Reviewed, UniProtKB/Swiss-Prot Q6G3B6 (SYY_BARHE)

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:	BH08670

Organism

Bartonella henselae (Rochalimaea henselae) [Complete proteome] [HAMAP]

Taxonomic identifier

38323 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Bartonellaceae › Bartonella

Protein attributes

Sequence length	417 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.
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 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	Tyrosyl-tRNA synthetase HAMAP MF_02006		PRO_0000234681
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)
	Q6G3B6-1 [UniParc]. Last modified July 19, 2004. Version 1. Checksum: 3FA1D2F89207D3A2	FASTA	417	47,043
	10 20 30 40 50 60 MLAFKSDFLN IMSERGFIHQ ISDEKGLDAL FSKEVVSAYI GFDPTASSLH AGSLLQIMML 70 80 90 100 110 120 YWLQKTGHRP IVLMGGGTGL IGDPSFKDEA RRLLTQDDIA ANIADIKKVF ARYLTFGERE 130 140 150 160 170 180 TDSCIVNNAE WLCTLNYLEF LRDIGKHFSV NRMLSFDSVR LRLEREHSLS FLEFNYMILQ 190 200 210 220 230 240 AYDFVELYKR YGLRMQMGGS DQWGNIINGI ELGHRLGTPQ LYALTSPLLT TSSGAKMGKS 250 260 270 280 290 300 LNGAVWLNAD MLSPYQFWQY WRNTEDADVT RFLKLYTPLP MDEILKLSAL QGTEINEAKK 310 320 330 340 350 360 ILATEITAML HGRDLANAVA ETARKTFEER TLGENLPTFE INANDLKMGT GLLILLVQAG 370 380 390 400 410 LSKSNSEARR HIQGGGVRVN DHIIEDETHL IREEDINAQG 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: ATCC 49882 / Houston 1.

Cross-references

Sequence databases
EMBLGenBankDDBJ	BX897699 Genomic DNA. Translation: CAF27665.1.
RefSeq	YP_033671.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	2864845.
GenomeReviews	Gene locus BH08670 in contig BX897699_GR.
KEGG	bhe:BH08670.
NMPDR	fig|283166.1.peg.799.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q6G3B6.
OMA	TFYIGFD.
Enzyme and pathway databases
BioCyc	BHEN283166:BH08670-MON.
BRENDA	6.1.1.1. 277357.
Family and domain databases
HAMAP	MF_02006. [Tree]
InterPro	IPR001412. 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]
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...

Entry information

Entry name

SYY_BARHE

Accession

Primary (citable) accession number: Q6G3B6

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 16, 2006
Last sequence update:	July 19, 2004
Last modified:	November 3, 2009
This is version 31 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)