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Database: UniProt
Entry: A0A0F3L4T2_9CAUL
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Original site: A0A0F3L4T2_9CAUL 
ID   A0A0F3L4T2_9CAUL        Unreviewed;       625 AA.
AC   A0A0F3L4T2;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   24-JAN-2024, entry version 36.
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=VH88_14590 {ECO:0000313|EMBL:KJV38401.1};
OS   Brevundimonas sp. KM4.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Brevundimonas.
OX   NCBI_TaxID=1628191 {ECO:0000313|EMBL:KJV38401.1, ECO:0000313|Proteomes:UP000033583};
RN   [1] {ECO:0000313|EMBL:KJV38401.1, ECO:0000313|Proteomes:UP000033583}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KM4 {ECO:0000313|EMBL:KJV38401.1,
RC   ECO:0000313|Proteomes:UP000033583};
RA   Sulaiman J., Priya K., Chan K.-G.;
RT   "Draft genome sequence of Brevundimonas sp. KM4.";
RL   Submitted (MAR-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:KJV38401.1}.
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DR   EMBL; JZRG01000038; KJV38401.1; -; Genomic_DNA.
DR   RefSeq; WP_017504422.1; NZ_JZRG01000038.1.
DR   AlphaFoldDB; A0A0F3L4T2; -.
DR   PATRIC; fig|1628191.3.peg.1800; -.
DR   Proteomes; UP000033583; 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; 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; PF08275; DNAG_N; 1.
DR   Pfam; PF13662; Toprim_4; 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          261..342
FT                   /note="Toprim"
FT                   /evidence="ECO:0000259|PROSITE:PS50880"
SQ   SEQUENCE   625 AA;  69189 MW;  9CED2A2EC8A2DDC1 CRC64;
     MRFDERFIDE LKARLRPSDV IGRTVKLKRQ GREYVGLSPF SKEKSPSFFV NDDKGFFHDF
     SSGKHGDIIS FLQETERLSF VEAVQRLAGE AGMQLPAEDP KEAEREQKRA GLSDWMDLAQ
     KWFAANLRRT PGKAAREYLD KRGLPEDQWE RFGLGYAPND REGLKQALVQ RGAKPAELVE
     AGLLISPESG GQPYDRFRDR LMFPILDARG RIVSFGGRAM NPDDRAKYLN GPESPLFHKG
     ATLYGLPEAR RILGAESKND QAIIVVEGYM DVIACQRAGL PAVAPMGTAL TEEQMALLWR
     VSSEPILCFD GDPAGQRAAF RAVERALPLL KPERSFRFVT LTGGQDPDDM LREKGAPALR
     EAMSVTTPFS RMLLDREMAE VGALDTPEKE AGLLVRLRKA AATIADPDLA RTYKDFLVGA
     FYQRVRPSPE EKRAANKVIY RDRKARSMAP IMDVTPEARA AAITLARAPR PVLAAIVEGL
     IAHPDTVNER GETLATQSFG DVGLDRLVSD LVRLTYEAQA MSNGLLRSRL LAMGHEETLR
     RIDRTAGIAH APFLDSAASL EVAAAGLSRA VDVLLQSMAL SRAMNEMKSE ESFDSQAFIG
     LKGQRDALDR FISSGEIWTD TATLH
//
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