ID A0A133VT82_9EURY Unreviewed; 377 AA.
AC A0A133VT82;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 20.
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=AKJ35_00510 {ECO:0000313|EMBL:KXB09637.1};
OS candidate division MSBL1 archaeon SCGC-AAA833F18.
OC Archaea; Euryarchaeota; candidate division MSBL1.
OX NCBI_TaxID=1698257 {ECO:0000313|EMBL:KXB09637.1, ECO:0000313|Proteomes:UP000070399};
RN [1] {ECO:0000313|EMBL:KXB09637.1, ECO:0000313|Proteomes:UP000070399}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCGC-AAA833F18 {ECO:0000313|EMBL:KXB09637.1};
RX PubMed=26758088; DOI=10.1038/srep19181;
RA Mwirichia R., Alam I., Rashid M., Vinu M., Ba-Alawi W., Anthony Kamau A.,
RA Kamanda Ngugi D., Goker M., Klenk H.P., Bajic V., Stingl U.;
RT "Metabolic traits of an uncultured archaeal lineage -MSBL1- from brine
RT pools of the Red Sea.";
RL Sci. Rep. 6:19181-19181(2016).
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:KXB09637.1}.
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DR EMBL; LHYO01000002; KXB09637.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A133VT82; -.
DR PATRIC; fig|1698257.3.peg.158; -.
DR Proteomes; UP000070399; 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 Reference proteome {ECO:0000313|Proteomes:UP000070399};
KW Transcription {ECO:0000256|ARBA:ARBA00023163, ECO:0000256|HAMAP-
KW Rule:MF_00007}; Transferase {ECO:0000256|HAMAP-Rule:MF_00007}.
FT DOMAIN 169..255
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
SQ SEQUENCE 377 AA; 40989 MW; D5BF25954856F4D0 CRC64;
MGNDNGTTKY LIKATMKADG VVERPDVVGA IFGQTEGLLS DDLDLRELQK DDKIGRIEVD
VESEKGKSKG SISIPSSLDK IKTAIIGAAL EAIDRVGPCK ATITVDAVQD VRDTKRKFII
DRAKELLGDI EKIEPQSADL SKSVKGPSVN KKIKKYKGQP AGPSASKSDA IIIVEGRSDV
INLLNSGIKN TIAIEGTSTP EPVAELTKNK TTTAFLDGDR GGDLILKELL QVAELDYVAR
APQGKTVEDL SKEEVRGALK KKIPASEAST TFLKKEEKEV PEENDLQKLA AAASNLRGTL
KAQLLDENLK QISKIPVRNL PDELNKKDNI RAVVFDGIVT QKLADLAAEK NFDYLVGMRE
RLKNKPKDVE ILTPENL
//
