ID F8D898_HALXS Unreviewed; 522 AA.
AC F8D898;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 63.
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=Halxa_2115 {ECO:0000313|EMBL:AEH36740.1};
OS Halopiger xanaduensis (strain DSM 18323 / JCM 14033 / SH-6).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Halopiger.
OX NCBI_TaxID=797210 {ECO:0000313|EMBL:AEH36740.1, ECO:0000313|Proteomes:UP000006794};
RN [1] {ECO:0000313|EMBL:AEH36740.1, ECO:0000313|Proteomes:UP000006794}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18323 / JCM 14033 / SH-6
RC {ECO:0000313|Proteomes:UP000006794};
RX PubMed=22675596; DOI=10.4056/sigs.2505605;
RA Anderson I., Tindall B.J., Rohde M., Lucas S., Han J., Lapidus A.,
RA Cheng J.F., Goodwin L., Pitluck S., Peters L., Pati A., Mikhailova N.,
RA Pagani I., Teshima H., Han C., Tapia R., Land M., Woyke T., Klenk H.P.,
RA Kyrpides N., Ivanova N.;
RT "Complete genome sequence of Halopiger xanaduensis type strain (SH-6(T)).";
RL Stand. Genomic Sci. 6:31-42(2012).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP002839; AEH36740.1; -; Genomic_DNA.
DR RefSeq; WP_013879633.1; NC_015666.1.
DR AlphaFoldDB; F8D898; -.
DR STRING; 797210.Halxa_2115; -.
DR GeneID; 10797077; -.
DR KEGG; hxa:Halxa_2115; -.
DR eggNOG; arCOG04281; Archaea.
DR HOGENOM; CLU_034626_0_0_2; -.
DR OrthoDB; 8643at2157; -.
DR Proteomes; UP000006794; 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; 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:UP000006794};
KW Transcription {ECO:0000256|ARBA:ARBA00023163, ECO:0000256|HAMAP-
KW Rule:MF_00007}; Transferase {ECO:0000256|HAMAP-Rule:MF_00007}.
FT DOMAIN 167..241
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT REGION 276..428
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 304..318
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 338..364
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 375..391
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 522 AA; 54651 MW; FC40A467778B910B CRC64;
MEDTSKYLIH ADVTADGVVE RSDVVGAVFG QTEGLLGDEL DLRDLRQSQK VGRIDVEIAS
TAGQSHGHLT IATSLDKVET ATLAAALETI TRIGPCRADL EVTEIEDVRA AKRKEVVDRA
KELLHTAFDD SVMTSEEILA EVRQHVRVED ITEYEGLPAG PRVGESDAII VVEGRADVLT
LLKYGVKNAI AVEGTNVPDA VAELTRHRTV TAFLDGDRGG DLILEELSQV GDIDYVAFAP
AGESVEELDH HQLFAALRNK VPYETVSGLN EPREAVAATD GSTTPAPAPG ATDATDATDA
IDATDATDET NGSDASADSN AGDALPRSPA IDGTRSASEY DSAGTDPTHS LESSAASDTR
PAADSSTGAD LEGEGETPKP AHDREPGAES AESAADAETE AGTAAESRTD DADATESEPT
TVYEHATDVI RGDSDRVRFL GAAGEAIADA DAGEAYDALA NLETVPTTVV LDGILSQRLL
DLAADRGVDR IVADALGQFT KRPTDVRIHA IEAVAEEPPN GN
//
