DPOD3_SCHPO
ID DPOD3_SCHPO Reviewed; 372 AA.
AC P30261;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=DNA polymerase delta subunit 3;
DE AltName: Full=Cell division control protein 27;
GN Name=cdc27; ORFNames=SPBC1734.02c, SPBC337.18c;
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 / MRNA].
RX PubMed=1538696; DOI=10.1007/bf00292709;
RA Hughes D.A., Macneill S.A., Fantes P.A.;
RT "Molecular cloning and sequence analysis of cdc27+ required for the G2-M
RT transition in the fission yeast Schizosaccharomyces pombe.";
RL Mol. Gen. Genet. 231:401-410(1992).
RN [2]
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 [3]
RP FUNCTION, AND SUBUNIT.
RX PubMed=10671561; DOI=10.1074/jbc.275.7.5153;
RA Zuo S., Bermudez V., Zhang G., Kelman Z., Hurwitz J.;
RT "Structure and activity associated with multiple forms of
RT Schizosaccharomyces pombe DNA polymerase delta.";
RL J. Biol. Chem. 275:5153-5162(2000).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-163, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
CC -!- SUBUNIT: Heterotetramer that consist of the pol3, cdc1, cdc27 and cdm1
CC subunits. Cdc27 interacts with cdc1 and is required for dimerization of
CC the tetramer. {ECO:0000269|PubMed:10671561}.
CC -!- INTERACTION:
CC P30261; P87324: cdc1; NbExp=3; IntAct=EBI-866919, EBI-865227;
CC P30261; Q03392: pcn1; NbExp=5; IntAct=EBI-866919, EBI-768724;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
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DR EMBL; M74062; AAA35295.1; -; Genomic_DNA.
DR EMBL; M83307; AAA35296.1; -; mRNA.
DR EMBL; CU329671; CAA21288.1; -; Genomic_DNA.
DR PIR; T39649; T39649.
DR RefSeq; NP_595419.1; NM_001021326.2.
DR AlphaFoldDB; P30261; -.
DR SMR; P30261; -.
DR BioGRID; 276184; 20.
DR ComplexPortal; CPX-2100; DNA polymerase delta complex.
DR ELM; P30261; -.
DR IntAct; P30261; 2.
DR STRING; 4896.SPBC1734.02c.1; -.
DR iPTMnet; P30261; -.
DR MaxQB; P30261; -.
DR PaxDb; P30261; -.
DR PRIDE; P30261; -.
DR EnsemblFungi; SPBC1734.02c.1; SPBC1734.02c.1:pep; SPBC1734.02c.
DR GeneID; 2539627; -.
DR KEGG; spo:SPBC1734.02c; -.
DR PomBase; SPBC1734.02c; cdc27.
DR VEuPathDB; FungiDB:SPBC1734.02c; -.
DR eggNOG; ENOG502QPSW; Eukaryota.
DR HOGENOM; CLU_809318_0_0_1; -.
DR InParanoid; P30261; -.
DR OMA; GFIHNEN; -.
DR Reactome; R-SPO-110314; Recognition of DNA damage by PCNA-containing replication complex.
DR Reactome; R-SPO-174437; Removal of the Flap Intermediate from the C-strand.
DR Reactome; R-SPO-5358565; Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha).
DR Reactome; R-SPO-5358606; Mismatch repair (MMR) directed by MSH2:MSH3 (MutSbeta).
DR Reactome; R-SPO-5651801; PCNA-Dependent Long Patch Base Excision Repair.
DR Reactome; R-SPO-5656169; Termination of translesion DNA synthesis.
DR Reactome; R-SPO-5696397; Gap-filling DNA repair synthesis and ligation in GG-NER.
DR Reactome; R-SPO-5696400; Dual Incision in GG-NER.
DR Reactome; R-SPO-6782135; Dual incision in TC-NER.
DR Reactome; R-SPO-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
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:P30261; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0043625; C:delta DNA polymerase complex; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0006271; P:DNA strand elongation involved in DNA replication; IDA:PomBase.
DR GO; GO:1904161; P:DNA synthesis involved in UV-damage excision repair; IDA:PomBase.
DR GO; GO:1903459; P:mitotic DNA replication lagging strand elongation; IC:PomBase.
DR GO; GO:1903460; P:mitotic DNA replication leading strand elongation; NAS:PomBase.
DR GO; GO:0090305; P:nucleic acid phosphodiester bond hydrolysis; IEA:GOC.
DR GO; GO:0006297; P:nucleotide-excision repair, DNA gap filling; IBA:GO_Central.
DR Gene3D; 3.90.1030.20; -; 1.
DR InterPro; IPR019038; POLD3.
DR InterPro; IPR041913; POLD3_sf.
DR PANTHER; PTHR17598; PTHR17598; 2.
DR Pfam; PF09507; CDC27; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; DNA replication; DNA-directed DNA polymerase;
KW Mitosis; Nucleotidyltransferase; Nucleus; Phosphoprotein;
KW Reference proteome; Transferase.
FT CHAIN 1..372
FT /note="DNA polymerase delta subunit 3"
FT /id="PRO_0000186049"
FT REGION 156..264
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 352..372
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 156..176
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 177..192
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 205..243
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 163
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MUTAGEN 57
FT /note="G->E: Cell cycle arrest at 35 degrees Celsius."
FT MUTAGEN 57
FT /note="G->R: Cell cycle arrest at 35 degrees Celsius."
SQ SEQUENCE 372 AA; 42350 MW; 6E6F9AD407B17673 CRC64;
MEEWRNFLDI KVINESSLVT VDNLSLQLDI SSEKAQEYLN MFYQGNDFLY PIYLIHGQPI
DDEINLEIDE ESQPISNFPV LQYILCDKSS LQEKQSRLKS GYKTVIFALS SAPLSDFDEL
LPAVYEIREK DVLYKKEDAD KYGFIFNENS VPRVLKKAPS THSPQLSVPS KTSTIDKTDT
RSTEKTKGKD IFSNARNQKG NSSRKNKKAP LENHKEKEPL LPKEEKLSEQ AKRERDDLKN
IMQLEDESVS TTSVHDSEDD NLDSNNFQLE IGTEAKSAAP DEPQEIIKSV SGGKRRGKRK
VKKYATTKDE EGFLVTKEEE VWESFSEDEN ISTGTSNVVR NKPTTVNIAT KKKNTAQSKP
QQKSIMSFFG KK
