P57990 (SYC_MYCLE) 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
Synonyms:	cysS1
Ordered Locus Names:	ML0323

Organism

Mycobacterium leprae [Complete proteome] [HAMAP]

Taxonomic identifier

1769 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium

Protein attributes

Sequence length	473 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
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	cysteinyl-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 cysteine-tRNA ligase activity Inferred from electronic annotation. Source: EC metal 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 – 473	473	Cysteine--tRNA ligase HAMAP MF_00041		PRO_0000159437
Regions
	Motif	35 – 45	11	"HIGH" region HAMAP MF_00041
	Motif	267 – 271	5	"KMSKS" region HAMAP MF_00041
Sites
	Metal binding	33	1	Zinc By similarity
	Metal binding	211	1	Zinc By similarity
	Metal binding	236	1	Zinc By similarity
	Metal binding	240	1	Zinc By similarity
	Binding site	270	1	ATP By similarity

Sequences

	Sequence		Length	Mass (Da)
	P57990 [UniParc]. Last modified April 27, 2001. Version 1. Checksum: 9FD6CF859C69316D	FASTA	473	52,125
	10 20 30 40 50 60 MIDSGHLRLH DTVAGAVRDF VPLRAGHVSI YLCGATVQGQ PHIGHVRSGV AFDILRRWLM 70 80 90 100 110 120 ARGYDVAFIR NVTDIDDKIL NKAAAAGRPW WEWAATHERA FTAAYDALDV LPPSAEPRAT 130 140 150 160 170 180 GHITQMIELI ELLIETGHAY TGGSDVYFDV LSYPDYGQLS GHKMDYIHQG EGVTTGKRDQ 190 200 210 220 230 240 RDFTLWKGAK SGEPSWPTPW GRGRPGWHLE CSAMARAYLG SEFDIHCGGM DLVFPHHENE 250 260 270 280 290 300 IAQSRAVGDG FARYWLHNGW VTMGGEKMSK SLGNVLSIPA VLQRVRPAEL RYYLGSAHYR 310 320 330 340 350 360 SMLEFSEAAL QDAVKAYVGV ENFLTRVRTR VGAVGTGELT PRFAAALDDD LAVPIALAEV 370 380 390 400 410 420 HHARVEGNRA LDIGDHEGAL TNAGAIRAMM GILGCDPLDE RWESRDETSA ALAAVDVLVA 430 440 450 460 470 AELESRQMAR EQRNWVLADQ IRDRLKDAGI EVTDTVNGPQ WELLAGDKQV DAR

References

[1]

"Massive gene decay in the leprosy bacillus." Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R., Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E., Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K., Duthoy S. , Feltwell T., Fraser A., Hamlin N., Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S., Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R., Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R., Barrell B.G. Nature 409:1007-1011(2001) [PubMed: 11234002] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: TN.

+

Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AL583918 Genomic DNA. Translation: CAC29831.1.
PIR	C86949.
RefSeq	NP_301350.1. NC_002677.1.
3D structure databases
ProteinModelPortal	P57990.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBMYCT00000028284; EBMYCP00000027890; EBMYCG00000028279.
GeneID	908923.
GenomeReviews	Gene locus ML0323 in contig AL450380_GR.
KEGG	mle:ML0323.
NMPDR	fig|272631.1.peg.222.
PATRIC	18051144. VBIMycLep78757_0521.
Organism-specific databases
Leproma	ML0323.
CMR	Search...
Phylogenomic databases
GeneTree	EBGT00050000016491.
HOGENOM	HBG327651.
OMA	DFDALNM.
ProtClustDB	PRK00260.
Enzyme and pathway databases
BioCyc	MLEP272631:ML0323-MONOMER.
Family and domain databases
HAMAP	MF_00041. Cys_tRNA_synth. [Tree]
InterPro	IPR015803. Cys-tRNA-synt. 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]
Gene3D	G3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 2 hits.
KO	K01883.
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]
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_MYCLE

Accession

Primary (citable) accession number: P57990

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 27, 2001
Last sequence update:	April 27, 2001
Last modified:	January 25, 2012
This is version 73 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program