Q65I63 (SYN_BACLD) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Asparagine--tRNA ligase
EC=6.1.1.22

Alternative name(s):
Asparaginyl-tRNA synthetase
Short name=AsnRS

Gene names

Name:	asnS
Ordered Locus Names:	BLi02371, BL02745

Organism

Bacillus licheniformis (strain DSM 13 / ATCC 14580) [Complete proteome] [HAMAP]

Taxonomic identifier

279010 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	430 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 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: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW asparagine-tRNA ligase activity Inferred from electronic annotation. Source: EC 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 – 430	430	Asparagine--tRNA ligase HAMAP MF_00534		PRO_1000051378

Sequences

	Sequence		Length	Mass (Da)
	Q65I63 [UniParc]. Last modified October 25, 2004. Version 1. Checksum: 11248ED6895D3F17	FASTA	430	48,984
	10 20 30 40 50 60 MKTTINQVYK HVGEEVTIGA WIANKRSSGK IAFLQLRDGT GFIQGVVVKA EVDEETFQTA 70 80 90 100 110 120 KSVTQETSLY VKGVVKEDER SPLGYELAVT SLEVIHEATD YPITPKEHGT EFLMDHRHLW 130 140 150 160 170 180 LRSKRQHATM KIRNEIIRAT YEFFNKEGFV KVDPPILTGS APEGTTELFA TKYFDEDAYL 190 200 210 220 230 240 SQSGQLYMEA AAMALGKVFS FGPTFRAEKS KTKRHLIEFW MIEPEMAFVE FNENLEVQEN 250 260 270 280 290 300 YVSFIVQSVL ENCKIELNTL GRDTSKLELI KAPFPRITYD EAIQFLKEKG FDDIEWGDDF 310 320 330 340 350 360 GAPHETAIAE SYDKPVFITH YPTSLKPFYM QPAPDREDVV LCADLIAPEG YGEIIGGSER 370 380 390 400 410 420 IHDLELLEAR LKEHGLESDA YQWYAELRKY GSVPHSGFGL GLERTVAWIC GSPHVRETIP 430 FPRLLNRLYP

References

[1]

"The complete genome sequence of Bacillus licheniformis DSM13, an organism with great industrial potential." Veith B., Herzberg C., Steckel S., Feesche J., Maurer K.H., Ehrenreich P., Baeumer S., Henne A., Liesegang H., Merkl R., Ehrenreich A., Gottschalk G. J. Mol. Microbiol. Biotechnol. 7:204-211(2004) [PubMed: 15383718] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: DSM 13 / ATCC 14580.

[2]

"Complete genome sequence of the industrial bacterium Bacillus licheniformis and comparisons with closely related Bacillus species." Rey M.W., Ramaiya P., Nelson B.A., Brody-Karpin S.D., Zaretsky E.J., Tang M., Lopez de Leon A., Xiang H., Gusti V., Clausen I.G., Olsen P.B., Rasmussen M.D., Andersen J.T., Joergensen P.L., Larsen T.S., Sorokin A., Bolotin A., Lapidus A. , Galleron N., Ehrlich S.D., Berka R.M. Genome Biol. 5:R77.1-R77.12(2004) [PubMed: 15461803] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: DSM 13 / ATCC 14580.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000002 Genomic DNA. Translation: AAU23897.1. AE017333 Genomic DNA. Translation: AAU41251.1.
RefSeq	YP_079535.1. NC_006270.3. YP_091944.1. NC_006322.1.
3D structure databases
HSSP	HSSP built from PDB template 1X56 based on UniProtKB O57980.
ProteinModelPortal	Q65I63.
ModBase	Search...
Protein-protein interaction databases
STRING	Q65I63.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBBACT00000056319; EBBACP00000054850; EBBACG00000056310. EBBACT00000058555; EBBACP00000056988; EBBACG00000058546.
GeneID	3029438. 3100932.
GenomeReviews	Gene locus BLi02371 in contig AE017333_GR. Gene locus BL02745 in contig CP000002_GR.
KEGG	bld:BLi02371. bli:BL02745.
NMPDR	fig|279010.5.peg.254.
PATRIC	18950400. VBIBacLic203714_2402.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0017.
GeneTree	EBGT00050000000858.
HOGENOM	HBG745843.
OMA	AVDYPIT.
PhylomeDB	Q65I63.
ProtClustDB	PRK03932.
Enzyme and pathway databases
BioCyc	BLIC279010-1:BLI02371-MONOMER. BLIC279010:BL02745-MONOMER.
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. IPR004522. Asn-tRNA-synth_IIb. IPR002312. Asp/Asn-tRNA-synth_IIb. IPR012340. NA-bd_OB-fold. IPR016027. NA-bd_OB-fold-like. IPR004365. NA-bd_OB_tRNA-helicase. [Graphical view]
Gene3D	G3DSA:2.40.50.140. OB_NA_bd_sub. 1 hit.
KO	K01893.
PANTHER	PTHR22594. aa-tRNA-synt_II. 1 hit. PTHR22594:SF6. PTHR22594:SF6. 1 hit.
Pfam	PF00152. tRNA-synt_2. 1 hit. PF01336. tRNA_anti. 1 hit. [Graphical view]
PRINTS	PR01042. TRNASYNTHASP.
SUPFAM	SSF50249. Nucleic_acid_OB. 1 hit.
TIGRFAMs	TIGR00457. AsnS. 1 hit.
PROSITE	PS50862. AA_TRNA_LIGASE_II. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SYN_BACLD

Accession

Primary (citable) accession number: Q65I63
Secondary accession number(s): Q62TL2

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	October 25, 2004
Last modified:	January 25, 2012
This is version 63 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program