PRIL_METBU
ID PRIL_METBU Reviewed; 364 AA.
AC Q12U19;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 03-AUG-2022, entry version 85.
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=Mbur_2192;
OS Methanococcoides burtonii (strain DSM 6242 / NBRC 107633 / OCM 468 /
OS ACE-M).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanococcoides.
OX NCBI_TaxID=259564;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6242 / NBRC 107633 / OCM 468 / ACE-M;
RX PubMed=19404327; DOI=10.1038/ismej.2009.45;
RA Allen M.A., Lauro F.M., Williams T.J., Burg D., Siddiqui K.S.,
RA De Francisci D., Chong K.W., Pilak O., Chew H.H., De Maere M.Z., Ting L.,
RA Katrib M., Ng C., Sowers K.R., Galperin M.Y., Anderson I.J., Ivanova N.,
RA Dalin E., Martinez M., Lapidus A., Hauser L., Land M., Thomas T.,
RA Cavicchioli R.;
RT "The genome sequence of the psychrophilic archaeon, Methanococcoides
RT burtonii: the role of genome evolution in cold adaptation.";
RL ISME J. 3:1012-1035(2009).
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; CP000300; ABE53057.1; -; Genomic_DNA.
DR RefSeq; WP_011500193.1; NC_007955.1.
DR AlphaFoldDB; Q12U19; -.
DR STRING; 259564.Mbur_2192; -.
DR EnsemblBacteria; ABE53057; ABE53057; Mbur_2192.
DR GeneID; 3997048; -.
DR KEGG; mbu:Mbur_2192; -.
DR HOGENOM; CLU_052778_0_0_2; -.
DR OMA; PSCATMQ; -.
DR OrthoDB; 29893at2157; -.
DR Proteomes; UP000001979; 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..364
FT /note="DNA primase large subunit PriL"
FT /id="PRO_1000045513"
FT REGION 345..364
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 237
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00701"
FT BINDING 309
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00701"
FT BINDING 318
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00701"
FT BINDING 325
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00701"
SQ SEQUENCE 364 AA; 41420 MW; ED2F0F47809FBA12 CRC64;
MDNRHLALYP FVTEASEYVG SLGFSPDKLL SSRALESARI RGRERVIQAL EGEIEKPSPS
SSEEGKILTE LLSYPFSRIL VSCIDDPFLT RKYALAEAKA AYHLLKTQQP EFLQDLATDF
RINAEIYENP ETHDIFFDLH FTDYIKLASP LKDLNWKLVN RKMKKGYVKI SKEELARLLQ
EAIRLRIQNS LPVTVPKEIC EACIPHTDTI SEELEKKKTE FGVGEFQRVE SDLFPPCITQ
AIANVRAGVN LAHSMRFAMT SFLINIGMSV DEVVAMFNIS PDFDEEKTRY QIEHIAGTSS
GTTYKPPSCN TMRTYGNCSA PDELCKGVKH PLGYYSRRVW VKNRMQNDNE KGHEEKKEGE
TPPQ