Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

B2FHC6 (B2FHC6_STRMK) Unreviewed, UniProtKB/TrEMBL

Last modified July 9, 2014. Version 40. Feed History...

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

Names and origin

Protein attributes

Sequence length189 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Function

Destroys radicals which are normally produced within the cells and which are toxic to biological systems By similarity. RuleBase RU000393

Catalytic activity

2 superoxide + 2 H+ = O2 + H2O2. RuleBase RU000393

Cofactor

Binds 1 copper ion per subunit By similarity. RuleBase RU000393

Binds 1 zinc ion per subunit By similarity. RuleBase RU000393

Sequence similarities

Belongs to the Cu-Zn superoxide dismutase family. RuleBase RU000393

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424 Potential EMBL CAQ43769.1
Chain25 – 189165 Potential EMBL CAQ43769.1
PRO_5000341744

Sequences

Sequence LengthMass (Da)Tools
B2FHC6 [UniParc].

Last modified June 10, 2008. Version 1.
Checksum: 2A7D8BC07C5958CA

FASTA18918,992
        10         20         30         40         50         60 
MRLSFAILPL SAAVLLSACG SAPKKTEPTP PPPTVVSAAK QGEANIAPAS ASIVSGRIAL 

        70         80         90        100        110        120 
MVEPGGIHIT GLIGGLQPMQ QAGFHIHERG DCSAVDASSA GNHFNPGGAA HGRAGTGKHH 

       130        140        150        160        170        180 
LGDMDNLRAD AQGRANVDIH LKGVTLGGGA ATDIAGRALV VHANADDYRS QPAGNAGVRI 


ACGVIRVVR 

« Hide

References

[1]"The complete genome, comparative and functional analysis of Stenotrophomonas maltophilia reveals an organism heavily shielded by drug resistance determinants."
Crossman L.C., Gould V.C., Dow J.M., Vernikos G.S., Okazaki A., Sebaihia M., Saunders D., Arrowsmith C., Carver T., Peters N., Adlem E., Kerhornou A., Lord A., Murphy L., Seeger K., Squares R., Rutter S., Quail M.A. expand/collapse author list , Rajandream M.A., Harris D., Churcher C., Bentley S.D., Parkhill J., Thomson N.R., Avison M.B.
Genome Biol. 9:R74.1-R74.13(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K279a EMBL CAQ43769.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM743169 Genomic DNA. Translation: CAQ43769.1.
RefSeqYP_001970084.1. NC_010943.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING522373.Smlt0160.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAQ43769; CAQ43769; Smlt0160.
GeneID6393785.
KEGGsml:Smlt0160.
PATRIC23696061. VBISteMal45202_0150.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2032.
HOGENOMHOG000263448.
KOK04565.
OMAANIAPAS.
OrthoDBEOG6K13RS.

Enzyme and pathway databases

BioCycSMAL522373:GJE8-150-MONOMER.

Family and domain databases

Gene3D2.60.40.200. 1 hit.
InterProIPR018152. SOD_Cu/Zn_BS.
IPR001424. SOD_Cu_Zn_dom.
[Graphical view]
PfamPF00080. Sod_Cu. 1 hit.
[Graphical view]
PRINTSPR00068. CUZNDISMTASE.
SUPFAMSSF49329. SSF49329. 1 hit.
PROSITEPS00087. SOD_CU_ZN_1. 1 hit.
PS00332. SOD_CU_ZN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameB2FHC6_STRMK
AccessionPrimary (citable) accession number: B2FHC6
Entry history
Integrated into UniProtKB/TrEMBL: June 10, 2008
Last sequence update: June 10, 2008
Last modified: July 9, 2014
This is version 40 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)