Description:
Uracil-DNA glycosylase (EC 3.2.2.-) (UDG).
Molecular weight: 36705
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:
11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
01-NOV-1998, sequence version 1.
07-FEB-2006, entry version 39.
Phylogenetic order:
Eukaryota Fungi Ascomycota Schizosaccharomycetes Schizosaccharomycetales Schizosaccharomycetaceae Schizosaccharomyces.
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_SCHPO:
| Database | Pointer | Add. info#1 | Add. info#2 |
| EMBL | AF174292 | AAD51974.1 | - |
| EMBL | AL031740 | CAA21086.1 | - |
| PIR | T40846 | T40846. | |
| HSSP | P12295 | 1LQG | |
| GeneDB_Spombe | SPCC1183.06 | -.1 | |
| BioCyc | SPOM-XXX-01:SPOM-XXX-01-002233-MONOMER | -.1 | |
| GO | GO:0005739 | C:mitochondrion | IMP. |
| GO | GO:0005634 | C:nucleus | IMP. |
| GO | GO:0004844 | F:uracil DNA N-glycosylase activity | IMP. |
| GO | GO:0006281 | P:DNA repair | IMP. |
| InterPro | IPR003249 | U_glycsylse_notp. | |
| InterPro | IPR002043 | UDNA_glycsylse. | |
| InterPro | IPR005122 | UDNA_glycsylseSF. | |
| PANTHER | PTHR11264 | U_glycsylse_notp.1 | 1. |
| Pfam | PF03167 | UDG | 1. |
| ProDom | PD001589 | U_glycsylse_notp | 1. |
| TIGRFAMs | TIGR00628 | ung | 1. |
| PROSITE | PS00130 | U_DNA_GLYCOSYLASE | 1. |
Keywords:
Complete proteome; DNA damage; DNA repair; Glycosidase; Hydrolase; Nuclear protein.
References:
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=SP223;
RX MEDLINE=22694182; PubMed=12810074; DOI=10.1016/S0006-291X(03)01036-2;
RA Elder R.T., Zhu X., Priet S., Chen M., Yu M., Navarro J.-M., Sire J.,
RA Zhao Y.;
RT "A fission yeast homologue of the human uracil-DNA-glycosylase and
RT their roles in causing DNA damage after overexpression.";
RL Biochem. Biophys. Res. Commun. 306:693-700(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972;
RX MEDLINE=21848401; PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M.,
RA Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A.,
RA Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G.,
RA Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K.,
RA James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J.,
RA Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C.,
RA Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E.,
RA Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S.,
RA Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K.,
RA Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S.,
RA Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B.,
RA Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S.,
RA Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D.,
RA Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R.,
RA Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B.,
RA Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S.,
RA Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M.,
RA Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G.,
RA Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J.,
RA Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L.,
RA Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J.,
RA Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
Feature:
CHAIN 1 322 Uracil-DNA glycosylase.
/FTId=PRO_0000176171.
ACT_SITE 142 142 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.
-!- SUBCELLULAR LOCATION: Nucleus.
-!- SIMILARITY: Belongs to the uracil-DNA glycosylase family.
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Sequence length: 322
MTVLNTTDKR KADDTVNKLD GKLKQPRLDN FFKTNTSSPA LKDTQVLDNK ENNSVSKFNK
EKWAENLTPA QRKLLQLEID TLESSWFDAL KDEFLKPYFL NLKEFLMKEW QSQRVFPPKE
DIYSWSHHTP LHKTKVILLG QDPYHNIGQA HGLCFSVRPG IPCPPSLVNI YKAIKIDYPD
FVIPKTGYLV PWADQGILML NASLTVRAHQ AASHSGKGWE TFTSAVLQVA LNRNRKGLVI
LAWGTPAAKR LQGLPLKAHY VLRSVHPSPL SAHRGFFECH HFKKTNEWLE EQYGPEKCIN
WSAVSEQKAK IKSSELESSS TE