ID L0ABI7_CALLD Unreviewed; 425 AA.
AC L0ABI7;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=DNA primase DnaG {ECO:0000256|HAMAP-Rule:MF_00007};
DE EC=2.7.7.101 {ECO:0000256|HAMAP-Rule:MF_00007};
GN Name=dnaG {ECO:0000256|HAMAP-Rule:MF_00007};
GN OrderedLocusNames=Calag_0753 {ECO:0000313|EMBL:AFZ70497.1};
OS Caldisphaera lagunensis (strain DSM 15908 / JCM 11604 / ANMR 0165 /
OS IC-154).
OC Archaea; Thermoproteota; Thermoprotei; Acidilobales; Caldisphaeraceae;
OC Caldisphaera.
OX NCBI_TaxID=1056495 {ECO:0000313|EMBL:AFZ70497.1, ECO:0000313|Proteomes:UP000010469};
RN [1] {ECO:0000313|Proteomes:UP000010469}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15908 / JCM 11604 / IC-154
RC {ECO:0000313|Proteomes:UP000010469};
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Peters L., Mikhailova N., Teshima H.,
RA Kyrpides N., Mavromatis K., Ivanova N., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA Woyke T., Wu D., Spring S., Schroeder M., Brambilla E., Klenk H.-P.,
RA Eisen J.A.;
RT "Complete genome of Caldisphaera lagunensis DSM 15908.";
RL Submitted (MAR-2012) 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 Also part of the exosome, which is a complex involved in RNA
CC degradation. Acts as a poly(A)-binding protein that enhances the
CC interaction between heteropolymeric, adenine-rich transcripts and the
CC exosome. {ECO:0000256|HAMAP-Rule:MF_00007}.
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_00007};
CC -!- SUBUNIT: Forms a ternary complex with MCM helicase and DNA. Component
CC of the archaeal exosome complex. {ECO:0000256|HAMAP-Rule:MF_00007}.
CC -!- SIMILARITY: Belongs to the archaeal DnaG primase family.
CC {ECO:0000256|HAMAP-Rule:MF_00007}.
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DR EMBL; CP003378; AFZ70497.1; -; Genomic_DNA.
DR AlphaFoldDB; L0ABI7; -.
DR STRING; 1056495.Calag_0753; -.
DR KEGG; clg:Calag_0753; -.
DR eggNOG; arCOG04281; Archaea.
DR HOGENOM; CLU_034626_0_0_2; -.
DR InParanoid; L0ABI7; -.
DR Proteomes; UP000010469; Chromosome.
DR GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
DR GO; GO:0000178; C:exosome (RNase complex); IEA:UniProtKB-KW.
DR GO; GO:1990077; C:primosome complex; IEA:UniProtKB-KW.
DR GO; GO:0003896; F:DNA primase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008143; F:poly(A) binding; IEA:InterPro.
DR CDD; cd01029; TOPRIM_primases; 1.
DR Gene3D; 3.40.1360.10; -; 1.
DR HAMAP; MF_00007; DNA_primase_DnaG_arc; 1.
DR InterPro; IPR020607; Primase_DnaG_arc.
DR InterPro; IPR034154; TOPRIM_DnaG/twinkle.
DR InterPro; IPR006171; TOPRIM_domain.
DR PANTHER; PTHR30313; DNA PRIMASE; 1.
DR PANTHER; PTHR30313:SF2; DNA PRIMASE; 1.
DR Pfam; PF01751; Toprim; 1.
DR SMART; SM00493; TOPRIM; 1.
DR SUPFAM; SSF110455; Toprim domain; 1.
DR PROSITE; PS50880; TOPRIM; 1.
PE 3: Inferred from homology;
KW DNA replication {ECO:0000256|HAMAP-Rule:MF_00007};
KW DNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022478,
KW ECO:0000256|HAMAP-Rule:MF_00007};
KW Exosome {ECO:0000256|ARBA:ARBA00022835, ECO:0000256|HAMAP-Rule:MF_00007};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, ECO:0000256|HAMAP-
KW Rule:MF_00007};
KW Primosome {ECO:0000256|ARBA:ARBA00022515, ECO:0000256|HAMAP-Rule:MF_00007};
KW Reference proteome {ECO:0000313|Proteomes:UP000010469};
KW Transcription {ECO:0000256|ARBA:ARBA00023163, ECO:0000256|HAMAP-
KW Rule:MF_00007}; Transferase {ECO:0000256|HAMAP-Rule:MF_00007}.
FT DOMAIN 165..241
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT REGION 278..309
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 278..302
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 425 AA; 47857 MW; 2B59037CA71C57A5 CRC64;
MKYLIKASFE VDGRVDKHDV IGAVFGQTEG LLGSEFNLEQ LQNKDKIGRV HIDMKYQGTK
SVGILQIPSN LDRVETVLLA AMIESVDRVG PYTSRITIDD IQDLRIEKLQ KIVERARQLL
QRVKEQEPDI KEILREISQK PEVQAKVIEI GEERLPAGPD VEKADTIIIV EGRADVINLM
KYGYTNTVAL EGAREKVPQT IVELAKNKKV IAFVDGDRGG DLILKNLLDQ VHVDYVARAP
KDMEVEQLTG KEIARALSQM MPAEAVKQQL LSIKETKEEA EAAHEQTLPE TQKIEKKEEI
VQPETPSQQV VQEEKVEQKH ELVSQLVVPK QVIDNIKNIK GTLEAIIYDR DWKEITRIKV
RDLFTWLDTA QQNSAYAIIF DGIITQRILD LAGEKGIVLL IGARIGSKIS SKRGDVKFAT
FSDLT
//
