PRIL_PYRHO
ID PRIL_PYRHO Reviewed; 394 AA.
AC O57935;
DT 29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 29-AUG-2003, sequence version 2.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=DNA primase large subunit PriL {ECO:0000255|HAMAP-Rule:MF_00701};
DE AltName: Full=DNA primase 46 kDa subunit;
DE Short=p46;
GN Name=priL {ECO:0000255|HAMAP-Rule:MF_00701}; Synonyms=priB;
GN OrderedLocusNames=PH0196;
OS Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC
OS 100139 / OT-3).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=70601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX PubMed=9679194; DOI=10.1093/dnares/5.2.55;
RA Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S.,
RA Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K.,
RA Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T., Tanaka T.,
RA Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T.,
RA Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.;
RT "Complete sequence and gene organization of the genome of a hyper-
RT thermophilic archaebacterium, Pyrococcus horikoshii OT3.";
RL DNA Res. 5:55-76(1998).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 1-219, SUBUNIT, AND MUTAGENESIS OF
RP 155-TYR--ILE-157.
RX PubMed=17286576; DOI=10.1111/j.1742-4658.2007.05690.x;
RA Ito N., Matsui I., Matsui E.;
RT "Molecular basis for the subunit assembly of the primase from an archaeon
RT Pyrococcus horikoshii.";
RL FEBS J. 274:1340-1351(2007).
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, ECO:0000269|PubMed:17286576}.
CC -!- SIMILARITY: Belongs to the eukaryotic-type primase large subunit
CC family. {ECO:0000255|HAMAP-Rule:MF_00701}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA29265.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; BA000001; BAA29265.1; ALT_INIT; Genomic_DNA.
DR PIR; B71242; B71242.
DR RefSeq; WP_048053055.1; NC_000961.1.
DR PDB; 2DLA; X-ray; 2.90 A; A/B/C=1-219.
DR PDBsum; 2DLA; -.
DR AlphaFoldDB; O57935; -.
DR SMR; O57935; -.
DR STRING; 70601.3256582; -.
DR DNASU; 1444087; -.
DR EnsemblBacteria; BAA29265; BAA29265; BAA29265.
DR GeneID; 1444087; -.
DR KEGG; pho:PH0196; -.
DR eggNOG; arCOG03013; Archaea.
DR OMA; KNIWYHL; -.
DR OrthoDB; 29893at2157; -.
DR BRENDA; 2.7.7.102; 5244.
DR BRENDA; 2.7.7.B16; 5244.
DR EvolutionaryTrace; O57935; -.
DR Proteomes; UP000000752; 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 Pfam; PF04104; DNA_primase_lrg; 1.
PE 1: Evidence at protein level;
KW 3D-structure; 4Fe-4S; DNA replication; Iron; Iron-sulfur; Metal-binding;
KW Primosome.
FT CHAIN 1..394
FT /note="DNA primase large subunit PriL"
FT /id="PRO_0000046786"
FT BINDING 231
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00701"
FT BINDING 340
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00701"
FT BINDING 351
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00701"
FT BINDING 357
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00701"
FT MUTAGEN 155..157
FT /note="YEG->AAA: 1000-fold decrease in PriS binding."
FT /evidence="ECO:0000269|PubMed:17286576"
FT HELIX 7..12
FT /evidence="ECO:0007829|PDB:2DLA"
FT TURN 13..16
FT /evidence="ECO:0007829|PDB:2DLA"
FT HELIX 19..25
FT /evidence="ECO:0007829|PDB:2DLA"
FT HELIX 26..28
FT /evidence="ECO:0007829|PDB:2DLA"
FT HELIX 32..39
FT /evidence="ECO:0007829|PDB:2DLA"
FT HELIX 40..42
FT /evidence="ECO:0007829|PDB:2DLA"
FT HELIX 45..47
FT /evidence="ECO:0007829|PDB:2DLA"
FT HELIX 49..52
FT /evidence="ECO:0007829|PDB:2DLA"
FT HELIX 56..70
FT /evidence="ECO:0007829|PDB:2DLA"
FT HELIX 77..94
FT /evidence="ECO:0007829|PDB:2DLA"
FT TURN 102..104
FT /evidence="ECO:0007829|PDB:2DLA"
FT STRAND 105..111
FT /evidence="ECO:0007829|PDB:2DLA"
FT HELIX 117..119
FT /evidence="ECO:0007829|PDB:2DLA"
FT HELIX 120..127
FT /evidence="ECO:0007829|PDB:2DLA"
FT STRAND 133..136
FT /evidence="ECO:0007829|PDB:2DLA"
FT HELIX 137..143
FT /evidence="ECO:0007829|PDB:2DLA"
FT HELIX 149..151
FT /evidence="ECO:0007829|PDB:2DLA"
FT STRAND 152..155
FT /evidence="ECO:0007829|PDB:2DLA"
FT STRAND 158..161
FT /evidence="ECO:0007829|PDB:2DLA"
FT HELIX 163..184
FT /evidence="ECO:0007829|PDB:2DLA"
FT STRAND 186..188
FT /evidence="ECO:0007829|PDB:2DLA"
FT HELIX 194..216
FT /evidence="ECO:0007829|PDB:2DLA"
SQ SEQUENCE 394 AA; 45949 MW; D7580A702EE171AC CRC64;
MLDPFSEKAK ELLKGFGSIN DFMDAIPKIV SVDDVIERIR VVKNEKLIDK FLDQDNVMDL
AQFYALLGAL SYSPYGIELE LVKKANLIIY SERLKRKKEI KPEEISIDVS TAIEFPTEDV
RKIERVYGKI PEYTMKISDF LDLVPDEKLA NYYIYEGRVY LKREDLIRIW SKAFERNVER
GVNMLYEIRD ELPEFYRKVL GEIQAFAEEE FGRKFGEIQG GKLRPEFFPP CIKNALKGVP
QGIRNYAITV LLTSFLSYAR ICPNPPRRNV RVKDCIKDIR VITEEILPII IEAANRCSPP
LFEDQPNEIK NIWYHLGFGY TANPSLEDSG NSTWYFPPNC EKIRANAPQL CTPDKHCKYI
RNPLTYYLRR LYLEGRRNAP KRGNKRGKKE LLHQ
