Cysteine--tRNA ligase - Mycobacterium tuberculosis

Contribute

Send feedback

Read comments (?) or add your own

P0A634 (SYC_MYCTU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 48. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

text xml rdf/xml gff fasta

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

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:	Rv3580c, MT3686
ORF Names:	MTCY06G11.27c

Organism

Mycobacterium tuberculosis

Taxonomic identifier

1773 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	469 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 Reference proteome
Gene Ontology (GO)
Biological process	cysteinyl-tRNA aminoacylation Inferred from electronic annotation. Source: InterPro growth Inferred from mutant phenotype. Source: MTBBASE
Cellular component	cytosol Inferred from direct assay. Source: MTBBASE
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 – 469

469

Cysteine--tRNA ligase HAMAP MF_00041

PRO_0000159441

Regions

Motif

35 – 45

"HIGH" region HAMAP MF_00041

Motif

267 – 271

"KMSKS" region HAMAP MF_00041

Sites

Metal binding

Zinc By similarity

Metal binding

211

Zinc By similarity

Metal binding

236

Zinc By similarity

Metal binding

240

Zinc By similarity

Binding site

270

ATP By similarity

Experimental info

Sequence conflict

457

D → E in AAK48044. Ref.2

Sequences

Sequence

Length

Mass (Da)

Tools

P0A634 [UniParc].

Last modified March 15, 2005. Version 1.
Checksum: 515F9D19482ADC0E
Show »

FASTA

469

51,855

        10         20         30         40         50         60 
MTDRARLRLH DTAAGVVRDF VPLRPGHVSI YLCGATVQGL PHIGHVRSGV AFDILRRWLL 

        70         80         90        100        110        120 
ARGYDVAFIR NVTDIEDKIL AKAAAAGRPW WEWAATHERA FTAAYDALDV LPPSAEPRAT 

       130        140        150        160        170        180 
GHITQMIEMI ERLIQAGHAY TGGGDVYFDV LSYPEYGQLS GHKIDDVHQG EGVAAGKRDQ 

       190        200        210        220        230        240 
RDFTLWKGEK PGEPSWPTPW GRGRPGWHLE CSAMARSYLG PEFDIHCGGM DLVFPHHENE 

       250        260        270        280        290        300 
IAQSRAAGDG FARYWLHNGW VTMGGEKMSK SLGNVLSMPA MLQRVRPAEL RYYLGSAHYR 

       310        320        330        340        350        360 
SMLEFSETAM QDAVKAYVGL EDFLHRVRTR VGAVCPGDPT PRFAEALDDD LSVPIALAEI 

       370        380        390        400        410        420 
HHVRAEGNRA LDAGDHDGAL RSASAIRAMM GILGCDPLDQ RWESRDETSA ALAAVDVLVQ 

       430        440        450        460 
AELQNREKAR EQRNWALADE IRGRLKRAGI EVTDTADGPQ WSLLGGDTK

« Hide

References

[1]	"Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence." Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K. Barrell B.G. Nature 393:537-544(1998) [PubMed: 9634230] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 25618 / H37Rv.
[2]	"Whole-genome comparison of Mycobacterium tuberculosis clinical and laboratory strains." Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O., Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K., Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L., Delcher A., Utterback T.R. Fraser C.M. J. Bacteriol. 184:5479-5490(2002) [PubMed: 12218036] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CDC 1551 / Oshkosh.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BX842583 Genomic DNA. Translation: CAE55617.1. AE000516 Genomic DNA. Translation: AAK48044.1.
PIR	B70607.
RefSeq	NP_338230.1. NC_002755.2. YP_177992.1. NC_000962.2.
3D structure databases
ProteinModelPortal	P0A634.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBMYCT00000000681; EBMYCP00000000681; EBMYCG00000000681. EBMYCT00000070720; EBMYCP00000068779; EBMYCG00000070715.
GeneID	888628. 922812.
GenomeReviews	Gene locus MT3686 in contig AE000516_GR. Gene locus Rv3580c in contig AL123456_GR.
KEGG	mtc:MT3686. mtu:Rv3580c.
PATRIC	18129861. VBIMycTub22151_4025.
TIGR	MT3686.
Organism-specific databases
TubercuList	Rv3580c.
Phylogenomic databases
GeneTree	EBGT00050000016491.
HOGENOM	HBG327651.
OMA	VDLHPRV.
PhylomeDB	P0A634.
ProtClustDB	PRK00260.
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_MYCTU

Accession

Primary (citable) accession number: P0A634
Secondary accession number(s): P96862

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 15, 2005
Last sequence update:	March 15, 2005
Last modified:	January 25, 2012
This is version 48 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Family and domain databases

Entry information

Relevant documents