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Description:
DNA polymerase IV (EC 2.7.7.7) (POL IV).
Molecular weight: 67396
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, gap-filling( GO:0006287 ) double-strand break repair( GO:0006302 ) double-strand break repair via nonhomologous end-joining( GO:0006303 )
Important dates:
01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
13-APR-2004, sequence version 3.
07-MAR-2006, entry version 56.
Phylogenetic order:
Eukaryota Fungi Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces.
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 DPO4_YEAST:
| Database | Pointer | Add. info#1 | Add. info#2 |
| EMBL | X59720 | CAA42331.2.1 | - |
| PIR | S19424 | S19424. | |
| HSSP | P09838 | 1JMS | |
| IntAct | P25615 | -.1 | |
| GermOnline | 138919 | -.1 | |
| Ensembl | YCR014C | Saccharomyces cerevisiae.1 | |
| GenomeReviews | X59720_GR | YCR014C.1 | |
| SGD | S000000607 | POL4. | |
| LinkHub | P25615 | -.1 | |
| GO | GO:0005634 | C:nucleus | TAS. |
| GO | GO:0003890 | F:beta DNA polymerase activity | TAS. |
| GO | GO:0005515 | F:protein binding | IPI. |
| GO | GO:0006287 | P:base-excision repair, gap-filling | TAS. |
| GO | GO:0006303 | P:double-strand break repair via nonhomologou... | IDA. |
| InterPro | IPR002054 | DNA_polX. | |
| InterPro | IPR002008 | DNA_polX_beta. | |
| PRINTS | PR00869 | DNAPOLX. | |
| PRINTS | PR00870 | DNAPOLXBETA. | |
| SMART | SM00483 | POLXc | 1. |
| PROSITE | PS00522 | DNA_POLYMERASE_X | 1. |
Keywords:
Complete proteome; Direct protein sequencing; DNA damage; DNA repair; DNA-directed DNA polymerase; Magnesium; Metal-binding; Nuclear protein; Nucleotidyltransferase; Transferase.
References:
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S288c;
RX MEDLINE=92244356; PubMed=1574125; DOI=10.1038/357038a0;
RA Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M.,
RA Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G.,
RA Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A.,
RA Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M., Carcano C.,
RA Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M.,
RA Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C.,
RA Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M.,
RA Fabre F., Fairhead C., Faye G., Feldmann H., Fiers W.,
RA Francingues-Gaillard M.-C., Franco L., Frontali L., Fukuhara H.,
RA Fuller L.J., Galland P., Gent M.E., Gigot D., Gilliquet V.,
RA Glansdorff N., Goffeau A., Grenson M., Grisanti P., Grivell L.A.,
RA de Haan M., Haasemann M., Hatat D., Hoenicka J., Hegemann J.H.,
RA Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P., Huse K.,
RA Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M.,
RA Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P.,
RA Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G.,
RA Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E.,
RA Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F.,
RA Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L.,
RA Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J.,
RA Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B.,
RA Pohl F.M., Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A.,
RA Remacha M.A., Richterich P., Roberts A.B., Rodriguez F., Sanz E.,
RA Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y.,
RA Skala J., Slonimski P.P., Sor F., Soustelle C., Spiegelberg R.,
RA Stateva L.I., Steensma H.Y., Steiner S., Thierry A., Thireos G.,
RA Tzermia M., Urrestarazu L.A., Valle G., Vetter I.,
RA van Vliet-Reedijk J.C., Voet M., Volckaert G., Vreken P., Wang H.,
RA Warmington J.R., von Wettstein D., Wicksteed B.L., Wilson C.,
RA Wurst H., Xu G., Yoshikawa A., Zimmermann F.K., Sgouros J.G.;
RT "The complete DNA sequence of yeast chromosome III.";
RL Nature 357:38-46(1992).
RN [2]
RP SEQUENCE REVISION TO 48; 170; 450 AND 481.
RA Valles G., Volckaerts G.;
RL Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 302-581.
RX MEDLINE=92327849; PubMed=1626432;
RA Skala J., Purnelle B., Goffeau A.;
RT "The complete sequence of a 10.8 kb segment distal of SUF2 on the
RT right arm of chromosome III from Saccharomyces cerevisiae reveals
RT seven open reading frames including the RVS161, ADP1 and PGK genes.";
RL Yeast 8:409-417(1992).
RN [4]
RP CHARACTERIZATION, AND PROTEIN SEQUENCE OF 1-14.
RX MEDLINE=94089375; PubMed=8265341;
RA Prasad R., Widen S.G., Singhal R.K., Watkins J., Prakash L.,
RA Wilson S.H.;
RT "Yeast open reading frame YCR14C encodes a DNA beta-polymerase-like
RT enzyme.";
RL Nucleic Acids Res. 21:5301-5307(1993).
RN [5]
RP PROTEIN SEQUENCE OF 66-78; 137-148; 286-298; 341-355 AND 364-372,
RP FUNCTION, AND INDUCTION.
RX MEDLINE=94344759; PubMed=8065914;
RA Leem S.-H., Ropp P.A., Sugino A.;
RT "The yeast Saccharomyces cerevisiae DNA polymerase IV: possible
RT involvement in double strand break DNA repair.";
RL Nucleic Acids Res. 22:3011-3017(1994).
RN [6]
RP FUNCTION, ENZYME REGULATION, AND INTERACTION WITH THE DNL4-LIF1
RP COMPLEX.
RX PubMed=12235149; DOI=10.1074/jbc.M206861200;
RA Tseng H.-M., Tomkinson A.E.;
RT "A physical and functional interaction between yeast Pol4 and Dnl4-
RT Lif1 links DNA synthesis and ligation in nonhomologous end joining.";
RL J. Biol. Chem. 277:45630-45637(2002).
RN [7]
RP FUNCTION, AND MUTAGENESIS OF LYS-246; LYS-247 AND ASP-366.
RX PubMed=10438542; DOI=10.1074/jbc.274.33.23599;
RA Wilson T.E., Lieber M.R.;
RT "Efficient processing of DNA ends during yeast nonhomologous end
RT joining. Evidence for a DNA polymerase beta (Pol4)-dependent
RT pathway.";
RL J. Biol. Chem. 274:23599-23609(1999).
RN [8]
RP SIMILARITY TO DNA POLYMERASE TYPE-X FAMILY.
RX MEDLINE=93284106; PubMed=1304897;
RA Bork P., Ouzounis C., Sander C., Scharf M., Schneider R.,
RA Sonnhammer E.;
RT "Comprehensive sequence analysis of the 182 predicted open reading
RT frames of yeast chromosome III.";
RL Protein Sci. 1:1677-1690(1992).
Feature:
INIT_MET 0 0
CHAIN 1 581 DNA polymerase IV.
/FTId=PRO_0000218789.
REGION 359 368 Involved in ssDNA binding (By
similarity).
COMPBIAS 471 477 Poly-Glu.
METAL 366 366 Magnesium (By similarity).
METAL 368 368 Magnesium (By similarity).
METAL 501 501 Magnesium (By similarity).
MUTAGEN 246 246 K->R: Weakened DNA-binding.
MUTAGEN 247 247 K->R: Weakened DNA-binding.
MUTAGEN 366 366 D->E: Loss of nucleotidyl transfer.
Comments:
-!- FUNCTION: Repair polymerase. Involved in gap-filling in DNA
nonhomologous end joining (NHEJ) required for double-strand break
repair. Seems to conduct DNA synthesis in a stepwise distributive
fashion rather than in a processive fashion as for other DNA
polymerases. Preferentially acts upon short gaps formed by the
alignment of linear duplexes with complementary single-strand
ends. Required for filling gaps that need removal of a 5'- or 3'-
terminal mismatch, however lacks nuclease activities.
-!- CATALYTIC ACTIVITY: Deoxynucleoside triphosphate + DNA(n) =
diphosphate + DNA(n+1).
-!- COFACTOR: Magnesium (By similarity).
-!- ENZYME REGULATION: Stimulated by the interaction with the DNL4-
LIF1 complex.
-!- SUBUNIT: Interacts with DNL4 subunit of the DNL4-LIF1 complex.
-!- INTERACTION:
P53879:RHO5; NbExp=1; IntAct=EBI-6115, EBI-29054;
-!- SUBCELLULAR LOCATION: Nucleus.
-!- INDUCTION: During meiosis.
-!- SIMILARITY: Belongs to the DNA polymerase type-X family.
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Sequence length: 581
SLKGKFFAFL PNPNTSSNKF FKSILEKKGA TIVSSIQNCL QSSRKEVVIL IEDSFVDSDM
HLTQKDIFQR EAGLNDVDEF LGKIEQSGIQ CVKTSCITKW VQNDKFAFQK DDLIKFQPSI
IVISDNADDG QSSTDKESEI STDVESERND DSNNKDMIQA SKPLKRLLQG DKGRASLVTD
KTKYKNNELI IGALKRLTKK YEIEGEKFRA RSYRLAKQSM ENCDFNVRSG EEAHTKLRNI
GPSIAKKIQV ILDTGVLPGL NDSVGLEDKL KYFKNCYGIG SEIAKRWNLL NFESFCVAAK
KDPEEFVSDW TILFGWSYYD DWLCKMSRNE CFTHLKKVQK ALRGIDPECQ VELQGSYNRG
YSKCGDIDLL FFKPFCNDTT ELAKIMETLC IKLYKDGYIH CFLQLTPNLE KLFLKRIVER
FRTAKIVGYG ERKRWYSSEI IKKFFMGVKL SPRELEELKE MKNDEGTLLI EEEEEEETKL
KPIDQYMSLN AKDGNYCRRL DFFCCKWDEL GAGRIHYTGS KEYNRWIRIL AAQKGFKLTQ
HGLFRNNILL ESFNERRIFE LLNLKYAEPE HRNIEWEKKT A