ID A0A2H9KYY4_9ARCH Unreviewed; 471 AA.
AC A0A2H9KYY4;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 24-JAN-2024, entry version 17.
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 ORFNames=COU37_03095 {ECO:0000313|EMBL:PIT84489.1};
OS Candidatus Micrarchaeota archaeon CG10_big_fil_rev_8_21_14_0_10_45_29.
OC Archaea; Candidatus Micrarchaeota.
OX NCBI_TaxID=1974417 {ECO:0000313|EMBL:PIT84489.1, ECO:0000313|Proteomes:UP000229978};
RN [1] {ECO:0000313|EMBL:PIT84489.1, ECO:0000313|Proteomes:UP000229978}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CG10_big_fil_rev_8_21_14_0_10_45_29
RC {ECO:0000313|EMBL:PIT84489.1};
RA Probst A.J., Ladd B., Jarett J.K., Geller-Mcgrath D.E., Sieber C.M.,
RA Emerson J.B., Anantharaman K., Thomas B.C., Malmstrom R., Stieglmeier M.,
RA Klingl A., Woyke T., Ryan C.M., Banfield J.F.;
RT "Depth-based differentiation of microbial function through sediment-hosted
RT aquifers and enrichment of novel symbionts in the deep terrestrial
RT subsurface.";
RL Submitted (SEP-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 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}.
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:PIT84489.1}.
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DR EMBL; PFCD01000011; PIT84489.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2H9KYY4; -.
DR Proteomes; UP000229978; Unassembled WGS sequence.
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; PF13662; Toprim_4; 1.
DR SMART; SM00493; TOPRIM; 1.
DR SUPFAM; SSF56731; DNA primase core; 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|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 Transcription {ECO:0000256|ARBA:ARBA00023163, ECO:0000256|HAMAP-
KW Rule:MF_00007}; Transferase {ECO:0000256|HAMAP-Rule:MF_00007}.
FT DOMAIN 173..259
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT REGION 271..380
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 271..296
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 301..324
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 325..346
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 471 AA; 51297 MW; 8F632B7FC831B6AB CRC64;
MGKTYVDTVK YQVYANVEID GLVEKPDVVG AIFGQTEGLL GDELDLRELQ KNGRIGRIEV
ELSPRGGKAV GKIKLPSSLD MVETSILAAA LETVDRVGPC DARINIEKIE DTRTLKRKGL
VDRAKGLLKT MLTSEIPESK EISEQVRSEV KIAEISSYGP EKLPAGPGVR TMDSVIIVEG
RADVLNLLRN DITNAVAVGG ANVAQSIAKL TREKETTVFL DGDRGGDIIL AELSRIGDLD
FIARAPRGKE VEELTRKELI KCLRSKVPYE SGAKASSSNG VAGNATNGSA PAPTNDYSSR
PRYERGAREE RYSRQGRDGY TGRQPRQRDS YSQSRQRTSS FSPSPAPMAA PNHAQKPASQ
MQEPFQPEPM QEPAPSMGEA PKQYLDALGE LENTLKARFY GEDGSVISEM PVRDMIKTLD
SKESVHAIVF DGIITQRLAD LAQAKKAKVL IGIKLGNVFK KPAGVLLHTK Q
//
