Cysteine--tRNA ligase - Escherichia coli (strain K12)

Contribute

Send feedback

Read comments (?) or add your own

P21888 (SYC_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 113. History...

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

Documents (4) |

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
Ordered Locus Names:	b0526, JW0515

Organism

Escherichia coli (strain K12)

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	461 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

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.
Subunit structure	Monomer.
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	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	cysteinyl-tRNA aminoacylation Inferred from direct assay. Source: EcoliWiki
Cellular component	cytosol Inferred from Biological aspect of Ancestor. Source: RefGenome
Molecular function	ATP binding Inferred from physical interaction Ref.8. Source: EcoliWiki RNA binding Inferred from physical interaction Ref.8. Source: EcoliWiki cysteine-tRNA ligase activity Inferred from direct assay. Source: EcoliWiki zinc ion binding Inferred from physical interaction. Source: EcoliWiki
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 461

461

Cysteine--tRNA ligase HAMAP MF_00041

PRO_0000159394

Regions

Motif

30 – 40

"HIGH" region HAMAP MF_00041

Motif

266 – 270

"KMSKS" region HAMAP MF_00041

Sites

Metal binding

Zinc

Metal binding

209

Zinc

Metal binding

234

Zinc

Metal binding

238

Zinc

Binding site

269

ATP By similarity

Experimental info

Sequence conflict

316

L → V in CAA39691. Ref.1

Secondary structure

461

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P21888 [UniParc].

Last modified May 1, 1992. Version 2.
Checksum: 2FA77FDBB7C5BA99
Show »

FASTA

461

52,202

        10         20         30         40         50         60 
MLKIFNTLTR QKEEFKPIHA GEVGMYVCGI TVYDLCHIGH GRTFVAFDVV ARYLRFLGYK 

        70         80         90        100        110        120 
LKYVRNITDI DDKIIKRANE NGESFVAMVD RMIAEMHKDF DALNILRPDM EPRATHHIAE 

       130        140        150        160        170        180 
IIELTEQLIA KGHAYVADNG DVMFDVPTDP TYGVLSRQDL DQLQAGARVD VVDDKRNPMD 

       190        200        210        220        230        240 
FVLWKMSKEG EPSWPSPWGA GRPGWHIECS AMNCKQLGNH FDIHGGGSDL MFPHHENEIA 

       250        260        270        280        290        300 
QSTCAHDGQY VNYWMHSGMV MVDREKMSKS LGNFFTVRDV LKYYDAETVR YFLMSGHYRS 

       310        320        330        340        350        360 
QLNYSEENLK QARAALERLY TALRGTDKTV APAGGEAFEA RFIEAMDDDF NTPEAYSVLF 

       370        380        390        400        410        420 
DMAREVNRLK AEDMAAANAM ASHLRKLSAV LGLLEQEPEA FLQSGAQADD SEVAEIEALI 

       430        440        450        460 
QQRLDARKAK DWAAADAARD RLNEMGIVLE DGPQGTTWRR K

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cysteinyl-tRNA synthetase: determination of the last E. coli aminoacyl-tRNA synthetase primary structure." Eriani G., Dirheimer G., Gangloff J. Nucleic Acids Res. 19:265-269(1991) [PubMed: 2014166] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-10. Strain: K12.
[2]	"Sequence determination and modeling of structural motifs for the smallest monomeric aminoacyl-tRNA synthetase." Hou Y.M., Shiba K., Mottes C., Schimmel P. Proc. Natl. Acad. Sci. U.S.A. 88:976-980(1991) [PubMed: 1992490] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Cysteinyl-tRNA synthetase is a direct descendant of the first aminoacyl-tRNA synthetase." Avalos J., Corrochano L.M., Brenner S. FEBS Lett. 286:176-180(1991) [PubMed: 1864365] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12.
[4]	"Sequence of minutes 4-25 of Escherichia coli." Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W. Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[5]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[6]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[7]	"Crystallization and preliminary diffraction analysis of Escherichia coli cysteinyl-tRNA synthetase." Newberry K.J., Kohn J., Hou Y.-M., Perona J.J. Acta Crystallogr. D 55:1046-1047(1999) [PubMed: 10216301] [Abstract] Cited for: CRYSTALLIZATION.
[8]	"Structural origins of amino acid selection without editing by cysteinyl-tRNA synthetase." Newberry K.J., Hou Y.-M., Perona J.J. EMBO J. 21:2778-2787(2002) [PubMed: 12032090] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X56234 Genomic DNA. Translation: CAA39691.1.
M59381 Genomic DNA. Translation: AAA23658.1.
X59293 Genomic DNA. Translation: CAA41983.1.
U82664 Genomic DNA. Translation: AAB40279.1.
U00096 Genomic DNA. Translation: AAC73628.1.
AP009048 Genomic DNA. Translation: BAE76303.1.

PIR

YYEC. A37868.

RefSeq

NP_415059.1. NC_000913.2.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1LI5	X-ray	2.30	A/B	1-461	[»]
1LI7	X-ray	2.60	A/B	1-461	[»]
1U0B	X-ray	2.30	B	1-461	[»]

ProteinModelPortal

P21888.

SMR

P21888. Positions 1-461.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-9386N.

IntAct

P21888. 3 interactions.

MINT

MINT-1240309.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBESCT00000001969; EBESCP00000001969; EBESCG00000001617.
EBESCT00000015968; EBESCP00000015259; EBESCG00000015028.

GeneID

946969.

GenomeReviews

Gene locus JW0515 in contig AP009048_GR.
Gene locus b0526 in contig U00096_GR.

KEGG

ecj:JW0515.
eco:b0526.

PATRIC

32116212. VBIEscCol129921_0547.

Organism-specific databases

EchoBASE

EB0193.

EcoGene

EG10196. cysS.

Phylogenomic databases

eggNOG

COG0215.

GeneTree

EBGT00050000010678.

HOGENOM

HBG327651.

OMA

DFDALNM.

PhylomeDB

P21888.

ProtClustDB

PRK00260.

Enzyme and pathway databases

BioCyc

EcoCyc:CYSS-MONOMER.
MetaCyc:CYSS-MONOMER.

Gene expression databases

Genevestigator

P21888.

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.

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_ECOLI

Accession

Primary (citable) accession number: P21888
Secondary accession number(s): Q2MBQ3

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1991
Last sequence update:	May 1, 1992
Last modified:	January 25, 2012
This is version 113 of the entry and version 2 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

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents