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Database: UniProt
Entry: A0A1I3A1K3_9MICO
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ID   A0A1I3A1K3_9MICO        Unreviewed;       621 AA.
AC   A0A1I3A1K3;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   31-JUL-2019, entry version 9.
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=E3O11_12625 {ECO:0000313|EMBL:TFB82717.1},
GN   SAMN05216274_105113 {ECO:0000313|EMBL:SFH43805.1};
OS   Cryobacterium levicorallinum.
OC   Bacteria; Actinobacteria; Micrococcales; Microbacteriaceae;
OC   Cryobacterium.
OX   NCBI_TaxID=995038 {ECO:0000313|EMBL:SFH43805.1, ECO:0000313|Proteomes:UP000199681};
RN   [1] {ECO:0000313|EMBL:SFH43805.1, ECO:0000313|Proteomes:UP000199681}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GMCC 1.11211 {ECO:0000313|EMBL:SFH43805.1,
RC   ECO:0000313|Proteomes:UP000199681};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:TFB82717.1, ECO:0000313|Proteomes:UP000297963}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hh34 {ECO:0000313|EMBL:TFB82717.1,
RC   ECO:0000313|Proteomes:UP000297963};
RA   Liu Q., Xin Y.-H.;
RT   "Genomics of glacier-inhabiting Cryobacterium strains.";
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; FOPW01000005; SFH43805.1; -; Genomic_DNA.
DR   EMBL; SOFE01000023; TFB82717.1; -; Genomic_DNA.
DR   Proteomes; UP000199681; Unassembled WGS sequence.
DR   Proteomes; UP000297963; 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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000199681,
KW   ECO:0000313|Proteomes:UP000297963};
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:UP000199681};
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      260    347       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   COILED      601    621       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   621 AA;  67981 MW;  E6BC462D3992CEEA CRC64;
     MAGLIRQSDI EEVKARTNIA DIIGDYVTLK SAGVGSMKGL CPFHDERSPS FHVRPQVGFY
     HCFGCGESGD VYSFLQKMDH VSFSEAVERL AGRVGLDLHY EDGSGAAPDH GNRARLLAAN
     QVASDFFIDQ LGSAGAEVGR AFLGQRGFDA AAATRFGVGF APKSWDELTN HLRAKGFTTE
     ELTLSGLVSS GDRGIYDRFR GRLVWPIRDI TGQTIGFGAR KLLDDDKGPK YLNTPESPVY
     HKAQVLYGLD LAKRDISRSH QVVVVEGYTD VMACHLAGIT TAVATCGTSF GVDHIKVLRR
     VLGDDSGVGE VVFTFDPDAA GQKAAMRAFS EEQRFSAQTY VAVGPEGLDP CDLRLQRGDD
     AVRRMVDAKK PMFEFMIRQI LSQYNLDTVE GRTAALRAAA PIVGDIRDPV LRPGYTRELS
     RMLGVDMGEV ARAVTNAQPG ARSSASGGPN APRHAGAVEV LPERPFSLVE LPGDPVTRLE
     RDGLMAMLQR PTLIGRDILD SAVQTSFANS SLAVVRDAIA SSLPHFEAPD WLDRVVAEVP
     DTLKNLVQEL AMANLPERTE KDVTRYVREI TIVLIDKDLL RLKAELLGRL QRADASETEI
     YRTLQRELVR VEAERRALRD E
//
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