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Database: UniProt
Entry: A0A0B2A9M2_9MICO
LinkDB: A0A0B2A9M2_9MICO
Original site: A0A0B2A9M2_9MICO 
ID   A0A0B2A9M2_9MICO        Unreviewed;       622 AA.
AC   A0A0B2A9M2;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   16-JAN-2019, entry version 28.
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=LK09_04665 {ECO:0000313|EMBL:KHK98321.1};
OS   Microbacterium mangrovi.
OC   Bacteria; Actinobacteria; Micrococcales; Microbacteriaceae;
OC   Microbacterium.
OX   NCBI_TaxID=1348253 {ECO:0000313|EMBL:KHK98321.1, ECO:0000313|Proteomes:UP000031030};
RN   [1] {ECO:0000313|EMBL:KHK98321.1, ECO:0000313|Proteomes:UP000031030}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MUSC 115 {ECO:0000313|EMBL:KHK98321.1,
RC   ECO:0000313|Proteomes:UP000031030};
RA   Lee L.-H.;
RT   "Genome sequence of Microbacterium mangrovi MUSC 115(T).";
RL   Submitted (NOV-2014) 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:KHK98321.1}.
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DR   EMBL; JTDK01000006; KHK98321.1; -; Genomic_DNA.
DR   RefSeq; WP_039396620.1; NZ_JTDK01000006.1.
DR   EnsemblBacteria; KHK98321; KHK98321; LK09_04665.
DR   OrthoDB; 1071997at2; -.
DR   Proteomes; UP000031030; 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; 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; PF13662; Toprim_4; 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   TIGRFAMs; TIGR01391; dnaG; 1.
DR   PROSITE; PS50880; TOPRIM; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000031030};
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:UP000031030};
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      262    348       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   622 AA;  67844 MW;  AE5EB41D07940522 CRC64;
     MAGRIVQADV DEVKSRTNIA DIIGEHVALK SAGVGSMKGL CPFHDERSPS FNVRPQVGFY
     HCFGCGESGD VYTFLRKIDH LSFTEAVERL AARIGYALHY EDGGGPAPES SGRARLYAAN
     SAAAEWFRTQ LMTPGADAAR RFLGERGFDA GAAAHFGVGY APQGWSHMLD ALTAQGYSRD
     ELLAAGLVSQ GQRGVYDRFR GRVIWPIRDV TGQTVGFGAR RLFDDDNGPK YLNTPETTLY
     RKTQVLYGLD LAKRDISRGD PRRVVVVEGY TDVMACHLAG ITTAVATCGT AFGSEHMNIV
     RRVMGDDSGA EVVFTFDPDA AGQKAAVRAF AETRGLKAQS YVAVAPEGLD PCDLRLKRGD
     GAVRALMDTK VPMFEFVIDQ RLSGFDLATV EGRVGALRSA AEVVAGIRDD IIRAEYERVL
     ARRIGMAPDE VHRAVKSAAR RADSREADGP RRFATPVADA AAEPAPPIER VTMASLPFEA
     ALERDALMGL LQFGHRLDRS EFDRAAAQPF RHPALDAVRQ VIAACDPERT GWSVEAVSSV
     REPYRSLAAE LLTAQFPARD DEHAVASTRA MARQLVRRSL DAEKQELLGA VQRIPANSDG
     GRAVRLRLRE LDAERQRLLD EE
//
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