Reviewed, UniProtKB/Swiss-Prot A0R8G1 (SYC_BACAH)

Names and origin

Protein names

Recommended name:
    Cysteinyl-tRNA synthetase
    EC=6.1.1.16
Alternative name(s):
    Cysteine--tRNA ligase
      Short name=CysRS

Gene names

Name:	cysS
Ordered Locus Names:	BALH_0089

Organism

Bacillus thuringiensis (strain Al Hakam) [Complete proteome] [HAMAP]

Taxonomic identifier

412694 [NCBI]

Taxonomic lineage

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

Protein attributes

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

General annotation (Comments)

Catalytic activity	ATP + L-cysteine + tRNA(Cys) = AMP + diphosphate + L-cysteinyl-tRNA(Cys). HAMAP MF_00041
Cofactor	Binds 1 zinc ion per subunit By similarity. HAMAP MF_00041
Subunit structure	Monomer By similarity. HAMAP MF_00041
Subcellular location	Cytoplasm HAMAP MF_00041.
Sequence similarities	Belongs to the class-I aminoacyl-tRNA synthetase family.

Ontologies

Keywords
Biological process	Protein biosynthesis
Cellular component	Cytoplasm
Ligand	ATP-binding Metal-binding Nucleotide-binding Zinc
Molecular function	Aminoacyl-tRNA synthetase Ligase
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	cysteinyl-tRNA aminoacylation Inferred from electronic annotation. Source: HAMAP
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: HAMAP cysteine-tRNA ligase activity Inferred from electronic annotation. Source: HAMAP zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 465	465	Cysteinyl-tRNA synthetase HAMAP MF_00041		PRO_0000332790
Regions
	Motif	31 – 41	11	"HIGH" region HAMAP MF_00041
	Motif	266 – 270	5	"KMSKS" region HAMAP MF_00041
Sites
	Metal binding	29	1	Zinc By similarity
	Metal binding	209	1	Zinc By similarity
	Metal binding	234	1	Zinc By similarity
	Metal binding	238	1	Zinc By similarity
	Binding site	269	1	ATP By similarity
Amino acid modifications
	Modified residue	270	1	Phosphoserine By similarity

Sequences

	Sequence		Length	Mass (Da)
	A0R8G1-1 [UniParc]. Last modified January 9, 2007. Version 1. Checksum: 905176C7C9DEB8CD	FASTA	465	53,958
	10 20 30 40 50 60 MTIHIYNTLT RQKEEFIPLE ENKVKMYVCG PTVYNYIHIG NARPPMVFDT VRRYLEYKGY 70 80 90 100 110 120 DVQYVSNFTD VDDKLIKAAN ELGEDVPTIA DRFVEAYFED VTALGCKHAT VHPRVTENMD 130 140 150 160 170 180 IIIEFIHELV NKGYAYESEG DVYFRTKEFE GYGKLSHQPI ADLRHGARIE VGEKKQDPLD 190 200 210 220 230 240 FALWKAAKEG EIFWESPWGQ GRPGWHIECS AMARKYLGDT IDIHAGGQDL AFPHHENEIA 250 260 270 280 290 300 QSEALTGKTF ARYWMHNGYI NINNEKMSKS LGNFILVHDI IKQYDPQLIR FFMLSVHYRH 310 320 330 340 350 360 PINFSEELLQ STNNGLERIK TAYGNLKHRM ESSTDLTDHN EKWLADLEKF QTAFEEAMND 370 380 390 400 410 420 DFNTANAITE LYNVANHANQ YLLEEHTSTV VIEAYVKQLE TLFDILGLEL AQEELLDEEI 430 440 450 460 EALIQKRIEA RKNRDFALSD QIRDDLKDRN IILEDTAQGT RWKRG

References

[1]

"The complete genome sequence of Bacillus thuringiensis Al Hakam." Challacombe J.F., Altherr M.R., Xie G., Bhotika S.S., Brown N., 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., Green L.D., Han C.S. , Hill K.K., Hitchcock P., Jackson P.J., Keim P., Kewalramani A.R., Longmire J., Lucas S., Malfatti S., Martinez D., 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., Saunders E., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Ticknor L.O., Wills P.L., Gilna P., Brettin T.S. J. Bacteriol. 189:3680-3681(2007) [PubMed: 17337577] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000485 Genomic DNA. Translation: ABK83504.1.
RefSeq	YP_893011.1.
3D structure databases
SMR	A0R8G1. Positions 3-406.
ModBase	Search...
Protein-protein interaction databases
STRING	A0R8G1.
Genome annotation databases
GeneID	4542658.
GenomeReviews	Gene locus BALH_0089 in contig CP000485_GR.
KEGG	btl:BALH_0089.
NMPDR	fig|412694.5.peg.145.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0215.
HOGENOM	HBG327651.
OMA	VLWKAAK.
Family and domain databases
HAMAP	MF_00041_B. Cys_tRNA_synth_B. [Tree]
InterPro	IPR015804. Cys-tRNA-synt_Ia_C. IPR015273. Cys-tRNA-synt_Ia_DALR. IPR015803. Cys-tRNA-synt_Ia_N. IPR002308. Cys-tRNA-synth_1a. IPR014729. Rossmann-like_a/b/a_fold. IPR009080. tRNAsynth_1a_anticodon-bd. [Graphical view]
Gene3D	G3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 1 hit.
PANTHER	PTHR10890. Cys_tRNA-synt_1a. 1 hit.
Pfam	PF09190. DALR_2. 1 hit. PF01406. tRNA-synt_1e. 1 hit. [Graphical view]
PRINTS	PR00983. TRNASYNTHCYS.
SMART	SM00840. DALR_2. 1 hit. [Graphical view]
TIGRFAMs	TIGR00435. cysS. 1 hit.
PROSITE	PS00178. AA_TRNA_LIGASE_I. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SYC_BACAH

Accession

Primary (citable) accession number: A0R8G1

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 29, 2008
Last sequence update:	January 9, 2007
Last modified:	February 9, 2010
This is version 27 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)