ID A0A0U5H3X3_9EURY Unreviewed; 442 AA.
AC A0A0U5H3X3;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 29.
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 ECO:0000313|EMBL:CQH59840.1};
GN ORFNames=HHUB_3072 {ECO:0000313|EMBL:CQH59840.1};
OS Halobacterium hubeiense.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Halobacteriaceae; Halobacterium.
OX NCBI_TaxID=1407499 {ECO:0000313|EMBL:CQH59840.1, ECO:0000313|Proteomes:UP000066737};
RN [1] {ECO:0000313|Proteomes:UP000066737}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=JI20-1 {ECO:0000313|Proteomes:UP000066737};
RX PubMed=26628271; DOI=10.1111/1462-2920.13130;
RA Jaakkola S.T., Pfeiffer F., Ravantti J.J., Guo Q., Liu Y., Chen X., Ma H.,
RA Yang C., Oksanen H.M., Bamford D.H.;
RT "The complete genome of a viable archaeum isolated from 123-million-year-
RT old rock salt.";
RL Environ. Microbiol. 18:565-579(2016).
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_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.
CC {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; LN831302; CQH59840.1; -; Genomic_DNA.
DR RefSeq; WP_059057456.1; NZ_LN831302.1.
DR AlphaFoldDB; A0A0U5H3X3; -.
DR STRING; 1407499.HHUB_3072; -.
DR GeneID; 26659694; -.
DR KEGG; hhb:Hhub_3072; -.
DR OrthoDB; 8643at2157; -.
DR Proteomes; UP000066737; Chromosome I.
DR GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
DR GO; GO:0000178; C:exosome (RNase complex); IEA:InterPro.
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 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:UP000066737};
KW Transcription {ECO:0000256|ARBA:ARBA00023163, ECO:0000256|HAMAP-
KW Rule:MF_00007};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00007, ECO:0000313|EMBL:CQH59840.1}.
FT DOMAIN 167..253
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT REGION 258..349
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 282..298
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 326..340
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 442 AA; 46108 MW; B629F2018FF9A770 CRC64;
MEDTAKYLIH ADFVADGVVE RTDVVGAAFG QTEGLLGDDL DIRDLQDSAK LGRIDVAVDS
EGGQSFGTIT IASSLDRVET ATLAAALEAV ERIGPCRAQV EVDRIEDVRA AKRREIVDRA
KELLASAFDE GAIDSDDILR EVRESVRVED VTEYEGLPAG PNVATSDAVL VVEGRADVVN
LLQYGIKNAV AVEGTNVPDA VADLTRERTA TAFLDGDRGG DLILRELRQV GDLDYVARPP
DGESVEDLSR GAVDAALREK SPADTATLVS EHEDNVDEDE TQQNAVADAS TAENASATED
APAETVASAV ESVEATAATD GSATPAPEAA TATTVQTEPD SAAEPEPVSK TVADHVEAVV
GSGTVRLLGD DLDVLAEGDA DGAMEVIDSA STVPRVVVLD GPVTQRLLDV AAQRGVAKLV
GTSAGEFVKQ PAGVRVHTAD DY
//
