ID A0A1F2P605_9EURY Unreviewed; 398 AA.
AC A0A1F2P605;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
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 ECO:0000313|EMBL:HEC56446.1};
GN ORFNames=ENI32_00950 {ECO:0000313|EMBL:HEC56446.1}, SBU_001013
GN {ECO:0000313|EMBL:OFV66076.1};
OS Candidatus Syntrophoarchaeum butanivorans.
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinales incertae sedis; ANME-2 cluster;
OC Syntrophoarchaeum.
OX NCBI_TaxID=1839936 {ECO:0000313|EMBL:OFV66076.1, ECO:0000313|Proteomes:UP000185779};
RN [1] {ECO:0000313|EMBL:OFV66076.1, ECO:0000313|Proteomes:UP000185779}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BOX1 {ECO:0000313|EMBL:OFV66076.1};
RA Laso-Perez R., Richter M., Wegener G., Musat F.;
RT "Microbial consortia oxidize butane by reversing methanogenesis.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:HEC56446.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HyVt-386 {ECO:0000313|EMBL:HEC56446.1};
RX PubMed=31911466;
RA Zhou Z., Liu Y., Xu W., Pan J., Luo Z.H., Li M.;
RT "Genome- and Community-Level Interaction Insights into Carbon Utilization
RT and Element Cycling Functions of Hydrothermarchaeota in Hydrothermal
RT Sediment.";
RL mSystems 5:e00795-e00719(2020).
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:OFV66076.1}.
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DR EMBL; DRIE01000013; HEC56446.1; -; Genomic_DNA.
DR EMBL; LYOR01000004; OFV66076.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F2P605; -.
DR STRING; 1839936.SBU_001013; -.
DR PATRIC; fig|1839936.3.peg.1022; -.
DR Proteomes; UP000185779; Unassembled WGS sequence.
DR Proteomes; UP000885936; 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 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:UP000185779};
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 95
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00700"
FT ACT_SITE 97
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00700"
FT ACT_SITE 296
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00700"
SQ SEQUENCE 398 AA; 45773 MW; 29B7B5F30FC94B13 CRC64;
MDERTRAFVK SIFRAYYRRE DIKMPLKFDR REWGFMPFEE GRMHRHKAFR TKRDVIEYLR
DEVPRHVYYS SAVYTDPSAP KMAEKGWEGA ELIFDLDADH LQIKAGSYEE MLDAVKKETI
KLLRFLEDDF GFSQDDIEIA FSGGRGYHVH VYHPKVWKLT SPERREIVDY ITARGLDLDR
IFRPKYSIVG DSGEGGTKDA KLTKIIHTSS WGERIHQGLV EFMEELSEME EDEAIEYLSG
IKGLGKKRAK KLLEVAKDKT QVNAIKDGNI IAKKIPTPIW RYIIEGRMRV ELGEVDEPVT
ADIKRLIRLP TSLHGGSSLK VVPLTRDAFN DFDPLVDAVA FDKGEITIDL TREASISLND
ENYSFDPGIN DVPLAVGLFL ICRGMAEFKE IRGNKLIF
//
