PRIL_HALS3
ID PRIL_HALS3 Reviewed; 360 AA.
AC B0R7F5;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 67.
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=OE_4163R;
OS Halobacterium salinarum (strain ATCC 29341 / DSM 671 / R1).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Halobacteriaceae; Halobacterium.
OX NCBI_TaxID=478009;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29341 / DSM 671 / R1;
RX PubMed=18313895; DOI=10.1016/j.ygeno.2008.01.001;
RA Pfeiffer F., Schuster S.C., Broicher A., Falb M., Palm P., Rodewald K.,
RA Ruepp A., Soppa J., Tittor J., Oesterhelt D.;
RT "Evolution in the laboratory: the genome of Halobacterium salinarum strain
RT R1 compared to that of strain NRC-1.";
RL Genomics 91:335-346(2008).
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; AM774415; CAP14674.1; -; Genomic_DNA.
DR RefSeq; WP_010903675.1; NC_010364.1.
DR AlphaFoldDB; B0R7F5; -.
DR EnsemblBacteria; CAP14674; CAP14674; OE_4163R.
DR GeneID; 5953307; -.
DR GeneID; 62887535; -.
DR KEGG; hsl:OE_4163R; -.
DR HOGENOM; CLU_052778_0_0_2; -.
DR OMA; PSCATMQ; -.
DR PhylomeDB; B0R7F5; -.
DR Proteomes; UP000001321; 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.
FT CHAIN 1..360
FT /note="DNA primase large subunit PriL"
FT /id="PRO_1000132351"
FT REGION 340..360
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 360 AA; 39739 MW; A24F0BA1309A940C CRC64;
MNARHARYPF LGDARDAVEE AGVDLARVVT EDDAVVERAR ERVVSALTDG TIGEPAATVS
TRVEVLSYPV ARVLVSIVDE SVLVRKYATA EADAAYDRFT ADESTDTDLK SVSDTTRVSR
DTLLSEFDLR AHVHATPDAH TVDVPTYLLL ASSLRDDDWR LVNRALDDGR VPVTDAELDT
LIREAIRERV ADGLPLSVPD QIADALDEPV AAIQDALADL DLTREIDTVV PELFPPCMKH
LLDQVQRGDH LPHHARFAIT SFLSNVGLST DEIVDIYEVN PGFGEEMTRY QTDHIQGDSS
PTEYTAPSCA TMKAYGNCVN PDDLCDAINH PLSYYEVKLD DGDDDDLADW RDREDDDSPD