Skip Header

Contribute Send feedback
Read comments (?) or add your own

D6ZJD8 (D6ZJD8_MOBCV) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 17. 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·Sequences·References·Cross-refs·Entry infoCustomize order

Protein attributes

Sequence length232 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Excises uracil residues from the DNA which can arise as a result of misincorporation of dUMP residues by DNA polymerase or due to deamination of cytosine By similarity. RuleBase RU003780

Catalytic activity

Hydrolyzes single-stranded DNA or mismatched double-stranded DNA and polynucleotides, releasing free uracil. RuleBase RU003780 SAAS SAAS002043

Sequence similarities

Belongs to the uracil-DNA glycosylase family. RuleBase RU003780

Ontologies

Keywords
   Biological processDNA damage
DNA repair SAAS SAAS002043 RuleBase RU003780
   Molecular functionGlycosidase RuleBase RU003780 SAAS SAAS002043 EMBL ADI66837.1
Hydrolase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processbase-excision repair

Inferred from electronic annotation. Source: HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionuracil DNA N-glycosylase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequences

Sequence LengthMass (Da)Tools
D6ZJD8 [UniParc].

Last modified August 10, 2010. Version 1.
Checksum: E3853EBA2A9A9AE1

FASTA23225,485
        10         20         30         40         50         60 
MQTGEERGGL ERIMSPDWAQ VMAPVEGQIH AMGDFLRAEL AAGRGYFPAG ENVFHAFQYP 

        70         80         90        100        110        120 
LERVKVLIVG QDPYPTPGHA MGLSFSVMSG TEIPRSLVNI FKELHQDLGL PLPTSGDLRP 

       130        140        150        160        170        180 
WAEQGVMLLN RALTVQPGKP ASHRGRGWEA ITEFAIRELA NHHAAQGLPL VAILWGADAR 

       190        200        210        220        230 
RTKEFMPHVP CLESVHPSPL SASRGFFGSR PFSRANELLV AQSGQPVDWR LP 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001992 Genomic DNA. Translation: ADI66837.1.
RefSeqYP_003718331.1. NC_014246.1.

3D structure databases

ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaADI66837; ADI66837; HMPREF0573_10518.
GeneID9336169.
KEGGmcu:HMPREF0573_10518.
PATRIC38203082. VBIMobCur30313_0504.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000229528.
KOK03648.

Enzyme and pathway databases

BioCycMCUR548479:GH17-539-MONOMER.

Family and domain databases

Gene3D3.40.470.10. 1 hit.
HAMAPMF_00148. UDG.
InterProIPR018085. Ura-DNA_Glyclase_AS.
IPR002043. Ura_DNA_glycsylse.
IPR005122. Uracil-DNA_glycosylase-like.
[Graphical view]
PANTHERPTHR11264. PTHR11264. 1 hit.
PfamPF03167. UDG. 1 hit.
[Graphical view]
SMARTSM00986. UDG. 1 hit.
[Graphical view]
SUPFAMSSF52141. UDNA_glycsylseSF. 1 hit.
TIGRFAMsTIGR00628. ung. 1 hit.
PROSITEPS00130. U_DNA_GLYCOSYLASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameD6ZJD8_MOBCV
AccessionPrimary (citable) accession number: D6ZJD8
Entry history
Integrated into UniProtKB/TrEMBL: August 10, 2010
Last sequence update: August 10, 2010
Last modified: May 1, 2013
This is version 17 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)