ID A0A135VJ76_9ARCH Unreviewed; 462 AA.
AC A0A135VJ76;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 24-JAN-2024, entry version 21.
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=AM325_00855 {ECO:0000313|EMBL:KXH72613.1};
OS Candidatus Thorarchaeota archaeon SMTZ1-45.
OC Archaea; Asgard group; Candidatus Thorarchaeota.
OX NCBI_TaxID=1706444 {ECO:0000313|EMBL:KXH72613.1, ECO:0000313|Proteomes:UP000070149};
RN [1] {ECO:0000313|EMBL:KXH72613.1, ECO:0000313|Proteomes:UP000070149}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SMTZ1-45 {ECO:0000313|EMBL:KXH72613.1};
RX PubMed=26824177;
RA Seitz K.W., Lazar C.S., Hinrichs K.U., Teske A.P., Baker B.J.;
RT "Genomic reconstruction of a novel, deeply branched sediment archaeal
RT phylum with pathways for acetogenesis and sulfur reduction.";
RL ISME J. 0:0-0(2016).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KXH72613.1}.
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DR EMBL; LRSL01000069; KXH72613.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A135VJ76; -.
DR STRING; 1706444.AM325_00855; -.
DR Proteomes; UP000070149; Unassembled WGS sequence.
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 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; 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|HAMAP-Rule:MF_00700,
KW ECO:0000256|RuleBase:RU003514};
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|HAMAP-Rule:MF_00700};
KW Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_00700};
KW Primosome {ECO:0000256|HAMAP-Rule:MF_00700, ECO:0000256|RuleBase:RU003514};
KW Transcription {ECO:0000256|HAMAP-Rule:MF_00700};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00700}.
FT ACT_SITE 147
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00700"
FT ACT_SITE 149
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00700"
FT ACT_SITE 364
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00700"
SQ SEQUENCE 462 AA; 52474 MW; B48F2E7BF77AE044 CRC64;
MPNQNQGFTS TVLKLRFMFH EYYKSNPNSI DVPDKIHNRE FGIQSWEYNW FCPVRKSRDE
SGHDITTGCG QSGTSLSNIK KCPNCGSDEI QTTTWRRHVG YLNRDELIRD LTSVAPHSVY
HSAAFYKIPV ARHMDEKEWF GAELVFDIDA DHLDLSCAKD HDAWRCNEKE CHKTGTGIHP
ENCPDCGGKS FSTRKWICEN CLGEAKKYTV KLYDKFIVND FGFDPELVQL NYSGHRGYHV
RVRDPRVYSL DSNSRIQIVH YIMGLGLNTE KVIVTQGRVN RVPDRDFPGW AGKIADAIVE
FVRNIDSYNG TERWVKSLRK GKVAALDGLL RNPPILNPEA KDIGLKSWQE IAEKAAELYG
GEIDRPVTHD IHRVIRLIGS LNGKTGFLVS QLNRDELDDF DPFRDAIAFN DGQMKIKFLQ
KSSGVPRFRI GDETYGPYHG ESVELPTPAA AFVLCKGVAI IE
//
