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Database: UniProt
Entry: A0A0Q6AI37_9FLAO
LinkDB: A0A0Q6AI37_9FLAO
Original site: A0A0Q6AI37_9FLAO 
ID   A0A0Q6AI37_9FLAO        Unreviewed;       658 AA.
AC   A0A0Q6AI37;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 38.
DE   RecName: Full=DNA primase {ECO:0000256|HAMAP-Rule:MF_00974, ECO:0000256|PIRNR:PIRNR002811};
DE            EC=2.7.7.101 {ECO:0000256|HAMAP-Rule:MF_00974};
GN   Name=dnaG {ECO:0000256|HAMAP-Rule:MF_00974};
GN   ORFNames=ASG22_05985 {ECO:0000313|EMBL:KQT26217.1};
OS   Chryseobacterium sp. Leaf405.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC   Chryseobacterium group; Chryseobacterium.
OX   NCBI_TaxID=1736367 {ECO:0000313|EMBL:KQT26217.1, ECO:0000313|Proteomes:UP000051197};
RN   [1] {ECO:0000313|EMBL:KQT26217.1, ECO:0000313|Proteomes:UP000051197}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf405 {ECO:0000313|EMBL:KQT26217.1,
RC   ECO:0000313|Proteomes:UP000051197};
RX   PubMed=26633631; DOI=10.1038/nature16192;
RA   Bai Y., Muller D.B., Srinivas G., Garrido-Oter R., Potthoff E., Rott M.,
RA   Dombrowski N., Munch P.C., Spaepen S., Remus-Emsermann M., Huttel B.,
RA   McHardy A.C., Vorholt J.A., Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiota.";
RL   Nature 528:364-369(2015).
RN   [2] {ECO:0000313|Proteomes:UP000051197}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf405 {ECO:0000313|Proteomes:UP000051197};
RA   Garrido-Oter R., Mueller D.B.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|Proteomes:UP000051197}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf405 {ECO:0000313|Proteomes:UP000051197};
RA   Vorholt J.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-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 replication.
CC       {ECO:0000256|HAMAP-Rule:MF_00974, ECO:0000256|PIRNR:PIRNR002811}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ssDNA + n NTP = ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate.;
CC         EC=2.7.7.101; Evidence={ECO:0000256|HAMAP-Rule:MF_00974};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|PIRNR:PIRNR002811};
CC       Note=Binds 1 zinc ion per monomer. {ECO:0000256|PIRNR:PIRNR002811};
CC   -!- SUBUNIT: Monomer. Interacts with DnaB. {ECO:0000256|HAMAP-
CC       Rule:MF_00974}.
CC   -!- SIMILARITY: Belongs to the DnaG primase family. {ECO:0000256|HAMAP-
CC       Rule:MF_00974, ECO:0000256|PIRNR:PIRNR002811}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00974}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KQT26217.1}.
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DR   EMBL; LMQN01000012; KQT26217.1; -; Genomic_DNA.
DR   RefSeq; WP_055983273.1; NZ_LMQN01000012.1.
DR   AlphaFoldDB; A0A0Q6AI37; -.
DR   STRING; 1736367.ASG22_05985; -.
DR   OrthoDB; 9803773at2; -.
DR   Proteomes; UP000051197; Unassembled WGS sequence.
DR   GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
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:InterPro.
DR   CDD; cd03364; TOPRIM_DnaG_primases; 1.
DR   Gene3D; 3.40.1360.10; -; 1.
DR   Gene3D; 3.90.980.10; DNA primase, catalytic core, N-terminal domain; 1.
DR   Gene3D; 3.90.580.10; Zinc finger, CHC2-type domain; 1.
DR   HAMAP; MF_00974; DNA_primase_DnaG; 1.
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; IPR013264; DNAG_N.
DR   InterPro; IPR034151; TOPRIM_DnaG_bac.
DR   InterPro; IPR006171; TOPRIM_domain.
DR   InterPro; IPR002694; Znf_CHC2.
DR   NCBIfam; TIGR01391; dnaG; 1.
DR   PANTHER; PTHR30313; DNA PRIMASE; 1.
DR   PANTHER; PTHR30313:SF2; DNA PRIMASE; 1.
DR   Pfam; PF10410; DnaB_bind; 1.
DR   Pfam; PF08275; DNAG_N; 1.
DR   Pfam; PF13155; Toprim_2; 1.
DR   Pfam; PF01807; zf-CHC2; 1.
DR   PIRSF; PIRSF002811; DnaG; 1.
DR   SMART; SM00493; TOPRIM; 1.
DR   SMART; SM00400; ZnF_CHCC; 1.
DR   SUPFAM; SSF56731; DNA primase core; 1.
DR   SUPFAM; SSF57783; Zinc beta-ribbon; 1.
DR   PROSITE; PS50880; TOPRIM; 1.
PE   3: Inferred from homology;
KW   DNA replication {ECO:0000256|ARBA:ARBA00022705, ECO:0000256|HAMAP-
KW   Rule:MF_00974};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW   Rule:MF_00974};
KW   DNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022478,
KW   ECO:0000256|HAMAP-Rule:MF_00974};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRNR:PIRNR002811};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, ECO:0000256|HAMAP-
KW   Rule:MF_00974};
KW   Primosome {ECO:0000256|ARBA:ARBA00022515, ECO:0000256|HAMAP-Rule:MF_00974};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163, ECO:0000256|HAMAP-
KW   Rule:MF_00974};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00974};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRNR:PIRNR002811};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT   DOMAIN          263..344
FT                   /note="Toprim"
FT                   /evidence="ECO:0000259|PROSITE:PS50880"
SQ   SEQUENCE   658 AA;  75884 MW;  C15D715680C4EEE1 CRC64;
     MISKQTIDKI FSTIRVEEIV GEYVQLKRAG SNFKGLSPFH EEKSPSFVVS PSKQIWKDFS
     TGKGGTAISF LMEIENFTYP EALRHAAKKY GIEIEEDQRE FSEEAKNAQS ERDTLYKIHE
     IANDYFQNFL WEEEEGKSIG LSYFKERELR DDIIKKFQLG YSPEKKNGFT EFALEKGYSK
     EILEKSGLSI FPENAPNGID RFRERVMFPI HSFSGRVLGF GARILRNNIK TAKYLNSPET
     EIYHKSNVLY GLNQSKQAIS RKNVCLLVEG YMDVISLHMS GIENVVASSG TSLTTEQIKL
     IKRLTENVTI LFDGDNAGIK ASFRSIDMLL TEGMNIRVML FPDGDDPDSF ARKHPQDYVE
     KFIENEAMDF IDFKAEILLK EVGNDPIKKA EAIRDIVKSV GFVQNALKRE VYLKEVSNKF
     GLSEQSLFNE LDVQKQITQN QHQKTQARVE AQPTKLEVVE KPKDETNHII FNVTKLENDL
     INHMLNYGDV VLHRKTPDNK DYDITVIEEI INHFEEDNYE FQIELNKRIV SEIKDGINKD
     ELRQGNFFFG LMDEELSSAA VKFMNIYNEL HDWETRNIHS PNYGDRIPEQ VAGDILIHKF
     RYVKFLIGET QKQLTEFSDS DEVKYFESLK KIQMLTLVSI ELAKMLDYSA ITGIYTGR
//
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