Q57DI5 (SYY_BRUAB) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Tyrosine--tRNA ligase
EC=6.1.1.1

Alternative name(s):
Tyrosyl-tRNA synthetase
Short name=TyrRS

Gene names

Name:	tyrS
Ordered Locus Names:	BruAb1_0935

Organism

Brucella abortus biovar 1 (strain 9-941) [Complete proteome] [HAMAP]

Taxonomic identifier

262698 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Brucellaceae › Brucella › Brucella abortus › Brucella abortus bv. 1

Protein attributes

Sequence length	417 AA.
Sequence status	Complete.
Protein existence	Inferred 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-Rule MF_02006
Catalytic activity	ATP + L-tyrosine + tRNA(Tyr) = AMP + diphosphate + L-tyrosyl-tRNA(Tyr). HAMAP-Rule MF_02006
Subunit structure	Homodimer By similarity. HAMAP-Rule MF_02006
Subcellular location	Cytoplasm By similarity HAMAP-Rule 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 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...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 417	417	Tyrosine--tRNA ligase HAMAP-Rule MF_02006		PRO_0000234688
Regions
	Domain	350 – 417	68	S4 RNA-binding
	Motif	44 – 53	10	"HIGH" region HAMAP-Rule MF_02006
	Motif	236 – 240	5	"KMSKS" region HAMAP-Rule MF_02006
Sites
	Binding site	39	1	Tyrosine By similarity
	Binding site	176	1	Tyrosine By similarity
	Binding site	180	1	Tyrosine By similarity
	Binding site	239	1	ATP By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q57DI5 [UniParc]. Last modified May 10, 2005. Version 1. Checksum: 2D734F3E7A2D83EC	FASTA	417	46,157
	10 20 30 40 50 60 MSGFKSDFLR TLSERGFIHQ ISDESGLDEL LAKETVTAYI GFDPTAPSLH AGGLIQIMML 70 80 90 100 110 120 YWLQQTGHKP VALMGGGTGM VGDPSFKDEA RKLMTEDTIA ENMASIKRVF ANYLTFGDGA 130 140 150 160 170 180 NDALMVNNGE WLRNINYLEF LRDVGRHFSV NRMLSFDSVK LRLDREQSLS FLEFNYMILQ 190 200 210 220 230 240 AYDFVELNKR YGLRLQMGGS DQWGNIVNGI DLGHRMGTPQ LYALTSPLLT TASGQKMGKS 250 260 270 280 290 300 LGGAIWLNAD MLSAYDFWQY WRNTEDADVE RFLKLYTTLP LDEIARLAEL GGAEINEAKK 310 320 330 340 350 360 ILATEVTAML HGRDAAEEAA ETARKTFEDG ELSENLPTVG VHKATLNDGI GVLALMVLAE 370 380 390 400 410 LCTTNGEARR HVEGGAVRIN DEPVSDPRMV VNAAALNDQG LIKLSLGKKR HVLIRPA

References

[1]

"Completion of the genome sequence of Brucella abortus and comparison to the highly similar genomes of Brucella melitensis and Brucella suis." Halling S.M., Peterson-Burch B.D., Bricker B.J., Zuerner R.L., Qing Z., Li L.-L., Kapur V., Alt D.P., Olsen S.C. J. Bacteriol. 187:2715-2726(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 9-941.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE017223 Genomic DNA. Translation: AAX74299.1.
RefSeq	YP_221660.1. NC_006932.1.
3D structure databases
ProteinModelPortal	Q57DI5.
ModBase	Search...
Protein-protein interaction databases
STRING	262698.BruAb1_0935.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAX74299; AAX74299; BruAb1_0935.
GeneID	3341098.
KEGG	bmb:BruAb1_0935.
PATRIC	17823508. VBIBruAbo15061_0984.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0162.
HOGENOM	HOG000242790.
KO	K01866.
OMA	GKKKHVL.
ProtClustDB	PRK05912.
Enzyme and pathway databases
BioCyc	BABO262698:GJC2-949-MONOMER.
Family and domain databases
Gene3D	3.10.290.10. 1 hit. 3.40.50.620. 1 hit.
HAMAP	MF_02006. Tyr_tRNA_synth_type1.
InterPro	IPR001412. aa-tRNA-synth_I_CS. IPR002305. aa-tRNA-synth_Ic. IPR014729. Rossmann-like_a/b/a_fold. IPR002942. S4_RNA-bd. IPR002307. Tyr-tRNA-ligase. IPR024088. Tyr-tRNA-ligase_bac-type. IPR024107. Tyr-tRNA-ligase_bac_1. [Graphical view]
PANTHER	PTHR11766. PTHR11766. 1 hit.
Pfam	PF00579. tRNA-synt_1b. 1 hit. [Graphical view]
PRINTS	PR01040. TRNASYNTHTYR.
TIGRFAMs	TIGR00234. tyrS. 1 hit.
PROSITE	PS00178. AA_TRNA_LIGASE_I. 1 hit. PS50889. S4. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SYY_BRUAB

Accession

Primary (citable) accession number: Q57DI5

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 16, 2006
Last sequence update:	May 10, 2005
Last modified:	May 1, 2013
This is version 50 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program