PRIL_METAR
ID PRIL_METAR Reviewed; 366 AA.
AC Q0W2J3;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=DNA primase large subunit PriL {ECO:0000255|HAMAP-Rule:MF_00701};
GN Name=priL {ECO:0000255|HAMAP-Rule:MF_00701}; Synonyms=priB;
GN OrderedLocusNames=UNCMA_08520; ORFNames=RCIX2295;
OS Methanocella arvoryzae (strain DSM 22066 / NBRC 105507 / MRE50).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanocellales; Methanocellaceae; Methanocella.
OX NCBI_TaxID=351160;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22066 / NBRC 105507 / MRE50;
RX PubMed=16857943; DOI=10.1126/science.1127062;
RA Erkel C., Kube M., Reinhardt R., Liesack W.;
RT "Genome of rice cluster I archaea -- the key methane producers in the rice
RT rhizosphere.";
RL Science 313:370-372(2006).
CC -!- FUNCTION: Regulatory subunit of DNA primase, an RNA polymerase that
CC catalyzes the synthesis of short RNA molecules used as primers for DNA
CC polymerase during DNA replication. Stabilizes and modulates the
CC activity of the small subunit, increasing the rate of DNA synthesis,
CC and conferring RNA synthesis capability. The DNA polymerase activity
CC may enable DNA primase to also catalyze primer extension after primer
CC synthesis. May also play a role in DNA repair. {ECO:0000255|HAMAP-
CC Rule:MF_00701}.
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00701};
CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000255|HAMAP-Rule:MF_00701};
CC -!- SUBUNIT: Heterodimer of a small subunit (PriS) and a large subunit
CC (PriL). {ECO:0000255|HAMAP-Rule:MF_00701}.
CC -!- SIMILARITY: Belongs to the eukaryotic-type primase large subunit
CC family. {ECO:0000255|HAMAP-Rule:MF_00701}.
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DR EMBL; AM114193; CAJ37400.1; -; Genomic_DNA.
DR RefSeq; WP_012035181.1; NC_009464.1.
DR AlphaFoldDB; Q0W2J3; -.
DR STRING; 351160.RCIX2295; -.
DR EnsemblBacteria; CAJ37400; CAJ37400; RCIX2295.
DR GeneID; 5143365; -.
DR KEGG; rci:RCIX2295; -.
DR PATRIC; fig|351160.9.peg.881; -.
DR eggNOG; arCOG03013; Archaea.
DR OMA; PSCATMQ; -.
DR OrthoDB; 29893at2157; -.
DR Proteomes; UP000000663; Chromosome.
DR GO; GO:1990077; C:primosome complex; IEA:UniProtKB-KW.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003896; F:DNA primase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd06560; PriL; 1.
DR HAMAP; MF_00701; DNA_primase_lrg_arc; 1.
DR InterPro; IPR007238; DNA_primase_lsu_euk/arc.
DR InterPro; IPR023642; DNA_primase_lsu_PriL.
DR PANTHER; PTHR10537; PTHR10537; 1.
DR Pfam; PF04104; DNA_primase_lrg; 1.
PE 3: Inferred from homology;
KW 4Fe-4S; DNA replication; Iron; Iron-sulfur; Metal-binding; Primosome;
KW Reference proteome.
FT CHAIN 1..366
FT /note="DNA primase large subunit PriL"
FT /id="PRO_1000045514"
FT BINDING 227
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00701"
FT BINDING 298
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00701"
FT BINDING 307
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00701"
FT BINDING 314
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00701"
SQ SEQUENCE 366 AA; 41463 MW; 5BDEC2E5D43DFE34 CRC64;
MDAVGFAKYP FTQEALSYVR DRNYSMEDIL QKPAYGQVRL RAKKRVLNSI KGDVQADDLL
PDPERELLSY PVARMLVAMT EDQYLMKRFA LWESKRAYTL LLDESDTGLM DVGRDFGITA
RAKDREFIIH FTDYLRYAAG LRNLEWKLIN RKVVAGMVYV SRETFTRLLE EAVREKIQAG
FGAKVPAEMK PVLEPYLAEI RESLDKLKSE KGLSGDGEVT QDSFPPCMKN LLADLQKGIN
LPHTARFALT SFLANIGLDK DAIMDLYRMA PDFREDLTHY QVQHITGGSG TEYTCPGCKT
MMTYGNCIGK NKLCEYVTHP LSYYRKSQRR RAKEMAAAQA FKGSKDKAVD TVAENVHVET
GNSPGN