ID A0A164J9A5_9NOCA Unreviewed; 643 AA.
AC A0A164J9A5;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 31-JUL-2019, entry version 20.
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=A2J03_09495 {ECO:0000313|EMBL:KZF01749.1};
OS Rhodococcus sp. EPR-157.
OC Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=1813677 {ECO:0000313|EMBL:KZF01749.1, ECO:0000313|Proteomes:UP000077673};
RN [1] {ECO:0000313|EMBL:KZF01749.1, ECO:0000313|Proteomes:UP000077673}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EPR-157 {ECO:0000313|EMBL:KZF01749.1,
RC ECO:0000313|Proteomes:UP000077673};
RA Ploux O.;
RL Submitted (MAR-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
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}.
CC -!- CAUTION: The sequence shown here is derived from an
CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC preliminary data. {ECO:0000313|EMBL:KZF01749.1}.
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DR EMBL; LVCV01000517; KZF01749.1; -; Genomic_DNA.
DR RefSeq; WP_068378811.1; NZ_LVCV01000517.1.
DR EnsemblBacteria; KZF01749; KZF01749; A2J03_09495.
DR Proteomes; UP000077673; Unassembled WGS sequence.
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; 3.90.580.10; -; 1.
DR Gene3D; 3.90.980.10; -; 1.
DR HAMAP; MF_00974; DNA_primase_DnaG; 1.
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; IPR013173; DNA_primase_DnaG_DnaB-bd_dom.
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; PF08278; DnaG_DnaB_bind; 1.
DR Pfam; PF13662; Toprim_4; 1.
DR Pfam; PF08275; Toprim_N; 1.
DR Pfam; PF01807; zf-CHC2; 1.
DR PIRSF; PIRSF002811; DnaG; 1.
DR SMART; SM00766; DnaG_DnaB_bind; 1.
DR SMART; SM00493; TOPRIM; 1.
DR SMART; SM00400; ZnF_CHCC; 1.
DR TIGRFAMs; TIGR01391; dnaG; 1.
DR PROSITE; PS50880; TOPRIM; 1.
PE 3: Inferred from homology;
KW Complete proteome {ECO:0000313|Proteomes:UP000077673};
KW DNA replication {ECO:0000256|HAMAP-Rule:MF_00974,
KW ECO:0000256|PIRNR:PIRNR002811, ECO:0000256|SAAS:SAAS00993445};
KW DNA-binding {ECO:0000256|HAMAP-Rule:MF_00974,
KW ECO:0000256|SAAS:SAAS00709369};
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:UP000077673};
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 263 349 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}.
FT REGION 443 480 Disordered. {ECO:0000256|SAM:MobiDB-
FT lite}.
FT COMPBIAS 443 463 Polyampholyte. {ECO:0000256|SAM:MobiDB-
FT lite}.
SQ SEQUENCE 643 AA; 70102 MW; EDD89E92C12C88AD CRC64;
MAGRIPERDI AAIRERTRIE DVVGDYVSLK RAGGDSMKGL CPFHDEKSPS FHVRPNHGHF
HCFGCGEGGD AYSFLQKIEH ISFVEAVEQL ADRLNYSITY EGGGPSVQRD RGTRARLIAA
NSAAQEFYAA RLREPDAQTA RDYLTERNFD GQAALTYGCG YAPDGWDTLT KHLLSSGFEA
KEIIDAGLAT PGKRGTPIDR FRRRLVWPIR SQSGDVIGFG ARKLFDDDTM PGKYINTPET
MLYKKSQVLF GLDLARKDIA KSHQAVIVEG YTDVMAMHLA GVKTAVASCG TAFGEDHLAM
LRRLMMDDSY FRGEVIYTFD GDAAGQAAAM KAFEGDQKIA GQTFVAVAPD GMDPCELRQK
SGDGAVRDLV ARRTPMFAFV VKSLLSEHDL DTPEGRVEAL RRTVPVVARI KDASLRDEYA
RQLAGWTGWD DTAMVLARVR DEAKKNARGG GDAKGKRVPF EKRQAPTPEV PAGPVRPQPT
DPSLWPQREA LKSALQNPAI AGSVFDSLPP ETFTHPAYAA VSQAVTAAGG TAAGLGGGEW
VDAVAKRAET PVVKSLVMEL AVEHIPVADI ALTRYIGGVL ARLQEVWVGE QVAELKSKMQ
RMSPQVNPDE YYALLGDVIA LEQYRRSLLE QAIGNVEDAS EAG
//
