Reviewed, UniProtKB/Swiss-Prot Q0SQ51 (SYN_CLOPS)

Names and origin

Protein names

Recommended name:
    Asparaginyl-tRNA synthetase
    EC=6.1.1.22
Alternative name(s):
    Asparagine--tRNA ligase
      Short name=AsnRS

Gene names

Name:	asnS
Ordered Locus Names:	CPR_2509

Organism

Clostridium perfringens (strain SM101 / Type A) [Complete proteome] [HAMAP]

Taxonomic identifier

289380 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Clostridia › Clostridiales › Clostridiaceae › Clostridium

Protein attributes

Sequence length	465 AA.
Sequence status	Complete.
Protein existence	Inferred from homology.

General annotation (Comments)

Catalytic activity	ATP + L-asparagine + tRNA(Asn) = AMP + diphosphate + L-asparaginyl-tRNA(Asn). HAMAP MF_00534
Subunit structure	Homodimer By similarity. HAMAP MF_00534
Subcellular location	Cytoplasm By similarity HAMAP MF_00534.
Sequence similarities	Belongs to the class-II aminoacyl-tRNA synthetase family.

Ontologies

Keywords
Biological process	Protein biosynthesis
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding
Molecular function	Aminoacyl-tRNA synthetase Ligase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	asparaginyl-tRNA aminoacylation Inferred from electronic annotation. Source: HAMAP aspartyl-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: HAMAP asparagine-tRNA ligase activity Inferred from electronic annotation. Source: HAMAP aspartate-tRNA ligase activity Inferred from electronic annotation. Source: InterPro nucleic acid binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 465	465	Asparaginyl-tRNA synthetase HAMAP MF_00534		PRO_1000128207

Sequences

	Sequence		Length	Mass (Da)
	Q0SQ51-1 [UniParc]. Last modified September 5, 2006. Version 1. Checksum: CE7C7AF9110FDEBC	FASTA	465	53,184
	10 20 30 40 50 60 MKDVVLVKSL YRNTSEYSDK KVKISGWIRT LRASNAFGFI EVNDGSFFKN VQVVFDSAKI 70 80 90 100 110 120 SNYKEISKLP ISSSISVIGT LVETPDSKQP FEIQAEEIIV EGMSDSDYPL QKKRHTFEYL 130 140 150 160 170 180 RTIAHLRPRS NAFSATFRVR SVAAYAIHKF FQDQGFVYTH TPILTGSDCE GAGEMFRVTT 190 200 210 220 230 240 LDMMAPPISE EGGIDFSQDF FGKETNLTVS GQLNAECFAL AFRNIYTFGP TFRAENSNTV 250 260 270 280 290 300 KHAAEFWMIE PEMAFADLID DMEVAENMLK YVIKYVMDEC PEEIAFFNQF VDKGLLERLN 310 320 330 340 350 360 HVVNSEFGKV TYTEAVKLLQ ESGKEFEYPV EWGIDLQTEH ERYLTEQIFK KPVFVTDYPK 370 380 390 400 410 420 DIKAFYMRLN EDGKTVAAMD CLVPGIGEII GGSQREERLD VLKARMAELN LNEEDYWWYL 430 440 450 460 ELRKYGETVH SGFGLGFERL IMYITGMANI RDVIPFPRTT GTAEF

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: 16825665] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000312 Genomic DNA. Translation: ABG85590.1.
RefSeq	YP_699756.1.
3D structure databases
SMR	Q0SQ51. Positions 15-463.
ModBase	Search...
Protein-protein interaction databases
STRING	Q0SQ51.
Genome annotation databases
GeneID	4203991.
GenomeReviews	Gene locus CPR_2509 in contig CP000312_GR.
KEGG	cpr:CPR_2509.
TIGR	CPR_2509.
Phylogenomic databases
eggNOG	COG0017.
HOGENOM	HBG745843.
OMA	LQKKRHS.
Family and domain databases
HAMAP	MF_00534. Asn_tRNA_synth. [Tree]
InterPro	IPR004364. aa-tRNA-synt_II. IPR018150. aa-tRNA-synt_II-like. IPR006195. aa-tRNA-synth_II_cons-dom. IPR004522. Asn-tRNA-synth_IIb. IPR002312. Asp-tRNA-synth_IIb. IPR016027. NA-bd_OB-fold-like. IPR004365. NA_bd_OB_tRNA-helicase. [Graphical view]
PANTHER	PTHR22594. aa-tRNA-synt_II. 1 hit.
Pfam	PF00152. tRNA-synt_2. 1 hit. PF01336. tRNA_anti. 1 hit. [Graphical view]
PRINTS	PR01042. TRNASYNTHASP.
TIGRFAMs	TIGR00457. asnS. 1 hit.
PROSITE	PS50862. AA_TRNA_LIGASE_II. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SYN_CLOPS

Accession

Primary (citable) accession number: Q0SQ51

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 14, 2009
Last sequence update:	September 5, 2006
Last modified:	February 9, 2010
This is version 33 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)