ID A0A1Q4F6Y7_9SPHI Unreviewed; 648 AA.
AC A0A1Q4F6Y7;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-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=BGP14_13475 {ECO:0000313|EMBL:OJY88443.1};
OS Sphingobacteriales bacterium 44-15.
OC Bacteria; Bacteroidetes; Sphingobacteriia; Sphingobacteriales.
OX NCBI_TaxID=1895837 {ECO:0000313|EMBL:OJY88443.1, ECO:0000313|Proteomes:UP000186250};
RN [1] {ECO:0000313|EMBL:OJY88443.1, ECO:0000313|Proteomes:UP000186250}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=44-15 {ECO:0000313|EMBL:OJY88443.1};
RA Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T.,
RA Anantharaman K., Tringe S., Hettich R.L., Harrison S.T.,
RA Banfield J.F.;
RT "Genome-resolved meta-omics ties microbial dynamics to process
RT performance in biotechnology for thiocyanate degradation.";
RL Submitted (SEP-2016) 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}.
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:OJY88443.1}.
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DR EMBL; MKWG01000017; OJY88443.1; -; Genomic_DNA.
DR Proteomes; UP000186250; 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; 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; 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:UP000186250};
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 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 259 340 Toprim. {ECO:0000259|PROSITE:PS50880}.
FT ZN_FING 37 61 CHC2-type. {ECO:0000256|HAMAP-Rule:
FT MF_00974}.
FT REGION 444 464 Disordered. {ECO:0000256|SAM:MobiDB-
FT lite}.
FT COMPBIAS 444 460 Polyampholyte. {ECO:0000256|SAM:MobiDB-
FT lite}.
SQ SEQUENCE 648 AA; 74117 MW; 74A7533CE23BD8C8 CRC64;
MITQHTIQQI LSRIDIIDIV GSFVKLKKRG TNYLGLCPFH NEKTPSFTVS PAKEIYKCFG
CGKSGNSISF LMEHEKYSYV EALKWLAARY NVEVEETEVS PAVKELQQTA DSLYIINSFA
QKFFSDNLWN NEEGRDIGLS YLHERGFQED IIQKFQIGYC SRDWNAFATA ATTAQYNPEY
LLKTGLVVLR DEKLTDNYRG RIIFPVHNQT GKIIGFGARI IGKNDRAPKY INTPENEIYV
KSRILYGSYF ARQAIDKADE CLLVEGYTDV VSLHQAGIEN VVASGGTSLT PDQLRLIKKY
TNNLTIIYDG DAAGIKAALR GLDLALEEGL NVQLVLIPDK EDPDSYVRKT GAAAFREFIE
GNKKDIVLFQ LEVSLKDAGN DLNKKSAIVN RIAETISRLN KAEDFTKQQD YIRQCAALLS
IDEEGLNALV NKFIRERIAK QENKAAASEE KNKEEASADT ASQENEDILD LISKDELVER
NMTRALLEFG NYSWDEQQNV ARHIFFELDH YGLQELIDNK QLLHIIDTYR KWVDEGITPT
PKSFLYHEDM AISTVAVGLM DTRYELSQNW KEHYDGPMPT REELYKEEVA STLTYLKIRK
IKRLIIENQR DLEQADSPED QLNLLQTHQH LKQMEIELIR DYGTVIYK
//
