Reviewed, UniProtKB/Swiss-Prot Q8A2S5 (SYY_BACTN)

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:	BT_3230

Organism

Bacteroides thetaiotaomicron [Complete proteome] [HAMAP]

Taxonomic identifier

818 [NCBI]

Taxonomic lineage

Bacteria › Bacteroidetes › Bacteroidia › Bacteroidales › Bacteroidaceae › Bacteroides

Protein attributes

Sequence length	430 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 – 430	430	Tyrosyl-tRNA synthetase HAMAP MF_02006		PRO_0000234680
Regions
	Domain	362 – 429	68	S4 RNA-binding
	Motif	37 – 46	10	"HIGH" region HAMAP MF_02006
	Motif	232 – 236	5	"KMSKS" region HAMAP MF_02006
Sites
	Binding site	32	1	Tyrosine By similarity
	Binding site	172	1	Tyrosine By similarity
	Binding site	176	1	Tyrosine By similarity
	Binding site	235	1	ATP By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8A2S5-1 [UniParc]. Last modified June 1, 2003. Version 1. Checksum: E7B3EBAFDB28E5B9	FASTA	430	48,380
	10 20 30 40 50 60 MNFVEELRWR GMLQDIMPGT EELLNKEQVT AYLGIDPTAD SLHIGHLCGV MILRHLQRCG 70 80 90 100 110 120 HKPLALIGGA TGMIGDPSGK SAERNLLNEE TLRHNQACIK KQLAKFLDFE SDVPNRAELV 130 140 150 160 170 180 NNYDWMKEFS FLDFVREVGK HITVNYMMAK DSVKRRLNGE ARDGLSFTEF TYQLLQGYDF 190 200 210 220 230 240 LHLYETKGCK LQMGGSDQWG NITTGAELIR RTNGGEVFAL TCPLITKADG GKFGKTESGN 250 260 270 280 290 300 IWLDPRYTSP YKFYQFWLNV SDSDAERYIK IFTSIEKEEI EALVAEHQQA PHLRALQKRL 310 320 330 340 350 360 AKEVTIMVHS EEDYNAAVDA SNILFGNATS ESLRKLDEDT LLAVFEGVPQ FEISRDALAE 370 380 390 400 410 420 GVKAVDLFVD NAAVFASKGE MRKLVQGGGV SLNKEKLEAF DQVITTADLL DGKYLLVQRG 430 KKNYFLLIAK

References

[1]

"A genomic view of the human-Bacteroides thetaiotaomicron symbiosis." Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K., Chiang H.C., Hooper L.V., Gordon J.I. Science 299:2074-2076(2003) [PubMed: 12663928] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE015928 Genomic DNA. Translation: AAO78336.1.
RefSeq	NP_812142.1.
3D structure databases
HSSP	HSSP built from PDB template 2TS1 based on UniProtKB P00952.
ModBase	Search...
Genome annotation databases
GeneID	1072868.
GenomeReviews	Gene locus BT_3230 in contig AE015928_GR.
KEGG	bth:BT_3230.
NMPDR	fig|226186.1.peg.3229.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q8A2S5.
OMA	TFYIGFD.
Enzyme and pathway databases
BioCyc	BTHE226186:BT_3230-MON.
BRENDA	6.1.1.1. 21018.
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	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. 1 hit. PS50889. S4. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SYY_BACTN

Accession

Primary (citable) accession number: Q8A2S5

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 16, 2006
Last sequence update:	June 1, 2003
Last modified:	November 3, 2009
This is version 44 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)