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Database: UniProt
Entry: DPOZ_YEAST
LinkDB: DPOZ_YEAST
Original site: DPOZ_YEAST 
ID   DPOZ_YEAST              Reviewed;        1504 AA.
AC   P14284; D6W3K1;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1990, sequence version 1.
DT   05-JUN-2019, entry version 179.
DE   RecName: Full=DNA polymerase zeta catalytic subunit;
DE            EC=2.7.7.7;
DE   AltName: Full=Protein reversionless 3;
GN   Name=REV3; Synonyms=PSO1; OrderedLocusNames=YPL167C; ORFNames=P2535;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX   PubMed=2676986; DOI=10.1128/jb.171.10.5659-5667.1989;
RA   Morrison A., Christensen R.B., Alley J., Beck A.K., Bernstine E.G.,
RA   Lemontt J.F., Lawrence C.W.;
RT   "REV3, a Saccharomyces cerevisiae gene whose function is required for
RT   induced mutagenesis, is predicted to encode a nonessential DNA
RT   polymerase.";
RL   J. Bacteriol. 171:5659-5667(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204511 / S288c / AB972;
RX   PubMed=8948103;
RX   DOI=10.1002/(SICI)1097-0061(199611)12:14<1483::AID-YEA34>3.0.CO;2-O;
RA   Purnelle B., Coster F., Goffeau A.;
RT   "The sequence of 55 kb on the left arm of yeast chromosome XVI
RT   identifies a small nuclear RNA, a new putative protein kinase and two
RT   new putative regulators.";
RL   Yeast 12:1483-1492(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169875;
RA   Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA   Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V.,
RA   Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M.,
RA   Chung E., Churcher C.M., Coster F., Davis K., Davis R.W.,
RA   Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A.,
RA   Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A.,
RA   Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W.,
RA   Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K.,
RA   Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J.,
RA   Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D.,
RA   Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA   Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA   Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA   Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA   Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V.,
RA   Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W.,
RA   Zollner A., Vo D.H., Hani J.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL   Nature 387:103-105(1997).
RN   [4]
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.,
RA   Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and
RT   now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [5]
RP   FUNCTION, AND INTERACTION WITH REV7.
RX   PubMed=8658138; DOI=10.1126/science.272.5268.1646;
RA   Nelson J.R., Lawrence C.W., Hinkle D.C.;
RT   "Thymine-thymine dimer bypass by yeast DNA polymerase zeta.";
RL   Science 272:1646-1649(1996).
RN   [6]
RP   FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=11316789; DOI=10.1101/gad.882301;
RA   Haracska L., Unk I., Johnson R.E., Johansson E., Burgers P.M.J.,
RA   Prakash S., Prakash L.;
RT   "Roles of yeast DNA polymerases delta and zeta and of Rev1 in the
RT   bypass of abasic sites.";
RL   Genes Dev. 15:945-954(2001).
RN   [7]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=16452144; DOI=10.1534/genetics.105.051029;
RA   Zhang H., Chatterjee A., Singh K.K.;
RT   "Saccharomyces cerevisiae polymerase zeta functions in mitochondria.";
RL   Genetics 172:2683-2688(2006).
RN   [8]
RP   COFACTOR, AND IRON-SULFUR-BINDING.
RX   PubMed=22119860; DOI=10.1038/nchembio.721;
RA   Netz D.J., Stith C.M., Stumpfig M., Kopf G., Vogel D., Genau H.M.,
RA   Stodola J.L., Lill R., Burgers P.M., Pierik A.J.;
RT   "Eukaryotic DNA polymerases require an iron-sulfur cluster for the
RT   formation of active complexes.";
RL   Nat. Chem. Biol. 8:125-132(2012).
CC   -!- FUNCTION: Nonessential DNA polymerase. Required for DNA damage
CC       induced mutagenesis. Involved in DNA repair, mitochondrial DNA
CC       repair and translesion synthesis. Translesion synthesis in
CC       S.cerevisiae may use a specialized DNA polymerase that is not
CC       required for other DNA replicative processes. Has a role in the
CC       bypass of abasic (AP) sites. Highly inefficient in incorporating
CC       nucleotides opposite the AP site, but efficiently extends from
CC       nucleotides, particularly an A, inserted opposite the lesion.
CC       {ECO:0000269|PubMed:11316789, ECO:0000269|PubMed:16452144,
CC       ECO:0000269|PubMed:2676986, ECO:0000269|PubMed:8658138}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) =
CC         diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-
CC         COMP:11130, Rhea:RHEA-COMP:11131, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:61560, ChEBI:CHEBI:83828; EC=2.7.7.7;
CC         Evidence={ECO:0000269|PubMed:11316789};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000269|PubMed:22119860};
CC       Note=Binds 1 [4Fe-4S] cluster. {ECO:0000269|PubMed:22119860};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=543 uM for dGTP (insertion opposite abasic site)
CC         {ECO:0000269|PubMed:11316789};
CC         KM=81 uM for dATP (insertion opposite abasic site)
CC         {ECO:0000269|PubMed:11316789};
CC         KM=125 uM for dTTP (insertion opposite abasic site)
CC         {ECO:0000269|PubMed:11316789};
CC         KM=113 uM for dCTP (insertion opposite abasic site)
CC         {ECO:0000269|PubMed:11316789};
CC         KM=0.11 uM for dGTP (insertion opposite C)
CC         {ECO:0000269|PubMed:11316789};
CC         KM=267 uM for dATP (insertion opposite C)
CC         {ECO:0000269|PubMed:11316789};
CC         KM=552 uM for dTTP (insertion opposite C)
CC         {ECO:0000269|PubMed:11316789};
CC         KM=321 uM for dCTP (insertion opposite C)
CC         {ECO:0000269|PubMed:11316789};
CC         KM=344 uM for dGTP (insertion opposite G)
CC         {ECO:0000269|PubMed:11316789};
CC         KM=118 uM for dATP (insertion opposite G)
CC         {ECO:0000269|PubMed:11316789};
CC         KM=428 uM for dTTP (insertion opposite G)
CC         {ECO:0000269|PubMed:11316789};
CC         KM=0.14 uM for dCTP (insertion opposite G)
CC         {ECO:0000269|PubMed:11316789};
CC         KM=6.5 uM for dTTP (extension from G, A, T, or C opposite abasic
CC         site) {ECO:0000269|PubMed:11316789};
CC         KM=2.3 uM for dTTP (extension from G, A, T, or C opposite abasic
CC         site) {ECO:0000269|PubMed:11316789};
CC         KM=49 uM for dTTP (extension from G, A, T, or C opposite abasic
CC         site) {ECO:0000269|PubMed:11316789};
CC         KM=21 uM for dTTP (extension from G, A, T, or C opposite abasic
CC         site) {ECO:0000269|PubMed:11316789};
CC         KM=0.35 uM for dTTP (extension from G, A, T, or C opposite C)
CC         {ECO:0000269|PubMed:11316789};
CC         KM=2.3 uM for dTTP (extension from G, A, T, or C opposite C)
CC         {ECO:0000269|PubMed:11316789};
CC         KM=15 uM for dTTP (extension from G, A, T, or C opposite C)
CC         {ECO:0000269|PubMed:11316789};
CC         KM=26 uM for dTTP (extension from G, A, T, or C opposite C)
CC         {ECO:0000269|PubMed:11316789};
CC         KM=6.9 uM for dTTP (extension from G, A, T, or C opposite G)
CC         {ECO:0000269|PubMed:11316789};
CC         KM=2.1 uM for dTTP (extension from G, A, T, or C opposite G)
CC         {ECO:0000269|PubMed:11316789};
CC         KM=28.8 uM for dTTP (extension from G, A, T, or C opposite G)
CC         {ECO:0000269|PubMed:11316789};
CC         KM=0.23 uM for dTTP (extension from G, A, T, or C opposite G)
CC         {ECO:0000269|PubMed:11316789};
CC   -!- SUBUNIT: Forms DNA polymerase zeta with REV7.
CC   -!- INTERACTION:
CC       P38927:REV7; NbExp=3; IntAct=EBI-6155, EBI-14960;
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:16452144}.
CC       Nucleus {ECO:0000305}.
CC   -!- DOMAIN: The CysB motif binds 1 4Fe-4S cluster and is required for
CC       the formation of polymerase complexes. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the DNA polymerase type-B family.
CC       {ECO:0000305}.
DR   EMBL; M29683; AAA34968.1; -; Genomic_DNA.
DR   EMBL; X96770; CAA65554.1; -; Genomic_DNA.
DR   EMBL; Z73523; CAA97873.1; -; Genomic_DNA.
DR   EMBL; BK006949; DAA11267.1; -; Genomic_DNA.
DR   PIR; A33602; A33602.
DR   RefSeq; NP_015158.1; NM_001183981.1.
DR   BioGrid; 36016; 137.
DR   ComplexPortal; CPX-1091; DNA polymerase zeta complex.
DR   DIP; DIP-8024N; -.
DR   IntAct; P14284; 3.
DR   MINT; P14284; -.
DR   STRING; 4932.YPL167C; -.
DR   PaxDb; P14284; -.
DR   PRIDE; P14284; -.
DR   EnsemblFungi; YPL167C_mRNA; YPL167C_mRNA; YPL167C.
DR   GeneID; 855936; -.
DR   KEGG; sce:YPL167C; -.
DR   EuPathDB; FungiDB:YPL167C; -.
DR   SGD; S000006088; REV3.
DR   GeneTree; ENSGT00940000169521; -.
DR   HOGENOM; HOG000194392; -.
DR   InParanoid; P14284; -.
DR   KO; K02350; -.
DR   OMA; AHIHGAF; -.
DR   BioCyc; YEAST:G3O-34063-MONOMER; -.
DR   Reactome; R-SCE-110312; Translesion synthesis by REV1.
DR   Reactome; R-SCE-5655862; Translesion synthesis by POLK.
DR   Reactome; R-SCE-5656121; Translesion synthesis by POLI.
DR   PRO; PR:P14284; -.
DR   Proteomes; UP000002311; Chromosome XVI.
DR   GO; GO:0005739; C:mitochondrion; IDA:SGD.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0016035; C:zeta DNA polymerase complex; IDA:SGD.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
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:0000166; F:nucleotide binding; IEA:InterPro.
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:0090305; P:nucleic acid phosphodiester bond hydrolysis; IEA:GOC.
DR   Gene3D; 1.10.132.60; -; 1.
DR   Gene3D; 3.30.420.10; -; 1.
DR   Gene3D; 3.90.1600.10; -; 1.
DR   InterPro; IPR006172; DNA-dir_DNA_pol_B.
DR   InterPro; IPR017964; DNA-dir_DNA_pol_B_CS.
DR   InterPro; IPR006133; DNA-dir_DNA_pol_B_exonuc.
DR   InterPro; IPR006134; DNA-dir_DNA_pol_B_multi_dom.
DR   InterPro; IPR042087; DNA_pol_B_C.
DR   InterPro; IPR023211; DNA_pol_palm_dom_sf.
DR   InterPro; IPR030559; PolZ_Rev3.
DR   InterPro; IPR012337; RNaseH-like_sf.
DR   InterPro; IPR036397; RNaseH_sf.
DR   InterPro; IPR025687; Znf-C4pol.
DR   PANTHER; PTHR45812; PTHR45812; 2.
DR   Pfam; PF00136; DNA_pol_B; 1.
DR   Pfam; PF03104; DNA_pol_B_exo1; 2.
DR   Pfam; PF14260; zf-C4pol; 1.
DR   PRINTS; PR00106; DNAPOLB.
DR   SMART; SM00486; POLBc; 1.
DR   SUPFAM; SSF53098; SSF53098; 1.
DR   PROSITE; PS00116; DNA_POLYMERASE_B; 1.
PE   1: Evidence at protein level;
KW   4Fe-4S; Complete proteome; DNA damage; DNA repair; DNA replication;
KW   DNA-binding; DNA-directed DNA polymerase; Iron; Iron-sulfur;
KW   Metal-binding; Mitochondrion; Nucleotidyltransferase; Nucleus;
KW   Reference proteome; Transferase; Zinc; Zinc-finger.
FT   CHAIN         1   1504       DNA polymerase zeta catalytic subunit.
FT                                /FTId=PRO_0000046470.
FT   ZN_FING    1398   1417       CysA-type.
FT   MOTIF      1446   1473       CysB motif.
FT   METAL      1398   1398       Zinc. {ECO:0000250}.
FT   METAL      1401   1401       Zinc. {ECO:0000250}.
FT   METAL      1414   1414       Zinc. {ECO:0000250}.
FT   METAL      1417   1417       Zinc. {ECO:0000250}.
FT   METAL      1446   1446       Iron-sulfur (4Fe-4S). {ECO:0000250}.
FT   METAL      1449   1449       Iron-sulfur (4Fe-4S). {ECO:0000250}.
FT   METAL      1468   1468       Iron-sulfur (4Fe-4S). {ECO:0000250}.
FT   METAL      1473   1473       Iron-sulfur (4Fe-4S). {ECO:0000250}.
SQ   SEQUENCE   1504 AA;  172957 MW;  54C2C6B664F734F5 CRC64;
     MSRESNDTIQ SDTVRSSSKS DYFRIQLNNQ DYYMSKPTFL DPSHGESLPL NQFSQVPNIR
     VFGALPTGHQ VLCHVHGILP YMFIKYDGQI TDTSTLRHQR CAQVHKTLEV KIRASFKRKK
     DDKHDLAGDK LGNLNFVADV SVVKGIPFYG YHVGWNLFYK ISLLNPSCLS RISELIRDGK
     IFGKKFEIYE SHIPYLLQWT ADFNLFGCSW INVDRCYFRS PVLNSILDID KLTINDDLQL
     LLDRFCDFKC NVLSRRDFPR VGNGLIEIDI LPQFIKNREK LQHRDIHHDF LEKLGDISDI
     PVKPYVSSAR DMINELTMQR EELSLKEYKE PPETKRHVSG HQWQSSGEFE AFYKKAQHKT
     STFDGQIPNF ENFIDKNQKF SAINTPYEAL PQLWPRLPQI EINNNSMQDK KNDDQVNASF
     TEYEICGVDN ENEGVKGSNI KSRSYSWLPE SIASPKDSTI LLDHQTKYHN TINFSMDCAM
     TQNMASKRKL RSSVSANKTS LLSRKRKKVM AAGLRYGKRA FVYGEPPFGY QDILNKLEDE
     GFPKIDYKDP FFSNPVDLEN KPYAYAGKRF EISSTHVSTR IPVQFGGETV SVYNKPTFDM
     FSSWKYALKP PTYDAVQKWY NKVPSMGNKK TESQISMHTP HSKFLYKFAS DVSGKQKRKK
     SSVHDSLTHL TLEIHANTRS DKIPDPAIDE VSMIIWCLEE ETFPLDLDIA YEGIMIVHKA
     SEDSTFPTKI QHCINEIPVM FYESEFEMFE ALTDLVLLLD PDILSGFEIH NFSWGYIIER
     CQKIHQFDIV RELARVKCQI KTKLSDTWGY AHSSGIMITG RHMINIWRAL RSDVNLTQYT
     IESAAFNILH KRLPHFSFES LTNMWNAKKS TTELKTVLNY WLSRAQINIQ LLRKQDYIAR
     NIEQARLIGI DFHSVYYRGS QFKVESFLIR ICKSESFILL SPGKKDVRKQ KALECVPLVM
     EPESAFYKSP LIVLDFQSLY PSIMIGYNYC YSTMIGRVRE INLTENNLGV SKFSLPRNIL
     ALLKNDVTIA PNGVVYAKTS VRKSTLSKML TDILDVRVMI KKTMNEIGDD NTTLKRLLNN
     KQLALKLLAN VTYGYTSASF SGRMPCSDLA DSIVQTGRET LEKAIDIIEK DETWNAKVVY
     GDTDSLFVYL PGKTAIEAFS IGHAMAERVT QNNPKPIFLK FEKVYHPSIL ISKKRYVGFS
     YESPSQTLPI FDAKGIETVR RDGIPAQQKI IEKCIRLLFQ TKDLSKIKKY LQNEFFKIQI
     GKVSAQDFCF AKEVKLGAYK SEKTAPAGAV VVKRRINEDH RAEPQYKERI PYLVVKGKQG
     QLLRERCVSP EEFLEGENLE LDSEYYINKI LIPPLDRLFN LIGINVGNWA QEIVKSKRAS
     TTTTKVENIT RVGTSATCCN CGEELTKICS LQLCDDCLEK RSTTTLSFLI KKLKRQKEYQ
     TLKTVCRTCS YRYTSDAGIE NDHIASKCNS YDCPVFYSRV KAERYLRDNQ SVQREEALIS
     LNDW
//
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