Protein data for UNG_XANCP:

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

Molecular weight: 26758

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:
08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
01-OCT-2002, sequence version 1.
07-MAR-2006, entry version 25.

Phylogenetic order:
Bacteria Proteobacteria Gammaproteobacteria Xanthomonadales Xanthomonadaceae Xanthomonas.

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_XANCP:

DatabasePointerAdd. info#1Add. info#2
EMBLAE012498AAM43472.1-
HSSPP122951LQG
GenomeReviewsAE008922_GRXCC3772.1
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=ATCC 33913 / NCPPB 528;
RX MEDLINE=22022145; PubMed=12024217; DOI=10.1038/417459a;
RA da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R.,
RA Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A.,
RA Almeida N.F. Jr., Alves L.M.C., do Amaral A.M., Bertolini M.C.,
RA Camargo L.E.A., Camarotte G., Cannavan F., Cardozo J., Chambergo F.,
RA Ciapina L.P., Cicarelli R.M.B., Coutinho L.L., Cursino-Santos J.R.,
RA El-Dorry H., Faria J.B., Ferreira A.J.S., Ferreira R.C.C.,
RA Ferro M.I.T., Formighieri E.F., Franco M.C., Greggio C.C., Gruber A.,
RA Katsuyama A.M., Kishi L.T., Leite R.P., Lemos E.G.M., Lemos M.V.F.,
RA Locali E.C., Machado M.A., Madeira A.M.B.N., Martinez-Rossi N.M.,
RA Martins E.C., Meidanis J., Menck C.F.M., Miyaki C.Y., Moon D.H.,
RA Moreira L.M., Novo M.T.M., Okura V.K., Oliveira M.C., Oliveira V.R.,
RA Pereira H.A., Rossi A., Sena J.A.D., Silva C., de Souza R.F.,
RA Spinola L.A.F., Takita M.A., Tamura R.E., Teixeira E.C., Tezza R.I.D.,
RA Trindade dos Santos M., Truffi D., Tsai S.M., White F.F.,
RA Setubal J.C., Kitajima J.P.;
RT "Comparison of the genomes of two Xanthomonas pathogens with differing
RT host specificities.";
RL Nature 417:459-463(2002).

Feature:
CHAIN 1 241 Uracil-DNA glycosylase.
/FTId=PRO_0000176167.
ACT_SITE 71 71 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.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------

Sequence length: 241

     MTEGEGRIQL EPSWKARVGE WLLQPQMQEL SAFLRQRKAA NARVFPPGPQ IFAAFDATPF
     EQVKVVVLGQ DPYHGEGQAH GLCFSVLPGV PVPPSLLNIY KEIQDDLGIP RPDHGYLMPW
     ARQGVLLLNA VLTVEQGRAG AHQNKGWEGF TDHVVETLNR EREGLVFLLW GSYAQSKGKV
     IDQARHRVFK APHPSPLSAH RGFLGCKHFS KTNEHLQRRG LSPIDWSLPS RAALDLSLAG
     G