Q6FZW4 (SYY_BARQU) 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:	BQ05920

Organism

Bartonella quintana (strain Toulouse) (Rochalimaea quintana) [Complete proteome] [HAMAP]

Taxonomic identifier

283165 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Bartonellaceae › Bartonella

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 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 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: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW RNA binding Inferred from electronic annotation. Source: UniProtKB-KW tyrosine-tRNA ligase activity Inferred from electronic annotation. Source: EC
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 MF_02006		PRO_0000234682
Regions
	Domain	350 – 417	68	S4 RNA-binding
	Motif	44 – 53	10	"HIGH" region HAMAP MF_02006
	Motif	236 – 240	5	"KMSKS" region HAMAP 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)
	Q6FZW4 [UniParc]. Last modified July 19, 2004. Version 1. Checksum: CDB16C5418A1EB34	FASTA	417	46,732
	10 20 30 40 50 60 MLAFKSDFLH IMSERGFIHQ ISDEKGLDAL FSKEVVSAYI GFDPTASSLH AGSLLQIMML 70 80 90 100 110 120 HWLQKTGHRP IALMGGGTGL IGDPSFKDEA RPLLTQDDIA TNIVSIKKVF ANYLTFGEKE 130 140 150 160 170 180 TDACIINNAE WLCKLNYLEF LRDVGKHFSI NRMLSFDSVR LRLEREHSLS FLEFNYMILQ 190 200 210 220 230 240 AYDFVELYKR YGLRMQMGGS DQWGNIINGI ELGHRLGTPQ LYAFTSPLLT TSSGAKMGKS 250 260 270 280 290 300 LNGAVWLNAD MLSPYQFWQY WRNTEDADVT RFLKLYTTLP MDEILKLSAL QGTEINEAKK 310 320 330 340 350 360 ILATEITAML HGRDLANTAA KTARKTFEEK TFGENLPTIE INASDLKTGA GLLALLVQAG 370 380 390 400 410 LAKSNSEARR HIQGGGIRVN DQIIEDETCL ILEEDINAQG IIKLSFGKKK HVLIKPL

References

[1]

"The louse-borne human pathogen Bartonella quintana is a genomic derivative of the zoonotic agent Bartonella henselae." Alsmark U.C.M., Frank A.C., Karlberg E.O., Legault B.-A., Ardell D.H., Canbaeck B., Eriksson A.-S., Naeslund A.K., Handley S.A., Huvet M., La Scola B., Holmberg M., Andersson S.G.E. Proc. Natl. Acad. Sci. U.S.A. 101:9716-9721(2004) [PubMed: 15210978] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Toulouse.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BX897700 Genomic DNA. Translation: CAF26084.1.
RefSeq	YP_032246.1. NC_005955.1.
3D structure databases
ProteinModelPortal	Q6FZW4.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	2866778.
GenomeReviews	Gene locus BQ05920 in contig BX897700_GR.
KEGG	bqu:BQ05920.
NMPDR	fig|283165.1.peg.516.
PATRIC	31952459. VBIBarQui58630_0658.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG288125.
OMA	TFYIGFD.
PhylomeDB	Q6FZW4.
ProtClustDB	PRK05912.
Enzyme and pathway databases
BioCyc	BQUI283165:BQ05920-MONOMER.
Family and domain databases
HAMAP	MF_02006. Tyr_tRNA_synth_type1. [Tree]
InterPro	IPR002305. aa-tRNA-synth_Ic. IPR014729. Rossmann-like_a/b/a_fold. IPR002942. S4_RNA-bd. IPR002307. Tyr-tRNA-synth. IPR024088. Tyr-tRNA-synth_bac-type. IPR024107. Tyr-tRNA-synth_bac_1. [Graphical view]
Gene3D	G3DSA:3.10.290.10. G3DSA:3.10.290.10. 1 hit. G3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 1 hit.
KO	K01866.
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...

Entry information

Entry name

SYY_BARQU

Accession

Primary (citable) accession number: Q6FZW4

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 16, 2006
Last sequence update:	July 19, 2004
Last modified:	January 25, 2012
This is version 46 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program