Q97LC5 (SYY1_CLOAB) 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:	CA_C0637

Organism

Clostridium acetobutylicum

Taxonomic identifier

1488 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Clostridia › Clostridiales › Clostridiaceae › Clostridium

Protein attributes

Sequence length	407 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 Reference 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 – 407	407	Tyrosine--tRNA ligase 1 HAMAP MF_02006		PRO_0000234697
Regions
	Domain	340 – 406	67	S4 RNA-binding
	Motif	40 – 49	10	"HIGH" region HAMAP MF_02006
	Motif	228 – 232	5	"KMSKS" region HAMAP 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)
	Q97LC5 [UniParc]. Last modified October 1, 2001. Version 1. Checksum: 5F8DF6AA81772D5C	FASTA	407	46,435
	10 20 30 40 50 60 MSNVLDELIE RGYAKQFTHE EETRKLLSEE KVTFYIGFDP TGDSLHVGHF IALMLMARMQ 70 80 90 100 110 120 KAGHRPIVLI GGGTAMVGDP TGKTDMRKML TREEINHNVE CLKKQMSRFI DFSDDKAIIV 130 140 150 160 170 180 NNAEWLMGQN YIEFLREVGV HFSVNKMLTA ECFKQRMEKG LSFLEFNYML MQGFDFYKLN 190 200 210 220 230 240 EKYDCKMELG GDDQWSNMIA GVELIRRKSN KKAYAMTSAL LTNSEGKKMG KTEKGALWLD 250 260 270 280 290 300 AEKTSPYDFF QYWRNVNDAD VEKCLSMLTF LPMDEVRRLA SLKDQEINKA KEVLAYEVTK 310 320 330 340 350 360 LVHGEEEAKK ALNSSKALFG GGTNMDNVPT VSIPEDMLSS SILDVLVHTK IIPSKGEGRR 370 380 390 400 LVQQGGITLN DTKVEDFNYE ITKEDFNDDG FALVRRGKKK YYKIVIG

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.

+

Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE001437 Genomic DNA. Translation: AAK78614.1.
PIR	C96978.
RefSeq	NP_347274.1. NC_003030.1.
3D structure databases
ProteinModelPortal	Q97LC5.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1116820.
GenomeReviews	Gene locus CA_C0637 in contig AE001437_GR.
KEGG	cac:CA_C0637.
NMPDR	fig|272562.1.peg.803.
PATRIC	32035637. VBICloAce74127_0840.
Phylogenomic databases
HOGENOM	HBG288125.
OMA	TFYIGFD.
PhylomeDB	Q97LC5.
ProtClustDB	PRK05912.
Enzyme and pathway databases
BioCyc	CACE272562:CAC0637-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_CLOAB

Accession

Primary (citable) accession number: Q97LC5

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 16, 2006
Last sequence update:	October 1, 2001
Last modified:	January 25, 2012
This is version 60 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program