ID A0A0D2JMB5_9BACT Unreviewed; 586 AA.
AC A0A0D2JMB5;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 42.
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=J120_00830 {ECO:0000313|EMBL:KIX85503.1};
OS candidate division TM6 bacterium JCVI TM6SC1.
OC Bacteria; Candidatus Dependentiae; Vermiphilus.
OX NCBI_TaxID=1306947 {ECO:0000313|EMBL:KIX85503.1, ECO:0000313|Proteomes:UP000032214};
RN [1] {ECO:0000313|EMBL:KIX85503.1, ECO:0000313|Proteomes:UP000032214}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TM6SC1 {ECO:0000313|EMBL:KIX85503.1,
RC ECO:0000313|Proteomes:UP000032214};
RX PubMed=23754396; DOI=10.1073/pnas.1219809110;
RA McLean J.S., Lombardo M.J., Badger J.H., Edlund A., Novotny M.,
RA Yee-Greenbaum J., Vyahhi N., Hall A.P., Yang Y., Dupont C.L., Ziegler M.G.,
RA Chitsaz H., Allen A.E., Yooseph S., Tesler G., Pevzner P.A., Friedman R.M.,
RA Nealson K.H., Venter J.C., Lasken R.S.;
RT "Candidate phylum TM6 genome recovered from a hospital sink biofilm
RT provides genomic insights into this uncultivated phylum.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:E2390-E2399(2013).
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|HAMAP-Rule:MF_00974,
CC ECO:0000256|PIRNR:PIRNR002811, ECO:0000256|PIRSR:PIRSR002811-1};
CC Note=Binds 1 zinc ion per monomer. {ECO:0000256|HAMAP-Rule:MF_00974,
CC ECO:0000256|PIRNR:PIRNR002811, ECO:0000256|PIRSR:PIRSR002811-1};
CC -!- SUBUNIT: Monomer. Interacts with DnaB. {ECO:0000256|HAMAP-
CC Rule:MF_00974}.
CC -!- DOMAIN: Contains an N-terminal zinc-binding domain, a central core
CC domain that contains the primase activity, and a C-terminal DnaB-
CC binding domain. {ECO:0000256|HAMAP-Rule:MF_00974}.
CC -!- SIMILARITY: Belongs to the DnaG primase family. {ECO:0000256|HAMAP-
CC Rule:MF_00974, ECO:0000256|PIRNR:PIRNR002811}.
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:KIX85503.1}.
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DR EMBL; ARQD01000001; KIX85503.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D2JMB5; -.
DR STRING; 1306947.J120_00830; -.
DR eggNOG; COG0358; Bacteria.
DR Proteomes; UP000032214; 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:UniProtKB-UniRule.
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; IPR016136; DNA_helicase_N/primase_C.
DR InterPro; IPR037068; DNA_primase_core_N_sf.
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; PF08275; DNAG_N; 1.
DR Pfam; PF13155; Toprim_2; 1.
DR Pfam; PF01807; zf-CHC2; 1.
DR PIRSF; PIRSF002811; DnaG; 1.
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 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, ECO:0000256|HAMAP-
KW Rule:MF_00974};
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 Reference proteome {ECO:0000313|Proteomes:UP000032214};
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|HAMAP-Rule:MF_00974};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|HAMAP-
KW Rule:MF_00974}.
FT DOMAIN 254..335
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT ZN_FING 34..58
FT /note="CHC2-type"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00974,
FT ECO:0000256|PIRSR:PIRSR002811-1"
SQ SEQUENCE 586 AA; 66197 MW; 240069FCEB3809BF CRC64;
MNIFSYIKSH VPILEVISGY VTLKRMGGYW KGPCPFHQER TASFTVSPAK DIFYCFGCHV
GGDVIAFTAK LESCSHLQAA HMLAEKFQLE LPEQIRSNIS SSMSDKEQHT KICTLFAQWC
AQELEKHHNA LNYLKLRTIN AQSLSTFCLG YVPSGSSGIK NLVQTMSQHN IMAKDLIQSG
IVQEGKHGLY CPFEDRIIFP IKDLVGRICG FGGRVFKTND TRAKYYNSKE HAFFDKGTIL
FGIDQAKKSM QSSGYVTLVE GYMDCIAMVQ HGYTNTVATL GTACTQMHLE QLARFVPKVI
ILYDSDKAGQ QALIRLAHMC WSVNLELYVA RLQAGHDPAS YLAAGLDIRP ALESATPIMT
FFISTIGDHY ENMSLADKMD ATQKIIEVIA KTPNLLRQEL LLEQACSHLN LPIGALRQEL
KKYSSGDIPE PSTVARESLP VAPETIDVHE DKVLEEKIFY AIMNNINLFR ELDQDFLINF
MAQPFADILK LLQHYSTEHN NITFGNFFDT LDDSSKQLVS QHLLKTYQET DLATTARLVL
FMKKRYWKEF IGSLKKRISQ AEKEKNFAKA AALVQQFVTL KKEWSL
//
