Q0TTF4 (SYY_CLOP1) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Tyrosine--tRNA ligase
EC=6.1.1.1

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

Gene names

Name:	tyrS
Ordered Locus Names:	CPF_0633

Organism

Clostridium perfringens (strain ATCC 13124 / NCTC 8237 / Type A) [Complete proteome] [HAMAP]

Taxonomic identifier

195103 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Clostridia › Clostridiales › Clostridiaceae › Clostridium › Clostridium perfringens

Protein attributes

Sequence length	406 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-Rule MF_02006
Catalytic activity	ATP + L-tyrosine + tRNA(Tyr) = AMP + diphosphate + L-tyrosyl-tRNA(Tyr). HAMAP-Rule 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 – 406	406	Tyrosine--tRNA ligase HAMAP-Rule MF_02006		PRO_1000189282
Regions
	Domain	340 – 404	65	S4 RNA-binding
	Motif	40 – 49	10	"HIGH" region HAMAP-Rule MF_02006
	Motif	228 – 232	5	"KMSKS" region HAMAP-Rule MF_02006
Sites
	Binding site	35	1	Tyrosine By similarity
	Binding site	168	1	Tyrosine By similarity
	Binding site	172	1	Tyrosine By similarity
	Binding site	231	1	ATP By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q0TTF4 [UniParc]. Last modified September 5, 2006. Version 1. Checksum: B9FC929ADA3CB890	FASTA	406	45,897
	10 20 30 40 50 60 MANVLDTLME RGYIKQFTHE AETRELLEKE KVTFYIGFDP TADSLHVGHF IAMMFMAHMQ 70 80 90 100 110 120 KAGHRPIALI GGGTATIGDP SGKTDMRKMM TNETIAHNVA CIKKQMEKFI DFSDDKAILV 130 140 150 160 170 180 NNADWLLNQN YVEFLREVGV HFSVNRMLSA ECFKQRLERG LSFLEFNYML MQGYDFYVLN 190 200 210 220 230 240 KKYNCKMELG GDDQWSNMIA GVELVRKKSQ ESAYAMTCTL LTNSEGQKMG KTVNGALWLD 250 260 270 280 290 300 PEKTSPYEFY QYWRNVNDAD VEKCLKLLTF IPMDEVRRLS SLEGSQINEA KKVLAFEVTK 310 320 330 340 350 360 LVHGEEEATK AKQAAEALFG KGGDMSNVPT YEMGKDKLGS ELLDILVEAE IVPSKAEGKR 370 380 390 400 LVKQGGLSLN GEKVADFKKT LEEADFENGE VLIKRGKKNY NKIVLA

References

[1]

"Skewed genomic variability in strains of the toxigenic bacterial pathogen, Clostridium perfringens." Myers G.S.A., Rasko D.A., Cheung J.K., Ravel J., Seshadri R., DeBoy R.T., Ren Q., Varga J., Awad M.M., Brinkac L.M., Daugherty S.C., Haft D.H., Dodson R.J., Madupu R., Nelson W.C., Rosovitz M.J., Sullivan S.A., Khouri H. , Dimitrov G.I., Watkins K.L., Mulligan S., Benton J., Radune D., Fisher D.J., Atkins H.S., Hiscox T., Jost B.H., Billington S.J., Songer J.G., McClane B.A., Titball R.W., Rood J.I., Melville S.B., Paulsen I.T. Genome Res. 16:1031-1040(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 13124 / NCTC 8237 / Type A.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000246 Genomic DNA. Translation: ABG83841.1.
RefSeq	YP_695086.1. NC_008261.1.
3D structure databases
ProteinModelPortal	Q0TTF4.
ModBase	Search...
Protein-protein interaction databases
STRING	195103.CPF_0633.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ABG83841; ABG83841; CPF_0633.
GeneID	4202984.
KEGG	cpf:CPF_0633.
PATRIC	19483576. VBICloPer106549_0611.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0162.
HOGENOM	HOG000242790.
KO	K01866.
OMA	GKKKHVL.
ProtClustDB	PRK05912.
Enzyme and pathway databases
BioCyc	CPER195103:GHAW-733-MONOMER.
Family and domain databases
Gene3D	3.10.290.10. 1 hit. 3.40.50.620. 1 hit.
HAMAP	MF_02006. Tyr_tRNA_synth_type1.
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-ligase. IPR024088. Tyr-tRNA-ligase_bac-type. IPR024107. Tyr-tRNA-ligase_bac_1. [Graphical view]
PANTHER	PTHR11766. PTHR11766. 1 hit.
Pfam	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

SYY_CLOP1

Accession

Primary (citable) accession number: Q0TTF4

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 28, 2009
Last sequence update:	September 5, 2006
Last modified:	May 1, 2013
This is version 56 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program