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Protein data for UNG_BORPA:

Description:
Uracil-DNA glycosylase (EC 3.2.2.-) (UDG).

Molecular weight: 26910

View which proteins in this organism that is involved with DNA Repair;
classified after biological processes (using data from the GOA project):

DNA repair( GO:0006281 ) base-excision repair( GO:0006284 )


Important dates:
15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
01-OCT-2003, sequence version 1.
07-MAR-2006, entry version 18.

Phylogenetic order:
Bacteria Proteobacteria Betaproteobacteria Burkholderiales Alcaligenaceae Bordetella.

To calculate the pI (Isoelectric point - the pH where a protein has a neutral charge),
go to this page and enter the protein ID (e.g 3MG_ECOLI): http://us.expasy.org/tools/pi_tool.html

Links to references in other databases for protein UNG_BORPA:

DatabasePointerAdd. info#1Add. info#2
EMBLBX640423CAE39947.1-
GenomeReviewsBX470249_GRBPP0206.1
BioCycBPAR519:BPP0206-MONOMER-.1
HAMAPMF_00148-1.
InterProIPR003249U_glycsylse_notp.
InterProIPR002043UDNA_glycsylse.
InterProIPR005122UDNA_glycsylseSF.
PANTHERPTHR11264U_glycsylse_notp.11.
PfamPF03167UDG1.
ProDomPD001589U_glycsylse_notp1.
TIGRFAMsTIGR00628ung1.
PROSITEPS00130U_DNA_GLYCOSYLASE1.

General information about the databases mentioned above

Keywords:
Complete proteome; DNA damage; DNA repair; Glycosidase; Hydrolase.

References:
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=12822 / ATCC BAA-587;
RX MEDLINE=22827954; PubMed=12910271; DOI=10.1038/ng1227;
RA Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R.,
RA Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L.,
RA Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A.,
RA Achtman M., Atkin R., Baker S., Basham D., Bason N., Cherevach I.,
RA Chillingworth T., Collins M., Cronin A., Davis P., Doggett J.,
RA Feltwell T., Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K.,
RA Leather S., Moule S., Norberczak H., O'Neil S., Ormond D., Price C.,
RA Rabbinowitsch E., Rutter S., Sanders M., Saunders D., Seeger K.,
RA Sharp S., Simmonds M., Skelton J., Squares R., Squares S., Stevens K.,
RA Unwin L., Whitehead S., Barrell B.G., Maskell D.J.;
RT "Comparative analysis of the genome sequences of Bordetella pertussis,
RT Bordetella parapertussis and Bordetella bronchiseptica.";
RL Nat. Genet. 35:32-40(2003).

Feature:
CHAIN 1 250 Uracil-DNA glycosylase.
/FTId=PRO_0000176073.
ACT_SITE 78 78 Proton acceptor (By similarity).

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).
-!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
-!- SIMILARITY: Belongs to the uracil-DNA glycosylase family.
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Sequence length: 250

     MPNDNRLAPA ALAAQAAALP AAWRHVLEQP AVARAFASVL GHVEQRLAEG AVVYPATPFR
     ALDQLAPADV RVVILGQDPY HGPGQAQGLA FSVPDDCKCP PSLRNIFNEI AVDYPRPTRH
     DLSAWTRQGV LLLNTSLTVE DGQPGSHAKR GWETVTDALI AEVARDPSPK VFLLWGAHAQ
     AKQALVPADA GHLVLAANHP SPLSARRPPV PFVGCGHFRQ TNAWLQQRGQ KPVDWSGEQN
     NASRQGEFAL

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