PRI1_SCHPO
ID PRI1_SCHPO Reviewed; 454 AA.
AC O14215;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=DNA primase small subunit {ECO:0000250|UniProtKB:P49642};
DE EC=2.7.7.102 {ECO:0000250|UniProtKB:P49642};
DE AltName: Full=DNA primase 1 {ECO:0000303|PubMed:11859360};
GN Name=spp1 {ECO:0000303|PubMed:11027257, ECO:0000312|PomBase:SPAC6B12.10c};
GN Synonyms=pri1 {ECO:0000312|PomBase:SPAC6B12.10c};
GN ORFNames=SPAC6B12.10c {ECO:0000312|PomBase:SPAC6B12.10c};
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 INTERACTION WITH POL1 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 [3]
RP INTERACTION WITH POL1 AND SPP2, SUBCELLULAR LOCATION, AND DEVELOPMENTAL
RP STAGE.
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 [4]
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).
CC -!- FUNCTION: Catalytic subunit of the DNA primase complex and component of
CC 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:P49642}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ssDNA + n NTP = ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate.;
CC EC=2.7.7.102; Evidence={ECO:0000250|UniProtKB:P49642};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P49642};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:P49642};
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:15314153, PubMed:11027257, PubMed:11160827).
CC {ECO:0000250|UniProtKB:P20664, ECO:0000269|PubMed:11027257,
CC ECO:0000269|PubMed:11160827, ECO:0000269|PubMed:15314153}.
CC -!- INTERACTION:
CC O14215; O74761: pri2; NbExp=2; IntAct=EBI-849063, EBI-849075;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11160827}.
CC -!- DEVELOPMENTAL STAGE: Constitutively expressed throughout the cell cycle
CC (at protein level). {ECO:0000269|PubMed:11160827}.
CC -!- MISCELLANEOUS: The bound zinc ion is not a cofactor. It is bound to a
CC zinc knuckle motif that may be involved in sequence recognition and the
CC binding of ssDNA (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the eukaryotic-type primase small subunit
CC family. {ECO:0000305}.
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DR EMBL; CU329670; CAB11078.1; -; Genomic_DNA.
DR PIR; T39017; T39017.
DR RefSeq; NP_593765.1; NM_001019195.2.
DR AlphaFoldDB; O14215; -.
DR SMR; O14215; -.
DR BioGRID; 279746; 7.
DR ComplexPortal; CPX-2092; DNA polymerase alpha:primase complex.
DR IntAct; O14215; 4.
DR STRING; 4896.SPAC6B12.10c.1; -.
DR MaxQB; O14215; -.
DR PaxDb; O14215; -.
DR EnsemblFungi; SPAC6B12.10c.1; SPAC6B12.10c.1:pep; SPAC6B12.10c.
DR GeneID; 2543323; -.
DR KEGG; spo:SPAC6B12.10c; -.
DR PomBase; SPAC6B12.10c; spp1.
DR VEuPathDB; FungiDB:SPAC6B12.10c; -.
DR eggNOG; KOG2851; Eukaryota.
DR HOGENOM; CLU_028288_1_0_1; -.
DR InParanoid; O14215; -.
DR OMA; NVTRGFN; -.
DR PhylomeDB; O14215; -.
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:O14215; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005658; C:alpha DNA polymerase:primase complex; IPI:ComplexPortal.
DR GO; GO:0000785; C:chromatin; IDA:PomBase.
DR GO; GO:0005737; C:cytoplasm; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0003896; F:DNA primase activity; ISO:PomBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006270; P:DNA replication initiation; IDA:ComplexPortal.
DR GO; GO:0006269; P:DNA replication, synthesis of RNA primer; IBA:GO_Central.
DR GO; GO:1902981; P:synthesis of RNA primer involved in mitotic DNA replication; ISO:PomBase.
DR CDD; cd04860; AE_Prim_S; 1.
DR InterPro; IPR002755; DNA_primase_S.
DR InterPro; IPR014052; DNA_primase_ssu_euk/arc.
DR PANTHER; PTHR10536; PTHR10536; 1.
DR Pfam; PF01896; DNA_primase_S; 1.
DR TIGRFAMs; TIGR00335; primase_sml; 1.
PE 1: Evidence at protein level;
KW DNA replication; DNA-directed RNA polymerase; Magnesium; Manganese;
KW Metal-binding; Nucleotidyltransferase; Nucleus; Primosome;
KW Reference proteome; Transcription; Transferase; Zinc.
FT CHAIN 1..454
FT /note="DNA primase small subunit"
FT /id="PRO_0000046735"
FT REGION 385..420
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 143..153
FT /note="Zinc knuckle motif"
FT /evidence="ECO:0000250|UniProtKB:P49642"
FT ACT_SITE 66
FT /evidence="ECO:0000255"
FT ACT_SITE 131
FT /evidence="ECO:0000255"
FT ACT_SITE 133
FT /evidence="ECO:0000255"
FT BINDING 131..133
FT /ligand="a ribonucleoside 5'-triphosphate"
FT /ligand_id="ChEBI:CHEBI:61557"
FT /evidence="ECO:0000250|UniProtKB:P49642"
FT BINDING 131
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P49642"
FT BINDING 131
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P49642"
FT BINDING 131
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P49642"
FT BINDING 131
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P49642"
FT BINDING 133
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P49642"
FT BINDING 133
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P49642"
FT BINDING 133
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P49642"
FT BINDING 133
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P49642"
FT BINDING 143
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P49642"
FT BINDING 144
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P49642"
FT BINDING 150
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P49642"
FT BINDING 153
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P49642"
FT BINDING 182..188
FT /ligand="a ribonucleoside 5'-triphosphate"
FT /ligand_id="ChEBI:CHEBI:61557"
FT /evidence="ECO:0000250|UniProtKB:P49642"
FT BINDING 333
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P49642"
FT BINDING 333
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P49642"
FT BINDING 342..345
FT /ligand="a ribonucleoside 5'-triphosphate"
FT /ligand_id="ChEBI:CHEBI:61557"
FT /evidence="ECO:0000250|UniProtKB:P49642"
SQ SEQUENCE 454 AA; 52009 MW; 71526FFAF7C2BBFA CRC64;
MTVQIDELDD KDLDEIIANG TLDGAKQGAV DSETMIQYYR HLFPWKYLFQ WLNHGPVVTN
DFAHREFAFT LPNDAYIRYL SFSNWEELKK EALNLCPSRF EVGPVYSANP RDRKTIRKST
FHPLKKELVF DIDMTDYDDV RTCCSKTNIC EKCWPFITIA VQVLDICFHE DFGFKHILWV
YSGRRGIHAW ICDEIACSLD DRSRRMIASY LQVVVGNPQG GVRLINNLKR PLHPHLTRSL
NILKSAFVKI VLEDQDPWAS KEGAENLLKL LPDKDLASAL RKKWEVDPER SSKNKWSDID
TVLASGSIAS ISPSVIAIAK QDIVLTYLYP RLDVEVSRHL NHLLKSPFCV HPGTSRVCVP
IDIERMDSFN PLKVPTVNDL LQELDKNSQN DNGHGPTMET NTTENQKDNA RGQSNKGHGF
STSLNPYTLY FKSFSSQLFK ETVGNKRKHE NLEF
