Reviewed, UniProtKB/Swiss-Prot Q5M2F3 (SYY1_STRT2)

Names and origin

Protein names

Recommended name:
    Tyrosyl-tRNA synthetase 1
    EC=6.1.1.1
Alternative name(s):
    Tyrosine--tRNA ligase 1
      Short name=TyrRS 1

Gene names

Name:	tyrS1
Ordered Locus Names:	stu1870

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	418 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 – 418	418	Tyrosyl-tRNA synthetase 1 HAMAP MF_02006		PRO_0000234795
Regions
	Domain	352 – 418	67	S4 RNA-binding
	Motif	39 – 48	10	"HIGH" region HAMAP MF_02006
	Motif	229 – 233	5	"KMSKS" region HAMAP MF_02006
Sites
	Binding site	34	1	Tyrosine By similarity
	Binding site	169	1	Tyrosine By similarity
	Binding site	173	1	Tyrosine By similarity
	Binding site	232	1	ATP By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q5M2F3-1 [UniParc]. Last modified May 16, 2006. Version 2. Checksum: BD7F0145B94E258F	FASTA	418	47,225
	10 20 30 40 50 60 MTIFEELKAR GLIFQTTDEE ALVKAFEEGP VSFYTGYDPT ADSLHLGHLV AILTSRRLQL 70 80 90 100 110 120 AGHKPYALVG GATGLIGDPS FKDAERSLQT KETVEGWVEK IQGQLSRFLD FENGDNKAVM 130 140 150 160 170 180 VNNYDWFGSV SFIDFLRDVG KYFTVNYMMS KESVKKRIET GISYTEFAYQ IMQGYDFYEL 190 200 210 220 230 240 NAKYGVTLQI GGSDQWGNMT AGTELLRRKA DKSGHVITVP LITDSTGKKF GKSEGNAVWL 250 260 270 280 290 300 DATKTTPYEM YQFWLNVMDD DAVRFLKIFT FLSLEEIEEI GKEFDQARHQ RLAQKVLARE 310 320 330 340 350 360 VVTLVHGKEA YEQAVHITEQ LFAGNLKALS ARDLKVALNG VPTYEISADE NLNIVELLVN 370 380 390 400 410 AKISPSKRQA REDVQNGAIY INGERVQDLD YTLSDTDKID NEITVIRRGK KKNFVLTY

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
EMBLGenBankDDBJ	CP000023 Genomic DNA. Translation: AAV61469.1. Different initiation.
RefSeq	YP_140284.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q5M2F3.
Genome annotation databases
GeneID	3163872.
GenomeReviews	Gene locus stu1870 in contig CP000023_GR.
KEGG	stl:stu1870.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q5M2F3.
OMA	TFYIGFD.
Enzyme and pathway databases
BioCyc	STHE264199:STU1870-MON.
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. 1 hit. PS50889. S4. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SYY1_STRT2

Accession

Primary (citable) accession number: Q5M2F3

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 16, 2006
Last sequence update:	May 16, 2006
Last modified:	November 3, 2009
This is version 31 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)