Tyrosyl-tRNA synthetase - Agrobacterium tumefaciens (strain C58 / ATCC 33970)

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Reviewed, UniProtKB/Swiss-Prot Q8UED2 (SYY_AGRT5)

Last modified February 9, 2010. Version 43. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended 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:	Atu1828
ORF Names:	AGR_C_3358

Organism

Agrobacterium tumefaciens (strain C58 / ATCC 33970) [Complete proteome] [HAMAP]

Taxonomic identifier

176299 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Rhizobiaceae › Rhizobium/Agrobacterium group › Agrobacterium

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Protein attributes

Sequence length	417 AA.
Sequence status	Complete.
Protein existence	Inferred from homology.

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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.

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Ontologies

Keywords
Biological process	Protein biosynthesis
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding RNA-binding
Molecular function	Aminoacyl-tRNA synthetase Ligase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	tyrosyl-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 RNA binding Inferred from electronic annotation. Source: UniProtKB-KW tyrosine-tRNA ligase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 417

417

Tyrosyl-tRNA synthetase HAMAP MF_02006

PRO_0000234663

Regions

Domain

350 – 416

S4 RNA-binding

Motif

44 – 53

"HIGH" region HAMAP MF_02006

Motif

236 – 240

"KMSKS" region HAMAP MF_02006

Sites

Binding site

Tyrosine By similarity

Binding site

176

Tyrosine By similarity

Binding site

180

Tyrosine By similarity

Binding site

239

ATP By similarity

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Sequences

Sequence

Length

Mass (Da)

Tools

Q8UED2-1 [UniParc].

Last modified June 1, 2002. Version 1.
Checksum: B0CD8353E7FFFEF6
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FASTA

417

46,117

        10         20         30         40         50         60 
MSRFKSDFLR TLDERGFIHQ ISDEAGLDEL FAKETVTAYI GYDPTASSLH VGHLTQIMML 

        70         80         90        100        110        120 
HWMQKTGHQP ISLMGGGTGM VGDPSFKEEA RKLMTIDMIE DNITSLKHVF ANYLDYDRAE 

       130        140        150        160        170        180 
NPALMINNAD WLRGLNYLEF LRDVGRHFSV NRMLSFDSVK TRLDREQSLS FLEFNYMILQ 

       190        200        210        220        230        240 
AYDFVELNQR TGCRLQMGGS DQWGNIINGI DLGHRMGTPQ LYALTSPLLT TSSGAKMGKS 

       250        260        270        280        290        300 
ASGAVWLNKD LLPVYDFWQY WRNTEDADVV RFAKLFTTLP MDEIARIATL GGSEINEAKK 

       310        320        330        340        350        360 
ILATEVTAIL HGRAAAEEAA ETARKTFEEG ALAENLPSIE VPTSELDAGV GVLSLIVRAG 

       370        380        390        400        410 
LASSNGEARR HVQGGAVKIN EQGVSDERQI IGTGEVTGDG VIKLSVGKKK HVLVRPA

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References

[1]

"The genome of the natural genetic engineer Agrobacterium tumefaciens C58."
Wood D.W., Setubal J.C., Kaul R., Monks D.E., Kitajima J.P., Okura V.K., Zhou Y., Chen L., Wood G.E., Almeida N.F. Jr., Woo L., Chen Y., Paulsen I.T., Eisen J.A., Karp P.D., Bovee D. Sr., Chapman P., Clendenning J.

Nester E.W.
Science 294:2317-2323(2001) [PubMed: 11743193] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

[2]

"Genome sequence of the plant pathogen and biotechnology agent Agrobacterium tumefaciens C58."
Goodner B., Hinkle G., Gattung S., Miller N., Blanchard M., Qurollo B., Goldman B.S., Cao Y., Askenazi M., Halling C., Mullin L., Houmiel K., Gordon J., Vaudin M., Iartchouk O., Epp A., Liu F., Wollam C.

Slater S.
Science 294:2323-2328(2001) [PubMed: 11743194] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

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Cross-references

Sequence databases
EMBL GenBank DDBJ	AE007869 Genomic DNA. Translation: AAK87597.2.
PIR	AB2801. D97580.
RefSeq	NP_354812.2.
3D structure databases
SMR	Q8UED2. Positions 6-321, 9-416.
ModBase	Search...
Protein-protein interaction databases
STRING	Q8UED2.
Genome annotation databases
GeneID	1133866.
GenomeReviews	Gene locus Atu1828 in contig AE007869_GR.
KEGG	atc:AGR_C_3358. atu:Atu1828.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0162.
HOGENOM	HBG288125.
OMA	TFYIGFD.
PhylomeDB	Q8UED2.
Enzyme and pathway databases
BioCyc	ATUM176299-1:ATU1828-MONOMER.
Family and domain databases
HAMAP	MF_02006. Tyr_tRNA_synth_type1. [Tree]
InterPro	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]
Gene3D	G3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 1 hit.
PANTHER	PTHR11766. Tyr_tRNA-synt_1b. 1 hit.
Pfam	PF01479. S4. 1 hit. PF00579. tRNA-synt_1b. 1 hit. [Graphical view]
PRINTS	PR01040. TRNASYNTHTYR.
SMART	SM00363. S4. 1 hit. [Graphical view]
TIGRFAMs	TIGR00234. tyrS. 1 hit.
PROSITE	PS00178. AA_TRNA_LIGASE_I. False negative. PS50889. S4. 1 hit. [Graphical view]
ProtoNet	Search...

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Entry information

Entry name

SYY_AGRT5

Accession

Primary (citable) accession number: Q8UED2
Secondary accession number(s): Q7CYF7

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 16, 2006
Last sequence update:	June 1, 2002
Last modified:	February 9, 2010
This is version 43 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)

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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)

Molecule processing

Regions

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents