UniProt: B0VJJ5

Database: UniProt
Entry: B0VJJ5_CLOAI

LinkDB:  B0VJJ5_CLOAI 
Original site:  B0VJJ5_CLOAI

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Ontology (7)   
   GO (7)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (1)   
   KEGG GENES (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (16)   
   InterPro (10)   
   Pfam (3)   
   PROSITE (1)   
   SMART (2)   
Literature (1)   
   PubMed (1)   
All databases (27)   

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ID   B0VJJ5_CLOAI            Unreviewed;       580 AA.
AC   B0VJJ5;
DT   08-APR-2008, integrated into UniProtKB/TrEMBL.
DT   08-APR-2008, sequence version 1.
DT   27-MAR-2024, entry version 99.
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   ECO:0000313|EMBL:CAO81655.1};
GN   OrderedLocusNames=CLOAM1825 {ECO:0000313|EMBL:CAO81655.1};
OS   Cloacimonas acidaminovorans (strain Evry).
OC   Bacteria; Candidatus Cloacimonadota; Candidatus Cloacimonadia;
OC   Candidatus Cloacimonadales; Candidatus Cloacimonadaceae; Cloacimonas.
OX   NCBI_TaxID=459349 {ECO:0000313|EMBL:CAO81655.1, ECO:0000313|Proteomes:UP000002019};
RN   [1] {ECO:0000313|EMBL:CAO81655.1, ECO:0000313|Proteomes:UP000002019}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Evry {ECO:0000313|Proteomes:UP000002019};
RX   PubMed=18245282; DOI=10.1128/JB.01248-07;
RA   Pelletier E., Kreimeyer A., Bocs S., Rouy Z., Gyapay G., Chouari R.,
RA   Riviere D., Ganesan A., Daegelen P., Sghir A., Cohen G.N., Medigue C.,
RA   Weissenbach J., Le Paslier D.;
RT   "'Candidatus Cloacamonas acidaminovorans': genome sequence reconstruction
RT   provides a first glimpse of a new bacterial division.";
RL   J. Bacteriol. 190:2572-2579(2008).
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|HAMAP-Rule:MF_00974,
CC         ECO:0000256|PIRNR:PIRNR002811, ECO:0000256|PIRSR:PIRSR002811-1};
CC       Note=Binds 1 zinc ion per monomer. {ECO:0000256|HAMAP-Rule:MF_00974,
CC       ECO:0000256|PIRNR:PIRNR002811, ECO:0000256|PIRSR:PIRSR002811-1};
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. {ECO:0000256|HAMAP-
CC       Rule:MF_00974, ECO:0000256|PIRNR:PIRNR002811}.
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DR   EMBL; CU466930; CAO81655.1; -; Genomic_DNA.
DR   AlphaFoldDB; B0VJJ5; -.
DR   STRING; 459349.CLOAM1825; -.
DR   KEGG; caci:CLOAM1825; -.
DR   eggNOG; COG0358; Bacteria.
DR   HOGENOM; CLU_013501_3_3_0; -.
DR   Proteomes; UP000002019; 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:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
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; 3.40.1360.10; -; 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; IPR036185; DNA_heli_DnaB-like_N_sf.
DR   InterPro; IPR016136; DNA_helicase_N/primase_C.
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   PIRSF; PIRSF002811; DnaG; 1.
DR   SMART; SM00493; TOPRIM; 1.
DR   SMART; SM00400; ZnF_CHCC; 1.
DR   SUPFAM; SSF56731; DNA primase core; 1.
DR   SUPFAM; SSF48024; N-terminal domain of DnaB helicase; 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, ECO:0000256|HAMAP-
KW   Rule:MF_00974};
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   Reference proteome {ECO:0000313|Proteomes:UP000002019};
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|HAMAP-Rule:MF_00974};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|HAMAP-
KW   Rule:MF_00974}.
FT   DOMAIN          259..340
FT                   /note="Toprim"
FT                   /evidence="ECO:0000259|PROSITE:PS50880"
FT   ZN_FING         43..67
FT                   /note="CHC2-type"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00974,
FT                   ECO:0000256|PIRSR:PIRSR002811-1"
SQ   SEQUENCE   580 AA;  65628 MW;  7AFCDFA56D8FE08B CRC64;
     MLFFREKMDQ NLIDQIRRAN DIVDVIQGYL PLKRVGSNFR GLCPFHNDSR PSLYVSQSKQ
     IFKCFACGKA GNVIGFVADF EKLTFIEAVK KLAQRAGIQV PEYEKTKVVN TKREQLLSVY
     KSAAEFFTSS LFAFGQNVLD YLKKRSFSPE TAKELQLGYA LNSEKALLNH LLKEGYSVSL
     LKDSGLFGNY GGGLTDLFKD RLMFPIHNSL GEVIAFGGRI LEPKEGVGKY INSPGTELYT
     KGKELYGLYK TKYNISKAGT AIICEGYFDF LRLYENGFTN SVASLGTALT EDQINLLARF
     CNRIIILYDG DSAGIKAAVR AGLLCLSRGM EVLIANLPAE EDPDSLILKQ GKIAMQEVVD
     KSIPLINFLA TDPRPEQPTA ERIELILDAL RILKDRIKQE LLLQEVSDAF GVTVGALNSK
     LRRSSASVSA ESSEQIVPQY ESFEERNVLA LALKDYESYK LLANDLDSSY FNNKRYRQVY
     NFLITQNLKS EPWEPAALLD NIENNEIKES LAELLFEDLQ QMCFEDCLSG LRIRKVQRDL
     EEMDRAISKD PKNMELLKEK EKLALKYRQM TRKVVNKVLY
//

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