ID A0A085LAR9_9FIRM Unreviewed; 744 AA.
AC A0A085LAR9;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 39.
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=DK28_0215040 {ECO:0000313|EMBL:KFD42065.1};
OS Peptococcaceae bacterium SCADC1_2_3.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae.
OX NCBI_TaxID=1487582 {ECO:0000313|EMBL:KFD42065.1, ECO:0000313|Proteomes:UP000027084};
RN [1] {ECO:0000313|EMBL:KFD42065.1, ECO:0000313|Proteomes:UP000027084}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCADC1_2_3 {ECO:0000313|EMBL:KFD42065.1};
RA Tan B.F., Charchuk R., Li C., Nesbo C., Abu-Laban N., Foght J.;
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KFD42065.1, ECO:0000313|Proteomes:UP000027084}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCADC1_2_3 {ECO:0000313|EMBL:KFD42065.1};
RA Tan B., Charchuk R., Li C., Nesbo C., Abu-Laban N., Foght J.;
RT "Draft genome sequence of an unculturable Firmicutes affiliated with
RT Peptococcaceae sorted using a microfluidic device from methanogenic alkane-
RT degrading cultures.";
RL Submitted (JUL-2014) 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}.
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:KFD42065.1}.
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DR EMBL; JJNX02000009; KFD42065.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A085LAR9; -.
DR STRING; 1487582.HY00_11075; -.
DR Proteomes; UP000027084; 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 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 SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
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:UP000027084};
KW Zinc {ECO:0000256|HAMAP-Rule:MF_00983};
KW Zinc-finger {ECO:0000256|HAMAP-Rule:MF_00983}.
FT DOMAIN 213..379
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 476..641
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT ZN_FING 442..454
FT /note="C4-type"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00983"
FT ZN_FING 468..484
FT /note="C4-type"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00983"
SQ SEQUENCE 744 AA; 82993 MW; 17F0788B4FCC113E CRC64;
MFAEVLVNIV VRQVDKTFLY AVPEELENKV QIGARVKVPF GRRAADGYVV GLNSDQPAEK
VKEITAVLDH GPLFTPSQLA LARWMAAYYL RPTVEAMQVV IGPRLKATVC RKLKEYWPVK
SDNTEISSSL LLTPKQTALW QVALTNPGLS RTKLAALAGV SSGLIDVLVK KGLLSERVYT
GPAGTSPLDK TPKNEVLVLN PNQKAASGLI NTAIQAKNPE VFLLHGITDS GKTEVYLQCV
QQVISLGGQA IILVPEIALT PQMVDIFYAR FGSTVAILHS RLSAGERFND WNRVQSGEAR
VILGTRSAIF APVTDLRLVV IDEEHEPSYK QEENPRYHAR TVALRLAKQY QAVVVLGSAT
PSLYSYSRAL SGGPFRLSEL SHRVDRRPLP EIRIIDMRQE AKGGNRHLFS QPLQEAIQDR
LNKKEQIILF LNRRGYATFV FCRACGLVMK CPHCNISLCY HANNNLICHY CNYLLPAPSL
CPDCQEQYLG YFGAGTQKIE KEITLLFPQA KVLRLDKDTV SRKNAHRQII MTFQEGEADI
LIGTQMVAKG LDIPGVTLVG VINADITLHM PDFRASERTF QLLMQVAGRA GRSSKGGEVL
VQTYSPQHYA IVAAQKQVYL DFFRQEMMVR RKMNYPPFTR LCRLVLSGTD PDIAAKAAGE
LGAKLKLKAL NLTPLQEEQI EILGPVMAPL AKIKDHYRWH LILKAKEITI LRAAAQIALN
WYEEKTVLKR KVKLVVDLDP QNMM
//
