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Reviewed, UniProtKB/Swiss-Prot A0LUB6 (SYY_ACIC1)

Last modified February 9, 2010. Version 28. 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
    EC=6.1.1.1
Alternative name(s):
    Tyrosine--tRNA ligase
      Short name=TyrRS
Gene names
Name: tyrS
Ordered Locus Names: Acel_1254
OrganismAcidothermus cellulolyticus (strain ATCC 43068 / 11B) [Complete proteome] [HAMAP]
Taxonomic identifier351607 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesFrankineaeAcidothermaceaeAcidothermus

Protein attributes

Sequence length426 AA.
Sequence statusComplete.
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. HAMAP MF_02006

Catalytic activity

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

Subunit structure

Homodimer By similarity. HAMAP MF_02006

Subcellular location

Cytoplasm By similarity HAMAP MF_02006.

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 – 426426Tyrosyl-tRNA synthetase HAMAP MF_02006
PRO_1000088573

Regions

Domain358 – 41861S4 RNA-binding
Motif40 – 4910"HIGH" region HAMAP MF_02006
Motif234 – 2385"KMSKS" region HAMAP MF_02006

Sites

Binding site351Tyrosine By similarity
Binding site1741Tyrosine By similarity
Binding site1781Tyrosine By similarity
Binding site2371ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
A0LUB6-1 [UniParc].

Last modified December 12, 2006. Version 1.
Checksum: 7B289F9D1732ADED

FASTA42646,247
        10         20         30         40         50         60 
MTHLLDDLAW RGLIAQSTDL EALRAAMNTG PITVYCGFDP TAPSLHIGHL VQILTLRRFQ 

        70         80         90        100        110        120 
DAGHRPIALV GGATGLIGDP SGRTTERALN DPDVVAGWAE RIHRQLAPFL DFTGERAGQP 

       130        140        150        160        170        180 
AIAVNNLEWT GRLTAIEFLR DVGKHFRVGR MLAKEVVAAR LRSEQGISYT EFSYQILQSL 

       190        200        210        220        230        240 
DFLELYRRYR CVLQIGGIDQ WGNLTSGIEL IHKVEGVDVH ALATPLVTKA DGTKFGKTAG 

       250        260        270        280        290        300 
GAVWLDPALT SPYAFYQFWI NTDDRDVPAY LRYFSLKNKD ELEALEKDAG RDPAARLGQR 

       310        320        330        340        350        360 
ALAEELTTLV HGATECGKVV AASAALFGRG ELAGVEPETL AAALAEAGLV TMPFDPPPRV 

       370        380        390        400        410        420 
VDALVATGLV ESRSAARRVI SEGGAYVNNE KVTDVDAQID PGRLLHGRWA VIRRGRRAVA 


GVERAG 

« Hide

References

[1]"Complete sequence of Acidothermus cellulolyticus 11B."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Zharchuk I., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N. expand/collapse author list , Berry A.M., Adney W.S., Normand P., Leu D., Pujic P., Richardson P.
Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000481 Genomic DNA. Translation: ABK53026.1.
RefSeqYP_873012.1.

3D structure databases

SMRA0LUB6. Positions 4-424.
ModBaseSearch...

Protein-protein interaction databases

STRINGA0LUB6.

Genome annotation databases

GeneID4485154.
GenomeReviewsGene locus Acel_1254 in contig CP000481_GR.
KEGGace:Acel_1254.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0162.
HOGENOMHBG288125.
OMATFYIGFD.
PhylomeDBA0LUB6.

Family and domain databases

HAMAPMF_02006. Tyr_tRNA_synth_type1.
[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.
SMARTSM00363. S4. 1 hit.
[Graphical view]
TIGRFAMsTIGR00234. tyrS. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
PS50889. S4. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYY_ACIC1
AccessionPrimary (citable) accession number: A0LUB6
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: December 12, 2006
Last modified: February 9, 2010
This is version 28 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