POLH_YEAST
ID POLH_YEAST Reviewed; 632 AA.
AC Q04049; D6VT49;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=DNA polymerase eta;
DE EC=2.7.7.7;
DE AltName: Full=Radiation-sensitive protein 30;
GN Name=RAD30; Synonyms=DBH1; OrderedLocusNames=YDR419W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP FUNCTION, AND INDUCTION.
RX PubMed=9409821; DOI=10.1093/genetics/147.4.1557;
RA McDonald J.P., Levine A.S., Woodgate R.;
RT "The Saccharomyces cerevisiae RAD30 gene, a homologue of Escherichia coli
RT dinB and umuC, is DNA damage inducible and functions in a novel error-free
RT postreplication repair mechanism.";
RL Genetics 147:1557-1568(1997).
RN [4]
RP FUNCTION, AND MUTAGENESIS OF 155-ASP-GLU-156.
RX PubMed=10347143; DOI=10.1074/jbc.274.23.15975;
RA Johnson R.E., Prakash S., Prakash L.;
RT "Requirement of DNA polymerase activity of yeast Rad30 protein for its
RT biological function.";
RL J. Biol. Chem. 274:15975-15977(1999).
RN [5]
RP FUNCTION.
RX PubMed=10601233; DOI=10.1074/jbc.274.52.36835;
RA Washington M.T., Johnson R.E., Prakash S., Prakash L.;
RT "Fidelity and processivity of Saccharomyces cerevisiae DNA polymerase
RT eta.";
RL J. Biol. Chem. 274:36835-36838(1999).
RN [6]
RP FUNCTION.
RX PubMed=9974380; DOI=10.1126/science.283.5404.1001;
RA Johnson R.E., Prakash S., Prakash L.;
RT "Efficient bypass of a thymine-thymine dimer by yeast DNA polymerase,
RT Poleta.";
RL Science 283:1001-1004(1999).
RN [7]
RP FUNCTION.
RX PubMed=10924462; DOI=10.1093/genetics/155.4.1633;
RA Xiao W., Chow B.L., Broomfield S., Hanna M.;
RT "The Saccharomyces cerevisiae RAD6 group is composed of an error-prone and
RT two error-free postreplication repair pathways.";
RL Genetics 155:1633-1641(2000).
RN [8]
RP FUNCTION.
RX PubMed=10713149; DOI=10.1074/jbc.275.11.8233;
RA Yuan F., Zhang Y., Rajpal D.K., Wu X., Guo D., Wang M., Taylor J.-S.,
RA Wang Z.;
RT "Specificity of DNA lesion bypass by the yeast DNA polymerase eta.";
RL J. Biol. Chem. 275:8233-8239(2000).
RN [9]
RP FUNCTION.
RX PubMed=11027270; DOI=10.1128/mcb.20.21.8001-8007.2000;
RA Haracska L., Prakash S., Prakash L.;
RT "Replication past O(6)-methylguanine by yeast and human DNA polymerase
RT eta.";
RL Mol. Cell. Biol. 20:8001-8007(2000).
RN [10]
RP FUNCTION.
RX PubMed=10932195; DOI=10.1038/78169;
RA Haracska L., Yu S.-L., Johnson R.E., Prakash L., Prakash S.;
RT "Efficient and accurate replication in the presence of 7,8-dihydro-8-
RT oxoguanine by DNA polymerase eta.";
RL Nat. Genet. 25:458-461(2000).
RN [11]
RP FUNCTION.
RX PubMed=10725365; DOI=10.1073/pnas.97.7.3094;
RA Washington M.T., Johnson R.E., Prakash S., Prakash L.;
RT "Accuracy of thymine-thymine dimer bypass by Saccharomyces cerevisiae DNA
RT polymerase eta.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:3094-3099(2000).
RN [12]
RP FUNCTION.
RX PubMed=11062246; DOI=10.1074/jbc.m007867200;
RA Minko I.G., Washington M.T., Prakash L., Prakash S., Lloyd R.S.;
RT "Translesion DNA synthesis by yeast DNA polymerase eta on templates
RT containing N2-guanine adducts of 1,3-butadiene metabolites.";
RL J. Biol. Chem. 276:2517-2522(2001).
RN [13]
RP FUNCTION, DOMAIN, INTERACTION WITH POL30, AND MUTAGENESIS OF
RP 627-PHE-PHE-628.
RX PubMed=11545742; DOI=10.1016/s1097-2765(01)00319-7;
RA Haracska L., Kondratick C.M., Unk I., Prakash S., Prakash L.;
RT "Interaction with PCNA is essential for yeast DNA polymerase eta
RT function.";
RL Mol. Cell 8:407-415(2001).
RN [14]
RP FUNCTION.
RX PubMed=11113193; DOI=10.1128/mcb.21.1.185-188.2001;
RA Yu S.-L., Johnson R.E., Prakash S., Prakash L.;
RT "Requirement of DNA polymerase eta for error-free bypass of UV-induced CC
RT and TC photoproducts.";
RL Mol. Cell. Biol. 21:185-188(2001).
RN [15]
RP FUNCTION, DOMAIN, AND MUTAGENESIS OF ASP-30; GLU-39; ASP-155 AND GLU-156.
RX PubMed=11238937; DOI=10.1128/mcb.21.6.2018-2025.2001;
RA Kondratick C.M., Washington M.T., Prakash S., Prakash L.;
RT "Acidic residues critical for the activity and biological function of yeast
RT DNA polymerase eta.";
RL Mol. Cell. Biol. 21:2018-2025(2001).
RN [16]
RP FUNCTION.
RX PubMed=11054429; DOI=10.1074/jbc.m009049200;
RA Washington M.T., Johnson R.E., Prakash S., Prakash L.;
RT "Mismatch extension ability of yeast and human DNA polymerase eta.";
RL J. Biol. Chem. 276:2263-2266(2001).
RN [17]
RP FUNCTION.
RX PubMed=12110599; DOI=10.1093/emboj/cdf363;
RA Bresson A., Fuchs R.P.;
RT "Lesion bypass in yeast cells: Pol eta participates in a multi-DNA
RT polymerase process.";
RL EMBO J. 21:3881-3887(2002).
RN [18]
RP FUNCTION.
RX PubMed=11861920; DOI=10.1093/nar/30.5.1262;
RA Zhang H., Siede W.;
RT "UV-induced T-->C transition at a TT photoproduct site is dependent on
RT Saccharomyces cerevisiae polymerase eta in vivo.";
RL Nucleic Acids Res. 30:1262-1267(2002).
RN [19]
RP FUNCTION.
RX PubMed=12899630; DOI=10.1021/bi0345687;
RA Sun L., Zhang K., Zhou L., Hohler P., Kool E.T., Yuan F., Wang Z.,
RA Taylor J.-S.;
RT "Yeast pol eta holds a cis-syn thymine dimer loosely in the active site
RT during elongation opposite the 3'-T of the dimer, but tightly opposite the
RT 5'-T.";
RL Biochemistry 42:9431-9437(2003).
RN [20]
RP FUNCTION, AND MUTAGENESIS OF TYR-64; ARG-67 AND LYS-279.
RX PubMed=12665597; DOI=10.1128/mcb.23.8.3008-3012.2003;
RA Johnson R.E., Trincao J., Aggarwal A.K., Prakash S., Prakash L.;
RT "Deoxynucleotide triphosphate binding mode conserved in Y family DNA
RT polymerases.";
RL Mol. Cell. Biol. 23:3008-3012(2003).
RN [21]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [22]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [23]
RP FUNCTION.
RX PubMed=12888515; DOI=10.1093/nar/gkg489;
RA Kozmin S.G., Pavlov Y.I., Kunkel T.A., Sage E.;
RT "Roles of Saccharomyces cerevisiae DNA polymerases Poleta and Polzeta in
RT response to irradiation by simulated sunlight.";
RL Nucleic Acids Res. 31:4541-4552(2003).
RN [24]
RP FUNCTION.
RX PubMed=12692307; DOI=10.1073/pnas.0837578100;
RA Washington M.T., Wolfle W.T., Spratt T.E., Prakash L., Prakash S.;
RT "Yeast DNA polymerase eta makes functional contacts with the DNA minor
RT groove only at the incoming nucleoside triphosphate.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:5113-5118(2003).
RN [25]
RP FUNCTION.
RX PubMed=14527996; DOI=10.1073/pnas.2134223100;
RA Washington M.T., Prakash L., Prakash S.;
RT "Mechanism of nucleotide incorporation opposite a thymine-thymine dimer by
RT yeast DNA polymerase eta.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:12093-12098(2003).
RN [26]
RP FUNCTION.
RX PubMed=15157108; DOI=10.1021/bi0497749;
RA Gu C., Wang Y.;
RT "LC-MS/MS identification and yeast polymerase eta bypass of a novel gamma-
RT irradiation-induced intrastrand cross-link lesion G[8-5]C.";
RL Biochemistry 43:6745-6750(2004).
RN [27]
RP FUNCTION.
RX PubMed=15544332; DOI=10.1021/bi0489558;
RA Hwang H., Taylor J.-S.;
RT "Role of base stacking and sequence context in the inhibition of yeast DNA
RT polymerase eta by pyrene nucleotide.";
RL Biochemistry 43:14612-14623(2004).
RN [28]
RP FUNCTION.
RX PubMed=15284331; DOI=10.1093/nar/gkh710;
RA Zhao B., Xie Z., Shen H., Wang Z.;
RT "Role of DNA polymerase eta in the bypass of abasic sites in yeast cells.";
RL Nucleic Acids Res. 32:3984-3994(2004).
RN [29]
RP FUNCTION.
RX PubMed=15333698; DOI=10.1093/nar/gkh777;
RA McCulloch S.D., Kokoska R.J., Chilkova O., Welch C.M., Johansson E.,
RA Burgers P.M.J., Kunkel T.A.;
RT "Enzymatic switching for efficient and accurate translesion DNA
RT replication.";
RL Nucleic Acids Res. 32:4665-4675(2004).
RN [30]
RP FUNCTION, AND MUTAGENESIS OF PHE-34.
RX PubMed=15024063; DOI=10.1128/mcb.24.7.2734-2746.2004;
RA Niimi A., Limsirichaikul S., Yoshida S., Iwai S., Masutani C., Hanaoka F.,
RA Kool E.T., Nishiyama Y., Suzuki M.;
RT "Palm mutants in DNA polymerases alpha and eta alter DNA replication
RT fidelity and translesion activity.";
RL Mol. Cell. Biol. 24:2734-2746(2004).
RN [31]
RP FUNCTION.
RX PubMed=15779911; DOI=10.1021/bi048244+;
RA Hwang H., Taylor J.-S.;
RT "Evidence for Watson-Crick and not Hoogsteen or wobble base pairing in the
RT selection of nucleotides for insertion opposite pyrimidines and a thymine
RT dimer by yeast DNA pol eta.";
RL Biochemistry 44:4850-4860(2005).
RN [32]
RP INDUCTION.
RX PubMed=15725627; DOI=10.1016/j.dnarep.2004.12.001;
RA Michan C., Monje-Casas F., Pueyo C.;
RT "Transcript copy number of genes for DNA repair and translesion synthesis
RT in yeast: contribution of transcription rate and mRNA stability to the
RT steady-state level of each mRNA along with growth in glucose-fermentative
RT medium.";
RL DNA Repair 4:469-478(2005).
RN [33]
RP FUNCTION.
RX PubMed=16181813; DOI=10.1016/j.dnarep.2005.08.012;
RA Xie Z., Zhang Y., Guliaev A.B., Shen H., Hang B., Singer B., Wang Z.;
RT "The p-benzoquinone DNA adducts derived from benzene are highly
RT mutagenic.";
RL DNA Repair 4:1399-1409(2005).
RN [34]
RP FUNCTION.
RX PubMed=15520252; DOI=10.1534/genetics.104.034611;
RA Gibbs P.E.M., McDonald J.P., Woodgate R., Lawrence C.W.;
RT "The relative roles in vivo of Saccharomyces cerevisiae Pol eta, Pol zeta,
RT Rev1 protein and Pol32 in the bypass and mutation induction of an abasic
RT site, T-T (6-4) photoadduct and T-T cis-syn cyclobutane dimer.";
RL Genetics 169:575-582(2005).
RN [35]
RP FUNCTION.
RX PubMed=16366567; DOI=10.1021/ja0549188;
RA Ober M., Mueller H., Pieck C., Gierlich J., Carell T.;
RT "Base pairing and replicative processing of the formamidopyrimidine-dG DNA
RT lesion.";
RL J. Am. Chem. Soc. 127:18143-18149(2005).
RN [36]
RP FUNCTION.
RX PubMed=15743815; DOI=10.1128/mcb.25.6.2169-2176.2005;
RA Carlson K.D., Washington M.T.;
RT "Mechanism of efficient and accurate nucleotide incorporation opposite 7,8-
RT dihydro-8-oxoguanine by Saccharomyces cerevisiae DNA polymerase eta.";
RL Mol. Cell. Biol. 25:2169-2176(2005).
RN [37]
RP FUNCTION.
RX PubMed=16866379; DOI=10.1021/bi0602009;
RA Vu B., Cannistraro V.J., Sun L., Taylor J.-S.;
RT "DNA synthesis past a 5-methylC-containing cis-syn-cyclobutane pyrimidine
RT dimer by yeast pol eta is highly nonmutagenic.";
RL Biochemistry 45:9327-9335(2006).
RN [38]
RP FUNCTION.
RX PubMed=16387871; DOI=10.1534/genetics.105.052480;
RA Abdulovic A.L., Jinks-Robertson S.;
RT "The in vivo characterization of translesion synthesis across UV-induced
RT lesions in Saccharomyces cerevisiae: insights into Pol zeta- and Pol eta-
RT dependent frameshift mutagenesis.";
RL Genetics 172:1487-1498(2006).
RN [39]
RP FUNCTION.
RX PubMed=16415180; DOI=10.1093/nar/gkj446;
RA Zhao B., Wang J., Geacintov N.E., Wang Z.;
RT "Poleta, Polzeta and Rev1 together are required for G to T transversion
RT mutations induced by the (+)- and (-)-trans-anti-BPDE-N2-dG DNA adducts in
RT yeast cells.";
RL Nucleic Acids Res. 34:417-425(2006).
RN [40]
RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 1-531.
RX PubMed=11545743; DOI=10.1016/s1097-2765(01)00306-9;
RA Trincao J., Johnson R.E., Escalante C.R., Prakash S., Prakash L.,
RA Aggarwal A.K.;
RT "Structure of the catalytic core of S. cerevisiae DNA polymerase eta:
RT implications for translesion DNA synthesis.";
RL Mol. Cell 8:417-426(2001).
CC -!- FUNCTION: DNA polymerase specifically involved in DNA repair. Plays an
CC important role in translesion synthesis, where the normal high fidelity
CC DNA polymerases cannot proceed and DNA synthesis stalls. Plays an
CC important role in the repair of UV-induced pyrimidine dimers. Depending
CC on the context, it inserts the correct base, but causes frequent base
CC transitions and transversions. Efficiently incorporates nucleotides
CC opposite to other UV or oxidative DNA damages like O(6)-methylguanine,
CC 7,8-dihydro-8-oxoguanine, 2,6-diamino-4-hydroxy-5-formamidopyrimidine
CC of 2'-deoxyguanosine (FaPydG), or p-benzoquinone DNA adducts.
CC {ECO:0000269|PubMed:10347143, ECO:0000269|PubMed:10601233,
CC ECO:0000269|PubMed:10713149, ECO:0000269|PubMed:10725365,
CC ECO:0000269|PubMed:10924462, ECO:0000269|PubMed:10932195,
CC ECO:0000269|PubMed:11027270, ECO:0000269|PubMed:11054429,
CC ECO:0000269|PubMed:11062246, ECO:0000269|PubMed:11113193,
CC ECO:0000269|PubMed:11238937, ECO:0000269|PubMed:11545742,
CC ECO:0000269|PubMed:11861920, ECO:0000269|PubMed:12110599,
CC ECO:0000269|PubMed:12665597, ECO:0000269|PubMed:12692307,
CC ECO:0000269|PubMed:12888515, ECO:0000269|PubMed:12899630,
CC ECO:0000269|PubMed:14527996, ECO:0000269|PubMed:15024063,
CC ECO:0000269|PubMed:15157108, ECO:0000269|PubMed:15284331,
CC ECO:0000269|PubMed:15333698, ECO:0000269|PubMed:15520252,
CC ECO:0000269|PubMed:15544332, ECO:0000269|PubMed:15743815,
CC ECO:0000269|PubMed:15779911, ECO:0000269|PubMed:16181813,
CC ECO:0000269|PubMed:16366567, ECO:0000269|PubMed:16387871,
CC ECO:0000269|PubMed:16415180, ECO:0000269|PubMed:16866379,
CC ECO:0000269|PubMed:9409821, ECO:0000269|PubMed:9974380}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) =
CC diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339,
CC Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560,
CC ChEBI:CHEBI:173112; EC=2.7.7.7;
CC -!- SUBUNIT: Interacts with POL30. This interaction is essential for the
CC polymerase eta function. {ECO:0000269|PubMed:11545742}.
CC -!- INTERACTION:
CC Q04049; P15873: POL30; NbExp=7; IntAct=EBI-36214, EBI-12993;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}.
CC -!- INDUCTION: By UV radiation and heat shock. The mRNA is stabilized
CC during stationary phase. {ECO:0000269|PubMed:15725627,
CC ECO:0000269|PubMed:9409821}.
CC -!- MISCELLANEOUS: Present with 1860 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-Y family. {ECO:0000305}.
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DR EMBL; U33007; AAB64856.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12259.1; -; Genomic_DNA.
DR PIR; S69702; S69702.
DR RefSeq; NP_010707.3; NM_001180727.3.
DR PDB; 1JIH; X-ray; 2.25 A; A/B=1-513.
DR PDB; 2R8J; X-ray; 3.10 A; A/B=1-531.
DR PDB; 2R8K; X-ray; 3.30 A; A/B=1-531.
DR PDB; 2WTF; X-ray; 2.50 A; A/B=1-513.
DR PDB; 2XGP; X-ray; 2.70 A; A/B=1-513.
DR PDB; 2XGQ; X-ray; 2.70 A; A/B=1-513.
DR PDB; 3MFH; X-ray; 2.00 A; A=1-513.
DR PDB; 3MFI; X-ray; 1.76 A; A=1-513.
DR PDB; 3OHA; X-ray; 2.00 A; A=1-513.
DR PDB; 3OHB; X-ray; 2.00 A; A=1-513.
DR PDB; 5VTP; X-ray; 2.80 A; A=1-528.
DR PDBsum; 1JIH; -.
DR PDBsum; 2R8J; -.
DR PDBsum; 2R8K; -.
DR PDBsum; 2WTF; -.
DR PDBsum; 2XGP; -.
DR PDBsum; 2XGQ; -.
DR PDBsum; 3MFH; -.
DR PDBsum; 3MFI; -.
DR PDBsum; 3OHA; -.
DR PDBsum; 3OHB; -.
DR PDBsum; 5VTP; -.
DR AlphaFoldDB; Q04049; -.
DR SMR; Q04049; -.
DR BioGRID; 32477; 150.
DR DIP; DIP-6500N; -.
DR IntAct; Q04049; 19.
DR MINT; Q04049; -.
DR STRING; 4932.YDR419W; -.
DR iPTMnet; Q04049; -.
DR MaxQB; Q04049; -.
DR PaxDb; Q04049; -.
DR PRIDE; Q04049; -.
DR EnsemblFungi; YDR419W_mRNA; YDR419W; YDR419W.
DR GeneID; 852028; -.
DR KEGG; sce:YDR419W; -.
DR SGD; S000002827; RAD30.
DR VEuPathDB; FungiDB:YDR419W; -.
DR eggNOG; KOG2095; Eukaryota.
DR GeneTree; ENSGT00940000157048; -.
DR HOGENOM; CLU_012348_7_3_1; -.
DR InParanoid; Q04049; -.
DR OMA; SACNKPN; -.
DR BioCyc; YEAST:G3O-29960-MON; -.
DR Reactome; R-SCE-110320; Translesion Synthesis by POLH.
DR EvolutionaryTrace; Q04049; -.
DR PRO; PR:Q04049; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q04049; protein.
DR GO; GO:0005739; C:mitochondrion; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0005657; C:replication fork; IPI:SGD.
DR GO; GO:0035861; C:site of double-strand break; IBA:GO_Central.
DR GO; GO:0003684; F:damaged DNA binding; IEA:InterPro.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IDA:SGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007059; P:chromosome segregation; IMP:SGD.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR GO; GO:0070987; P:error-free translesion synthesis; IDA:SGD.
DR GO; GO:0042276; P:error-prone translesion synthesis; IDA:SGD.
DR GO; GO:0007064; P:mitotic sister chromatid cohesion; IMP:SGD.
DR GO; GO:0009314; P:response to radiation; IBA:GO_Central.
DR DisProt; DP02736; -.
DR Gene3D; 3.30.1490.100; -; 1.
DR Gene3D; 3.30.70.270; -; 1.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR036775; DNA_pol_Y-fam_lit_finger_sf.
DR InterPro; IPR017961; DNA_pol_Y-fam_little_finger.
DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR InterPro; IPR041298; UBZ3.
DR InterPro; IPR001126; UmuC.
DR Pfam; PF00817; IMS; 1.
DR Pfam; PF11799; IMS_C; 1.
DR SUPFAM; SSF100879; SSF100879; 1.
DR SUPFAM; SSF56672; SSF56672; 1.
DR PROSITE; PS50173; UMUC; 1.
DR PROSITE; PS51907; ZF_UBZ3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA damage; DNA repair; DNA replication; DNA synthesis;
KW DNA-binding; DNA-directed DNA polymerase; Magnesium; Metal-binding;
KW Mutator protein; Nucleotidyltransferase; Nucleus; Reference proteome;
KW Transferase; Zinc; Zinc-finger.
FT CHAIN 1..632
FT /note="DNA polymerase eta"
FT /id="PRO_0000268698"
FT DOMAIN 26..309
FT /note="UmuC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00216"
FT ZN_FING 545..580
FT /note="UBZ3-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01255"
FT REGION 598..632
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 625..632
FT /note="POL30-binding"
FT COMPBIAS 604..626
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 30
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00216"
FT BINDING 155
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00216"
FT BINDING 552
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01255"
FT BINDING 553
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01255"
FT BINDING 568
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01255"
FT BINDING 572
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01255"
FT MUTAGEN 30
FT /note="D->A: Abolishes DNA polymerase activity."
FT /evidence="ECO:0000269|PubMed:11238937"
FT MUTAGEN 34
FT /note="F->L: Alters translesion activity."
FT /evidence="ECO:0000269|PubMed:15024063"
FT MUTAGEN 39
FT /note="E->A: Abolishes DNA polymerase activity."
FT /evidence="ECO:0000269|PubMed:11238937"
FT MUTAGEN 64
FT /note="Y->F,A: Decreases efficiency of nucleotide
FT incorporation."
FT /evidence="ECO:0000269|PubMed:12665597"
FT MUTAGEN 67
FT /note="R->A: Decreases efficiency of nucleotide
FT incorporation."
FT /evidence="ECO:0000269|PubMed:12665597"
FT MUTAGEN 155
FT /note="D->A: Abolishes DNA polymerase activity and
FT increases UV-induced mutations."
FT /evidence="ECO:0000269|PubMed:11238937"
FT MUTAGEN 156
FT /note="E->A: Decreases efficiency of nucleotide
FT incorporation."
FT /evidence="ECO:0000269|PubMed:11238937"
FT MUTAGEN 279
FT /note="K->A: Decreases efficiency of nucleotide
FT incorporation."
FT /evidence="ECO:0000269|PubMed:12665597"
FT MUTAGEN 627
FT /note="F->A: Abolishes POL30-binding; when associated with
FT A-628."
FT MUTAGEN 628
FT /note="F->A: Abolishes POL30-binding; when associated with
FT A-627."
FT STRAND 1..5
FT /evidence="ECO:0007829|PDB:3MFI"
FT HELIX 6..10
FT /evidence="ECO:0007829|PDB:3MFI"
FT HELIX 11..13
FT /evidence="ECO:0007829|PDB:3MFI"
FT TURN 15..17
FT /evidence="ECO:0007829|PDB:3MFI"
FT HELIX 18..20
FT /evidence="ECO:0007829|PDB:3MFI"
FT STRAND 21..23
FT /evidence="ECO:0007829|PDB:2R8K"
FT STRAND 26..31
FT /evidence="ECO:0007829|PDB:3MFI"
FT HELIX 34..42
FT /evidence="ECO:0007829|PDB:3MFI"
FT STRAND 51..55
FT /evidence="ECO:0007829|PDB:3MFI"
FT STRAND 58..62
FT /evidence="ECO:0007829|PDB:3MFI"
FT HELIX 64..67
FT /evidence="ECO:0007829|PDB:3MFI"
FT TURN 68..70
FT /evidence="ECO:0007829|PDB:3MFI"
FT HELIX 77..81
FT /evidence="ECO:0007829|PDB:3MFI"
FT STRAND 88..91
FT /evidence="ECO:0007829|PDB:3MFI"
FT STRAND 93..96
FT /evidence="ECO:0007829|PDB:3MFI"
FT STRAND 100..103
FT /evidence="ECO:0007829|PDB:3OHB"
FT HELIX 115..117
FT /evidence="ECO:0007829|PDB:3OHA"
FT STRAND 123..127
FT /evidence="ECO:0007829|PDB:3MFI"
FT HELIX 129..145
FT /evidence="ECO:0007829|PDB:3MFI"
FT STRAND 149..153
FT /evidence="ECO:0007829|PDB:3MFI"
FT STRAND 156..160
FT /evidence="ECO:0007829|PDB:3MFI"
FT HELIX 162..171
FT /evidence="ECO:0007829|PDB:3MFI"
FT STRAND 176..178
FT /evidence="ECO:0007829|PDB:3MFI"
FT HELIX 183..186
FT /evidence="ECO:0007829|PDB:3MFI"
FT HELIX 188..196
FT /evidence="ECO:0007829|PDB:3MFI"
FT STRAND 203..206
FT /evidence="ECO:0007829|PDB:3MFI"
FT HELIX 210..214
FT /evidence="ECO:0007829|PDB:3MFI"
FT STRAND 219..221
FT /evidence="ECO:0007829|PDB:3MFI"
FT HELIX 233..256
FT /evidence="ECO:0007829|PDB:3MFI"
FT STRAND 260..267
FT /evidence="ECO:0007829|PDB:3MFI"
FT HELIX 268..275
FT /evidence="ECO:0007829|PDB:3MFI"
FT TURN 276..278
FT /evidence="ECO:0007829|PDB:1JIH"
FT STRAND 280..285
FT /evidence="ECO:0007829|PDB:3MFI"
FT HELIX 288..290
FT /evidence="ECO:0007829|PDB:3MFI"
FT HELIX 291..295
FT /evidence="ECO:0007829|PDB:3MFI"
FT STRAND 297..299
FT /evidence="ECO:0007829|PDB:3MFI"
FT HELIX 302..304
FT /evidence="ECO:0007829|PDB:3MFI"
FT HELIX 306..308
FT /evidence="ECO:0007829|PDB:1JIH"
FT HELIX 311..319
FT /evidence="ECO:0007829|PDB:3MFI"
FT STRAND 324..326
FT /evidence="ECO:0007829|PDB:3MFI"
FT HELIX 327..334
FT /evidence="ECO:0007829|PDB:3MFI"
FT HELIX 339..351
FT /evidence="ECO:0007829|PDB:3MFI"
FT STRAND 352..355
FT /evidence="ECO:0007829|PDB:2WTF"
FT TURN 357..359
FT /evidence="ECO:0007829|PDB:3OHA"
FT HELIX 364..366
FT /evidence="ECO:0007829|PDB:3MFH"
FT HELIX 367..377
FT /evidence="ECO:0007829|PDB:3MFI"
FT TURN 378..380
FT /evidence="ECO:0007829|PDB:3MFI"
FT STRAND 395..400
FT /evidence="ECO:0007829|PDB:3MFI"
FT TURN 403..406
FT /evidence="ECO:0007829|PDB:3MFI"
FT HELIX 409..434
FT /evidence="ECO:0007829|PDB:3MFI"
FT STRAND 436..448
FT /evidence="ECO:0007829|PDB:3MFI"
FT STRAND 454..460
FT /evidence="ECO:0007829|PDB:3MFI"
FT HELIX 466..468
FT /evidence="ECO:0007829|PDB:3MFI"
FT HELIX 469..487
FT /evidence="ECO:0007829|PDB:3MFI"
FT TURN 488..490
FT /evidence="ECO:0007829|PDB:3MFI"
FT STRAND 497..510
FT /evidence="ECO:0007829|PDB:3MFI"
SQ SEQUENCE 632 AA; 71515 MW; CFB1A9FBC8AFE39B CRC64;
MSKFTWKELI QLGSPSKAYE SSLACIAHID MNAFFAQVEQ MRCGLSKEDP VVCVQWNSII
AVSYAARKYG ISRMDTIQEA LKKCSNLIPI HTAVFKKGED FWQYHDGCGS WVQDPAKQIS
VEDHKVSLEP YRRESRKALK IFKSACDLVE RASIDEVFLD LGRICFNMLM FDNEYELTGD
LKLKDALSNI REAFIGGNYD INSHLPLIPE KIKSLKFEGD VFNPEGRDLI TDWDDVILAL
GSQVCKGIRD SIKDILGYTT SCGLSSTKNV CKLASNYKKP DAQTIVKNDC LLDFLDCGKF
EITSFWTLGG VLGKELIDVL DLPHENSIKH IRETWPDNAG QLKEFLDAKV KQSDYDRSTS
NIDPLKTADL AEKLFKLSRG RYGLPLSSRP VVKSMMSNKN LRGKSCNSIV DCISWLEVFC
AELTSRIQDL EQEYNKIVIP RTVSISLKTK SYEVYRKSGP VAYKGINFQS HELLKVGIKF
VTDLDIKGKN KSYYPLTKLS MTITNFDIID LQKTVVDMFG NQVHTFKSSA GKEDEEKTTS
SKADEKTPKL ECCKYQVTFT DQKALQEHAD YHLALKLSEG LNGAEESSKN LSFGEKRLLF
SRKRPNSQHT ATPQKKQVTS SKNILSFFTR KK
