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Database: UniProt
Entry: A0A1Y0ETW2_9BURK
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ID   A0A1Y0ETW2_9BURK        Unreviewed;       703 AA.
AC   A0A1Y0ETW2;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   31-JUL-2019, entry version 9.
DE   RecName: Full=DNA primase {ECO:0000256|HAMAP-Rule:MF_00974, ECO:0000256|SAAS:SAAS00993443};
DE            EC=2.7.7.- {ECO:0000256|HAMAP-Rule:MF_00974, ECO:0000256|SAAS:SAAS00993444};
GN   Name=dnaG {ECO:0000256|HAMAP-Rule:MF_00974};
GN   ORFNames=CCO03_12860 {ECO:0000313|EMBL:ARU06841.1};
OS   Comamonas serinivorans.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Comamonas.
OX   NCBI_TaxID=1082851 {ECO:0000313|EMBL:ARU06841.1, ECO:0000313|Proteomes:UP000196138};
RN   [1] {ECO:0000313|EMBL:ARU06841.1, ECO:0000313|Proteomes:UP000196138}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 26136 {ECO:0000313|EMBL:ARU06841.1,
RC   ECO:0000313|Proteomes:UP000196138};
RA   Song R., Chenine A.L., Ruprecht R.M.;
RL   Submitted (MAY-2017) 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|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};
CC       Note=Binds 1 zinc ion per monomer. {ECO:0000256|HAMAP-
CC       Rule:MF_00974};
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|SAAS:SAAS00709351}.
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DR   EMBL; CP021455; ARU06841.1; -; Genomic_DNA.
DR   KEGG; cser:CCO03_12860; -.
DR   KO; K02316; -.
DR   BioCyc; GCF_002158865:CCO03_RS12860-MONOMER; -.
DR   Proteomes; UP000196138; 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; 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   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:UP000196138};
KW   DNA replication {ECO:0000256|HAMAP-Rule:MF_00974,
KW   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|SAAS:SAAS00709327};
KW   Magnesium {ECO:0000256|SAAS:SAAS00709345};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00974,
KW   ECO:0000256|SAAS:SAAS00709338};
KW   Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_00974,
KW   ECO:0000256|SAAS:SAAS00709339};
KW   Primosome {ECO:0000256|HAMAP-Rule:MF_00974,
KW   ECO:0000256|SAAS:SAAS00709304};
KW   Reference proteome {ECO:0000313|Proteomes:UP000196138};
KW   Transcription {ECO:0000256|HAMAP-Rule:MF_00974,
KW   ECO:0000256|SAAS:SAAS00709341};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00974,
KW   ECO:0000256|SAAS:SAAS00993442};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_00974, ECO:0000256|SAAS:SAAS00709300};
KW   Zinc-finger {ECO:0000256|HAMAP-Rule:MF_00974,
KW   ECO:0000256|SAAS:SAAS00709301}.
FT   DOMAIN      258    340       Toprim. {ECO:0000259|PROSITE:PS50880}.
FT   ZN_FING      38     62       CHC2-type. {ECO:0000256|HAMAP-Rule:
FT                                MF_00974}.
FT   REGION      434    559       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   COMPBIAS    458    472       Polyampholyte. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   COMPBIAS    502    543       Polyampholyte. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
SQ   SEQUENCE   703 AA;  77435 MW;  76B99045A502EE13 CRC64;
     MAIPQGFIDD LLARTDVVEV VGRHVQLKRA GANYQGLCPF HSEKSPSFTV SPSKQFYHCF
     GCGKSGNAIG FLMDHLGSGF VETVQDLAQQ AGLTVPQEQV SPQEMARQQA QREQRKTLTE
     VLEQAAQAYR ERLRTTPLAI DYLKKRGLSG AIAQRFGLGY APDTWRGLAS VFAAYDDPLL
     EHSGLVIHNA EEDKRYDRFR GRVMFPIRNE RGECIGFGGR VLGDEKPKYL NSPETPVFSK
     GHELYGLYEA RNAIRDAGHV LVTEGYMDVV ALAQLGLPNA VATLGTACTP DHMTKLFRVT
     DQVVFSFDGD AAGRRAAHKA LHVALPLATD VRTVKFLFLP AEHDPDSFVR TQGKAAFDQA
     VQQAVPLSRF VMDVASETLD LETAEGRAQT AVRAGELWRL LPQGTLAQQM LGDLASLVRM
     EAAQLLESWQ RQGLLGKGRP GRGEAPARPT SPSIKPSPFA DERKHDHTAH PPGSDWSQDL
     GGFDSWPTAE STWPQDGHGA WPGARHEGRE SRDSRSSHGG RGERGAFRND RGNRFKGKDT
     TAGKRWQSHS GPPGMPTPRS EHAARLLLAQ MELWATLSET EHSLLCEQPA PVGPLIRWLD
     RQFQDHGTVA WGVLVEQLQG QPFADFASQL MRTHKDLTAP QANFAELESE MRSIMFGIRR
     DACAAQETRA ALANDIEGLK RAKLAREELD RAQAAWAAQR AAS
//
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