ID U5Q5E4_METII Unreviewed; 406 AA.
AC U5Q5E4;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 46.
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 ORFNames=MMINT_19390 {ECO:0000313|EMBL:AGY50234.1};
OS Methanomassiliicoccus intestinalis (strain Issoire-Mx1).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata;
OC Methanomassiliicoccales; Methanomassiliicoccaceae; Methanomassiliicoccus.
OX NCBI_TaxID=1295009 {ECO:0000313|EMBL:AGY50234.1, ECO:0000313|Proteomes:UP000014070};
RN [1] {ECO:0000313|EMBL:AGY50234.1, ECO:0000313|Proteomes:UP000014070}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Issoire-Mx1 {ECO:0000313|EMBL:AGY50234.1,
RC ECO:0000313|Proteomes:UP000014070};
RX PubMed=23846268; DOI=10.1128/genomeA.00453-13;
RA Borrel G., Harris H.M., Parisot N., Gaci N., Tottey W., Mihajlovski A.,
RA Deane J., Gribaldo S., Bardot O., Peyretaillade E., Peyret P.,
RA O'Toole P.W., Brugere J.F.;
RT "Genome sequence of 'Candidatus Methanomassiliicoccus intestinalis'
RT Issoire-Mx1, a third thermoplasmatales-related methanogenic archaeon from
RT human feces.";
RL Genome Announc. 1:142-142(2013).
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; CP005934; AGY50234.1; -; Genomic_DNA.
DR AlphaFoldDB; U5Q5E4; -.
DR STRING; 1295009.MMINT_19390; -.
DR KEGG; mer:MMINT_19390; -.
DR HOGENOM; CLU_056123_1_0_2; -.
DR InParanoid; U5Q5E4; -.
DR Proteomes; UP000014070; 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 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|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:UP000014070};
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 94
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00700"
FT ACT_SITE 96
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00700"
FT ACT_SITE 306
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00700"
SQ SEQUENCE 406 AA; 47215 MW; C25DFB9426BE15AC CRC64;
MASDKEFMME RFRRYYSKNH PYIPTMFKNR EFGFMFFDRS FVQRHMAFTS DDALYSFLQT
QVPSHSYHST AYYQYPGAAT MEDKQWIGAD LIFDLDADHI PGAELMSYDE MLARIKIEVL
RLVDDFLLGD LGFDESHLRI VFSGGRGYHI HVSDERVARL KSHERREIVD YIAGNNLNMD
WVFPTKTVNI TEIKGRVQES RVRCIPPGGS GGWKGKMRIG IAWLIEEMRS LDVKDLRTRL
PYLNTYSETL VNGMLKDLYE KRGERSGSDM LLEKNIFDCF TSKRHEDIFL GLLENEVIPR
FRCEIDEPVT ADIKRLIRLP GSLHGKSGLR VVPMEREDLD DFNPLLDAVP DTYTDREIEI
FLKHKVDITI RGKRITGEGI CRVPEYAAMF LIGRREATLE FVESLE
//
