2007
Last modified: July 28, 2009
This is version 55 of the entry and version 2 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

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