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Database: UniProt
Entry: R6EXG4_9FIRM
LinkDB: R6EXG4_9FIRM
Original site: R6EXG4_9FIRM 
ID   R6EXG4_9FIRM            Unreviewed;       745 AA.
AC   R6EXG4;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 45.
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=BN538_00576 {ECO:0000313|EMBL:CDB01824.1};
OS   Lachnospiraceae bacterium CAG:215.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX   NCBI_TaxID=1262985 {ECO:0000313|EMBL:CDB01824.1, ECO:0000313|Proteomes:UP000018007};
RN   [1] {ECO:0000313|EMBL:CDB01824.1, ECO:0000313|Proteomes:UP000018007}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:215 {ECO:0000313|Proteomes:UP000018007};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) 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:CDB01824.1}.
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DR   EMBL; CBCV010000448; CDB01824.1; -; Genomic_DNA.
DR   AlphaFoldDB; R6EXG4; -.
DR   Proteomes; UP000018007; 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};
KW   DNA replication {ECO:0000256|ARBA:ARBA00022705, ECO:0000256|HAMAP-
KW   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   Zinc {ECO:0000256|HAMAP-Rule:MF_00983};
KW   Zinc-finger {ECO:0000256|HAMAP-Rule:MF_00983}.
FT   DOMAIN          219..385
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          481..648
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   ZN_FING         447..459
FT                   /note="C4-type"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00983"
FT   ZN_FING         473..489
FT                   /note="C4-type"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00983"
SQ   SEQUENCE   745 AA;  84912 MW;  F51FD2B9EC599744 CRC64;
     MFANIIVDIT HEKLDKIFQY RVPSRLAGEL SVGMEVFVPF GKWNRQTKGY VVGFSEICDY
     DLSKVKEIAD ISRGGIAIEG KLVALAAWMK EQYGGTMIQA LKTVLPIKQK ENAKMKKRIR
     LLLDKDTGKK KLDYYLEKNQ KARARLLAAL LDEPVLEYEL VSKKLNITLS VIRALEEQGV
     VALEEERVFR NPVRGKEQEA RTITFTEEQQ HAIDVFREDY EQKRYGTYLV HGVTGSGKTE
     VYIEMIRRVA DSGRQAIVLI PEIALTFQTV MRFYRCFGDR VSIMNSRLSA GERYDQLMRA
     KSGEVDVMIG PRSALFTPFP NLGLIVIDEE HENTYKSEQT PRYHARETAE ARAKMEGASV
     VLGSATPSME SMYRARLGEY RLLELKKRSR EQEMADVYVT DLREELKNGN RSILSEKLQE
     LMEDRLNRHE QIMLFLNRRG YAGFISCREC GYVVKCPHCD VSLSFHRGGK MVCHYCGHEE
     AKPNVCPECG SRHIGEFKAG TQQIEDIVKR RFPEARVLRM DMDTTREKDG HEKILAAFAN
     EEADVLVGTQ MIVKGHDFPN VTLVGVLAAD MSLYSDDYRA GERTFQLLTQ AVGRAGRGEK
     KGEAVIQTYS PEHYAVVTAA AQDYAAFYEE EIRYRSLMGY PPVENLLAVF ASGKDEAHLE
     TGCRYLKEYA KRVCQADPSS PVEIIGPASP GIGKINDVYR KVLYLKTERY DTLVKIKNRL
     EQYIEVNSGF NTIRIQFDFN PMNVF
//
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