ID A0A1F8RM87_9CHLR Unreviewed; 636 AA.
AC A0A1F8RM87;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=DNA primase {ECO:0000256|HAMAP-Rule:MF_00974, ECO:0000256|PIRNR:PIRNR002811};
DE EC=2.7.7.101 {ECO:0000256|HAMAP-Rule:MF_00974};
GN Name=dnaG {ECO:0000256|HAMAP-Rule:MF_00974};
GN ORFNames=A2W34_05200 {ECO:0000313|EMBL:OGO48793.1};
OS Chloroflexi bacterium RBG_16_64_32.
OC Bacteria; Chloroflexota.
OX NCBI_TaxID=1797658 {ECO:0000313|EMBL:OGO48793.1, ECO:0000313|Proteomes:UP000179752};
RN [1] {ECO:0000313|EMBL:OGO48793.1, ECO:0000313|Proteomes:UP000179752}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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|HAMAP-Rule:MF_00974, ECO:0000256|PIRNR:PIRNR002811}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ssDNA + n NTP = ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate.;
CC EC=2.7.7.101; Evidence={ECO:0000256|HAMAP-Rule:MF_00974};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRNR:PIRNR002811,
CC ECO:0000256|PIRSR:PIRSR002811-1};
CC Note=Binds 1 zinc ion per monomer. {ECO:0000256|PIRNR:PIRNR002811,
CC ECO:0000256|PIRSR:PIRSR002811-1};
CC -!- SUBUNIT: Monomer. Interacts with DnaB. {ECO:0000256|HAMAP-
CC Rule:MF_00974}.
CC -!- SIMILARITY: Belongs to the DnaG primase family. {ECO:0000256|HAMAP-
CC Rule:MF_00974, ECO:0000256|PIRNR:PIRNR002811}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00974}.
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:OGO48793.1}.
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DR EMBL; MGNZ01000016; OGO48793.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F8RM87; -.
DR STRING; 1797658.A2W34_05200; -.
DR Proteomes; UP000179752; 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:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003896; F:DNA primase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd03364; TOPRIM_DnaG_primases; 1.
DR Gene3D; 3.40.1360.10; -; 1.
DR Gene3D; 3.90.980.10; DNA primase, catalytic core, N-terminal domain; 1.
DR Gene3D; 3.90.580.10; Zinc finger, CHC2-type domain; 1.
DR HAMAP; MF_00974; DNA_primase_DnaG; 1.
DR InterPro; IPR037068; DNA_primase_core_N_sf.
DR InterPro; IPR019475; DNA_primase_DnaB-bd.
DR InterPro; IPR006295; DNA_primase_DnaG.
DR InterPro; IPR036977; DNA_primase_Znf_CHC2.
DR InterPro; IPR030846; DnaG_bac.
DR InterPro; IPR013264; DNAG_N.
DR InterPro; IPR034151; TOPRIM_DnaG_bac.
DR InterPro; IPR006171; TOPRIM_domain.
DR InterPro; IPR002694; Znf_CHC2.
DR NCBIfam; TIGR01391; dnaG; 1.
DR PANTHER; PTHR30313; DNA PRIMASE; 1.
DR PANTHER; PTHR30313:SF2; DNA PRIMASE; 1.
DR Pfam; PF10410; DnaB_bind; 1.
DR Pfam; PF08275; DNAG_N; 1.
DR Pfam; PF13155; Toprim_2; 1.
DR Pfam; PF01807; zf-CHC2; 1.
DR PIRSF; PIRSF002811; DnaG; 2.
DR SMART; SM00493; TOPRIM; 1.
DR SMART; SM00400; ZnF_CHCC; 1.
DR SUPFAM; SSF56731; DNA primase core; 1.
DR SUPFAM; SSF57783; Zinc beta-ribbon; 1.
DR PROSITE; PS50880; TOPRIM; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705, ECO:0000256|HAMAP-
KW Rule:MF_00974};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW Rule:MF_00974};
KW DNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022478,
KW ECO:0000256|HAMAP-Rule:MF_00974};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRNR:PIRNR002811};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, ECO:0000256|HAMAP-
KW Rule:MF_00974};
KW Primosome {ECO:0000256|ARBA:ARBA00022515, ECO:0000256|HAMAP-Rule:MF_00974};
KW Transcription {ECO:0000256|ARBA:ARBA00023163, ECO:0000256|HAMAP-
KW Rule:MF_00974};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00974};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRNR:PIRNR002811};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PIRSR:PIRSR002811-
KW 1}.
FT DOMAIN 251..338
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT ZN_FING 34..59
FT /note="CHC2-type"
FT /evidence="ECO:0000256|PIRSR:PIRSR002811-1"
FT REGION 444..466
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 543..579
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 636 AA; 70728 MW; EF591B20F356F955 CRC64;
MNEIEEVKAR LDIADVVGQY VQLQRAGRSY KAPCPFHSEK TPSFFVSPDR QSWHCFGACG
TGGDVFSFVM RREGIEFSEA LGVLAARAGV ALPERQRRPE EERERERSYA ANEAAARWYH
ELLVSGDPGK AAREYIQGRG VDEPTAEAFL VGFSPPSWEA TREQLRERGF SDAELLSAGL
LVEGDKGLHD RFRGRLMFPI RDARGRFVGF GARALDDSVP KYLNTAQTAT FDKGSMLYAL
ERAQDGIRRE GCAVIVEGYM DAIACHQRGF DNAVATMGTS LTERQVRLLK RQTGNIVLAL
DADAAGSEAA LRGHEVVDEA MRQGSDRETV PVLTWRGLVR YQDAASVDLR VAVLPEGSDP
DDVIQSDPAA WRELIAAARP VLDYRFDAVA TRHDLSMPRG RSEAVQELLP LLEPITDAVV
RAHYLQRLSR LSLVREAELS RMVSRRRGSR RPPVSDMETP SLDNARGDTR REGFLLALLL
RFPHLREAGL EFPDVLLTES ENREVLAAWK RCPELDVVKN SLPEELNGYL ERLVDWRLPK
YAVKEAEAAL LDCRQRLERR QVEAEKQMTA ALLAATEEEL GASSLVEAVV SDTEDADETV
REAVNLHRRD LETGLRLHGK EGNVEGGGAA KTTVNG
//
