DPOD3_YEAST
ID DPOD3_YEAST Reviewed; 350 AA.
AC P47110; D6VWL4;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=DNA polymerase delta subunit 3;
GN Name=POL32; OrderedLocusNames=YJR043C; ORFNames=J1626;
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 [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7668047; DOI=10.1002/yea.320110809;
RA Huang M.-E., Chuat J.-C., Galibert F.;
RT "Analysis of a 42.5 kb DNA sequence of chromosome X reveals three tRNA
RT genes and 14 new open reading frames including a gene most probably
RT belonging to the family of ubiquitin-protein ligases.";
RL Yeast 11:775-781(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL EMBO J. 15:2031-2049(1996).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [5]
RP CHARACTERIZATION.
RX PubMed=9677405; DOI=10.1074/jbc.273.31.19747;
RA Gerik K.J., Li X., Pautz A., Burgers P.M.;
RT "Characterization of the two small subunits of Saccharomyces cerevisiae DNA
RT polymerase delta.";
RL J. Biol. Chem. 273:19747-19755(1998).
RN [6]
RP COMPOSITION OF THE DNA POLYMERASE DELTA COMPLEX.
RX PubMed=11568188; DOI=10.1074/jbc.m108842200;
RA Johansson E., Majka J., Burgers P.M.;
RT "Structure of DNA polymerase delta from Saccharomyces cerevisiae.";
RL J. Biol. Chem. 276:43824-43828(2001).
RN [7]
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 [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-223 AND SER-230, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: DNA polymerase delta (DNA polymerase III) participates in
CC chromosomal DNA replication. It is required during synthesis of the
CC leading and lagging DNA strands at the replication fork and binds at/or
CC near replication origins and moves along DNA with the replication fork.
CC It has 3'-5' proofreading exonuclease activity that correct errors
CC arising during DNA replication. It is also involved in DNA synthesis
CC during DNA repair.
CC -!- SUBUNIT: DNA polymerase delta is a heterotrimer of POL3, POL32 and
CC HYS2. POL32 can form homodimers.
CC -!- INTERACTION:
CC P47110; P15873: POL30; NbExp=4; IntAct=EBI-6084, EBI-12993;
CC P47110; P12689: REV1; NbExp=4; IntAct=EBI-6084, EBI-14951;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- MISCELLANEOUS: Present with 2410 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; L36344; AAA88745.1; -; Genomic_DNA.
DR EMBL; Z49543; CAA89571.1; -; Genomic_DNA.
DR EMBL; AY557918; AAS56244.1; -; Genomic_DNA.
DR EMBL; BK006943; DAA08830.1; -; Genomic_DNA.
DR PIR; S57062; S57062.
DR RefSeq; NP_012577.1; NM_001181701.1.
DR PDB; 6P1H; EM; 3.20 A; C=1-350.
DR PDB; 6V8P; EM; 4.10 A; G=1-350.
DR PDB; 6V93; EM; 3.10 A; G=1-350.
DR PDB; 7KC0; EM; 3.20 A; C=8-350.
DR PDB; 7LXD; EM; 4.11 A; G=1-350.
DR PDB; 7S0T; EM; 3.05 A; G=1-350.
DR PDBsum; 6P1H; -.
DR PDBsum; 6V8P; -.
DR PDBsum; 6V93; -.
DR PDBsum; 7KC0; -.
DR PDBsum; 7LXD; -.
DR PDBsum; 7S0T; -.
DR AlphaFoldDB; P47110; -.
DR SMR; P47110; -.
DR BioGRID; 33794; 457.
DR ComplexPortal; CPX-2101; DNA polymerase delta complex.
DR DIP; DIP-2523N; -.
DR ELM; P47110; -.
DR IntAct; P47110; 12.
DR MINT; P47110; -.
DR STRING; 4932.YJR043C; -.
DR iPTMnet; P47110; -.
DR MaxQB; P47110; -.
DR PaxDb; P47110; -.
DR PRIDE; P47110; -.
DR EnsemblFungi; YJR043C_mRNA; YJR043C; YJR043C.
DR GeneID; 853500; -.
DR KEGG; sce:YJR043C; -.
DR SGD; S000003804; POL32.
DR VEuPathDB; FungiDB:YJR043C; -.
DR eggNOG; ENOG502QW2D; Eukaryota.
DR HOGENOM; CLU_794694_0_0_1; -.
DR InParanoid; P47110; -.
DR OMA; DCFIYAF; -.
DR BioCyc; YEAST:G3O-31678-MON; -.
DR PRO; PR:P47110; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P47110; protein.
DR GO; GO:0043625; C:delta DNA polymerase complex; IPI:ComplexPortal.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IDA:SGD.
DR GO; GO:0006284; P:base-excision repair; TAS:SGD.
DR GO; GO:0006277; P:DNA amplification; IMP:SGD.
DR GO; GO:0006259; P:DNA metabolic process; IDA:ComplexPortal.
DR GO; GO:0043137; P:DNA replication, removal of RNA primer; IDA:SGD.
DR GO; GO:0000727; P:double-strand break repair via break-induced replication; IMP:SGD.
DR GO; GO:0006273; P:lagging strand elongation; TAS:SGD.
DR GO; GO:0006272; P:leading strand elongation; TAS:SGD.
DR GO; GO:0090305; P:nucleic acid phosphodiester bond hydrolysis; IEA:GOC.
DR GO; GO:0006289; P:nucleotide-excision repair; TAS:SGD.
DR GO; GO:0006278; P:RNA-templated DNA biosynthetic process; IDA:SGD.
DR DisProt; DP02847; -.
PE 1: Evidence at protein level;
KW 3D-structure; DNA replication; DNA-directed DNA polymerase;
KW Nucleotidyltransferase; Nucleus; Phosphoprotein; Reference proteome;
KW Transferase.
FT CHAIN 1..350
FT /note="DNA polymerase delta subunit 3"
FT /id="PRO_0000186050"
FT REGION 131..350
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 169..217
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 236..252
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 271..290
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 319..338
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 223
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 230
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT HELIX 4..14
FT /evidence="ECO:0007829|PDB:6V93"
FT HELIX 22..29
FT /evidence="ECO:0007829|PDB:6V93"
FT HELIX 33..44
FT /evidence="ECO:0007829|PDB:6V93"
FT STRAND 52..60
FT /evidence="ECO:0007829|PDB:6V93"
FT TURN 61..63
FT /evidence="ECO:0007829|PDB:6V93"
FT STRAND 64..67
FT /evidence="ECO:0007829|PDB:6V93"
FT STRAND 69..72
FT /evidence="ECO:0007829|PDB:6V93"
FT STRAND 79..93
FT /evidence="ECO:0007829|PDB:6V93"
FT STRAND 108..110
FT /evidence="ECO:0007829|PDB:6V93"
SQ SEQUENCE 350 AA; 40310 MW; D0B9CC52F26E20B2 CRC64;
MDQKASYFIN EKLFTEVKPV LFTDLIHHLK IGPSMAKKLM FDYYKQTTNA KYNCVVICCY
KDQTIKIIHD LSNIPQQDSI IDCFIYAFNP MDSFIPYYDI IDQKDCLTIK NSYELKVSES
SKIIERTKTL EEKSKPLVRP TARSKTTPEE TTGRKSKSKD MGLRSTALLA KMKKDRDDKE
TSRQNELRKR KEENLQKINK QNPEREAQMK ELNNLFVEDD LDTEEVNGGS KPNSPKETDS
NDKDKNNDDL EDLLETTAED SLMDVPKIQQ TKPSETEHSK EPKSEEEPSS FIDEDGYIVT
KRPATSTPPR KPSPVVKRAL SSSKKQETPS SNKRLKKQGT LESFFKRKAK
