PRI2_DICDI
ID PRI2_DICDI Reviewed; 470 AA.
AC Q55BM5;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=DNA primase large subunit;
GN Name=prim2; Synonyms=polA3; ORFNames=DDB_G0270442;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- FUNCTION: DNA primase is the polymerase that synthesizes small RNA
CC primers for the Okazaki fragments made during discontinuous DNA
CC replication. {ECO:0000250}.
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250};
CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000250};
CC -!- SUBUNIT: Heterodimer of a small subunit and a large subunit.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the eukaryotic-type primase large subunit
CC family. {ECO:0000305}.
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DR EMBL; AAFI02000005; EAL72571.1; -; Genomic_DNA.
DR RefSeq; XP_646806.1; XM_641714.1.
DR AlphaFoldDB; Q55BM5; -.
DR SMR; Q55BM5; -.
DR STRING; 44689.DDB0232281; -.
DR PaxDb; Q55BM5; -.
DR EnsemblProtists; EAL72571; EAL72571; DDB_G0270442.
DR GeneID; 8617779; -.
DR KEGG; ddi:DDB_G0270442; -.
DR dictyBase; DDB_G0270442; polA3.
DR eggNOG; KOG2267; Eukaryota.
DR HOGENOM; CLU_026253_2_0_1; -.
DR InParanoid; Q55BM5; -.
DR OMA; KTSMPLC; -.
DR PhylomeDB; Q55BM5; -.
DR Reactome; R-DDI-113501; Inhibition of replication initiation of damaged DNA by RB1/E2F1.
DR Reactome; R-DDI-68952; DNA replication initiation.
DR Reactome; R-DDI-68962; Activation of the pre-replicative complex.
DR Reactome; R-DDI-69091; Polymerase switching.
DR Reactome; R-DDI-69166; Removal of the Flap Intermediate.
DR Reactome; R-DDI-69183; Processive synthesis on the lagging strand.
DR PRO; PR:Q55BM5; -.
DR Proteomes; UP000002195; Chromosome 1.
DR GO; GO:0005658; C:alpha DNA polymerase:primase complex; ISS:dictyBase.
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; IEA:UniProt.
DR GO; GO:0006269; P:DNA replication, synthesis of RNA primer; ISS:dictyBase.
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 3: Inferred from homology;
KW 4Fe-4S; DNA replication; DNA-binding; Iron; Iron-sulfur; Metal-binding;
KW Primosome; Reference proteome.
FT CHAIN 1..470
FT /note="DNA primase large subunit"
FT /id="PRO_0000328102"
FT REGION 449..470
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 279
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 358
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 376
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 414
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
SQ SEQUENCE 470 AA; 54483 MW; 89037CC3F44F7D11 CRC64;
MLRAGKKTNS QTSTSNDACS LLYINVPDFN CNMSQIENYC IDRFNLLNEV SKLKDTLSAQ
KSNTSKDNED FRNLSSRFLG STKDEQFKIK DELSHYCLRL AMCDSTDRNW FITTESILLA
NRLNQSDLTT IISSFKGFGW SPVSQEEYEQ YQDDLGYLVK KANLNLNEVN NTHFYKLPFQ
DIPKLIDTKK AIIIKGEAYI YISNFKDMVI HTFKNYMNFA LDRIKADKTR IKEEFPELIQ
FFTTLPKAGD GTNKPQLGNT KHIRKEDVSP LSKTSFPMCM RVMYDSLVET SSLKYEGRLQ
FGTFLKGIGL PYDEAINFWR IAFSKRVSNT DFDKEYLYNI RHNYGLEGKS TNYSPYSCPR
IISKSPHNGD KLVHGCPYIQ SLERLEQKLL DLGIDDFQRI QILEATKTSP NVACTKHFNF
LHPNNTLTKL INHPNQFYDQ SMEYYKTLEE KKSAKQSNNK ENENQSIDEK
