Reviewed, UniProtKB/Swiss-Prot Q5M4D1 (SYY2_STRT2)

Names and origin

Protein names

Recommended name:
    Tyrosyl-tRNA synthetase 2
    EC=6.1.1.1
Alternative name(s):
    Tyrosine--tRNA ligase 2
      Short name=TyrRS 2

Gene names

Name:	tyrS2
Synonyms:	tyrSE
Ordered Locus Names:	stu1043

Organism

Streptococcus thermophilus (strain ATCC BAA-250 / LMG 18311) [Complete proteome] [HAMAP]

Taxonomic identifier

264199 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Lactobacillales › Streptococcaceae › Streptococcus

Protein attributes

Sequence length	302 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.

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 – 302	302	Tyrosyl-tRNA synthetase 2 HAMAP MF_02006		PRO_0000234796
Regions
	Motif	38 – 47	10	"HIGH" region HAMAP MF_02006
	Motif	220 – 224	5	"KMSKS" region HAMAP MF_02006
Sites
	Binding site	33	1	Tyrosine By similarity
	Binding site	160	1	Tyrosine By similarity
	Binding site	164	1	Tyrosine By similarity
	Binding site	223	1	ATP By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q5M4D1-1 [UniParc]. Last modified February 1, 2005. Version 1. Checksum: DED6C3109420909F	FASTA	302	34,298
	10 20 30 40 50 60 MKLFEDLQWR GLVKQYSSDS LIEKLNNGKL TFYIGTDPTA DSLHLGHYSS FLIAKRLAKY 70 80 90 100 110 120 GHQPIILIGG ATALVGDPRG TSERDLAEQE KIFDNFEKLK NQIQKIFPYE IVNNYDWTKN 130 140 150 160 170 180 IMAIDFLREF GKHITAGYMS NKELVKRQFA TGISFTEFSY MLLQGMDFYH LFTTKGVTLQ 190 200 210 220 230 240 IAGSDQWGNM TTGIDLVRKK TGEEVFAMTM PLITDEEGKK FGKSEGNAIW ISENKNTPEE 250 260 270 280 290 300 LHNFLLNVSD DIVISLLKKL TFLSRKDIEE IESRHKNGTG YAQGILADTV TFDIHGVSIN KK

References

[1]

"Complete sequence and comparative genome analysis of the dairy bacterium Streptococcus thermophilus." Bolotin A., Quinquis B., Renault P., Sorokin A., Ehrlich S.D., Kulakauskas S., Lapidus A., Goltsman E., Mazur M., Pusch G.D., Fonstein M., Overbeek R., Kyprides N., Purnelle B., Prozzi D., Ngui K., Masuy D., Hancy F. , Burteau S., Boutry M., Delcour J., Goffeau A., Hols P. Nat. Biotechnol. 22:1554-1558(2004) [PubMed: 15543133] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000023 Genomic DNA. Translation: AAV60695.1.
RefSeq	YP_139510.1.
3D structure databases
SMR	Q5M4D1. Positions 3-298.
ModBase	Search...
Genome annotation databases
GeneID	3165091.
GenomeReviews	Gene locus stu1043 in contig CP000023_GR.
KEGG	stl:stu1043.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0162.
HOGENOM	HBG288125.
OMA	GNYVQIV.
PhylomeDB	Q5M4D1.
Enzyme and pathway databases
BioCyc	STHE264199:STU1043-MONOMER.
Family and domain databases
HAMAP	MF_02006. Tyr_tRNA_synth_type1. Divergent sequence. [Tree]
InterPro	IPR001412. aa-tRNA-synth_I_CS. IPR002305. aa-tRNA-synth_Ib. IPR014729. Rossmann-like_a/b/a_fold. 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.
TIGRFAMs	TIGR00234. tyrS. 1 hit.
PROSITE	PS00178. AA_TRNA_LIGASE_I. 1 hit. PS50889. S4. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SYY2_STRT2

Accession

Primary (citable) accession number: Q5M4D1

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 16, 2006
Last sequence update:	February 1, 2005
Last modified:	February 9, 2010
This is version 35 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)