DPOD2_SCHPO
ID DPOD2_SCHPO Reviewed; 462 AA.
AC P87324;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 25-MAY-2022, entry version 153.
DE RecName: Full=DNA polymerase subunit delta-2;
DE EC=2.7.7.7;
GN Name=cdc1; ORFNames=SPAC27E2.05;
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].
RC STRAIN=972 / ATCC 24843;
RX PubMed=8887553; DOI=10.1002/j.1460-2075.1996.tb00839.x;
RA MacNeill S.A., Moreno S., Reynolds N., Nurse P., Fantes P.A.;
RT "The fission yeast Cdc1 protein, a homologue of the small subunit of DNA
RT polymerase delta, binds to Pol3 and Cdc27.";
RL EMBO J. 15:4613-4628(1996).
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).
CC -!- FUNCTION: Required for replication of the leading DNA strand and for
CC completion of lagging strand synthesis. It is essential for cell cycle
CC progression.
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 -!- SUBUNIT: Heterodimer with subunits of 125 kDa and 50 kDa. Interacts
CC with cdc27, however the function of this complex is not known.
CC -!- INTERACTION:
CC P87324; P30261: cdc27; NbExp=3; IntAct=EBI-865227, EBI-866919;
CC P87324; P30316: pol3; NbExp=2; IntAct=EBI-865227, EBI-865207;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- SIMILARITY: Belongs to the DNA polymerase delta/II small subunit
CC family. {ECO:0000305}.
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DR EMBL; Y12562; CAA73149.1; -; mRNA.
DR EMBL; Y12561; CAA73148.1; -; Genomic_DNA.
DR EMBL; CU329670; CAB11679.1; -; Genomic_DNA.
DR PIR; T38453; T38453.
DR RefSeq; NP_594406.1; NM_001019837.2.
DR AlphaFoldDB; P87324; -.
DR SMR; P87324; -.
DR BioGRID; 278560; 18.
DR ComplexPortal; CPX-2100; DNA polymerase delta complex.
DR IntAct; P87324; 3.
DR STRING; 4896.SPAC27E2.05.1; -.
DR MaxQB; P87324; -.
DR PaxDb; P87324; -.
DR EnsemblFungi; SPAC27E2.05.1; SPAC27E2.05.1:pep; SPAC27E2.05.
DR GeneID; 2542083; -.
DR KEGG; spo:SPAC27E2.05; -.
DR PomBase; SPAC27E2.05; cdc1.
DR VEuPathDB; FungiDB:SPAC27E2.05; -.
DR eggNOG; KOG2732; Eukaryota.
DR HOGENOM; CLU_021763_1_0_1; -.
DR InParanoid; P87324; -.
DR OMA; DPANFML; -.
DR PhylomeDB; P87324; -.
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:P87324; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0043625; C:delta DNA polymerase complex; IDA:PomBase.
DR GO; GO:0042575; C:DNA polymerase complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
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:0006279; P:premeiotic DNA replication; IMP:PomBase.
DR CDD; cd07387; MPP_PolD2_C; 1.
DR InterPro; IPR007185; DNA_pol_a/d/e_bsu.
DR InterPro; IPR040663; DNA_pol_D_N.
DR InterPro; IPR024826; DNA_pol_delta/II_ssu.
DR InterPro; IPR041863; PolD2_C.
DR PANTHER; PTHR10416; PTHR10416; 1.
DR Pfam; PF18018; DNA_pol_D_N; 1.
DR Pfam; PF04042; DNA_pol_E_B; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; DNA replication; DNA-directed DNA polymerase;
KW Mitosis; Nucleotidyltransferase; Nucleus; Reference proteome; Transferase.
FT CHAIN 1..462
FT /note="DNA polymerase subunit delta-2"
FT /id="PRO_0000096173"
FT MUTAGEN 293
FT /note="G->S: Loss of function and does not bind cdc27."
FT MUTAGEN 381
FT /note="W->R: No loss of function and binds cdc27."
FT MUTAGEN 389
FT /note="D->G: Loss of function and does not bind cdc27."
SQ SEQUENCE 462 AA; 51326 MW; 3FF35E22D996580B CRC64;
MVEVRHSIPC EETKRLELSL SQQTYSQQYA SIYFARLTAL RPRITEAASK KWPDKQRLER
VLDVKSDEDC WVVATAYMTT ALKPNVMNDV TQLHTIVTTT EESPYVSPED AASGDIEYAL
EDDYGRIDCS GSFLYDAGVV TGVVLAVLGH EDEQGRFVVV DVCFPGIFSH SIPMTTDESQ
AQPEYIAAVS GLGLSNDGIE GIQVHQLVDF LRGTLPHVSS FSPSSIKRLI ILGNCLAPSI
EIADSASASV PIGKKKVKRY GYDTSAYNPN PTFQLDNFLD QVCSSIDVTL MPGPYDYSST
ILPQQPLHPA LLTKSKVWLG SSLQTVTNPT WLSLGNHFVL ATSGQNINDL RKYHPKKSSL
QCMENTLLWN HITPTSPDTL WCYPFTDKDT FVMEEMPDLY LCGNQPKFGC KTVINEGNRI
QLVSVPEFRK TGVLVLINMH TLNVEIIQFR PMSVKAETPI TS
