DNAG_AQUAE
ID DNAG_AQUAE Reviewed; 498 AA.
AC O67465;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=DNA primase {ECO:0000255|HAMAP-Rule:MF_00974};
DE EC=2.7.7.101 {ECO:0000255|HAMAP-Rule:MF_00974};
GN Name=dnaG {ECO:0000255|HAMAP-Rule:MF_00974}; OrderedLocusNames=aq_1493;
OS Aquifex aeolicus (strain VF5).
OC Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX NCBI_TaxID=224324;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VF5;
RX PubMed=9537320; DOI=10.1038/32831;
RA Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL Nature 392:353-358(1998).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 1-405 IN COMPLEX WITH ZINC, AND
RP COFACTOR.
RX PubMed=16285921; DOI=10.1016/j.molcel.2005.09.004;
RA Corn J.E., Pease P.J., Hura G.L., Berger J.M.;
RT "Crosstalk between primase subunits can act to regulate primer synthesis in
RT trans.";
RL Mol. Cell 20:391-401(2005).
CC -!- FUNCTION: RNA polymerase that catalyzes the synthesis of short RNA
CC molecules used as primers for DNA polymerase during DNA replication.
CC {ECO:0000255|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:0000255|HAMAP-Rule:MF_00974};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00974,
CC ECO:0000269|PubMed:16285921};
CC Note=Binds 1 zinc ion per monomer. {ECO:0000255|HAMAP-Rule:MF_00974,
CC ECO:0000269|PubMed:16285921};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00974};
CC Note=Binds two Mg(2+) per subunit. {ECO:0000255|HAMAP-Rule:MF_00974};
CC -!- SUBUNIT: Monomer. Interacts with DnaB. {ECO:0000255|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:0000255|HAMAP-Rule:MF_00974}.
CC -!- SIMILARITY: Belongs to the DnaG primase family. {ECO:0000255|HAMAP-
CC Rule:MF_00974}.
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DR EMBL; AE000657; AAC07430.1; -; Genomic_DNA.
DR PIR; G70429; G70429.
DR RefSeq; NP_214030.1; NC_000918.1.
DR RefSeq; WP_010880968.1; NC_000918.1.
DR PDB; 2AU3; X-ray; 2.00 A; A=1-405.
DR PDBsum; 2AU3; -.
DR AlphaFoldDB; O67465; -.
DR SMR; O67465; -.
DR STRING; 224324.aq_1493; -.
DR PRIDE; O67465; -.
DR EnsemblBacteria; AAC07430; AAC07430; aq_1493.
DR KEGG; aae:aq_1493; -.
DR PATRIC; fig|224324.8.peg.1163; -.
DR eggNOG; COG0358; Bacteria.
DR HOGENOM; CLU_013501_3_2_0; -.
DR InParanoid; O67465; -.
DR OMA; WITESEI; -.
DR OrthoDB; 1071997at2; -.
DR EvolutionaryTrace; O67465; -.
DR Proteomes; UP000000798; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006269; P:DNA replication, synthesis of RNA primer; IBA:GO_Central.
DR CDD; cd03364; TOPRIM_DnaG_primases; 1.
DR Gene3D; 3.90.580.10; -; 1.
DR Gene3D; 3.90.980.10; -; 1.
DR HAMAP; MF_00974; DNA_primase_DnaG; 1.
DR InterPro; IPR013264; DNA_primase_core_N.
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; IPR034151; TOPRIM_DnaG_bac.
DR InterPro; IPR006171; TOPRIM_domain.
DR InterPro; IPR002694; Znf_CHC2.
DR Pfam; PF08275; Toprim_N; 1.
DR Pfam; PF01807; zf-CHC2; 1.
DR SMART; SM00493; TOPRIM; 1.
DR SMART; SM00400; ZnF_CHCC; 1.
DR TIGRFAMs; TIGR01391; dnaG; 1.
DR PROSITE; PS50880; TOPRIM; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA replication; DNA-binding; DNA-directed RNA polymerase;
KW Magnesium; Metal-binding; Nucleotidyltransferase; Primosome;
KW Reference proteome; Transcription; Transferase; Zinc; Zinc-finger.
FT CHAIN 1..498
FT /note="DNA primase"
FT /id="PRO_0000180476"
FT DOMAIN 243..324
FT /note="Toprim"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00974"
FT ZN_FING 35..59
FT /note="CHC2-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00974"
FT BINDING 249
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00974"
FT BINDING 293
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00974"
FT BINDING 293
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00974"
FT BINDING 295
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00974"
FT HELIX 4..11
FT /evidence="ECO:0007829|PDB:2AU3"
FT HELIX 14..21
FT /evidence="ECO:0007829|PDB:2AU3"
FT STRAND 25..27
FT /evidence="ECO:0007829|PDB:2AU3"
FT STRAND 30..33
FT /evidence="ECO:0007829|PDB:2AU3"
FT STRAND 36..38
FT /evidence="ECO:0007829|PDB:2AU3"
FT STRAND 45..48
FT /evidence="ECO:0007829|PDB:2AU3"
FT TURN 49..52
FT /evidence="ECO:0007829|PDB:2AU3"
FT STRAND 53..56
FT /evidence="ECO:0007829|PDB:2AU3"
FT TURN 57..59
FT /evidence="ECO:0007829|PDB:2AU3"
FT HELIX 65..73
FT /evidence="ECO:0007829|PDB:2AU3"
FT HELIX 77..88
FT /evidence="ECO:0007829|PDB:2AU3"
FT HELIX 99..120
FT /evidence="ECO:0007829|PDB:2AU3"
FT HELIX 122..130
FT /evidence="ECO:0007829|PDB:2AU3"
FT HELIX 135..140
FT /evidence="ECO:0007829|PDB:2AU3"
FT HELIX 149..159
FT /evidence="ECO:0007829|PDB:2AU3"
FT HELIX 162..166
FT /evidence="ECO:0007829|PDB:2AU3"
FT TURN 167..169
FT /evidence="ECO:0007829|PDB:2AU3"
FT TURN 182..185
FT /evidence="ECO:0007829|PDB:2AU3"
FT STRAND 186..192
FT /evidence="ECO:0007829|PDB:2AU3"
FT STRAND 198..205
FT /evidence="ECO:0007829|PDB:2AU3"
FT STRAND 213..216
FT /evidence="ECO:0007829|PDB:2AU3"
FT HELIX 225..227
FT /evidence="ECO:0007829|PDB:2AU3"
FT HELIX 232..242
FT /evidence="ECO:0007829|PDB:2AU3"
FT STRAND 245..247
FT /evidence="ECO:0007829|PDB:2AU3"
FT HELIX 251..259
FT /evidence="ECO:0007829|PDB:2AU3"
FT STRAND 264..272
FT /evidence="ECO:0007829|PDB:2AU3"
FT HELIX 275..282
FT /evidence="ECO:0007829|PDB:2AU3"
FT STRAND 286..291
FT /evidence="ECO:0007829|PDB:2AU3"
FT HELIX 296..311
FT /evidence="ECO:0007829|PDB:2AU3"
FT STRAND 315..319
FT /evidence="ECO:0007829|PDB:2AU3"
FT HELIX 327..334
FT /evidence="ECO:0007829|PDB:2AU3"
FT HELIX 336..345
FT /evidence="ECO:0007829|PDB:2AU3"
FT HELIX 349..356
FT /evidence="ECO:0007829|PDB:2AU3"
FT HELIX 357..359
FT /evidence="ECO:0007829|PDB:2AU3"
FT HELIX 361..372
FT /evidence="ECO:0007829|PDB:2AU3"
FT HELIX 378..392
FT /evidence="ECO:0007829|PDB:2AU3"
FT HELIX 396..399
FT /evidence="ECO:0007829|PDB:2AU3"
SQ SEQUENCE 498 AA; 57206 MW; 941D95ECEF6E16D3 CRC64;
MSSDIDELRR EIDIVDVISE YLNLEKVGSN YRTNCPFHPD DTPSFYVSPS KQIFKCFGCG
VGGDAIKFVS LYEDISYFEA ALELAKRYGK KLDLEKISKD EKVYVALDRV CDFYRESLLK
NREASEYVKS RGIDPKVARK FDLGYAPSSE ALVKVLKEND LLEAYLETKN LLSPTKGVYR
DLFLRRVVIP IKDPRGRVIG FGGRRIVEDK SPKYINSPDS RVFKKGENLF GLYEAKEYIK
EEGFAILVEG YFDLLRLFSE GIRNVVAPLG TALTQNQANL LSKFTKKVYI LYDGDDAGRK
AMKSAIPLLL SAGVEVYPVY LPEGYDPDEF IKEFGKEELR RLINSSGELF ETLIKTAREN
LEEKTREFRY YLGFISDGVR RFALASEFHT KYKVPMEILL MKIEKNSQEK EIKLSFKEKI
FLKGLIELKP KIDLEVLNLS PELKELAVNA LNGEEHLLPK EVLEYQVDNL EKLFNNILRD
LQKSGKKRKK RGLKNVNT
