ID A0A0D1XMX2_ANEMI Unreviewed; 809 AA.
AC A0A0D1XMX2;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=Primosomal protein N' {ECO:0000256|HAMAP-Rule:MF_00983};
DE EC=3.6.4.- {ECO:0000256|HAMAP-Rule:MF_00983};
DE AltName: Full=ATP-dependent helicase PriA {ECO:0000256|HAMAP-Rule:MF_00983};
GN Name=priA {ECO:0000256|HAMAP-Rule:MF_00983};
GN ORFNames=AF333_09690 {ECO:0000313|EMBL:KON95707.1},
GN SAMN04487909_103167 {ECO:0000313|EMBL:SDI34981.1};
OS Aneurinibacillus migulanus (Bacillus migulanus).
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae;
OC Aneurinibacillus group; Aneurinibacillus.
OX NCBI_TaxID=47500 {ECO:0000313|EMBL:KON95707.1, ECO:0000313|Proteomes:UP000037269};
RN [1] {ECO:0000313|EMBL:KON95707.1, ECO:0000313|Proteomes:UP000037269}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2895 {ECO:0000313|EMBL:KON95707.1,
RC ECO:0000313|Proteomes:UP000037269};
RA Liu B., Wang J., Zhu Y., Liu G., Chen Q., Chen Z., Lan J., Che J., Ge C.,
RA Shi H., Pan Z., Liu X.;
RT "Fjat-14205 dsm 2895.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:SDI34981.1, ECO:0000313|Proteomes:UP000182836}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2895 {ECO:0000313|EMBL:SDI34981.1,
RC ECO:0000313|Proteomes:UP000182836};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in the restart of stalled replication forks.
CC Recognizes and binds the arrested nascent DNA chain at stalled
CC replication forks. It can open the DNA duplex, via its helicase
CC activity, and promote assembly of the primosome and loading of the
CC major replicative helicase DnaB onto DNA. {ECO:0000256|HAMAP-
CC Rule:MF_00983}.
CC -!- SUBUNIT: Component of the primosome. {ECO:0000256|HAMAP-Rule:MF_00983}.
CC -!- SIMILARITY: Belongs to the helicase family. PriA subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_00983}.
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DR EMBL; LGUG01000004; KON95707.1; -; Genomic_DNA.
DR EMBL; FNED01000003; SDI34981.1; -; Genomic_DNA.
DR RefSeq; WP_043066037.1; NZ_LGUG01000004.1.
DR AlphaFoldDB; A0A0D1XMX2; -.
DR STRING; 47500.AF333_09690; -.
DR PATRIC; fig|47500.8.peg.6922; -.
DR OrthoDB; 9759544at2; -.
DR Proteomes; UP000037269; Unassembled WGS sequence.
DR Proteomes; UP000182836; Unassembled WGS sequence.
DR GO; GO:1990077; C:primosome complex; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006269; P:DNA replication, synthesis of RNA primer; IEA:UniProtKB-KW.
DR GO; GO:0006268; P:DNA unwinding involved in DNA replication; IEA:UniProtKB-UniRule.
DR CDD; cd17929; DEXHc_priA; 1.
DR CDD; cd18804; SF2_C_priA; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 3.40.1440.60; PriA, 3(prime) DNA-binding domain; 1.
DR HAMAP; MF_00983; PriA; 1.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005259; PriA.
DR InterPro; IPR041222; PriA_3primeBD.
DR InterPro; IPR042115; PriA_3primeBD_sf.
DR InterPro; IPR041236; PriA_C.
DR InterPro; IPR040498; PriA_CRR.
DR NCBIfam; TIGR00595; priA; 1.
DR PANTHER; PTHR30580; PRIMOSOMAL PROTEIN N; 1.
DR PANTHER; PTHR30580:SF0; PRIMOSOMAL PROTEIN N; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF17764; PriA_3primeBD; 1.
DR Pfam; PF18074; PriA_C; 1.
DR Pfam; PF18319; PriA_CRR; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00983}; DNA replication {ECO:0000256|HAMAP-Rule:MF_00983};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW Rule:MF_00983};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|HAMAP-Rule:MF_00983};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00983};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_00983};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00983};
KW Primosome {ECO:0000256|ARBA:ARBA00022515, ECO:0000256|HAMAP-Rule:MF_00983};
KW Reference proteome {ECO:0000313|Proteomes:UP000037269};
KW Zinc {ECO:0000256|HAMAP-Rule:MF_00983};
KW Zinc-finger {ECO:0000256|HAMAP-Rule:MF_00983}.
FT DOMAIN 295..452
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 549..708
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT ZN_FING 514..526
FT /note="C4-type"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00983"
FT ZN_FING 541..557
FT /note="C4-type"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00983"
SQ SEQUENCE 809 AA; 92562 MW; 5C161344DBFF4CF9 CRC64;
MFAQVVVDVP VVDTDRPFDY RIPESLAPFV FVGSRVSVPF GPRKLQGFVV GLADTSEVEK
TRDILDVLDV EPPLTEEMVW LARRISERYM CTYYTALQSM VPAVLRSSYD KQIFLTAAGE
AFVSVLSDEQ AFYEYIRNRQ PVLWNKIMKE FPFAAAWLDE GLKKNRIRVE QIVGDRVTKK
TITILSPAVS VEELEAAQGE LSKTAVRQKE VLSHFIHFYG PIPQPELLSL LGVSNQAVKG
LVDKGLLIKE EVEGYRDPFS GRTFTPAPKH PFTAQQKTVI DGIVEGMNPP VYYPCLLHGV
TGSGKTEVYL EIMERTIDQG REAILLVPEI SLTPQMVNRF KGRFGSQVAV MHSRLSQGER
YDEWRKIRRG EVKVAIGARS AIFAPFQNLG LIILDEEHEG SYKQEETPRY HARTIAQYRG
MHHHAVVILG SATPSMESYH EAKKGRIHFF EMRERVGNRP LPEVTVVDMR EELRDGNRTM
FSKPLMDSIN NRLEKNEQIV MFLNRRGFST FVMCRSCGYV AQCPHCDISL TYHRSNQTLR
CHYCGYTERE PQICPECGSE HIRFFGTGTQ KVEEELARYF PGIRVIRMDV DTTGRKGAHE
KLLQDFREGK GDVLLGTQMI AKGLDFPNVT LVGVLAADSL LNLPDFRAAE RTFQLVTQVG
GRAGRHEKKG EVILQTYNTE HYSIQYASRH DYESFFVEEI KQRYEKNYPP YYRLVLFTFA
HENVPLLVKI SERFARKLRE TIPPGAYLLG PVASPIARIK DRYRFQCMIK YKNDPRVLPA
IHQVVRAFDE ERKKTGIMLT VDVDPQMMM
//
