DPOLA_YEAST
ID DPOLA_YEAST Reviewed; 1468 AA.
AC P13382; D6W177;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 211.
DE RecName: Full=DNA polymerase alpha catalytic subunit A;
DE EC=2.7.7.7;
DE AltName: Full=DNA polymerase I subunit A;
DE AltName: Full=DNA polymerase alpha:primase complex p180 subunit;
DE Short=DNA polymerase-primase complex p180 subunit;
DE Short=Pol alpha-primase complex p180 subunit;
GN Name=POL1; Synonyms=CDC17; OrderedLocusNames=YNL102W; ORFNames=N2181;
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], AND VARIANT ARG-493.
RX PubMed=3287376; DOI=10.1073/pnas.85.11.3772;
RA Pizzagalli A., Valsasnini P., Plevani P., Lucchini G.;
RT "DNA polymerase I gene of Saccharomyces cerevisiae: nucleotide sequence,
RT mapping of a temperature-sensitive mutation, and protein homology with
RT other DNA polymerases.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:3772-3776(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=8701612;
RX DOI=10.1002/(sici)1097-0061(19960330)12:4<403::aid-yea923>3.0.co;2-h;
RA Saiz J.E., Buitrago M.J., Soler A., del Rey F., Revuelta J.L.;
RT "The sequence of a 21.3 kb DNA fragment from the left arm of yeast
RT chromosome XIV reveals LEU4, MET4, POL1, RAS2, and six new open reading
RT frames.";
RL Yeast 12:403-409(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(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., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-26.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8446029; DOI=10.1111/j.1365-2958.1993.tb01113.x;
RA Mountain H.A., Bystroem A.S., Korch C.;
RT "The general amino acid control regulates MET4, which encodes a methionine-
RT pathway-specific transcriptional activator of Saccharomyces cerevisiae.";
RL Mol. Microbiol. 7:215-228(1993).
RN [6]
RP COMPOSITION OF THE DNA POLYMERASE ALPHA:PRIMASE COMPLEX.
RX PubMed=3061469; DOI=10.1016/0167-4781(88)90096-6;
RA Plevani P., Foiani M., Muzi Falconi M., Pizzagalli A., Santocanale C.,
RA Francesconi S., Valsasnini P., Comedini A., Piatti S., Lucchini G.;
RT "The yeast DNA polymerase-primase complex: genes and proteins.";
RL Biochim. Biophys. Acta 951:268-273(1988).
RN [7]
RP PHOSPHORYLATION, AND IDENTIFICATION IN THE DNA POLYMERASE ALPHA:PRIMASE
RP COMPLEX.
RX PubMed=8621497; DOI=10.1074/jbc.271.15.8661;
RA Ferrari M., Lucchini G., Plevani P., Foiani M.;
RT "Phosphorylation of the DNA polymerase alpha-primase B subunit is dependent
RT on its association with the p180 polypeptide.";
RL J. Biol. Chem. 271:8661-8666(1996).
RN [8]
RP INTERACTION WITH POB3 AND SPT16.
RX PubMed=9199353; DOI=10.1128/mcb.17.7.4178;
RA Wittmeyer J., Formosa T.;
RT "The Saccharomyces cerevisiae DNA polymerase alpha catalytic subunit
RT interacts with Cdc68/Spt16 and with Pob3, a protein similar to an HMG1-like
RT protein.";
RL Mol. Cell. Biol. 17:4178-4190(1997).
RN [9]
RP FUNCTION, INTERACTION WITH CDC13, AND MUTAGENESIS OF ASP-236; GLU-238 AND
RP PRO-241.
RX PubMed=10898792;
RA Qi H., Zakian V.A.;
RT "The Saccharomyces telomere-binding protein Cdc13p interacts with both the
RT catalytic subunit of DNA polymerase alpha and the telomerase-associated
RT est1 protein.";
RL Genes Dev. 14:1777-1788(2000).
RN [10]
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 [11]
RP INTERACTION WITH MCM10.
RX PubMed=16675460; DOI=10.1074/jbc.m513551200;
RA Ricke R.M., Bielinsky A.-K.;
RT "A conserved Hsp10-like domain in Mcm10 is required to stabilize the
RT catalytic subunit of DNA polymerase-alpha in budding yeast.";
RL J. Biol. Chem. 281:18414-18425(2006).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-170 AND THR-313, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [13]
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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31; SER-240 AND SER-274, AND
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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31; SER-82; SER-83; SER-84;
RP SER-169; SER-170; THR-172; SER-240; SER-274; THR-309 AND THR-313, 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).
RN [16]
RP FUNCTION, AND CATALYTIC ACTIVITY.
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).
RN [17]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [18]
RP FUNCTION, AND MUTAGENESIS OF LEU-868.
RX PubMed=31488849; DOI=10.1038/s41467-019-11995-z;
RA Zhou Z.X., Lujan S.A., Burkholder A.B., Garbacz M.A., Kunkel T.A.;
RT "Roles for DNA polymerase delta in initiating and terminating leading
RT strand DNA replication.";
RL Nat. Commun. 10:3992-3992(2019).
RN [19] {ECO:0007744|PDB:3FLO}
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 1263-1468 IN COMPLEX WITH ZINC
RP AND POL12.
RX PubMed=19494830; DOI=10.1038/emboj.2009.150;
RA Klinge S., Nunez-Ramirez R., Llorca O., Pellegrini L.;
RT "3D architecture of DNA Pol alpha reveals the functional core of multi-
RT subunit replicative polymerases.";
RL EMBO J. 28:1978-1987(2009).
CC -!- FUNCTION: Catalytic component of DNA polymerase alpha, which in complex
CC with DNA primase (DNA polymerase alpha:primase) constitutes a
CC replicative polymerase (PubMed:10898792, PubMed:22119860,
CC PubMed:31488849). POL1 has a role in promoting telomere replication
CC during interaction with CDC13 (PubMed:10898792).
CC {ECO:0000269|PubMed:10898792, ECO:0000269|PubMed:22119860,
CC ECO:0000269|PubMed:31488849}.
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 Evidence={ECO:0000269|PubMed:22119860};
CC -!- SUBUNIT: DNA polymerase alpha:primase is a four subunit enzyme complex,
CC which is assembled throughout the cell cycle, and consists of the two
CC DNA polymerase subunits A POL1 and B POL12, and the DNA primase large
CC PRI2 and small PRI1 subunits (PubMed:3061469). Subunit B POL12 binds to
CC subunit A POL1 (PubMed:19494830). POL1 interacts with CDC13, POB3,
CC SPT16 and MCM10 (PubMed:10898792, PubMed:16675460, PubMed:8621497,
CC PubMed:9199353). {ECO:0000269|PubMed:10898792,
CC ECO:0000269|PubMed:16675460, ECO:0000269|PubMed:19494830,
CC ECO:0000269|PubMed:3061469, ECO:0000269|PubMed:8621497,
CC ECO:0000269|PubMed:9199353}.
CC -!- INTERACTION:
CC P13382; P32797: CDC13; NbExp=4; IntAct=EBI-6128, EBI-4187;
CC P13382; Q01454: CTF4; NbExp=14; IntAct=EBI-6128, EBI-5209;
CC P13382; P38121: POL12; NbExp=4; IntAct=EBI-6128, EBI-6111;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- DOMAIN: The CysA-type zinc finger is required for PCNA-binding.
CC {ECO:0000250|UniProtKB:P15436}.
CC -!- MISCELLANEOUS: In eukaryotes there are five DNA polymerases: alpha,
CC beta, gamma, delta, and epsilon which are responsible for different
CC reactions of DNA synthesis.
CC -!- MISCELLANEOUS: Present with 1050 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-B family. {ECO:0000305}.
CC -!- CAUTION: A structure shows that CysB motif binds zinc but a later study
CC has suggested it might bind 1 4Fe-4S cluster instead.
CC {ECO:0000305|PubMed:19494830, ECO:0000305|PubMed:22119860}.
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DR EMBL; J03268; AAA34888.1; -; Genomic_DNA.
DR EMBL; Z50161; CAA90524.1; -; Genomic_DNA.
DR EMBL; Z71378; CAA95978.1; -; Genomic_DNA.
DR EMBL; Z12126; CAA78111.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10443.1; -; Genomic_DNA.
DR PIR; S58250; S58250.
DR RefSeq; NP_014297.3; NM_001182940.3.
DR PDB; 3FLO; X-ray; 2.50 A; B/D/F/H=1263-1468.
DR PDB; 3OIQ; X-ray; 2.40 A; B=215-250.
DR PDB; 4B08; X-ray; 2.67 A; A=349-1258.
DR PDB; 4C93; X-ray; 2.69 A; D/E=137-149.
DR PDB; 4FVM; X-ray; 2.30 A; A=349-1258.
DR PDB; 4FXD; X-ray; 3.00 A; A/B=349-1258.
DR PDB; 4FYD; X-ray; 3.10 A; A/B=349-1258.
DR PDBsum; 3FLO; -.
DR PDBsum; 3OIQ; -.
DR PDBsum; 4B08; -.
DR PDBsum; 4C93; -.
DR PDBsum; 4FVM; -.
DR PDBsum; 4FXD; -.
DR PDBsum; 4FYD; -.
DR AlphaFoldDB; P13382; -.
DR SMR; P13382; -.
DR BioGRID; 35721; 711.
DR ComplexPortal; CPX-2091; DNA polymerase alpha:primase complex.
DR DIP; DIP-2526N; -.
DR IntAct; P13382; 16.
DR MINT; P13382; -.
DR STRING; 4932.YNL102W; -.
DR iPTMnet; P13382; -.
DR MaxQB; P13382; -.
DR PaxDb; P13382; -.
DR PRIDE; P13382; -.
DR EnsemblFungi; YNL102W_mRNA; YNL102W; YNL102W.
DR GeneID; 855621; -.
DR KEGG; sce:YNL102W; -.
DR SGD; S000005046; POL1.
DR VEuPathDB; FungiDB:YNL102W; -.
DR eggNOG; KOG0970; Eukaryota.
DR GeneTree; ENSGT00550000074891; -.
DR HOGENOM; CLU_001718_1_0_1; -.
DR InParanoid; P13382; -.
DR OMA; WLKIEDA; -.
DR BioCyc; YEAST:G3O-33130-MON; -.
DR BRENDA; 2.7.7.7; 984.
DR Reactome; R-SCE-113501; Inhibition of replication initiation of damaged DNA by RB1/E2F1.
DR Reactome; R-SCE-68952; DNA replication initiation.
DR Reactome; R-SCE-68962; Activation of the pre-replicative complex.
DR Reactome; R-SCE-69091; Polymerase switching.
DR Reactome; R-SCE-69166; Removal of the Flap Intermediate.
DR Reactome; R-SCE-69183; Processive synthesis on the lagging strand.
DR EvolutionaryTrace; P13382; -.
DR PRO; PR:P13382; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P13382; protein.
DR GO; GO:0005658; C:alpha DNA polymerase:primase complex; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0005657; C:replication fork; IDA:SGD.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0003688; F:DNA replication origin binding; IBA:GO_Central.
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:0017076; F:purine nucleotide binding; IBA:GO_Central.
DR GO; GO:0019103; F:pyrimidine nucleotide binding; IBA:GO_Central.
DR GO; GO:0003697; F:single-stranded DNA binding; IBA:GO_Central.
DR GO; GO:0006260; P:DNA replication; IMP:SGD.
DR GO; GO:0006270; P:DNA replication initiation; IC:SGD.
DR GO; GO:0000731; P:DNA synthesis involved in DNA repair; IMP:SGD.
DR GO; GO:0006302; P:double-strand break repair; IMP:SGD.
DR GO; GO:0006273; P:lagging strand elongation; IBA:GO_Central.
DR GO; GO:0006272; P:leading strand elongation; IBA:GO_Central.
DR GO; GO:1902975; P:mitotic DNA replication initiation; IBA:GO_Central.
DR GO; GO:0006279; P:premeiotic DNA replication; IMP:SGD.
DR GO; GO:0006278; P:RNA-templated DNA biosynthetic process; IDA:SGD.
DR CDD; cd05532; POLBc_alpha; 1.
DR Gene3D; 1.10.132.60; -; 1.
DR Gene3D; 1.10.3200.20; -; 1.
DR Gene3D; 3.30.420.10; -; 1.
DR Gene3D; 3.90.1600.10; -; 2.
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; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR024647; DNA_pol_a_cat_su_N.
DR InterPro; IPR042087; DNA_pol_B_thumb.
DR InterPro; IPR023211; DNA_pol_palm_dom_sf.
DR InterPro; IPR038256; Pol_alpha_znc_sf.
DR InterPro; IPR045846; POLBc_alpha.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR InterPro; IPR015088; Znf_DNA-dir_DNA_pol_B_alpha.
DR Pfam; PF12254; DNA_pol_alpha_N; 1.
DR Pfam; PF00136; DNA_pol_B; 1.
DR Pfam; PF03104; DNA_pol_B_exo1; 1.
DR Pfam; PF08996; zf-DNA_Pol; 1.
DR PRINTS; PR00106; DNAPOLB.
DR SMART; SM00486; POLBc; 1.
DR SUPFAM; SSF53098; SSF53098; 1.
DR SUPFAM; SSF56672; SSF56672; 1.
DR PROSITE; PS00116; DNA_POLYMERASE_B; 1.
PE 1: Evidence at protein level;
KW 3D-structure; 4Fe-4S; Acetylation; DNA replication; DNA-binding;
KW DNA-directed DNA polymerase; Iron; Iron-sulfur; Metal-binding;
KW Nucleotidyltransferase; Nucleus; Phosphoprotein; Reference proteome;
KW Transferase; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..1468
FT /note="DNA polymerase alpha catalytic subunit A"
FT /id="PRO_0000046440"
FT ZN_FING 1287..1317
FT /note="CysA-type"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 71..135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 166..205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 256..275
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 813..837
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1246..1381
FT /note="DNA-binding"
FT /evidence="ECO:0000255"
FT MOTIF 1348..1372
FT /note="CysB motif"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT COMPBIAS 71..114
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 180..205
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 817..836
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1287
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:19494830,
FT ECO:0007744|PDB:3FLO"
FT BINDING 1290
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:19494830,
FT ECO:0007744|PDB:3FLO"
FT BINDING 1314
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:19494830,
FT ECO:0007744|PDB:3FLO"
FT BINDING 1317
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:19494830,
FT ECO:0007744|PDB:3FLO"
FT BINDING 1348
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:19494830,
FT ECO:0007744|PDB:3FLO"
FT BINDING 1353
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:19494830,
FT ECO:0007744|PDB:3FLO"
FT BINDING 1367
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:19494830,
FT ECO:0007744|PDB:3FLO"
FT BINDING 1372
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:19494830,
FT ECO:0007744|PDB:3FLO"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 31
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 82
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 83
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 84
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 169
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 170
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 172
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 240
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 274
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 309
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 313
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT VARIANT 493
FT /note="G -> R (in temperature sensitive mutant)"
FT /evidence="ECO:0000269|PubMed:3287376"
FT MUTAGEN 236
FT /note="D->N: Increase in length of X' and Y' telomeres. No
FT effect on telomere position effect. Reduced interaction
FT with CDC13."
FT /evidence="ECO:0000269|PubMed:10898792"
FT MUTAGEN 238
FT /note="E->K: Increase in length of X' and Y' telomeres.
FT Reduced interaction with CDC13."
FT /evidence="ECO:0000269|PubMed:10898792"
FT MUTAGEN 241
FT /note="P->T: Increase in length of X' and Y' telomeres.
FT Reduced interaction with CDC13."
FT /evidence="ECO:0000269|PubMed:10898792"
FT MUTAGEN 868
FT /note="L->M: Increases rates of C-to-A transversion
FT substitutions."
FT /evidence="ECO:0000269|PubMed:31488849"
FT CONFLICT 759..760
FT /note="MI -> IV (in Ref. 1; AAA34888)"
FT /evidence="ECO:0000305"
FT HELIX 141..148
FT /evidence="ECO:0007829|PDB:4C93"
FT HELIX 217..239
FT /evidence="ECO:0007829|PDB:3OIQ"
FT STRAND 351..362
FT /evidence="ECO:0007829|PDB:4FVM"
FT STRAND 365..373
FT /evidence="ECO:0007829|PDB:4FVM"
FT STRAND 379..386
FT /evidence="ECO:0007829|PDB:4FVM"
FT STRAND 390..397
FT /evidence="ECO:0007829|PDB:4FVM"
FT HELIX 403..418
FT /evidence="ECO:0007829|PDB:4FVM"
FT STRAND 425..431
FT /evidence="ECO:0007829|PDB:4FVM"
FT STRAND 441..453
FT /evidence="ECO:0007829|PDB:4FVM"
FT STRAND 469..476
FT /evidence="ECO:0007829|PDB:4FVM"
FT HELIX 481..488
FT /evidence="ECO:0007829|PDB:4FVM"
FT STRAND 496..499
FT /evidence="ECO:0007829|PDB:4FVM"
FT STRAND 503..506
FT /evidence="ECO:0007829|PDB:4FVM"
FT STRAND 511..520
FT /evidence="ECO:0007829|PDB:4FVM"
FT HELIX 522..524
FT /evidence="ECO:0007829|PDB:4FVM"
FT STRAND 525..527
FT /evidence="ECO:0007829|PDB:4FVM"
FT STRAND 536..548
FT /evidence="ECO:0007829|PDB:4FVM"
FT TURN 549..552
FT /evidence="ECO:0007829|PDB:4FVM"
FT STRAND 553..567
FT /evidence="ECO:0007829|PDB:4FVM"
FT STRAND 569..571
FT /evidence="ECO:0007829|PDB:4B08"
FT STRAND 580..586
FT /evidence="ECO:0007829|PDB:4FVM"
FT STRAND 589..593
FT /evidence="ECO:0007829|PDB:4FVM"
FT HELIX 598..605
FT /evidence="ECO:0007829|PDB:4FVM"
FT STRAND 606..612
FT /evidence="ECO:0007829|PDB:4FVM"
FT HELIX 616..630
FT /evidence="ECO:0007829|PDB:4FVM"
FT STRAND 633..639
FT /evidence="ECO:0007829|PDB:4FVM"
FT TURN 640..643
FT /evidence="ECO:0007829|PDB:4FVM"
FT HELIX 644..654
FT /evidence="ECO:0007829|PDB:4FVM"
FT HELIX 660..663
FT /evidence="ECO:0007829|PDB:4FVM"
FT STRAND 664..666
FT /evidence="ECO:0007829|PDB:4FVM"
FT TURN 673..676
FT /evidence="ECO:0007829|PDB:4FXD"
FT HELIX 682..691
FT /evidence="ECO:0007829|PDB:4FVM"
FT STRAND 694..698
FT /evidence="ECO:0007829|PDB:4FVM"
FT HELIX 702..706
FT /evidence="ECO:0007829|PDB:4FVM"
FT HELIX 716..724
FT /evidence="ECO:0007829|PDB:4FVM"
FT HELIX 739..742
FT /evidence="ECO:0007829|PDB:4FVM"
FT HELIX 744..767
FT /evidence="ECO:0007829|PDB:4FVM"
FT HELIX 770..781
FT /evidence="ECO:0007829|PDB:4FVM"
FT HELIX 785..790
FT /evidence="ECO:0007829|PDB:4FVM"
FT HELIX 794..807
FT /evidence="ECO:0007829|PDB:4FVM"
FT STRAND 854..856
FT /evidence="ECO:0007829|PDB:4FVM"
FT STRAND 860..864
FT /evidence="ECO:0007829|PDB:4FVM"
FT HELIX 868..875
FT /evidence="ECO:0007829|PDB:4FVM"
FT TURN 880..882
FT /evidence="ECO:0007829|PDB:4FVM"
FT HELIX 905..926
FT /evidence="ECO:0007829|PDB:4FVM"
FT HELIX 930..947
FT /evidence="ECO:0007829|PDB:4FVM"
FT HELIX 948..950
FT /evidence="ECO:0007829|PDB:4FVM"
FT HELIX 951..955
FT /evidence="ECO:0007829|PDB:4FVM"
FT HELIX 964..987
FT /evidence="ECO:0007829|PDB:4FVM"
FT STRAND 991..995
FT /evidence="ECO:0007829|PDB:4FVM"
FT STRAND 997..1003
FT /evidence="ECO:0007829|PDB:4FVM"
FT HELIX 1009..1026
FT /evidence="ECO:0007829|PDB:4FVM"
FT STRAND 1033..1045
FT /evidence="ECO:0007829|PDB:4FVM"
FT STRAND 1048..1054
FT /evidence="ECO:0007829|PDB:4FVM"
FT STRAND 1064..1071
FT /evidence="ECO:0007829|PDB:4FVM"
FT HELIX 1072..1074
FT /evidence="ECO:0007829|PDB:4FXD"
FT HELIX 1080..1093
FT /evidence="ECO:0007829|PDB:4FVM"
FT STRAND 1094..1097
FT /evidence="ECO:0007829|PDB:4FVM"
FT HELIX 1101..1118
FT /evidence="ECO:0007829|PDB:4FVM"
FT HELIX 1124..1127
FT /evidence="ECO:0007829|PDB:4FVM"
FT STRAND 1129..1132
FT /evidence="ECO:0007829|PDB:4FVM"
FT HELIX 1137..1139
FT /evidence="ECO:0007829|PDB:4FVM"
FT HELIX 1143..1145
FT /evidence="ECO:0007829|PDB:4FVM"
FT HELIX 1147..1158
FT /evidence="ECO:0007829|PDB:4FVM"
FT STRAND 1167..1173
FT /evidence="ECO:0007829|PDB:4FVM"
FT TURN 1189..1192
FT /evidence="ECO:0007829|PDB:4FVM"
FT STRAND 1193..1195
FT /evidence="ECO:0007829|PDB:4FVM"
FT HELIX 1196..1200
FT /evidence="ECO:0007829|PDB:4FVM"
FT HELIX 1202..1204
FT /evidence="ECO:0007829|PDB:4FVM"
FT HELIX 1210..1215
FT /evidence="ECO:0007829|PDB:4FVM"
FT TURN 1216..1218
FT /evidence="ECO:0007829|PDB:4FVM"
FT HELIX 1219..1225
FT /evidence="ECO:0007829|PDB:4FVM"
FT TURN 1226..1228
FT /evidence="ECO:0007829|PDB:4FXD"
FT HELIX 1234..1239
FT /evidence="ECO:0007829|PDB:4FXD"
FT TURN 1274..1279
FT /evidence="ECO:0007829|PDB:3FLO"
FT STRAND 1283..1286
FT /evidence="ECO:0007829|PDB:3FLO"
FT TURN 1288..1290
FT /evidence="ECO:0007829|PDB:3FLO"
FT STRAND 1293..1296
FT /evidence="ECO:0007829|PDB:3FLO"
FT STRAND 1298..1300
FT /evidence="ECO:0007829|PDB:3FLO"
FT STRAND 1303..1308
FT /evidence="ECO:0007829|PDB:3FLO"
FT STRAND 1311..1314
FT /evidence="ECO:0007829|PDB:3FLO"
FT TURN 1315..1317
FT /evidence="ECO:0007829|PDB:3FLO"
FT HELIX 1323..1343
FT /evidence="ECO:0007829|PDB:3FLO"
FT STRAND 1346..1349
FT /evidence="ECO:0007829|PDB:3FLO"
FT TURN 1351..1353
FT /evidence="ECO:0007829|PDB:3FLO"
FT STRAND 1356..1358
FT /evidence="ECO:0007829|PDB:3FLO"
FT STRAND 1375..1380
FT /evidence="ECO:0007829|PDB:3FLO"
FT HELIX 1382..1395
FT /evidence="ECO:0007829|PDB:3FLO"
FT HELIX 1398..1402
FT /evidence="ECO:0007829|PDB:3FLO"
FT HELIX 1424..1433
FT /evidence="ECO:0007829|PDB:3FLO"
FT HELIX 1435..1449
FT /evidence="ECO:0007829|PDB:3FLO"
SQ SEQUENCE 1468 AA; 166809 MW; 50C9032DBE95B5AE CRC64;
MSSKSEKLEK LRKLQAARNG TSIDDYEGDE SDGDRIYDEI DEKEYRARKR QELLHDDFVV
DDDGVGYVDR GVEEDWREVD NSSSDEDTGN LASKDSKRKK NIKREKDHQI TDMLRTQHSK
STLLAHAKKS QKKSIPIDNF DDILGEFESG EVEKPNILLP SKLRENLNSS PTSEFKSSIK
RVNGNDESSH DAGISKKVKI DPDSSTDKYL EIESSPLKLQ SRKLRYANDV QDLLDDVENS
PVVATKRQNV LQDTLLANPP SAQSLADEED DEDSDEDIIL KRRTMRSVTT TRRVNIDSRS
NPSTSPFVTA PGTPIGIKGL TPSKSLQSNT DVATLAVNVK KEDVVDPETD TFQMFWLDYC
EVNNTLILFG KVKLKDDNCV SAMVQINGLC RELFFLPREG KTPTDIHEEI IPLLMDKYGL
DNIRAKPQKM KYSFELPDIP SESDYLKVLL PYQTPKSSRD TIPSDLSSDT FYHVFGGNSN
IFESFVIQNR IMGPCWLDIK GADFNSIRNA SHCAVEVSVD KPQNITPTTT KTMPNLRCLS
LSIQTLMNPK ENKQEIVSIT LSAYRNISLD SPIPENIKPD DLCTLVRPPQ STSFPLGLAA
LAKQKLPGRV RLFNNEKAML SCFCAMLKVE DPDVIIGHRL QNVYLDVLAH RMHDLNIPTF
SSIGRRLRRT WPEKFGRGNS NMNHFFISDI CSGRLICDIA NEMGQSLTPK CQSWDLSEMY
QVTCEKEHKP LDIDYQNPQY QNDVNSMTMA LQENITNCMI SAEVSYRIQL LTLTKQLTNL
AGNAWAQTLG GTRAGRNEYI LLHEFSRNGF IVPDKEGNRS RAQKQRQNEE NADAPVNSKK
AKYQGGLVFE PEKGLHKNYV LVMDFNSLYP SIIQEFNICF TTVDRNKEDI DELPSVPPSE
VDQGVLPRLL ANLVDRRREV KKVMKTETDP HKRVQCDIRQ QALKLTANSM YGCLGYVNSR
FYAKPLAMLV TNKGREILMN TRQLAESMNL LVVYGDTDSV MIDTGCDNYA DAIKIGLGFK
RLVNERYRLL EIDIDNVFKK LLLHAKKKYA ALTVNLDKNG NGTTVLEVKG LDMKRREFCP
LSRDVSIHVL NTILSDKDPE EALQEVYDYL EDIRIKVETN NIRIDKYKIN MKLSKDPKAY
PGGKNMPAVQ VALRMRKAGR VVKAGSVITF VITKQDEIDN AADTPALSVA ERAHALNEVM
IKSNNLIPDP QYYLEKQIFA PVERLLERID SFNVVRLSEA LGLDSKKYFR REGGNNNGED
INNLQPLETT ITDVERFKDT VTLELSCPSC DKRFPFGGIV SSNYYRVSYN GLQCKHCEQL
FTPLQLTSQI EHSIRAHISL YYAGWLQCDD STCGIVTRQV SVFGKRCLND GCTGVMRYKY
SDKQLYNQLL YFDSLFDCEK NKKQELKPIY LPDDLDYPKE QLTESSIKAL TEQNRELMET
GRSVVQKYLN DCGRRYVDMT SIFDFMLN
