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Reviewed, UniProtKB/Swiss-Prot Q3II62 (SYY1_PSEHT)

Last modified November 3, 2009. Version 30. 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:
    Tyrosyl-tRNA synthetase 1
    EC=6.1.1.1
Alternative name(s):
    Tyrosine--tRNA ligase 1
      Short name=TyrRS 1
Gene names
Name: tyrS1
Ordered Locus Names: PSHAa2413
OrganismPseudoalteromonas haloplanktis (strain TAC 125) [Complete proteome] [HAMAP]
Taxonomic identifier326442 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesPseudoalteromonadaceaePseudoalteromonas

Protein attributes

Sequence length420 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Function

Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr) By similarity.

Catalytic activity

ATP + L-tyrosine + tRNA(Tyr) = AMP + diphosphate + L-tyrosyl-tRNA(Tyr). HAMAP MF_02006

Subunit structure

Homodimer By similarity.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the class-I aminoacyl-tRNA synthetase family. TyrS type 1 subfamily.

Contains 1 S4 RNA-binding domain.

Ontologies

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

RNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

tyrosine-tRNA ligase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 420420Tyrosyl-tRNA synthetase 1 HAMAP MF_02006
PRO_0000234752

Regions

Domain355 – 41965S4 RNA-binding
Motif40 – 4910"HIGH" region HAMAP MF_02006
Motif232 – 2365"KMSKS" region HAMAP MF_02006

Sites

Binding site351Tyrosine By similarity
Binding site1721Tyrosine By similarity
Binding site1761Tyrosine By similarity
Binding site2351ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q3II62-1 [UniParc].

Last modified November 8, 2005. Version 1.
Checksum: 66DFB6C036EC6824

FASTA42046,895
        10         20         30         40         50         60 
MTTQLLEDIT HRGLVSQVSD LAQLEQLLAT SQVVYCGFDP TAGSLHIGHL VPLLMLKRFN 

        70         80         90        100        110        120 
DAGHKAVALI GGATGLIGDP SFKATERSLN SKETVQGWVA DLSSQVESVM NPHLSEPIQL 

       130        140        150        160        170        180 
KNNADWFSGI EVLDFFRDVG KHFSINNMIN RESVKQRLQR PDQGLSFTEF SYTLLQSYDF 

       190        200        210        220        230        240 
AKLNSELGCS VQIGGNDQWG NIVSGIDLTR RLNKQTVYGL TLPLITKSDG TKFGKTEGGA 

       250        260        270        280        290        300 
IWLDPKKTSP YRFYQFWLNC DDADVYNFLR FYTFLSVKEI EAIEANDITS QQKPQAQGIL 

       310        320        330        340        350        360 
AEQLTRFVHG EQGLASAQRI TQLLFNGQVQ TLTLAELEQL EQDGLAVHAI SDAKINIAEL 

       370        380        390        400        410        420 
LVKSELASSK RTARELINAN AIKINGEAIT DEHAQLDFPL FDRFWVMQRG KKQFRLIKLA 

« Hide

References

[1]"Coping with cold: the genome of the versatile marine Antarctica bacterium Pseudoalteromonas haloplanktis TAC125."
Medigue C., Krin E., Pascal G., Barbe V., Bernsel A., Bertin P.N., Cheung F., Cruveiller S., D'Amico S., Duilio A., Fang G., Feller G., Ho C., Mangenot S., Marino G., Nilsson J., Parrilli E., Rocha E.P.C. expand/collapse author list , Rouy Z., Sekowska A., Tutino M.L., Vallenet D., von Heijne G., Danchin A.
Genome Res. 15:1325-1335(2005) [PubMed: 16169927] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CR954246 Genomic DNA. Translation: CAI87462.1.
RefSeqYP_340904.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGQ3II62.

Genome annotation databases

GeneID3710330.
GenomeReviewsGene locus PSHAa2413 in contig CR954246_GR.
KEGGpha:PSHAa2413.
NMPDRfig|326442.4.peg.2503.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ3II62.
OMATFYIGFD.

Enzyme and pathway databases

BioCycPHAL326442:PSHAA2413-MON.

Family and domain databases

HAMAPMF_02006.
[Tree]
InterProIPR001412. aa-tRNA-synth_I_CS.
IPR002305. aa-tRNA-synth_Ib.
IPR014729. Rossmann-like_a/b/a_fold.
IPR002942. S4_RNA_bd.
IPR002307. Tyr-tRNA-synth_Ib_bac/mito.
[Graphical view]
Gene3DG3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 1 hit.
PANTHERPTHR11766. Tyr_tRNA-synt_1b. 1 hit.
PfamPF01479. S4. 1 hit.
PF00579. tRNA-synt_1b. 1 hit.
[Graphical view]
PRINTSPR01040. TRNASYNTHTYR.
TIGRFAMsTIGR00234. tyrS. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
PS50889. S4. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYY1_PSEHT
AccessionPrimary (citable) accession number: Q3II62
Entry history
Integrated into UniProtKB/Swiss-Prot: May 16, 2006
Last sequence update: November 8, 2005
Last modified: November 3, 2009
This is version 30 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

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