Reviewed, UniProtKB/Swiss-Prot Q72Y10 (SYY2_BACC1)

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
Ordered Locus Names:	BCE_5211

Organism

Bacillus cereus (strain ATCC 10987) [Complete proteome] [HAMAP]

Taxonomic identifier

222523 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group

Protein attributes

Sequence length	419 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 – 419	419	Tyrosyl-tRNA synthetase 2 HAMAP MF_02006		PRO_0000234670
Regions
	Domain	352 – 418	67	S4 RNA-binding
	Motif	39 – 48	10	"HIGH" region HAMAP MF_02006
	Motif	230 – 234	5	"KMSKS" region HAMAP MF_02006
Sites
	Binding site	34	1	Tyrosine By similarity
	Binding site	168	1	Tyrosine By similarity
	Binding site	172	1	Tyrosine By similarity
	Binding site	233	1	ATP By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q72Y10-1 [UniParc]. Last modified July 5, 2004. Version 1. Checksum: A5DDD47141B85805	FASTA	419	47,422
	10 20 30 40 50 60 MNIIDELEWR GAINQQTDEE GLRKLVEEKK ISLYCGVDPT GDSMHIGHLI PFMMMKRFQL 70 80 90 100 110 120 AGHHPVILIG GATGTIGDPS GRQSERQLQT LEVVQHNVDA LTAQMKKLFD FGGNSEVKMV 130 140 150 160 170 180 NNYDWTHEIN IIEFLRDYGK NFSINSMLAK DIVASRLDTG ISFTEFTYQI LQAMDFHHLY 190 200 210 220 230 240 TKEDVQLQIG GSDQWGNITS GLDLIRKLEG HEAKVFGLTI PLLLKSDGTK FGKSAGGAVW 250 260 270 280 290 300 LDPEKTTPFE FYQFWVNTDD RDVVKYLKYF TFLTKERIDE LAVKVETEPH KREAQKVLAE 310 320 330 340 350 360 EMTKFVHGEE ALLQAVKITE ALFSGDIKSL TADEIEQGFK EMPTFQSSKE TKNIVEWLVD 370 380 390 400 410 LGIEPSRRQA REDINNGAIS MNGEKVTDVG TDVTVENSFD GRFIIIRKGK KNYSLVKLG

References

[1]

"The genome sequence of Bacillus cereus ATCC 10987 reveals metabolic adaptations and a large plasmid related to Bacillus anthracis pXO1." Rasko D.A., Ravel J., Oekstad O.A., Helgason E., Cer R.Z., Jiang L., Shores K.A., Fouts D.E., Tourasse N.J., Angiuoli S.V., Kolonay J.F., Nelson W.C., Kolstoe A.-B., Fraser C.M., Read T.D. Nucleic Acids Res. 32:977-988(2004) [PubMed: 14960714] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE017194 Genomic DNA. Translation: AAS44112.1.
RefSeq	NP_981504.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q72Y10.
Genome annotation databases
GeneID	2751401.
GenomeReviews	Gene locus BCE_5211 in contig AE017194_GR.
KEGG	bca:BCE_5211.
NMPDR	fig|222523.1.peg.5176.
TIGR	BCE_5211.
Phylogenomic databases
HOGENOM	Q72Y10.
OMA	ISLYCGV.
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

SYY2_BACC1

Accession

Primary (citable) accession number: Q72Y10

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 16, 2006
Last sequence update:	July 5, 2004
Last modified:	November 3, 2009
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)