ID C7NYQ1_HALMD Unreviewed; 392 AA.
AC C7NYQ1;
DT 13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT 13-OCT-2009, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE RecName: Full=DNA primase small subunit PriS {ECO:0000256|HAMAP-Rule:MF_00700};
DE EC=2.7.7.- {ECO:0000256|HAMAP-Rule:MF_00700};
GN Name=priS {ECO:0000256|HAMAP-Rule:MF_00700};
GN OrderedLocusNames=Hmuk_2482 {ECO:0000313|EMBL:ACV48590.1};
OS Halomicrobium mukohataei (strain ATCC 700874 / DSM 12286 / JCM 9738 / NCIMB
OS 13541) (Haloarcula mukohataei).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Halomicrobium.
OX NCBI_TaxID=485914 {ECO:0000313|EMBL:ACV48590.1, ECO:0000313|Proteomes:UP000001746};
RN [1] {ECO:0000313|EMBL:ACV48590.1, ECO:0000313|Proteomes:UP000001746}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700874 / DSM 12286 / JCM 9738 / NCIMB 13541
RC {ECO:0000313|Proteomes:UP000001746};
RX PubMed=21304667; DOI=10.4056/sigs.42644;
RA Tindall B.J., Schneider S., Lapidus A., Copeland A., Glavina Del Rio T.,
RA Nolan M., Lucas S., Chen F., Tice H., Cheng J.F., Saunders E., Bruce D.,
RA Goodwin L., Pitluck S., Mikhailova N., Pati A., Ivanova N., Mavrommatis K.,
RA Chen A., Palaniappan K., Chain P., Land M., Hauser L., Chang Y.J.,
RA Jeffries C.D., Brettin T., Han C., Rohde M., Goker M., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Klenk H.P., Kyrpides N.C.,
RA Detter J.C.;
RT "Complete genome sequence of Halomicrobium mukohataei type strain (arg-
RT 2).";
RL Stand. Genomic Sci. 1:270-277(2009).
CC -!- FUNCTION: Catalytic 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. The small subunit contains the
CC primase catalytic core and has DNA synthesis activity on its own.
CC Binding to the large subunit stabilizes and modulates the activity,
CC increasing the rate of DNA synthesis while decreasing the length of the
CC DNA fragments, and conferring RNA synthesis capability. The DNA
CC polymerase activity may enable DNA primase to also catalyze primer
CC extension after primer synthesis. May also play a role in DNA repair.
CC {ECO:0000256|HAMAP-Rule:MF_00700}.
CC -!- FUNCTION: RNA polymerase that catalyzes the synthesis of short RNA
CC molecules used as primers for DNA polymerase during DNA replication.
CC {ECO:0000256|RuleBase:RU004224}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00700};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00700};
CC -!- SUBUNIT: Heterodimer of a small subunit (PriS) and a large subunit
CC (PriL). {ECO:0000256|HAMAP-Rule:MF_00700}.
CC -!- SIMILARITY: Belongs to the eukaryotic-type primase small subunit
CC family. {ECO:0000256|ARBA:ARBA00009762, ECO:0000256|HAMAP-
CC Rule:MF_00700, ECO:0000256|RuleBase:RU003514}.
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DR EMBL; CP001688; ACV48590.1; -; Genomic_DNA.
DR RefSeq; WP_015763432.1; NC_013202.1.
DR AlphaFoldDB; C7NYQ1; -.
DR STRING; 485914.Hmuk_2482; -.
DR GeneID; 8412026; -.
DR KEGG; hmu:Hmuk_2482; -.
DR eggNOG; arCOG04110; Archaea.
DR HOGENOM; CLU_056123_1_0_2; -.
DR OrthoDB; 31125at2157; -.
DR Proteomes; UP000001746; Chromosome.
DR GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
DR GO; GO:1990077; C:primosome complex; IEA:UniProtKB-KW.
DR GO; GO:0003896; F:DNA primase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd04860; AE_Prim_S; 1.
DR Gene3D; 3.90.920.10; DNA primase, PRIM domain; 1.
DR HAMAP; MF_00700; DNA_primase_sml_arc; 1.
DR InterPro; IPR002755; DNA_primase_S.
DR InterPro; IPR014052; DNA_primase_ssu_euk/arc.
DR InterPro; IPR023639; DNA_primase_ssu_PriS.
DR NCBIfam; TIGR00335; primase_sml; 1.
DR PANTHER; PTHR10536; DNA PRIMASE SMALL SUBUNIT; 1.
DR PANTHER; PTHR10536:SF0; DNA PRIMASE SMALL SUBUNIT; 1.
DR Pfam; PF01896; DNA_primase_S; 1.
DR SUPFAM; SSF56747; Prim-pol domain; 1.
PE 3: Inferred from homology;
KW DNA replication {ECO:0000256|ARBA:ARBA00022705, ECO:0000256|HAMAP-
KW Rule:MF_00700};
KW DNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022478,
KW ECO:0000256|HAMAP-Rule:MF_00700};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_00700};
KW Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|HAMAP-Rule:MF_00700};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_00700};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, ECO:0000256|HAMAP-
KW Rule:MF_00700};
KW Primosome {ECO:0000256|ARBA:ARBA00022515, ECO:0000256|HAMAP-Rule:MF_00700};
KW Reference proteome {ECO:0000313|Proteomes:UP000001746};
KW Transcription {ECO:0000256|ARBA:ARBA00023163, ECO:0000256|HAMAP-
KW Rule:MF_00700};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00700}.
FT ACT_SITE 98
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00700"
FT ACT_SITE 100
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00700"
FT ACT_SITE 295
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00700"
SQ SEQUENCE 392 AA; 43728 MW; EE0433AA250B853E CRC64;
MEERTQAYLR GRFGDHYRRS EFTPPPDANE REWGFIPWTD GPGETMVRHR SLLDLGELGE
FLQRKRPKHV YFSAGRYRDP SASSMSAKEW RSSDLVFDLD ADHLPAVELG EDSYAQMLAK
CKDALLRLLD FLENDFGFED LTVVFSGGRG YHVHVRDAGI QQLERDARRE IVDYVRGIGL
EFEQLVDEEA VAGTAGRSSP AQKRTLSTEG GWSRRAHRHV MSVVDDLLER DEEAAIERLM
EYEGIGEGKA TAALSAARQN YDQLAAGNID VHPAFFQIAK PLMTEVVAMD NAPIDEPVTT
DTNRLIRLPG SLHGGSGLEV RRIERDDIDE FDPLVDAVPE TFRGHDITIE VTDGGPVELG
GDSFTLEPGI GTYPEHVGVF AMARGRAEKG PE
//
