Reviewed, UniProtKB/Swiss-Prot Q815S0 (SYY2_BACCR)

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:	BC_5062

Organism

Bacillus cereus (strain ATCC 14579 / DSM 31) [Complete proteome] [HAMAP]

Taxonomic identifier

226900 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	420 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 – 420	420	Tyrosyl-tRNA synthetase 2 HAMAP MF_02006		PRO_0000234672
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)
	Q815S0-1 [UniParc]. Last modified June 1, 2003. Version 1. Checksum: CC04F6E7FE2D2648	FASTA	420	47,557
	10 20 30 40 50 60 MNIIDELEWR GAVNQQTDEE 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 RDVIKYLKYF TFLTKERIDE LATKVEVEPH KREAQKVLAE 310 320 330 340 350 360 EMTKFVHGEE AFLQAEKITA ALFSGDIKSL TADEIEQGFK EMPTFQSSKE TKNIVEWLVD 370 380 390 400 410 420 LGIEPSRRQA REDINNGAIS MNGEKVTDVG TDVTVENSFD GRFIIIRKGK KNYSLVKLGE

References

[1]

"Genome sequence of Bacillus cereus and comparative analysis with Bacillus anthracis." Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., Kapatral V., Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., Chu L., Mazur M., Goltsman E., Larsen N., D'Souza M., Walunas T., Grechkin Y., Pusch G. , Haselkorn R., Fonstein M., Ehrlich S.D., Overbeek R., Kyrpides N.C. Nature 423:87-91(2003) [PubMed: 12721630] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE016877 Genomic DNA. Translation: AAP11931.1.
RefSeq	NP_834730.1.
3D structure databases
HSSP	HSSP built from PDB template 2TS1 based on UniProtKB P00952.
ModBase	Search...
Protein-protein interaction databases
STRING	Q815S0.
Genome annotation databases
GeneID	1207403.
GenomeReviews	Gene locus BC_5062 in contig AE016877_GR.
KEGG	bce:BC5062.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q815S0.
OMA	ISLYCGV.
Enzyme and pathway databases
BioCyc	BCER226900:BC_5062-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

SYY2_BACCR

Accession

Primary (citable) accession number: Q815S0

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 16, 2006
Last sequence update:	June 1, 2003
Last modified:	November 3, 2009
This is version 34 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)