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C1FQU5 (C1FQU5_CLOBJ) Unreviewed, UniProtKB/TrEMBL

Last modified April 16, 2014. Version 37. 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 namesRecommended name:
Endonuclease III PIRNR PIRNR001435 HAMAP-Rule MF_00942

EC=4.2.99.18 PIRNR PIRNR001435 HAMAP-Rule MF_00942
Alternative name(s):
DNA-(apurinic or apyrimidinic site) lyase HAMAP-Rule MF_00942
Gene names
Name:nth HAMAP-Rule MF_00942 EMBL ACO87117.1
Ordered Locus Names:CLM_0259 EMBL ACO87117.1
OrganismClostridium botulinum (strain Kyoto / Type A2) [Complete proteome] [HAMAP] EMBL ACO87117.1
Taxonomic identifier536232 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

Protein attributes

Sequence length213 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

DNA repair enzyme that has both DNA N-glycosylase activity and AP-lyase activity By similarity. PIRNR PIRNR001435

DNA repair enzyme that has both DNA N-glycosylase activity and AP-lyase activity. The DNA N-glycosylase activity releases various damaged pyrimidines from DNA by cleaving the N-glycosidic bond, leaving an AP (apurinic/apyrimidinic) site. The AP-lyase activity cleaves the phosphodiester bond 3' to the AP site by a beta-elimination, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'-phosphate By similarity. HAMAP-Rule MF_00942

Catalytic activity

The C-O-P bond 3' to the apurinic or apyrimidinic site in DNA is broken by a beta-elimination reaction, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'-phosphate. PIRNR PIRNR001435 HAMAP-Rule MF_00942

Cofactor

Binds 1 4Fe-4S cluster By similarity. PIRNR PIRNR001435 HAMAP-Rule MF_00942

Sequence similarities

Belongs to the Nth/MutY family. PIRNR PIRNR001435 HAMAP-Rule MF_00942

Contains 1 HhH domain. HAMAP-Rule MF_00942

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Domain100 – 12728HhH By similarity HAMAP-Rule MF_00942

Sites

Metal binding1871Iron-sulfur (4Fe-4S) By similarity HAMAP-Rule MF_00942
Metal binding1941Iron-sulfur (4Fe-4S) By similarity HAMAP-Rule MF_00942
Metal binding1971Iron-sulfur (4Fe-4S) By similarity HAMAP-Rule MF_00942
Metal binding2031Iron-sulfur (4Fe-4S) By similarity HAMAP-Rule MF_00942

Sequences

Sequence LengthMass (Da)Tools
C1FQU5 [UniParc].

Last modified May 26, 2009. Version 1.
Checksum: FC371696A57984C4

FASTA21324,574
        10         20         30         40         50         60 
MNNHEIKNVI DILVDTYPDA NCELEHRNPF ELLIATVLSA QTTDKKVNEI TKELFKEYST 

        70         80         90        100        110        120 
PKDFLKLTRE ELEEKIKKIG LYRNKSKNIL LLCKELEEKF GSQVPNDFND LTSLPGVGRK 

       130        140        150        160        170        180 
TANVVLANAF KVPTIAVDTH VFRVSNRIGL VDASNVLKTE EQLQQAIPKE LWILMHHVLI 

       190        200        210 
FHGRRCCVAR KPKCEECTIK KYCKYYNEEI KPS 

« Hide

References

[1]"Genome sequence of Clostridium botulinum A2 Kyoto."
Shrivastava S., Brinkac L.M., Brown J.L., Bruce D., Detter C.C., Johnson E.A., Munk C.A., Smith L.A., Smith T.J., Sutton G., Brettin T.S.
Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Kyoto / Type A2.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001581 Genomic DNA. Translation: ACO87117.1.
RefSeqYP_002802521.1. NC_012563.1.

3D structure databases

ProteinModelPortalC1FQU5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING536232.CLM_0259.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACO87117; ACO87117; CLM_0259.
GeneID7764409.
KEGGcby:CLM_0259.
PATRIC19377137. VBICloBot91161_0201.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0177.
HOGENOMHOG000252208.
KOK10773.
OMANNKSKHL.
OrthoDBEOG6H4KC5.
ProtClustDBCLSK899320.

Enzyme and pathway databases

BioCycCBOT536232:GCO3-245-MONOMER.

Family and domain databases

Gene3D1.10.1670.10. 1 hit.
1.10.340.30. 1 hit.
HAMAPMF_00942. Nth.
InterProIPR011257. DNA_glycosylase.
IPR004036. Endonuclease-III-like_CS2.
IPR004035. Endouclease-III_FeS-bd_BS.
IPR003651. Endouclease3_FeS-loop_motif.
IPR003265. HhH-GPD_domain.
IPR000445. HhH_motif.
IPR003583. Hlx-hairpin-Hlx_DNA-bd_motif.
IPR023170. HTH_base_excis_C.
IPR005759. Nth.
[Graphical view]
PfamPF10576. EndIII_4Fe-2S. 1 hit.
PF00633. HHH. 1 hit.
PF00730. HhH-GPD. 1 hit.
[Graphical view]
PIRSFPIRSF001435. Nth. 1 hit.
SMARTSM00478. ENDO3c. 1 hit.
SM00525. FES. 1 hit.
SM00278. HhH1. 1 hit.
[Graphical view]
SUPFAMSSF48150. SSF48150. 1 hit.
TIGRFAMsTIGR01083. nth. 1 hit.
PROSITEPS00764. ENDONUCLEASE_III_1. 1 hit.
PS01155. ENDONUCLEASE_III_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameC1FQU5_CLOBJ
AccessionPrimary (citable) accession number: C1FQU5
Entry history
Integrated into UniProtKB/TrEMBL: May 26, 2009
Last sequence update: May 26, 2009
Last modified: April 16, 2014
This is version 37 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)