Reviewed, UniProtKB/Swiss-Prot Q97KY6 (SYY2_CLOAB)

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:	CA_C0780

Organism

Clostridium acetobutylicum [Complete proteome] [HAMAP]

Taxonomic identifier

1488 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Clostridia › Clostridiales › Clostridiaceae › Clostridium

Protein attributes

Sequence length	400 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_02007
Subunit structure	Homodimer By similarity.
Subcellular location	Cytoplasm By similarity.
Sequence similarities	Belongs to the class-I aminoacyl-tRNA synthetase family. TyrS type 2 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 – 400	400	Tyrosyl-tRNA synthetase 2 HAMAP MF_02007		PRO_0000236710
Regions
	Domain	339 – 399	61	S4 RNA-binding
	Motif	46 – 55	10	"HIGH" region HAMAP MF_02007
	Motif	230 – 234	5	"KMSKS" region HAMAP MF_02007
Sites
	Binding site	233	1	ATP By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q97KY6-1 [UniParc]. Last modified October 1, 2001. Version 1. Checksum: 421D142476818B55	FASTA	400	45,990
	10 20 30 40 50 60 MKNIDEQIKI IKKGAEEIID AKELKEKLIK AEKENTQLVV KLGLDPSAPD IHLGHAVVLR 70 80 90 100 110 120 KLKQLQDLGH KIVIIIGDFT GMIGDPTGKS KTRKQLSSQQ VMKNAETYEK QIFKILDRNK 130 140 150 160 170 180 TDLRFNSQWL EKLNFKEVIE LASKYTVARM LEREDFKKRF KNQQSIGIHE FFYPLMQAYD 190 200 210 220 230 240 SMAIKADIEF GGTDQRFNLL MGRTLQAEYG EEKQIAIFMP LLEGIDGKEK MSKSLGNYIG 250 260 270 280 290 300 IEESAKDMYV KVMQIPDSLI IKYFELCTDM HPDAIDIIRK QLNEDKVNPR DIKMKLAKEI 310 320 330 340 350 360 VCLYHNEAEA LNAEIYFKNL FQDKEIPEDI PIFKVRSENN LIEAIVKINS NTSKSEARRL 370 380 390 400 IAQGGVKLNG RKVIDFNDII LKSNDVIQIG KKKIVKLLVE

References

[1]

"Genome sequence and comparative analysis of the solvent-producing bacterium Clostridium acetobutylicum." Noelling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., Gibson R., Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., Tatusov R.L., Sabathe F., Doucette-Stamm L.A., Soucaille P., Daly M.J., Bennett G.N., Koonin E.V., Smith D.R. J. Bacteriol. 183:4823-4838(2001) [PubMed: 11466286] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE001437 Genomic DNA. Translation: AAK78756.1.
PIR	A96996.
RefSeq	NP_347416.1.
3D structure databases
HSSP	HSSP built from PDB template 1H3F based on UniProtKB P83453.
ModBase	Search...
Genome annotation databases
GeneID	1116963.
GenomeReviews	Gene locus CA_C0780 in contig AE001437_GR.
KEGG	cac:CAC0780.
NMPDR	fig|272562.1.peg.945.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q97KY6.
OMA	YVVQVGK.
Enzyme and pathway databases
BioCyc	CACE272562:CAC0780-MON.
BRENDA	6.1.1.1. 2866.
Family and domain databases
HAMAP	MF_02007. [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_CLOAB

Accession

Primary (citable) accession number: Q97KY6

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2006
Last sequence update:	October 1, 2001
Last modified:	November 3, 2009
This is version 41 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)