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D5TM54 (D5TM54_BACT1) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 22. Feed History...

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

Protein namesSubmitted name:
Superoxide dismutase (Cu-Zn) EMBL ADH09330.1
Gene names
Name:sodC EMBL ADH09330.1
Ordered Locus Names:BMB171_C4522 EMBL ADH09330.1
OrganismBacillus thuringiensis (strain BMB171) [Complete proteome] [HAMAP] EMBL ADH09330.1
Taxonomic identifier714359 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group ›

Protein attributes

Sequence length179 AA.
Sequence statusComplete.
Protein existencePredicted

Ontologies

Keywords
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processsuperoxide metabolic process

Inferred from electronic annotation. Source: InterPro

   Molecular_functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

superoxide dismutase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequences

Sequence LengthMass (Da)Tools
D5TM54 [UniParc].

Last modified July 13, 2010. Version 1.
Checksum: 24684667C6D67C58

FASTA17919,122
        10         20         30         40         50         60 
MKKRLFFSCC LLFLMAGCDQ GKPKEIEVKL HNASGDEVGT AKVVQQTSGV KITIKGEGFT 

        70         80         90        100        110        120 
PGPHGLHVHE IGECKAPRFE SSGNHFNPDD KKHGLLNPKG AENGDLPNVV ADGSGKIKAE 

       130        140        150        160        170 
IDAPHITLEE GKTTIHRKDG ASIIITENPD DGMTQPTGKS GDRIACGVIV KKASDMKKK

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References

[1]"Complete genome sequence of Bacillus thuringiensis mutant strain BMB171."
He J., Shao X., Zheng H., Li M., Wang J., Zhang Q., Li L., Liu Z., Sun M., Wang S., Yu Z.
J. Bacteriol. 192:4074-4075(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: BMB171 EMBL ADH09330.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP001903 Genomic DNA. Translation: ADH09330.1.
RefSeqYP_003667050.1. NC_014171.1.

3D structure databases

ProteinModelPortalD5TM54.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaADH09330; ADH09330; BMB171_C4522.
GeneID9195563.
KEGGbtb:BMB171_C4522.
PATRIC38136169. VBIBacThu148000_4839.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000263448.
KOK04565.

Enzyme and pathway databases

BioCycBTHU714359:GJBQ-4666-MONOMER.

Family and domain databases

Gene3D2.60.40.200. 1 hit.
InterProIPR024134. SOD_Cu/Zn_/chaperones.
IPR001424. SOD_Cu_Zn_dom.
[Graphical view]
PANTHERPTHR10003. PTHR10003. 1 hit.
PfamPF00080. Sod_Cu. 1 hit.
[Graphical view]
SUPFAMSSF49329. SOD_Cu_Zn. 1 hit.
ProtoNetSearch...

Entry information

Entry nameD5TM54_BACT1
AccessionPrimary (citable) accession number: D5TM54
Entry history
Integrated into UniProtKB/TrEMBL: July 13, 2010
Last sequence update: July 13, 2010
Last modified: May 1, 2013
This is version 22 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
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