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Q6LHY2 (SYC2_PHOPR) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 52. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Putative cysteine--tRNA ligase 2

EC=6.1.1.16
Alternative name(s):
Cysteinyl-tRNA synthetase 2
Short name=CysRS 2
Gene names
Name:cysS2
Ordered Locus Names:PBPRB1226
OrganismPhotobacterium profundum (Photobacterium sp. (strain SS9)) [Complete proteome] [HAMAP]
Taxonomic identifier74109 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaePhotobacterium

Protein attributes

Sequence length457 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
   Technical termComplete proteome
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 – 457457Putative cysteine--tRNA ligase 2 HAMAP MF_00041
PRO_0000159454

Sites

Metal binding321Zinc By similarity
Metal binding2231Zinc By similarity
Metal binding2481Zinc By similarity
Metal binding2521Zinc By similarity
Binding site2831ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6LHY2 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: EC931FE165B1B0CA

FASTA45752,294
        10         20         30         40         50         60 
MSQPELLLFD TMARELRPFN SIRANKVGLY ACGPTVYDYA HAGNLRTYLF VDVLRRTLEI 

        70         80         90        100        110        120 
NGYEVNHVMN ITDVGHLVSD ADTGEDKMEK GARKQNKSAW EIAQFFEQAF FDDLKLLNIS 

       130        140        150        160        170        180 
TPSVTCRATE HIQEQIKFIQ ELETKGFTYQ TSDGVYFNTD RLADYGKLAR LDKQGLEAGI 

       190        200        210        220        230        240 
RVEMAEKKHP TDFALWKFSG DKPRQMEWQG PWGIGFPGWH IECSAMAEKY LGDVFDIHVG 

       250        260        270        280        290        300 
GEDHIPVHHT NEIAQCQAKN GHVQANYWLH GYFLQLKKEK ISKSGTSLRL DALVAKGYEP 

       310        320        330        340        350        360 
MAYRYLTLTS HYRSHLSFTW EGLSGAQKAL HRLRNKVAFL PSNGNVDESY RELFMRHINR 

       370        380        390        400        410        420 
DLNMPQALAL VWDVLNSELL PENKRATALF FDRILGLDIH KIETVEIPEH ISRLVELRTQ 

       430        440        450 
VKRQGNFKKA DAIRNQIHDL GYQVNDSGDG STVTIRS 

« Hide

References

[1]"Life at depth: Photobacterium profundum genome sequence and expression analysis."
Vezzi A., Campanaro S., D'Angelo M., Simonato F., Vitulo N., Lauro F.M., Cestaro A., Malacrida G., Simionati B., Cannata N., Romualdi C., Bartlett D.H., Valle G.
Science 307:1459-1461(2005) [PubMed: 15746425] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: SS9.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR378678 Genomic DNA. Translation: CAG23098.1.
RefSeqYP_132898.1. NC_006371.1.

3D structure databases

ProteinModelPortalQ6LHY2.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3121512.
GenomeReviewsGene locus PBPRB1226 in contig CR354532_GR.
KEGGppr:PBPRB1226.
NMPDRfig|298386.1.peg.1319.
PATRIC22941048. VBIPhoPro109272_5090.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG327651.
OMAIGNLRTY.
PhylomeDBQ6LHY2.
ProtClustDBCLSK2395547.

Enzyme and pathway databases

BioCycPPRO298386:PBPRB1226-MONOMER.

Family and domain databases

HAMAPMF_00041. Cys_tRNA_synth. Divergent sequence.
[Tree]
InterProIPR015803. Cys-tRNA-synt.
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. 1 hit.
KOK01883.
PANTHERPTHR10890. Cys_tRNA-synt_1a. 1 hit.
PfamPF01406. tRNA-synt_1e. 1 hit.
[Graphical view]
PRINTSPR00983. TRNASYNTHCYS.
SUPFAMSSF47323. tRNAsyn_1a_bind. 1 hit.
TIGRFAMsTIGR00435. CysS. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYC2_PHOPR
AccessionPrimary (citable) accession number: Q6LHY2
Entry history
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: July 5, 2004
Last modified: January 25, 2012
This is version 52 of the entry and version 1 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