Reviewed, UniProtKB/Swiss-Prot A5HZE1 (SYN_CLOBH)

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:	CBO0597, CLC_0651

Organism

Clostridium botulinum (strain Hall / ATCC 3502 / NCTC 13319 / Type A) [Complete proteome] [HAMAP]

Taxonomic identifier

441771 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Clostridia › Clostridiales › Clostridiaceae › Clostridium

Protein attributes

Sequence length	463 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.
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: 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 – 463	463	Asparaginyl-tRNA synthetase HAMAP MF_00534		PRO_1000051384

Sequences

	Sequence		Length	Mass (Da)
	A5HZE1-1 [UniParc]. Last modified June 26, 2007. Version 1. Checksum: F8AC032C1F94EF89	FASTA	463	53,323
	10 20 30 40 50 60 MDITLVKSLY RETEKHMDKE VKINGWVRTV RDSKNFAFVE VNDGSFFKNV QVILESSLEN 70 80 90 100 110 120 FKELCKMPIS TSVEVEGIVQ PTPNAKQPFE IKATRISIEG KSSTDYPLQK KRHTFEYLRT 130 140 150 160 170 180 IAHLRPRSNA FSAVFRVRSL AAYAVHKFFQ ERGFVYTNTP IITGSDCEGA GEMFQLTTMD 190 200 210 220 230 240 LNNIPKTEEG KIDFSKDFFG SPANLTVSGQ LSAETFALAF RNVYTFGPTF RAENSNTARH 250 260 270 280 290 300 ASEFWMIEPE MAFAELTDYL DNAEDMVKFV INYVMENAPE EMAFFNSFVD KGLFDRLDNV 310 320 330 340 350 360 VNSDFKRITY TEAVELLQKS GVKFDYEVEW GIDLQTEHER YLTEQIFKKP VFVTDYPKDI 370 380 390 400 410 420 KAFYMRLNDD GKTVAAADLL VPGVGEIIGG SQREERLDVL EKRMEELNLN KEDYWWYLEL 430 440 450 460 RKYGETKHSG YGLGFERILM YITGMTNIRD VIPFPRTPGS AEF

References

[1]

"Genome sequence of a proteolytic (Group I) Clostridium botulinum strain Hall A and comparative analysis of the clostridial genomes." Sebaihia M., Peck M.W., Minton N.P., Thomson N.R., Holden M.T.G., Mitchell W.J., Carter A.T., Bentley S.D., Mason D.R., Crossman L., Paul C.J., Ivens A., Wells-Bennik M.H.J., Davis I.J., Cerdeno-Tarraga A.M., Churcher C., Quail M.A., Chillingworth T. , Feltwell T., Fraser A., Goodhead I., Hance Z., Jagels K., Larke N., Maddison M., Moule S., Mungall K., Norbertczak H., Rabbinowitsch E., Sanders M., Simmonds M., White B., Whithead S., Parkhill J. Genome Res. 17:1082-1092(2007) [PubMed: 17519437] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

[2]

"Analysis of the neurotoxin complex genes in Clostridium botulinum A1-A4 and B1 strains: BoNT/A3, /Ba4 and /B1 clusters are located within plasmids." Smith T.J., Hill K.K., Foley B.T., Detter J.C., Munk A.C., Bruce D.C., Doggett N.A., Smith L.A., Marks J.D., Xie G., Brettin T.S. PLoS ONE 2:E1271-E1271(2007) [PubMed: 18060065] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000727 Genomic DNA. Translation: ABS36590.1. AM412317 Genomic DNA. Translation: CAL82150.1.
RefSeq	YP_001253139.1. YP_001386531.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	A5HZE1.
Genome annotation databases
GeneID	5184852. 5399371.
GenomeReviews	Gene locus CBO0597 in contig AM412317_GR. Gene locus CLC_0651 in contig CP000727_GR.
KEGG	cbh:CLC_0651. cbo:CBO0597.
Organism-specific databases
CMR	Search...
Phylogenomic databases
OMA	LQKKRHS.
Family and domain databases
HAMAP	MF_00534. [Tree]
InterPro	IPR004364. aa-tRNA-synt_II. IPR018150. aa-tRNA-synt_II-like. IPR006195. aa-tRNA-synth_II_cons-reg. IPR004522. Asn-tRNA-synth_IIb. IPR002312. Asp-tRNA-synth_IIb. IPR012340. NA-bd_OB-fold. IPR004365. NA_bd_OB_tRNA-helicase. [Graphical view]
Gene3D	G3DSA:2.40.50.140. OB_NA_bd_sub. 1 hit.
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_CLOBH

Accession

Primary (citable) accession number: A5HZE1
Secondary accession number(s): A7G197

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	June 26, 2007
Last modified:	November 3, 2009
This is version 20 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)