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Database: UniProt
Entry: A0A0U2U455_9BACL
LinkDB: A0A0U2U455_9BACL
Original site: A0A0U2U455_9BACL 
ID   A0A0U2U455_9BACL        Unreviewed;       611 AA.
AC   A0A0U2U455;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   31-JUL-2019, entry version 21.
DE   RecName: Full=DNA primase {ECO:0000256|HAMAP-Rule:MF_00974, ECO:0000256|PIRNR:PIRNR002811, ECO:0000256|SAAS:SAAS00993443};
DE            EC=2.7.7.- {ECO:0000256|HAMAP-Rule:MF_00974, ECO:0000256|PIRNR:PIRNR002811, ECO:0000256|SAAS:SAAS00993444};
GN   Name=dnaG {ECO:0000256|HAMAP-Rule:MF_00974};
GN   ORFNames=IJ22_09390 {ECO:0000313|EMBL:ALS21321.1}, PN4B1_25040
GN   {ECO:0000313|EMBL:GCL72577.1};
OS   Paenibacillus naphthalenovorans.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae;
OC   Paenibacillus.
OX   NCBI_TaxID=162209 {ECO:0000313|EMBL:ALS21321.1, ECO:0000313|Proteomes:UP000061660};
RN   [1] {ECO:0000313|Proteomes:UP000061660}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=32O-Y {ECO:0000313|Proteomes:UP000061660};
RA   Butler R.III., Wang J., Stark B.C., Pombert J.-F.;
RT   "Complete genome sequences of two moderately thermophilic
RT   Paenibacillus species.";
RL   Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ALS21321.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=32O-Y {ECO:0000313|EMBL:ALS21321.1};
RA   Shamseldin A., Moawad H., Abd El-Rahim W.M., Sadowsky M.J.;
RL   Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:ALS21321.1, ECO:0000313|Proteomes:UP000061660}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=32O-Y {ECO:0000313|EMBL:ALS21321.1,
RC   ECO:0000313|Proteomes:UP000061660};
RX   PubMed=26868401;
RA   Butler R.R.III., Wang J., Stark B.C., Pombert J.F.;
RT   "Complete Genome Sequences of Two Interactive Moderate Thermophiles,
RT   Paenibacillus napthalenovorans 32O-Y and Paenibacillus sp. 32O-W.";
RL   Genome Announc. 4:e01717-15(2016).
RN   [4] {ECO:0000313|EMBL:GCL72577.1, ECO:0000313|Proteomes:UP000299945}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=4B1 {ECO:0000313|EMBL:GCL72577.1,
RC   ECO:0000313|Proteomes:UP000299945};
RA   Ha-Thanh L.T., Ngoc-Thi T.V., Shintani M., Moriuchi R., Dohra H.,
RA   Hoang-Loc N., Kimbara K.;
RT   "Isolation and characterization of a moderate thermophilic
RT   Paenibacillus naphthalenovorans strain 4B1 capable of degrading
RT   dibenzofuran from dioxin-contaminated soil in Vietnam.";
RL   Submitted (MAR-2019) 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
CC       replication. {ECO:0000256|HAMAP-Rule:MF_00974,
CC       ECO:0000256|PIRNR:PIRNR002811, ECO:0000256|SAAS:SAAS00709340}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|SAAS:SAAS00709317};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00974, ECO:0000256|PIRNR:PIRNR002811,
CC         ECO:0000256|PIRSR:PIRSR002811-1};
CC       Note=Binds 1 zinc ion per monomer. {ECO:0000256|HAMAP-
CC       Rule:MF_00974, ECO:0000256|PIRNR:PIRNR002811,
CC       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.
CC       {ECO:0000256|HAMAP-Rule:MF_00974, ECO:0000256|PIRNR:PIRNR002811,
CC       ECO:0000256|SAAS:SAAS00709351}.
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DR   EMBL; CP013652; ALS21321.1; -; Genomic_DNA.
DR   EMBL; BJCS01000006; GCL72577.1; -; Genomic_DNA.
DR   RefSeq; WP_062407576.1; NZ_FNDY01000002.1.
DR   EnsemblBacteria; ALS21321; ALS21321; IJ22_09390.
DR   KEGG; pnp:IJ22_09390; -.
DR   PATRIC; fig|162209.4.peg.1000; -.
DR   KO; K02316; -.
DR   OrthoDB; 1071997at2; -.
DR   Proteomes; UP000061660; Chromosome.
DR   Proteomes; UP000299945; Unassembled WGS sequence.
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; 1.10.860.10; -; 1.
DR   Gene3D; 3.90.580.10; -; 1.
DR   Gene3D; 3.90.980.10; -; 1.
DR   HAMAP; MF_00974; DNA_primase_DnaG; 1.
DR   InterPro; IPR036185; DNA_heli_DnaB-like_N_sf.
DR   InterPro; IPR016136; DNA_helicase_N/primase_C.
DR   InterPro; IPR013264; DNA_primase_core_N.
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; IPR034151; TOPRIM_DnaG_bac.
DR   InterPro; IPR006171; TOPRIM_domain.
DR   InterPro; IPR002694; Znf_CHC2.
DR   Pfam; PF10410; DnaB_bind; 1.
DR   Pfam; PF08275; Toprim_N; 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; SSF48024; SSF48024; 1.
DR   TIGRFAMs; TIGR01391; dnaG; 1.
DR   PROSITE; PS50880; TOPRIM; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000061660,
KW   ECO:0000313|Proteomes:UP000299945};
KW   DNA replication {ECO:0000256|HAMAP-Rule:MF_00974,
KW   ECO:0000256|PIRNR:PIRNR002811, ECO:0000256|SAAS:SAAS00740714};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_00974,
KW   ECO:0000256|SAAS:SAAS00740674};
KW   DNA-directed RNA polymerase {ECO:0000256|HAMAP-Rule:MF_00974,
KW   ECO:0000256|PIRNR:PIRNR002811, ECO:0000256|SAAS:SAAS00709327};
KW   Magnesium {ECO:0000256|SAAS:SAAS00709345};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00974,
KW   ECO:0000256|PIRNR:PIRNR002811, ECO:0000256|PIRSR:PIRSR002811-1,
KW   ECO:0000256|SAAS:SAAS00709338};
KW   Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_00974,
KW   ECO:0000256|PIRNR:PIRNR002811, ECO:0000256|SAAS:SAAS00709339};
KW   Primosome {ECO:0000256|HAMAP-Rule:MF_00974,
KW   ECO:0000256|PIRNR:PIRNR002811, ECO:0000256|SAAS:SAAS00709304};
KW   Reference proteome {ECO:0000313|Proteomes:UP000061660};
KW   Transcription {ECO:0000256|HAMAP-Rule:MF_00974,
KW   ECO:0000256|PIRNR:PIRNR002811, ECO:0000256|SAAS:SAAS00709341};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00974,
KW   ECO:0000256|PIRNR:PIRNR002811, ECO:0000256|SAAS:SAAS00993442};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_00974, ECO:0000256|PIRNR:PIRNR002811,
KW   ECO:0000256|PIRSR:PIRSR002811-1, ECO:0000256|SAAS:SAAS00709300};
KW   Zinc-finger {ECO:0000256|HAMAP-Rule:MF_00974,
KW   ECO:0000256|PIRSR:PIRSR002811-1, ECO:0000256|SAAS:SAAS00709301}.
FT   DOMAIN      263    344       Toprim. {ECO:0000259|PROSITE:PS50880}.
FT   ZN_FING      41     65       CHC2-type. {ECO:0000256|HAMAP-Rule:
FT                                MF_00974, ECO:0000256|PIRSR:PIRSR002811-
FT                                1}.
SQ   SEQUENCE   611 AA;  69145 MW;  FF2996F36BF6EC29 CRC64;
     MSNGRIPEHV IDAVLKAHDI VEIVGRHVHL TKQGHYLKGL CPFHSEKTPS FTVTPERQIY
     HCFGCGAGGN AIRFISEVEG LSFGQAVRKL ANEANLDVGF GLQNAQEETK EQAERAKLLE
     GYEMAAKLYQ YILHNTEQGK AAKAYLRDRG MNDKLIETFG LGYAPARWDT LTNLLDKKQY
     FLPLMEQGGL LSAKHDGNGY VDKFRDRIMF PIYDWKGQVI AFGGRAMGNV QPKYLNSPES
     MLFHKSRTLY NLHLARPQIR KTQEIVLFEG YMDVIRAWEA GIKNGVATMG TALTSEQAES
     IRRLAERVTV VYDGDQAGQT AAYKSIPLLE NAGCQVRIAM LPDALDPDEY IAKYGSERFV
     REVIETAVPS IKYKLLYFRN NYRLQEDGEK LRYIKQALKL IAGLSSPIER EHYLRELSSE
     FRYSLEALQQ NLNEIRLQTE KNVRSGDNNG NPWNNVMNNG KPRKEIPSMV PAYQFAERQL
     LAVMMLDRDI AGYVERRLGD GFNVEAHAAL AAYLYSYYAQ GYEPNAGTFI GMLQDDKLES
     LASSLTLIDN RNGINDAVID DYIREIKKYP LLQSLELKKE EVKQAERSGD IPRALQLGSE
     IISLEKQLKS S
//
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