ID A0A263D8J9_9PSEU Unreviewed; 649 AA.
AC A0A263D8J9;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-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=CFN78_04100 {ECO:0000313|EMBL:OZM74328.1};
OS Amycolatopsis antarctica.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Amycolatopsis.
OX NCBI_TaxID=1854586 {ECO:0000313|EMBL:OZM74328.1, ECO:0000313|Proteomes:UP000242444};
RN [1] {ECO:0000313|EMBL:OZM74328.1, ECO:0000313|Proteomes:UP000242444}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AU-G6 {ECO:0000313|EMBL:OZM74328.1,
RC ECO:0000313|Proteomes:UP000242444};
RA Wang J., Leiva S., Huang J., Huang Y.;
RT "Amycolatopsis antarcticus sp. nov., isolated from the surface of an
RT Antarcticus brown macroalga.";
RL Submitted (JUL-2017) 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|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}.
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:OZM74328.1}.
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DR EMBL; NKYE01000002; OZM74328.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A263D8J9; -.
DR InParanoid; A0A263D8J9; -.
DR OrthoDB; 9803773at2; -.
DR Proteomes; UP000242444; 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: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; IPR037068; DNA_primase_core_N_sf.
DR InterPro; IPR019475; DNA_primase_DnaB-bd.
DR InterPro; IPR006295; DNA_primase_DnaG.
DR InterPro; IPR013173; DNA_primase_DnaG_DnaB-bd_dom.
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; PF08278; DnaG_DnaB_bind; 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; SM00766; DnaG_DnaB_bind; 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, 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:UP000242444};
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 284..370
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT ZN_FING 63..87
FT /note="CHC2-type"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00974,
FT ECO:0000256|PIRSR:PIRSR002811-1"
FT REGION 461..493
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 649 AA; 71212 MW; 4CA1F8C644D05125 CRC64;
MCRVCRIHGP VRGPRASTRL GYVAGRIRDS DIAEVRERNR IDEVVGDYVA LRRAGGGALK
GLCPFHEEKT PSFNVRPTHG TFHCFGCGEG GDVIKFLTQY EKLSFVEAVE RLADRIGYKL
TYEGGGGSVQ RDRGTRARLA EINKAAQEFY AEQLLIPDAQ VARDFLRDRG FDSAAAQTFG
CGFAPSGWDK LTKVLLNKGF ELTELYKAQI SKEGRRGPID RFHRRLVWPI RDLAGDVVGF
GARRLFDDDP IQAKYLNTSE SPVYRKSEVL FGLDLAKREI SKRHQVVVVE GYTDVMAMHA
SGVPTAVASS GTAFGDEHMK LLRRLLMDDD AFRGEVIFTF DGDAAGQKAA LKAFEGDQTF
AGQTYIAVAP DGMDPCELRL AKGDTAVRDL VARRTPLFEF AIRSMLVEYD LDSVDGQVAA
LQRTVPVVAR IKDRAKRDGY ATKLSWWVGW PDESMVVRRV REEAGSPSKR APVRRTAQRP
GPDEDITRPS AADPQLRAQR EALKAALQEP ALAGPLYDSL PEDAFTHPAY VMVHSAILAA
GGTGSGLSGP GLLEAASQNC PQGTVQSLLS ELAVESLRAR GEADLRYISS VLAAVQENLV
GRQIADLKSK LQRLSPVEAP EEYRALFGDL VALEQYRKAL REQAGGGLE
//
