Q02WZ9 (SYC_LACLS) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Cysteine--tRNA ligase
EC=6.1.1.16

Alternative name(s):
Cysteinyl-tRNA synthetase
Short name=CysRS

Gene names

Name:	cysS
Ordered Locus Names:	LACR_2043

Organism

Lactococcus lactis subsp. cremoris (strain SK11) [Complete proteome] [HAMAP]

Taxonomic identifier

272622 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Lactobacillales › Streptococcaceae › Lactococcus › Lactococcus lactis › Lactococcus lactis subsp. cremoris

Protein attributes

Sequence length	448 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-Rule MF_00041
Cofactor	Binds 1 zinc ion per subunit By similarity.
Subunit structure	Monomer By similarity.
Subcellular location	Cytoplasm By similarity.
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
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: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 448	448	Cysteine--tRNA ligase HAMAP-Rule MF_00041		PRO_0000332841
Regions
	Motif	29 – 39	11	"HIGH" region HAMAP-Rule MF_00041
	Motif	267 – 271	5	"KMSKS" region HAMAP-Rule MF_00041
Sites
	Metal binding	27	1	Zinc By similarity
	Metal binding	210	1	Zinc By similarity
	Metal binding	235	1	Zinc By similarity
	Metal binding	239	1	Zinc By similarity
	Binding site	270	1	ATP By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q02WZ9 [UniParc]. Last modified November 14, 2006. Version 1. Checksum: 250AEEDFE69791FD	FASTA	448	50,935
	10 20 30 40 50 60 MKIYNTYSRQ LEDFQPIEPG KVKMYVCGPT VYNYIHVGNA RSVVAFDLVR KYLEFRGFEV 70 80 90 100 110 120 EYISNFTDVD DKIIKAAVSE NISTKELSER YIAAFYEDTD LLNVKRASQN PKATEFIEAM 130 140 150 160 170 180 IDFIQELLDK DYAYISEGDV YFRVAKSKNY AKLANKNLAD LLAGASGRTD EETNLKESPA 190 200 210 220 230 240 DFALWKSVKA DEVSWQAPWG AGRPGWHIEC SVMSTSLLGE TIDIHGGGAD LEFPHHTNEI 250 260 270 280 290 300 AQSEAKTGQK FVNYWMHNGF VNVDGEKMSK SLGNFTTVHE LLQVVDPQIL RFFLATTHYR 310 320 330 340 350 360 RPLNFTDDAL TEAENNIKKI ENAYRHLDDQ AESNLSALTT FRNDFVAAMD EDFNIANGMT 370 380 390 400 410 420 VFYDFVSWVN KGNGGAEVKA FFDQVLEILG IKFEIEQSLD SEIEAMIEAR QLAREVRDFA 430 440 KSDEIRDALK AQGIVLEDTK DGVRWHRE

References

[1]

"Comparative genomics of the lactic acid bacteria." Makarova K.S., Slesarev A., Wolf Y.I., Sorokin A., Mirkin B., Koonin E.V., Pavlov A., Pavlova N., Karamychev V., Polouchine N., Shakhova V., Grigoriev I., Lou Y., Rohksar D., Lucas S., Huang K., Goodstein D.M., Hawkins T. , Plengvidhya V., Welker D., Hughes J., Goh Y., Benson A., Baldwin K., Lee J.-H., Diaz-Muniz I., Dosti B., Smeianov V., Wechter W., Barabote R., Lorca G., Altermann E., Barrangou R., Ganesan B., Xie Y., Rawsthorne H., Tamir D., Parker C., Breidt F., Broadbent J.R., Hutkins R., O'Sullivan D., Steele J., Unlu G., Saier M.H. Jr., Klaenhammer T., Richardson P., Kozyavkin S., Weimer B.C., Mills D.A. Proc. Natl. Acad. Sci. U.S.A. 103:15611-15616(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: SK11.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000425 Genomic DNA. Translation: ABJ73523.1.
RefSeq	YP_811636.1. NC_008527.1.
3D structure databases
ProteinModelPortal	Q02WZ9.
ModBase	Search...
Protein-protein interaction databases
STRING	272622.LACR_2043.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ABJ73523; ABJ73523; LACR_2043.
GeneID	4432417.
KEGG	llc:LACR_2043.
PATRIC	22290959. VBILacLac38071_2222.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0215.
HOGENOM	HOG000245250.
KO	K01883.
OMA	DFDALNM.
ProtClustDB	PRK00260.
Enzyme and pathway databases
BioCyc	LLAC272622:GJUG-2043-MONOMER.
Family and domain databases
Gene3D	3.40.50.620. 1 hit.
HAMAP	MF_00041. Cys_tRNA_synth.
InterPro	IPR015803. Cys-tRNA-ligase. IPR015273. Cys-tRNA-synt_Ia_DALR. IPR024909. Cys-tRNA/MSH_ligase. IPR014729. Rossmann-like_a/b/a_fold. IPR009080. tRNAsynth_1a_anticodon-bd. [Graphical view]
PANTHER	PTHR10890. PTHR10890. 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]
SUPFAM	SSF47323. tRNAsyn_1a_bind. 1 hit.
TIGRFAMs	TIGR00435. cysS. 1 hit.
PROSITE	PS00178. AA_TRNA_LIGASE_I. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SYC_LACLS

Accession

Primary (citable) accession number: Q02WZ9

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 29, 2008
Last sequence update:	November 14, 2006
Last modified:	May 1, 2013
This is version 53 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program