ID A0A1I0FSA7_9BACI Unreviewed; 606 AA.
AC A0A1I0FSA7;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
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=SAMN05216389_11717 {ECO:0000313|EMBL:SET61089.1};
OS Oceanobacillus limi.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Oceanobacillus.
OX NCBI_TaxID=930131 {ECO:0000313|EMBL:SET61089.1, ECO:0000313|Proteomes:UP000198618};
RN [1] {ECO:0000313|EMBL:SET61089.1, ECO:0000313|Proteomes:UP000198618}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBRC-M 10780 {ECO:0000313|EMBL:SET61089.1,
RC ECO:0000313|Proteomes:UP000198618};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FOHE01000017; SET61089.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I0FSA7; -.
DR STRING; 930131.SAMN05216389_11717; -.
DR Proteomes; UP000198618; 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:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
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; 6.10.140.360; -; 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; IPR036185; DNA_heli_DnaB-like_N_sf.
DR InterPro; IPR007693; DNA_helicase_DnaB-like_N.
DR InterPro; IPR016136; DNA_helicase_N/primase_C.
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; PF00772; DnaB; 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; 1.
DR SMART; SM00493; TOPRIM; 1.
DR SMART; SM00400; ZnF_CHCC; 1.
DR SUPFAM; SSF56731; DNA primase core; 1.
DR SUPFAM; SSF48024; N-terminal domain of DnaB helicase; 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:UP000198618};
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 263..344
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT ZN_FING 44..68
FT /note="CHC2-type"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00974,
FT ECO:0000256|PIRSR:PIRSR002811-1"
SQ SEQUENCE 606 AA; 69803 MW; CC62AC7600DDB2A9 CRC64;
MVMDMSNQIP EDVIEDIRKS NDIVDVIGEY VQLKKQGRNY FGLCPFHGEK TPSFSVTQEK
QIFHCFGCGK GGNVVSFIME IESFSFFEAI KHLADRSGVS LPETAVQRDS TLSQESQSML
SAYDWLTKLY HHLLRYTKDG KDGYRYFRDR GITDETIDTF QLGFAPNIKD FTATFLEKKG
FHQQLLIKSG ILTLKDDDSV SDRFRGRVIY PIRNHLGKTV AFGGRTITDQ GPKYLNSSES
ELFHKGRILY NFDLAKKHIR KTNEVILFEG QMDVISSYQA GINNVVATMG TALTESQAKL
LRRYVDKVII CYDADHAGIE ATYKAATLLQ SVGCQVKIAR MNNGMDPDEF IRENGADSFR
TEVIETSDTF LTFYMNYLKK DYNLSLEGDR IQYIEMVIKE LAKIDSPIER EYYVKELSNE
YGLMMDTLLE QVHTYREKSS SPKDKSTKER YTKKVQNQYQ KRKLLPAYHN AERKLLAYML
QDRTITDKVQ EELGASFNID EHKIIATHLY AYYEEGLPVD VSLFVERLTD EKLKHLVIEL
AMLPVYEEIS DAEINDYIRI IRSQSSEVAS IKQLKDEQRL AEQQQDPIKA AQIAMQIIEL
KKQVKN
//
