ID A0A0U3NNU2_9LACT Unreviewed; 621 AA.
AC A0A0U3NNU2;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 31-JUL-2019, entry version 22.
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=NY10_594 {ECO:0000313|EMBL:ALV21212.1};
OS Carnobacterium sp. CP1.
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Carnobacteriaceae;
OC Carnobacterium.
OX NCBI_TaxID=1564681 {ECO:0000313|EMBL:ALV21212.1, ECO:0000313|Proteomes:UP000064734};
RN [1] {ECO:0000313|EMBL:ALV21212.1, ECO:0000313|Proteomes:UP000064734}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CP1 {ECO:0000313|EMBL:ALV21212.1,
RC ECO:0000313|Proteomes:UP000064734};
RA Chen J., Yang J., Zhu S., Zhang D., Xiong S.;
RT "Whole genome Sequence of Carnobacterium sp. strain CP1 Isolated from
RT Amanda bay, East Antarctic.";
RL Submitted (FEB-2015) 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; CP010796; ALV21212.1; -; Genomic_DNA.
DR RefSeq; WP_058918565.1; NZ_CP010796.1.
DR EnsemblBacteria; ALV21212; ALV21212; NY10_594.
DR KEGG; carc:NY10_594; -.
DR PATRIC; fig|1564681.3.peg.594; -.
DR KO; K02316; -.
DR OrthoDB; 1071997at2; -.
DR Proteomes; UP000064734; Chromosome.
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; 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; 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 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:UP000064734};
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:UP000064734};
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 267 349 Toprim. {ECO:0000259|PROSITE:PS50880}.
FT ZN_FING 40 64 CHC2-type. {ECO:0000256|HAMAP-Rule:
FT MF_00974, ECO:0000256|PIRSR:PIRSR002811-
FT 1}.
FT REGION 448 477 Disordered. {ECO:0000256|SAM:MobiDB-
FT lite}.
FT COILED 578 605 {ECO:0000256|SAM:Coils}.
FT COMPBIAS 458 474 Polar. {ECO:0000256|SAM:MobiDB-lite}.
SQ SEQUENCE 621 AA; 71758 MW; 870A70B7DCFFDDB7 CRC64;
MAMMIPEETI NKVRQATNIT DVVSQYVQLK KKGKNLFGFC PFHDERTPSF SVTEEKQIFH
CFSCGRGGNV FTFLMEVDGL SFPEAVIKTA EISQIELEES LINDRNTNPQ ATDSKKELLL
KAHEESLELF HHILLNTKIG EQALAYLTDR GLTREVIETF GIGFAPRERT MLHQYLIGKD
YQPTLLKESG LFVERDNGEL LDRFYNRIIF PIRNQQGKVV AFSGRIFEVD DHEDGPKYLN
SPETYLFNKR NVLFNYDKAR AAIRREKEVV LFEGFMDVIA AWQAGVQNGV ASMGTSLTNE
QIHMLDRVTD HVLIAYDSDN AGIEAAKRAA DLLSEQTDFD IEILSFSEGM DPDDFIKENG
AAAFKELLSH GRTTLFGFKM RYFRRSLNLA NESERLGYIE KILTEMLTIT SAVEREMYFK
QLAAEFDVSL DSLKEQFQKY FYEQRNERAK ETKRNTPSSP EIRSTTFPQV QNQRRKIDST
ERAEQLLLNR LFHFEEAWIQ LKNLPNEFHF VHDDYQMLYI LYESFLDHAQ SDTSIEAFID
FVKESSLKSK LVEIELLSVS EEMTAREIED YIDVISRKSI LQSQLKEKQE AMTEASRRGD
QAQLRTLMIE VVNLSRSLKN S
//
