PRI2_SCHPO
ID PRI2_SCHPO Reviewed; 459 AA.
AC O74761; Q9US83;
DT 29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=DNA primase large subunit {ECO:0000305};
DE AltName: Full=DNA primase 2 {ECO:0000303|PubMed:11027257};
GN Name=spp2 {ECO:0000303|PubMed:11027257, ECO:0000312|PomBase:SPBC17D11.06};
GN Synonyms=p58 {ECO:0000303|PubMed:11027257},
GN pri2 {ECO:0000312|PomBase:SPBC17D11.06};
GN ORFNames=SPBC17D11.06 {ECO:0000312|PomBase:SPBC17D11.06};
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 [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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 121-248, 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 [3]
RP INTERACTION WITH SPP1 AND POL1.
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 [4]
RP INTERACTION WITH SPP1 AND POL1.
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 [5]
RP IDENTIFICATION IN THE DNA POLYMERASE ALPHA COMPLEX, INTERACTION WITH ORC2,
RP AND SUBCELLULAR LOCATION.
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).
CC -!- FUNCTION: Regulatory subunit of the DNA primase complex and component
CC of the DNA polymerase alpha complex (also known as the alpha DNA
CC polymerase-primase complex - primosome/replisome) which play an
CC essential role in the initiation of DNA synthesis (By similarity).
CC During the S phase of the cell cycle, the DNA polymerase alpha complex
CC (composed of a catalytic subunit pol1, an accessory subunit spb70/pol12
CC and two primase subunits, the catalytic subunit spp1/pri1 and the
CC regulatory subunit spp2/pri2) is recruited to DNA at the replicative
CC forks (By similarity). The primase subunit of the polymerase alpha
CC complex initiates DNA synthesis by oligomerising short RNA primers on
CC both leading and lagging strands (By similarity).
CC {ECO:0000250|UniProtKB:P33610}.
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000250|UniProtKB:P49643};
CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000250|UniProtKB:P49643};
CC -!- SUBUNIT: Heterodimer of a catalytic subunit spp1/pri1 and a regulatory
CC subunit spp2/pri2, also known as the DNA primase complex (By
CC similarity). Component of the alpha DNA polymerase complex (also known
CC as the alpha DNA polymerase-primase complex) consisting of four
CC subunits: the catalytic subunit pol1, the accessory subunit
CC spb70/pol12, and the primase complex subunits spp1/pri1 and spp2/pri2
CC respectively (PubMed:11027257, PubMed:11160827, PubMed:15314153).
CC Interacts with orc2; preferentially associates with the
CC unphosphorylated orc2 in G1 pre-Start prior to orc2 being
CC phosphorylated by cdc2, the interaction is mediated by spb70 and might
CC enable the association of the whole alpha DNA polymerase complex to
CC orc2/spb70 complex on chromatin (PubMed:15314153).
CC {ECO:0000250|UniProtKB:P49643, ECO:0000269|PubMed:11027257,
CC ECO:0000269|PubMed:11160827, ECO:0000269|PubMed:15314153}.
CC -!- INTERACTION:
CC O74761; O14215: pri1; NbExp=2; IntAct=EBI-849075, EBI-849063;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10759889}. Chromosome
CC {ECO:0000269|PubMed:15314153}. Note=Present on chromatin fraction at 40
CC min after release from G2 arrest and from G1 to S phase.
CC {ECO:0000269|PubMed:15314153}.
CC -!- SIMILARITY: Belongs to the eukaryotic-type primase large subunit
CC family. {ECO:0000305}.
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DR EMBL; CU329671; CAA21077.1; -; Genomic_DNA.
DR EMBL; AB027983; BAA87287.1; -; Genomic_DNA.
DR PIR; T39717; T39717.
DR RefSeq; NP_596380.1; NM_001022301.2.
DR AlphaFoldDB; O74761; -.
DR SMR; O74761; -.
DR BioGRID; 276477; 13.
DR ComplexPortal; CPX-2092; DNA polymerase alpha:primase complex.
DR IntAct; O74761; 2.
DR STRING; 4896.SPBC17D11.06.1; -.
DR iPTMnet; O74761; -.
DR SwissPalm; O74761; -.
DR MaxQB; O74761; -.
DR PaxDb; O74761; -.
DR EnsemblFungi; SPBC17D11.06.1; SPBC17D11.06.1:pep; SPBC17D11.06.
DR GeneID; 2539933; -.
DR KEGG; spo:SPBC17D11.06; -.
DR PomBase; SPBC17D11.06; spp2.
DR VEuPathDB; FungiDB:SPBC17D11.06; -.
DR eggNOG; KOG2267; Eukaryota.
DR HOGENOM; CLU_026253_1_0_1; -.
DR InParanoid; O74761; -.
DR OMA; KTSMPLC; -.
DR PhylomeDB; O74761; -.
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:O74761; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005658; C:alpha DNA polymerase:primase complex; IPI:ComplexPortal.
DR GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006270; P:DNA replication initiation; IDA:ComplexPortal.
DR GO; GO:1902981; P:synthesis of RNA primer involved in mitotic DNA replication; ISO:PomBase.
DR CDD; cd07322; PriL_PriS_Eukaryotic; 1.
DR InterPro; IPR016558; DNA_primase_lsu_euk.
DR InterPro; IPR007238; DNA_primase_lsu_euk/arc.
DR PANTHER; PTHR10537; PTHR10537; 1.
DR Pfam; PF04104; DNA_primase_lrg; 1.
DR PIRSF; PIRSF009449; DNA_primase_large_subunit; 1.
PE 1: Evidence at protein level;
KW 4Fe-4S; Chromosome; DNA replication; DNA-binding; Iron; Iron-sulfur;
KW Metal-binding; Nucleus; Primosome; Reference proteome.
FT CHAIN 1..459
FT /note="DNA primase large subunit"
FT /id="PRO_0000046775"
FT BINDING 291
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 369
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 386
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 428
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
SQ SEQUENCE 459 AA; 53053 MW; 811172102DDFC42E CRC64;
MFRTTKSRVV EKNQNFSSAS FESLSYPTRL NFYKKPPVSE ISIEEFETWA IDRLVVLGEI
ESAMLRNKTK NELNGIIKKI LDKRLPMSSN MARTVKGNSL DEERRKDHYS HFILRLAFSR
SDELRIRFLR AESTLFRFRF VNEETRERQA FIDSLDFQWE SVSQEEKDVF YEKLQASSQR
NIENESFFKV PFFKVPDLVE RRAVFVHKGY AYVPFSEQVS LVVEEFEENL KKALESTAKS
LPRLDEDDRL LPILNHLSKG FVAPESSIVA PKSGAITAGQ VDSFVSHFPL CAKHLHEVLK
RDKHLRHFGR LQYGLFLKDI GLSVDEALVF WRKSFTNVTE DKFNKEYRYN IRHTYGLEGN
RKNYKGYNCQ QILTGPQLGP GDAHGCPYRT YSVNNLVSAL ASMGIAPDSA GCREVVEAVK
ARHYHIACTR VFELTHPNVG SLEESIHHPL QYFQLSLES
