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
//
