Reviewed, UniProtKB/Swiss-Prot Q633D2 (SYY1_BACCZ)

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:	BCE33L4407

Organism

Bacillus cereus (strain ZK / E33L) [Complete proteome] [HAMAP]

Taxonomic identifier

288681 [NCBI]

Taxonomic lineage

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

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_0000234673
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	169	1	Tyrosine By similarity
	Binding site	173	1	Tyrosine By similarity
	Binding site	233	1	ATP By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q633D2-1 [UniParc]. Last modified October 25, 2004. Version 1. Checksum: 6D95DA9182AAC32A	FASTA	418	47,035
	10 20 30 40 50 60 MGILQDLEFR GLINQQTDAE GLEQLLEKES VKLYCGFDPT ADSLHIGHML PVLMLRRFQL 70 80 90 100 110 120 AGHQPIALVG GGTGMIGDPS GKKAERTLNT KDTVAYYTES IKNQLSNFLE FENVENPATM 130 140 150 160 170 180 ANNYDWLGNL DVISFLRDIG KNFGLNYMLA KDTVASRLET GISFTEFSYM ILQSYDFLNL 190 200 210 220 230 240 YQHHNCRLQI GGSDQWGNIT AGLELIRKSE EDAKAFGLTI PLVTKSDGTK FGKTEGGAIW 250 260 270 280 290 300 LDPEKTTPYE FYQFWINTDD RDVVKYLKYF TFLSHEEILE LEKQVAEAPE KRAAQKALGA 310 320 330 340 350 360 EMTKLVHGEE ALEQAIKISA ALFSGSVAEL TASEIEQGFK DVPSVERTAE DTVLIDLLVE 370 380 390 400 410 SKISPSKRQA REDVTNGAIY VNGERTQALD YVVTEKDRIE GKFTIIRRGK KKYFLIRY

References

[1]

"Pathogenomic sequence analysis of Bacillus cereus and Bacillus thuringiensis isolates closely related to Bacillus anthracis." Han C.S., Xie G., Challacombe J.F., Altherr M.R., Bhotika S.S., Bruce D., Campbell C.S., Campbell M.L., Chen J., Chertkov O., Cleland C., Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T., Goodwin L.A., Hill K.K., Hitchcock P. , Jackson P.J., Keim P., Kewalramani A.R., Longmire J., Lucas S., Malfatti S., McMurry K., Meincke L.J., Misra M., Moseman B.L., Mundt M., Munk A.C., Okinaka R.T., Parson-Quintana B., Reilly L.P., Richardson P., Robinson D.L., Rubin E., Saunders E., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Ticknor L.O., Wills P.L., Brettin T.S., Gilna P. J. Bacteriol. 188:3382-3390(2006) [PubMed: 16621833] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000001 Genomic DNA. Translation: AAU15863.1.
RefSeq	YP_085985.1.
3D structure databases
SMR	Q633D2. Positions 1-319.
ModBase	Search...
Protein-protein interaction databases
STRING	Q633D2.
Genome annotation databases
GeneID	3023925.
GenomeReviews	Gene locus BCE33L4407 in contig CP000001_GR.
KEGG	bcz:BCZK4407.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q633D2.
OMA	PGYVPNT.
Enzyme and pathway databases
BioCyc	BCER288681:BCE33L4407-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_BACCZ

Accession

Primary (citable) accession number: Q633D2

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 16, 2006
Last sequence update:	October 25, 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)