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O07045 (SYC_AZOBR) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 70. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Cysteine--tRNA ligase
EC=6.1.1.16
Alternative name(s):
Cysteinyl-tRNA synthetase
Short name=CysRS
Gene names
Name:cysS
OrganismAzospirillum brasilense
Taxonomic identifier192 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Alphaproteobacteria › Rhodospirillales › Rhodospirillaceae › Azospirillum

Protein attributes

Sequence length448 AA.
Sequence statusComplete.
Protein existenceInferred 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 processProtein biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Metal-binding
Nucleotide-binding
Zinc
   Molecular functionAminoacyl-tRNA synthetase
Ligase
Gene Ontology (GO)
   Biological processcysteinyl-tRNA aminoacylation

Inferred from electronic annotation. Source: InterPro

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP 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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 448448Cysteine--tRNA ligase HAMAP MF_00041
PRO_0000159341

Regions

Motif31 – 4111"HIGH" region HAMAP MF_00041
Motif265 – 2695"KMSKS" region HAMAP MF_00041

Sites

Metal binding291Zinc By similarity
Metal binding2061Zinc By similarity
Metal binding2351Zinc By similarity
Binding site2681ATP By similarity

Experimental info

Sequence conflict246 – 27631EPLAR…NLLHR → SRWPATGSTNGFVTVEGREG CPSRWATFFTG in CAA67901. Ref.1

Sequences

Sequence LengthMass (Da)Tools
O07045 [UniParc].

Last modified July 15, 1998. Version 2.
Checksum: 45203E2255D5E1D1

FASTA44849,574
        10         20         30         40         50         60 
MPLDLYNTLT RRKERFEPMT PDRVGMYVCG PTVYDTAHIG NARPVVFDLL FRLLRRLYPA 

        70         80         90        100        110        120 
VTYVRNITAS DDKIIDRRAT TGADRGADQA HRGPLPRRHG PLNAAPTIEP RATHHISHMV 

       130        140        150        160        170        180 
ALIGLLIEPA TPTPRKGTCC SPCRRWRSTG QLSRRSLDEM IAGARVEVAP YKRDSSDFVL 

       190        200        210        220        230        240 
WKPSTDGQPG WDSPWGRGRP GWHIECSAMA KEHLGVTFDI HGGGLDLILP DHENEIAQSR 

       250        260        270        280        290        300 
CAHAGEPLAR YWVHQRLRDR RGARRMSKSL GNLLHRGTSC WTEFPGGGHP LGVRPYRSRG 

       310        320        330        340        350        360 
LPEAEESKAT LDRWYQALRG DPAPAQAELP FDVLAALEDD LNSPLAISHL HELASAVNKA 

       370        380        390        400        410        420 
TGEAEKAAAK GRCRSAERWA APETRSVVPL GAEGAAALSD ADIQQRIEDR SAARKAKNYA 

       430        440 
EADRIRKELA DLGIVLEDGP QGTTWKRA

« Hide

References

[1]"Identification and isolation of the indole-3-pyruvate decarboxylase gene from Azospirillum brasilense Sp7: sequencing and functional analysis of the gene locus."
Zimmer W., Wesche M., Timmermans L.
Curr. Microbiol. 36:327-331(1998) [PubMed: 9608743] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 29145 / Sp7 / DSM 1690 / IMET 11303.
[2]Bairoch A.
Unpublished observations (APR-1998)
Cited for: IDENTIFICATION OF PROBABLE FRAMESHIFT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X99587 Genomic DNA. Translation: CAA67901.1. Frameshift.

3D structure databases

ProteinModelPortalO07045.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

HAMAPMF_00041. Cys_tRNA_synth.
[Tree]
InterProIPR015803. 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]
Gene3DG3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 2 hits.
PANTHERPTHR10890. Cys_tRNA-synt_1a. 1 hit.
PfamPF09190. DALR_2. 1 hit.
PF01406. tRNA-synt_1e. 1 hit.
[Graphical view]
PRINTSPR00983. TRNASYNTHCYS.
SMARTSM00840. DALR_2. 1 hit.
[Graphical view]
SUPFAMSSF47323. tRNAsyn_1a_bind. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYC_AZOBR
AccessionPrimary (citable) accession number: O07045
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: July 15, 1998
Last modified: January 25, 2012
This is version 70 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

SIMILARITY comments

Index of protein domains and families

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