PRIS_METKA
ID PRIS_METKA Reviewed; 296 AA.
AC Q8TXS4;
DT 29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 29-AUG-2003, sequence version 2.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=DNA primase small subunit PriS {ECO:0000255|HAMAP-Rule:MF_00700};
DE EC=2.7.7.- {ECO:0000255|HAMAP-Rule:MF_00700};
GN Name=priS {ECO:0000255|HAMAP-Rule:MF_00700}; Synonyms=pri1, priA;
GN OrderedLocusNames=MK0586;
OS Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938).
OC Archaea; Euryarchaeota; Methanopyri; Methanopyrales; Methanopyraceae;
OC Methanopyrus.
OX NCBI_TaxID=190192;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AV19 / DSM 6324 / JCM 9639 / NBRC 100938;
RX PubMed=11930014; DOI=10.1073/pnas.032671499;
RA Slesarev A.I., Mezhevaya K.V., Makarova K.S., Polushin N.N.,
RA Shcherbinina O.V., Shakhova V.V., Belova G.I., Aravind L., Natale D.A.,
RA Rogozin I.B., Tatusov R.L., Wolf Y.I., Stetter K.O., Malykh A.G.,
RA Koonin E.V., Kozyavkin S.A.;
RT "The complete genome of hyperthermophile Methanopyrus kandleri AV19 and
RT monophyly of archaeal methanogens.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:4644-4649(2002).
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:0000255|HAMAP-Rule:MF_00700}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00700};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00700};
CC -!- SUBUNIT: Heterodimer of a small subunit (PriS) and a large subunit
CC (PriL). {ECO:0000255|HAMAP-Rule:MF_00700}.
CC -!- SIMILARITY: Belongs to the eukaryotic-type primase small subunit
CC family. {ECO:0000255|HAMAP-Rule:MF_00700}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM01801.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AE009439; AAM01801.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; Q8TXS4; -.
DR SMR; Q8TXS4; -.
DR EnsemblBacteria; AAM01801; AAM01801; MK0586.
DR KEGG; mka:MK0586; -.
DR HOGENOM; CLU_878822_0_0_2; -.
DR Proteomes; UP000001826; 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 HAMAP; MF_00700; DNA_primase_sml_arc; 1.
DR InterPro; IPR023639; DNA_primase_ssu_PriS.
PE 3: Inferred from homology;
KW DNA replication; DNA-directed RNA polymerase; Magnesium; Manganese;
KW Metal-binding; Nucleotidyltransferase; Primosome; Reference proteome;
KW Transcription; Transferase.
FT CHAIN 1..296
FT /note="DNA primase small subunit PriS"
FT /id="PRO_0000046743"
FT ACT_SITE 82
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00700"
FT ACT_SITE 84
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00700"
FT ACT_SITE 191
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00700"
SQ SEQUENCE 296 AA; 33662 MW; 7619D544064CFC4A CRC64;
MDVKTLVGEY YASLPSGVLR EFVEDPSSRE WAYTFLKGRD IVFTRKRRLD EVSGFLELYH
STGKFKNPKS WEGLLGWDLV IDVDAELPEE PEAFLKSLGR LLKDVVIACD ELRRALGFPR
PDVVNFSGSK GFHVRYFDST VRRWLRWDLH ERRGIKPGEI IQRVGRGVVW LAREGFVAGD
RVRALREGLL DDSMYDLKRL IRCVGSMNVK SLLPAVPVWS REGGRWVDFR DEVLGMNDLE
LGCLVAHRTL TWPGRGGLGV VLSRVLDLDT DADPEDPSDF VEVWGNVMSV LGELKP