Q8G5G1 (SYY_BIFLO) 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:	BL1051

Organism

Bifidobacterium longum (strain NCC 2705)

Taxonomic identifier

206672 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Bifidobacteriales › Bifidobacteriaceae › Bifidobacterium

Protein attributes

Sequence length	440 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 Reference 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 – 440	440	Tyrosine--tRNA ligase HAMAP MF_02006		PRO_0000234683
Regions
	Domain	373 – 439	67	S4 RNA-binding
	Motif	51 – 60	10	"HIGH" region HAMAP MF_02006
	Motif	241 – 245	5	"KMSKS" region HAMAP MF_02006
Sites
	Binding site	46	1	Tyrosine By similarity
	Binding site	181	1	Tyrosine By similarity
	Binding site	185	1	Tyrosine By similarity
	Binding site	244	1	ATP By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8G5G1 [UniParc]. Last modified March 1, 2003. Version 1. Checksum: FBDE326CB54AA636	FASTA	440	48,443
	10 20 30 40 50 60 MAHVTDFKEA GFNTLLEELE WRGLISQSTD RDRLAEALNG EPITYYCGFD PTAASLHIGN 70 80 90 100 110 120 LVQLINMRHL QLAGHHPIAL VGGATGLIGD PRQSGERTLN PKDVVAGWAD RLKNQIGGIL 130 140 150 160 170 180 DTEGANAVRF VSNYDWTASM TVIDFLRDVG KNFRLGTMLA KDTVARRLNS EEGISFTEFS 190 200 210 220 230 240 YQVLQGNDFL HLFDEYHCTL ELGGSDQWGN LTSGLDLIHK VRGVDVNVFT SPIITDASGK 250 260 270 280 290 300 KFGKSEGNAV WLDATMLSPY KFYQFWINRP DVEMESLLKA FTFLPKAEIE RLVEESKTNP 310 320 330 340 350 360 GKREAQKTLA WEVTSFVHGE AATQAAIDAS GALFGRGGNL EDIDEEMLES VLDGFKVVDE 370 380 390 400 410 420 NGEHVFPVSK PGDRVIDAAQ AAGLFKSASE ARRAIKSGGV YLNNNRIEDE EQVLAEADFL 430 440 AGRFALIRRG KKALGAVENR

References

[1]

"The genome sequence of Bifidobacterium longum reflects its adaptation to the human gastrointestinal tract." Schell M.A., Karmirantzou M., Snel B., Vilanova D., Berger B., Pessi G., Zwahlen M.-C., Desiere F., Bork P., Delley M., Pridmore R.D., Arigoni F. Proc. Natl. Acad. Sci. U.S.A. 99:14422-14427(2002) [PubMed: 12381787] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: NCC 2705.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE014295 Genomic DNA. Translation: AAN24857.1.
RefSeq	NP_696221.1. NC_004307.2.
3D structure databases
ProteinModelPortal	Q8G5G1.
SMR	Q8G5G1. Positions 15-326.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1022580.
GenomeReviews	Gene locus BL1051 in contig AE014295_GR.
KEGG	blo:BL1051.
NMPDR	fig|206672.1.peg.988.
PATRIC	21118583. VBIBifLon107831_0756.
Phylogenomic databases
HOGENOM	HBG288125.
OMA	TFYIGFD.
PhylomeDB	Q8G5G1.
ProtClustDB	PRK05912.
Enzyme and pathway databases
BioCyc	BLON206672:BL1051-MONOMER.
Family and domain databases
HAMAP	MF_02006. Tyr_tRNA_synth_type1. [Tree]
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-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. 1 hit. PS50889. S4. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SYY_BIFLO

Accession

Primary (citable) accession number: Q8G5G1

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 16, 2006
Last sequence update:	March 1, 2003
Last modified:	January 25, 2012
This is version 55 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program