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Database: UniProt
Entry: A0A1F8LVR8_9CHLR
LinkDB: A0A1F8LVR8_9CHLR
Original site: A0A1F8LVR8_9CHLR 
ID   A0A1F8LVR8_9CHLR        Unreviewed;       584 AA.
AC   A0A1F8LVR8;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 24.
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=A2158_08695 {ECO:0000313|EMBL:OGN90458.1};
OS   Chloroflexi bacterium RBG_13_46_14.
OC   Bacteria; Chloroflexota.
OX   NCBI_TaxID=1797618 {ECO:0000313|EMBL:OGN90458.1, ECO:0000313|Proteomes:UP000179827};
RN   [1] {ECO:0000313|EMBL:OGN90458.1, ECO:0000313|Proteomes:UP000179827}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27774985; DOI=10.1038/ncomms13219;
RA   Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA   Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA   Williams K.H., Hubbard S.S., Banfield J.F.;
RT   "Thousands of microbial genomes shed light on interconnected biogeochemical
RT   processes in an aquifer system.";
RL   Nat. Commun. 7:13219-13219(2016).
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         ECO:0000256|PIRSR:PIRSR002811-1};
CC       Note=Binds 1 zinc ion per monomer. {ECO:0000256|PIRNR:PIRNR002811,
CC       ECO:0000256|PIRSR:PIRSR002811-1};
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:OGN90458.1}.
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DR   EMBL; MGML01000032; OGN90458.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1F8LVR8; -.
DR   Proteomes; UP000179827; 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, ECO:0000256|PIRSR:PIRSR002811-
KW   1}.
FT   DOMAIN          251..332
FT                   /note="Toprim"
FT                   /evidence="ECO:0000259|PROSITE:PS50880"
FT   ZN_FING         34..59
FT                   /note="CHC2-type"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002811-1"
SQ   SEQUENCE   584 AA;  66126 MW;  7EAEEA714584796F CRC64;
     MSIIDDVKQK TDIVEVISQY VTLKKSGRNF SAPCPFHSER NPSFFVYPEG QSWHCFGACN
     TGGDVLSFVM KKENMDFGEA LRHLAARAGI EVPTRVQPDT RKDEKDRIFQ INSAAALYFH
     NLLLNSPGAE NARKYLEKRG LNEKTVSDFQ LGFALNSWEG LKEHLEREYT EREILEDGLL
     VESDDGRTHD RFRNRLIFTI CDNRGRITGF GARVLDDSLP KYVNSPQTLV FDKSGTLYGI
     NLAAQAIRQK NQAVLVEGYM DVITAHQNGI TNVVASMGTA VTERQVNDLK KLTKNILLAL
     DADTAGEEAM LRCVGYENSL DIELKVVILP EGQDPDNVIR EDTGKWYALL DKALPVMDFI
     FTVVGNDLDL TRASDKQEAV EHIGPHVVAI PNPVRRAHYV QKLARLVGTD ERTIEATLRV
     KKVTPVSAKS KRGQPVRFSR SPQILWSRPI EEQFLALLLK HPEFKERSAG VPAEYLENSE
     NREIFVAWQQ SPDEEALKEK LDEILLDYLD ILSSKNILAT KVNERYNEYV LRLKEDHLRS
     LARKGETVKT AGEFPGEKDI ELTDNLREIF NIRARREGGK GDRK
//
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