DPOLA_SCHPO
ID DPOLA_SCHPO Reviewed; 1405 AA.
AC P28040; Q9UTY1;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=DNA polymerase alpha catalytic subunit;
DE EC=2.7.7.7;
DE AltName: Full=DNA polymerase I;
GN Name=pol1 {ECO:0000312|PomBase:SPAC3H5.06c};
GN Synonyms=polA {ECO:0000303|PubMed:11160827,
GN ECO:0000312|PomBase:SPAC3H5.06c}, swi7 {ECO:0000312|PomBase:SPAC3H5.06c};
GN ORFNames=SPAC3H5.06c {ECO:0000312|PomBase:SPAC3H5.06c};
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2034212; DOI=10.1007/bf00273602;
RA Damagnez V., Tillit J., de Recondo A.-M., Baldacci G.;
RT "The POL1 gene from the fission yeast, Schizosaccharomyces pombe, shows
RT conserved amino acid blocks specific for eukaryotic DNA polymerases
RT alpha.";
RL Mol. Gen. Genet. 226:182-189(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8423854; DOI=10.1038/361271a0;
RA Jagmohan S., Klar A.J.S.;
RT "DNA polymerase-alpha is essential for mating-type switching in fission
RT yeast.";
RL Nature 361:271-273(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 159-339, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=ATCC 38364 / 968;
RX PubMed=10759889; DOI=10.1046/j.1365-2443.2000.00317.x;
RA Ding D.-Q., Tomita Y., Yamamoto A., Chikashige Y., Haraguchi T.,
RA Hiraoka Y.;
RT "Large-scale screening of intracellular protein localization in living
RT fission yeast cells by the use of a GFP-fusion genomic DNA library.";
RL Genes Cells 5:169-190(2000).
RN [5]
RP INTERACTION WITH SPP1 AND SPP2.
RX PubMed=11027257; DOI=10.1128/mcb.20.21.7853-7866.2000;
RA Tan S., Wang T.S.;
RT "Analysis of fission yeast primase defines the checkpoint responses to
RT aberrant S phase initiation.";
RL Mol. Cell. Biol. 20:7853-7866(2000).
RN [6]
RP INTERACTION WITH SPP1 AND SPP2.
RX PubMed=11160827; DOI=10.1091/mbc.12.1.115;
RA Griffiths D.J., Liu V.F., Nurse P., Wang T.S.;
RT "Role of fission yeast primase catalytic subunit in the replication
RT checkpoint.";
RL Mol. Biol. Cell 12:115-128(2001).
RN [7]
RP INTERACTION WITH MCM10.
RX PubMed=14766746; DOI=10.1074/jbc.m400142200;
RA Fien K., Cho Y.-S., Lee J.-K., Raychaudhuri S., Tappin I., Hurwitz J.;
RT "Primer utilization by DNA polymerase alpha-primase is influenced by its
RT interaction with Mcm10p.";
RL J. Biol. Chem. 279:16144-16153(2004).
RN [8]
RP IDENTIFICATION IN THE DNA POLYMERASE ALPHA COMPLEX.
RX PubMed=15314153; DOI=10.1128/mcb.24.17.7419-7434.2004;
RA Uchiyama M., Wang T.S.;
RT "The B-subunit of DNA polymerase alpha-primase associates with the origin
RT recognition complex for initiation of DNA replication.";
RL Mol. Cell. Biol. 24:7419-7434(2004).
RN [9]
RP INTERACTION WITH MCL1.
RX PubMed=15915339; DOI=10.1007/s00294-005-0584-2;
RA Tsutsui Y., Morishita T., Natsume T., Yamashita K., Iwasaki H., Yamao F.,
RA Shinagawa H.;
RT "Genetic and physical interactions between Schizosaccharomyces pombe Mcl1
RT and Rad2, Dna2 and DNA polymerase alpha: evidence for a multifunctional
RT role of Mcl1 in DNA replication and repair.";
RL Curr. Genet. 48:34-43(2005).
RN [10]
RP FUNCTION, AND INTERACTION WITH MCL1.
RX PubMed=15643072; DOI=10.1128/ec.4.1.166-177.2005;
RA Williams D.R., McIntosh J.R.;
RT "Mcl1p is a polymerase alpha replication accessory factor important for S-
RT phase DNA damage survival.";
RL Eukaryot. Cell 4:166-177(2005).
RN [11]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
CC -!- FUNCTION: Catalytic subunit of the DNA polymerase alpha complex (also
CC known as the alpha DNA polymerase-primase complex) which plays an
CC essential role in the initiation of DNA synthesis (PubMed:15314153,
CC PubMed:15643072). During the S phase of the cell cycle, the DNA
CC polymerase alpha complex (composed of a catalytic subunit pol1, an
CC accessory subunit spb70/pol12 and two primase subunits, the catalytic
CC subunit spp1/pri1 and the regulatory subunit spp2/pri2) is recruited to
CC DNA at the replicative forks. The primase subunit of the polymerase
CC alpha complex initiates DNA synthesis by oligomerising short RNA
CC primers on both leading and lagging strands (By similarity).
CC {ECO:0000250|UniProtKB:P09884, ECO:0000269|PubMed:15314153,
CC ECO:0000269|PubMed:15643072}.
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:0000250|UniProtKB:P09884};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22509;
CC Evidence={ECO:0000250|UniProtKB:P09884};
CC -!- SUBUNIT: Component of the alpha DNA polymerase complex (also known as
CC the alpha DNA polymerase-primase complex) consisting of four subunits:
CC the catalytic subunit pol1, the accessoryy subunit spb70/pol12, and the
CC primase complex subunits spp1/pri1 and spp2/pri2 respectively
CC (PubMed:11027257, PubMed:15314153). Interacts with mcl1 and mcm10
CC (PubMed:14766746, PubMed:15643072, PubMed:15915339).
CC {ECO:0000269|PubMed:11027257, ECO:0000269|PubMed:14766746,
CC ECO:0000269|PubMed:15314153, ECO:0000269|PubMed:15643072,
CC ECO:0000269|PubMed:15915339}.
CC -!- INTERACTION:
CC P28040; Q9C107: mcl1; NbExp=10; IntAct=EBI-455823, EBI-1203666;
CC P28040; O13814: mdm10; NbExp=2; IntAct=EBI-455823, EBI-849180;
CC P28040; O74946: pol12; NbExp=2; IntAct=EBI-455823, EBI-849056;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10759889,
CC ECO:0000269|PubMed:16823372}.
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 -!- SIMILARITY: Belongs to the DNA polymerase type-B family. {ECO:0000305}.
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DR EMBL; X58299; CAA41232.1; -; Genomic_DNA.
DR EMBL; X69673; CAB57881.1; -; Genomic_DNA.
DR EMBL; CU329670; CAB16598.1; -; Genomic_DNA.
DR EMBL; AB027936; BAA87240.1; -; Genomic_DNA.
DR PIR; S15993; DJZPA.
DR RefSeq; NP_594186.1; NM_001019610.2.
DR AlphaFoldDB; P28040; -.
DR SMR; P28040; -.
DR BioGRID; 280043; 42.
DR ComplexPortal; CPX-2092; DNA polymerase alpha:primase complex.
DR IntAct; P28040; 4.
DR STRING; 4896.SPAC3H5.06c.1; -.
DR iPTMnet; P28040; -.
DR MaxQB; P28040; -.
DR PaxDb; P28040; -.
DR PRIDE; P28040; -.
DR EnsemblFungi; SPAC3H5.06c.1; SPAC3H5.06c.1:pep; SPAC3H5.06c.
DR GeneID; 2543629; -.
DR KEGG; spo:SPAC3H5.06c; -.
DR PomBase; SPAC3H5.06c; pol1.
DR VEuPathDB; FungiDB:SPAC3H5.06c; -.
DR eggNOG; KOG0970; Eukaryota.
DR HOGENOM; CLU_001718_1_0_1; -.
DR InParanoid; P28040; -.
DR OMA; WLKIEDA; -.
DR PhylomeDB; P28040; -.
DR Reactome; R-SPO-113501; Inhibition of replication initiation of damaged DNA by RB1/E2F1.
DR Reactome; R-SPO-68952; DNA replication initiation.
DR Reactome; R-SPO-68962; Activation of the pre-replicative complex.
DR Reactome; R-SPO-69091; Polymerase switching.
DR Reactome; R-SPO-69166; Removal of the Flap Intermediate.
DR Reactome; R-SPO-69183; Processive synthesis on the lagging strand.
DR PRO; PR:P28040; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005658; C:alpha DNA polymerase:primase complex; IGI:PomBase.
DR GO; GO:0000785; C:chromatin; IDA:PomBase.
DR GO; GO:0140445; C:chromosome, telomeric repeat region; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0035861; C:site of double-strand break; IDA:PomBase.
DR GO; GO:0003682; F:chromatin binding; IDA:PomBase.
DR GO; GO:0003688; F:DNA replication origin binding; IDA:PomBase.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IDA:PomBase.
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; IDA:PomBase.
DR GO; GO:0006281; P:DNA repair; IMP:PomBase.
DR GO; GO:0006270; P:DNA replication initiation; IDA:ComplexPortal.
DR GO; GO:0007534; P:gene conversion at mating-type locus; IMP:PomBase.
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; IMP:PomBase.
DR GO; GO:0006279; P:premeiotic DNA replication; IMP:PomBase.
DR GO; GO:0061806; P:regulation of DNA recombination at centromere; IMP:PomBase.
DR GO; GO:1902981; P:synthesis of RNA primer involved in mitotic DNA replication; IGI:PomBase.
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 DNA replication; DNA-binding; DNA-directed DNA polymerase; Metal-binding;
KW Nucleotidyltransferase; Nucleus; Reference proteome; Transferase; Zinc;
KW Zinc-finger.
FT CHAIN 1..1405
FT /note="DNA polymerase alpha catalytic subunit"
FT /id="PRO_0000046439"
FT ZN_FING 1256..1285
FT /note="CysA-type"
FT REGION 63..110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 118..634
FT /note="Interaction with mcl1"
FT REGION 141..241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1316..1340
FT /note="CysB motif"
FT COMPBIAS 85..105
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 171..191
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1256
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P13382"
FT BINDING 1259
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P13382"
FT BINDING 1283
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P13382"
FT BINDING 1285
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P13382"
FT BINDING 1316
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P13382"
FT BINDING 1321
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P13382"
FT BINDING 1335
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P13382"
FT BINDING 1340
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P13382"
SQ SEQUENCE 1405 AA; 159349 MW; 06082A3BAD6347C2 CRC64;
MRKRNAGIKP SQRFAELRAL RQAGKTRAST YESKENEELY DNVSEEEYRK IVRQRLDEDD
FVVDDNGAGY VDNGYDEWDQ SHYSDEDDEN EKGSSGRKRK KSKNVLAEPN QQIGAFFKAN
AIQPASRIAN RKNNEKEDEF MAEILGSIDQ DIPERLSTKK GNRSHTTSNA KRRSQKAASS
ISTTNVVSSD PKKYIPETVP STPQPASSLP IPSSPPAALE TEENVDSQPM ELDEPELPVG
SDAPIIDVEE SIAMKPLMSH DQVDDTASLS KATISQQPLS PMTPLSSELD VSAFSEINSK
IKNVDVPASS YSSPISKVSP SDVTEEDGSL FFFWMDYTEM YGSLCLFGKV YDKATKQYVS
CFLKVDGIMR SLYFLPRPSS SSVSEDSIAA QTKDVYDEVA NLLSKRGVKE WKSRVSKYKY
AFELEDVPRT ADYLEVIYSY SYPALPTDLT GSSFSHVFGT NTALFEQFVL SRRVMGPCWL
KIQQPNFDAV KNASWCRVEI GCSSPQNISV SFEKNEITSK TPPMTVMSLA FRTLINKEQN
KQEVVMISAR IFENVDIEKG LPANDMPSYS FSLIRPLKQI FPNGFEKLAR QHKSSIFCER
SEVSLLNNFL NKVRTYDPDV YFGHDFEMCY SVLLSRLKER KIHNWSSIGR LRRSEWPRSF
NRSSQQFVEK QIIAGRLMCD LSNDFGRSMI KAQSWSLSEI VLKELDIKRQ DINQEKALQS
WTDTAHGLLD YLVHCEIDTF FIAAVAFKIQ MLQLSKNLTN IAGNSWARTL TGTRAERNEY
ILLHEFKKNG YIVPDKQQSI RRHAEAFGAE DGLQEESLGK KKDKYKGGLV FEPQKGLYET
CILVMDFNSL YPSIIQEYNI CFTTVDRSPS NSDSDDQIPD TPSASANQGI FPRLIANLVE
RRRQIKGLLK DNSATPTQRL QWDIQQQALK LTANSMYGCL GYTKSRFYAR PLAVLITYKG
REALMNTKEL ADQMGLQVIY GDTDSVMLNT NVTDKNHALR IGNEFKEKVN ERYSKLEIDI
DNVYQRMLLH AKKKYAALQL DSQGKPNLDV KGLDMKRREF CTLAKEASKF CLDQILSGEL
TETVIENIHS YLMDFSEKMR NGKFPANKFI IFNRLGKNPE DYPNGKTMPF VQVALKKKAR
GENVRVGDVI PFIIAGSDAD GHPADRAYSP QEIMNTNSTL VIDYNYYLSH QILPPIERVI
APIEGTNRAR LAECLGLDAR KYYSHETSES SAFQRYESTL TDDQCFINVS PLLLKCPSCN
ATSFSLRSVK SLKETLYANT VECDCGYEYS DFTIILQFSS QLRDFINLYY EGILVCDDSS
CGNRTRQMSV YGKRCCNKSC RGSVHFEYND EQLYNQIKFL LKAVQTTTGA TRNGIIRCNA
INKNISRIMN KNAREFVDMG LIFSS
