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Database: UniProt
Entry: D5VN94_CAUST
LinkDB: D5VN94_CAUST
Original site: D5VN94_CAUST 
ID   D5VN94_CAUST            Unreviewed;       642 AA.
AC   D5VN94;
DT   13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT   13-JUL-2010, sequence version 1.
DT   27-MAR-2024, entry version 76.
DE   RecName: Full=DNA primase {ECO:0000256|HAMAP-Rule:MF_00974};
DE            EC=2.7.7.101 {ECO:0000256|HAMAP-Rule:MF_00974};
GN   Name=dnaG {ECO:0000256|HAMAP-Rule:MF_00974};
GN   OrderedLocusNames=Cseg_3538 {ECO:0000313|EMBL:ADG11967.1};
OS   Caulobacter segnis (strain ATCC 21756 / DSM 7131 / JCM 7823 / NBRC 15250 /
OS   LMG 17158 / TK0059) (Mycoplana segnis).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Caulobacter.
OX   NCBI_TaxID=509190 {ECO:0000313|EMBL:ADG11967.1, ECO:0000313|Proteomes:UP000002629};
RN   [1] {ECO:0000313|Proteomes:UP000002629}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 21756 / DSM 7131 / JCM 7823 / NBRC 15250 / LMG 17158 /
RC   TK0059 {ECO:0000313|Proteomes:UP000002629};
RX   PubMed=21705585; DOI=10.1128/JB.05453-11;
RG   US DOE Joint Genome Institute;
RA   Brown P.J., Kysela D.T., Buechlein A., Hemmerich C., Brun Y.V.;
RT   "Genome sequences of eight morphologically diverse alphaproteobacteria.";
RL   J. Bacteriol. 193:4567-4568(2011).
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}.
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   -!- 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}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00974}.
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DR   EMBL; CP002008; ADG11967.1; -; Genomic_DNA.
DR   RefSeq; WP_013080613.1; NC_014100.1.
DR   AlphaFoldDB; D5VN94; -.
DR   STRING; 509190.Cseg_3538; -.
DR   KEGG; cse:Cseg_3538; -.
DR   eggNOG; COG0358; Bacteria.
DR   HOGENOM; CLU_013501_5_3_5; -.
DR   Proteomes; UP000002629; Chromosome.
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; PF13155; Toprim_2; 1.
DR   Pfam; PF01807; zf-CHC2; 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   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}; Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT   DOMAIN          263..344
FT                   /note="Toprim"
FT                   /evidence="ECO:0000259|PROSITE:PS50880"
FT   REGION          433..465
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        433..460
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   642 AA;  70913 MW;  0B6086945FD7D0C4 CRC64;
     MRFDDRFLEE LKSRLRPSDV VGKTVKLRRQ GREYAGLSPF TKEKSPSFFV NDEKGFYHCF
     SSGKHGDIIS FLQETERLTF AEAVERLAAE AGMSLPEVDP RAAREEQKRS SLGDWMELAA
     AWFESELRRP VGQAARAYLE KRGLPESEWS RFRIGFAPNN RTGLKDYLIA KGAKPGDLVD
     AGVLIAPEDG GQPYDRFRDR IIFPIADSRG KVVSFGGRAM DPAARAKYLN GPETSLFHKG
     RVLYGLFEAR KILHAGQSGG EKPPMVVVEG YMDVIACQRA GIPAVAAMGT ALTEEQMEGL
     WRLHPTPTLC FDGDKAGRRA ADRAIDRALP LLKPGRSFLF SMPVGGKDPD DVLREQGPAA
     LKAQISNTKP FVEALFERER ELEPFDTPEQ RTNLKVRLRT LAATIADKDL AHAYKEELLD
     RLDEMRAARR VKADASDAGR ALSRQRWDNT PRRGGKGRLE GSTAEGRQAA AALQQAPRPF
     SAALLIAAIR DPKVVDDRIE VLMNQGFGDQ RLDAIAQELV NLRMDADHVE AGMVRGRLAT
     AGYDDATLAA LERSAAHVKA LDAAQSAAQS PEDAIRGLWS QAFDLLIRLT ALERAVDEAK
     ADLAHEGDSH TLFRLKTERD AVKRLIDSGG WTDPSLVAQV LH
//
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