Q634E3 (SYD_BACCZ) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Aspartate--tRNA ligase
EC=6.1.1.12

Alternative name(s):
Aspartyl-tRNA synthetase
Short name=AspRS

Gene names

Name:	aspS
Ordered Locus Names:	BCE33L4145

Organism

Bacillus cereus (strain ZK / E33L) [Complete proteome] [HAMAP]

Taxonomic identifier

288681 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group

Protein attributes

Sequence length	591 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Catalytic activity	ATP + L-aspartate + tRNA(Asp) = AMP + diphosphate + L-aspartyl-tRNA(Asp). HAMAP MF_00044_B
Subunit structure	Homodimer By similarity. HAMAP MF_00044_B
Subcellular location	Cytoplasm HAMAP MF_00044_B.
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	tRNA aminoacylation for protein translation 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 aspartate-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 – 591	591	Aspartate--tRNA ligase HAMAP MF_00044_B		PRO_0000110823

Sequences

	Sequence		Length	Mass (Da)
	Q634E3 [UniParc]. Last modified October 25, 2004. Version 1. Checksum: FDA649913AB07C70	FASTA	591	66,321
	10 20 30 40 50 60 MAERTHACGK VTVEAVGQTV QLKGWVQKRR DLGGLIFIDL RDRTGIVQVV FNPETSKEAL 70 80 90 100 110 120 EVAETIRSEY VLHVEGTVVE RGEGAINDNM ATGRIEVQAT KVNVLNAAKT TPIIIADDTD 130 140 150 160 170 180 ASEDVRLKYR YLDLRRPVMF NTFKMRHDVT KTIRNFLDTE EFLEVETPIL TKSTPEGARD 190 200 210 220 230 240 YLVPSRVHDG EFYALPQSPQ LFKQLLMVGG FERYYQVARC FRDEDLRADR QPEFTQIDIE 250 260 270 280 290 300 ASFLTQDEIL DMMERMMTKV MKDAKGVEVS APFPRMKYAD AMARYGSDKP DTRFEMELTD 310 320 330 340 350 360 LSEFAAGCGF KVFTSAVESG GQVKAINAKG AASKYSRKDI DALTEFVKVY GAKGLAWLKV 370 380 390 400 410 420 EEDGLKGPIA KFFGEEDANV LMNTLEATAG DLLLFVADKK SVVADSLGAL RLRLGKELEL 430 440 450 460 470 480 IDESKFNFLW VTDWPLLEYD EDADRYFAAH HPFTMPFRED VELLETAPEK ARAQAYDLVL 490 500 510 520 530 540 NGYELGGGSL RIYERDVQEK MFKALGFSQE DAQEQFGFLL EAFEYGTPPH GGIALGLDRL 550 560 570 580 590 VMLLAGRTNL RDTIAFPKTA SASCLLTEAP SPVAEAQLEE LNLKLSLKEE K

References

[1]

"Pathogenomic sequence analysis of Bacillus cereus and Bacillus thuringiensis isolates closely related to Bacillus anthracis." Han C.S., Xie G., Challacombe J.F., Altherr M.R., Bhotika S.S., Bruce D., Campbell C.S., Campbell M.L., Chen J., Chertkov O., Cleland C., Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T., Goodwin L.A., Hill K.K., Hitchcock P. , Jackson P.J., Keim P., Kewalramani A.R., Longmire J., Lucas S., Malfatti S., McMurry K., Meincke L.J., Misra M., Moseman B.L., Mundt M., Munk A.C., Okinaka R.T., Parson-Quintana B., Reilly L.P., Richardson P., Robinson D.L., Rubin E., Saunders E., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Ticknor L.O., Wills P.L., Brettin T.S., Gilna P. J. Bacteriol. 188:3382-3390(2006) [PubMed: 16621833] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ZK / E33L.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000001 Genomic DNA. Translation: AAU16125.1.
RefSeq	YP_085724.1. NC_006274.1.
3D structure databases
ProteinModelPortal	Q634E3.
SMR	Q634E3. Positions 4-585.
ModBase	Search...
Protein-protein interaction databases
STRING	Q634E3.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBBACT00000043208; EBBACP00000042109; EBBACG00000043199.
GeneID	3025907.
GenomeReviews	Gene locus BCE33L4145 in contig CP000001_GR.
KEGG	bcz:BCZK4145.
PATRIC	18892115. VBIBacCer95304_4394.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0173.
GeneTree	EBGT00050000000858.
HOGENOM	HBG396032.
OMA	AFPKTQQ.
PhylomeDB	Q634E3.
ProtClustDB	PRK00476.
Enzyme and pathway databases
BioCyc	BCER288681:BCE33L4145-MONOMER.
Family and domain databases
HAMAP	MF_00044_B. Asp_tRNA_synth_B. [Tree]
InterPro	IPR004364. aa-tRNA-synt_II. IPR018150. aa-tRNA-synt_II-like. IPR006195. aa-tRNA-synth_II. IPR004524. Asp-tRNA-synth_IIb_bac/mt. IPR002312. Asp/Asn-tRNA-synth_IIb. IPR004115. GAD_dom. IPR012340. NA-bd_OB-fold. IPR016027. NA-bd_OB-fold-like. IPR004365. NA-bd_OB_tRNA-helicase. [Graphical view]
Gene3D	G3DSA:3.30.1360.30. GAD_dom. 1 hit. G3DSA:2.40.50.140. OB_NA_bd_sub. 1 hit.
KO	K01876.
PANTHER	PTHR22594. aa-tRNA-synt_II. 1 hit. PTHR22594:SF5. AspS_bac. 1 hit.
Pfam	PF02938. GAD. 1 hit. PF00152. tRNA-synt_2. 1 hit. PF01336. tRNA_anti. 1 hit. [Graphical view]
PRINTS	PR01042. TRNASYNTHASP.
SUPFAM	SSF50249. Nucleic_acid_OB. 1 hit. SSF55261. SSF55261. 1 hit.
TIGRFAMs	TIGR00459. AspS_bact. 1 hit.
PROSITE	PS50862. AA_TRNA_LIGASE_II. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SYD_BACCZ

Accession

Primary (citable) accession number: Q634E3

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 29, 2005
Last sequence update:	October 25, 2004
Last modified:	January 25, 2012
This is version 59 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program