Q6HCM0 (SYY1_BACHK) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Tyrosine--tRNA ligase 1
EC=6.1.1.1

Alternative name(s):
Tyrosyl-tRNA synthetase 1
Short name=TyrRS 1

Gene names

Name:	tyrS1
Ordered Locus Names:	BT9727_4391

Organism

Bacillus thuringiensis subsp. konkukian (strain 97-27) [Complete proteome] [HAMAP]

Taxonomic identifier

281309 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	418 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. 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: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW RNA binding Inferred from electronic annotation. Source: UniProtKB-KW tyrosine-tRNA ligase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 418	418	Tyrosine--tRNA ligase 1 HAMAP MF_02006		PRO_0000234676
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)
	Q6HCM0 [UniParc]. Last modified July 19, 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]. Strain: 97-27.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE017355 Genomic DNA. Translation: AAT63895.1.
RefSeq	YP_038706.1. NC_005957.1.
3D structure databases
ProteinModelPortal	Q6HCM0.
SMR	Q6HCM0. Positions 1-319, 321-418.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBBACT00000072370; EBBACP00000070456; EBBACG00000072361.
GeneID	2856886.
GenomeReviews	Gene locus BT9727_4391 in contig AE017355_GR.
KEGG	btk:BT9727_4391.
PATRIC	18989913. VBIBacThu119411_4680.
Organism-specific databases
CMR	Search...
Phylogenomic databases
GeneTree	EBGT00050000000599.
HOGENOM	HBG288125.
OMA	TFYIGFD.
ProtClustDB	PRK05912.
Enzyme and pathway databases
BioCyc	BTHU281309:BT9727_4391-MONOMER.
Family and domain databases
HAMAP	MF_02006. Tyr_tRNA_synth_type1. [Tree]
InterPro	IPR001412. aa-tRNA-synth_I_CS. IPR002305. aa-tRNA-synth_Ic. IPR014729. Rossmann-like_a/b/a_fold. IPR002942. S4_RNA-bd. IPR002307. Tyr-tRNA-synth. IPR024088. Tyr-tRNA-synth_bac-type. IPR024107. Tyr-tRNA-synth_bac_1. [Graphical view]
Gene3D	G3DSA:3.10.290.10. G3DSA:3.10.290.10. 1 hit. G3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 1 hit.
KO	K01866.
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_BACHK

Accession

Primary (citable) accession number: Q6HCM0

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 16, 2006
Last sequence update:	July 19, 2004
Last modified:	January 25, 2012
This is version 52 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program