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Database: UniProt
Entry: A7HND9_FERNB
LinkDB: A7HND9_FERNB
Original site: A7HND9_FERNB 
ID   A7HND9_FERNB            Unreviewed;       775 AA.
AC   A7HND9;
DT   11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT   11-SEP-2007, sequence version 1.
DT   27-MAR-2024, entry version 99.
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   OrderedLocusNames=Fnod_1579 {ECO:0000313|EMBL:ABS61422.1};
OS   Fervidobacterium nodosum (strain ATCC 35602 / DSM 5306 / Rt17-B1).
OC   Bacteria; Thermotogota; Thermotogae; Thermotogales; Fervidobacteriaceae;
OC   Fervidobacterium.
OX   NCBI_TaxID=381764 {ECO:0000313|EMBL:ABS61422.1, ECO:0000313|Proteomes:UP000002415};
RN   [1] {ECO:0000313|EMBL:ABS61422.1, ECO:0000313|Proteomes:UP000002415}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35602 / DSM 5306 / Rt17-B1
RC   {ECO:0000313|Proteomes:UP000002415};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Saunders E., Brettin T., Bruce D., Detter J.C.,
RA   Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Nelson K., Gogarten J.P., Noll K., Richardson P.;
RT   "Complete sequence of Fervidobacterium nodosum Rt17-B1.";
RL   Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ABS61422.1, ECO:0000313|Proteomes:UP000002415}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35602 / DSM 5306 / Rt17-B1
RC   {ECO:0000313|Proteomes:UP000002415};
RX   PubMed=19307556; DOI=10.1073/pnas.0901260106;
RA   Zhaxybayeva O., Swithers K.S., Lapierre P., Fournier G.P., Bickhart D.M.,
RA   DeBoy R.T., Nelson K.E., Nesbo C.L., Doolittle W.F., Gogarten J.P.,
RA   Noll K.M.;
RT   "On the chimeric nature, thermophilic origin, and phylogenetic placement of
RT   the Thermotogales.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:5865-5870(2009).
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; CP000771; ABS61422.1; -; Genomic_DNA.
DR   AlphaFoldDB; A7HND9; -.
DR   STRING; 381764.Fnod_1579; -.
DR   KEGG; fno:Fnod_1579; -.
DR   eggNOG; COG1198; Bacteria.
DR   HOGENOM; CLU_013353_4_1_0; -.
DR   OrthoDB; 9759544at2; -.
DR   Proteomes; UP000002415; Chromosome.
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   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
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; 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; 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; 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}; Coiled coil {ECO:0000256|SAM:Coils};
KW   DNA replication {ECO:0000256|HAMAP-Rule:MF_00983};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_00983};
KW   Helicase {ECO:0000256|HAMAP-Rule:MF_00983};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00983};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00983};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00983}; Primosome {ECO:0000256|HAMAP-Rule:MF_00983};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002415};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_00983};
KW   Zinc-finger {ECO:0000256|HAMAP-Rule:MF_00983}.
FT   DOMAIN          259..421
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          511..687
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   ZN_FING         479..491
FT                   /note="C4-type"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00983"
FT   ZN_FING         506..522
FT                   /note="C4-type"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00983"
FT   COILED          688..715
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   775 AA;  89056 MW;  9E0CD1B48E83585F CRC64;
     MIYIVALSNS SQIEPVFCEY NGHIEIGERV LLQHKGKKVL GYVIGNQEWA PCDEFLPNQK
     SSSEYSKIVE RMDYISFLEK SRVKALYGLA NFYFSGLGKY FDISFPNKFD DYFSLFVESV
     SPFVNIEKMP YEEFKKIKNY KEYINNGLVK VYRDFETKKP RPRKRGECVY LKISSIELSK
     LKLTVSQSTV VNYLLFKGPT EVEQIIEDLD VKKDVVVQLK NKGIIEILEQ CSDFETLNIK
     PQRVILSDEQ KSIVDKILSY DFRKEKKHLV FGPTGSGKTE VYLEVIEKYL PFGNVLYLVP
     EVSLTEQTIA RLRKRFPDLS IAVYHSYLTE SKRVEIWAKA VKGEINILVG PRSAAFVPLK
     NLNLAIVDEE HDEGYYNNSE PFYEIHTFLN ALPITVVYGS ATPSLESYKK AKDGEYVFHK
     LTKRYNVELP EVEIVDMNKT KKVTFSISEI LYNNLSKVLE ADKSAIIFTR RKGFSRVQCA
     VCGYIVKCEH CDVAMTYHLD SNNLKCHICG SEKELSLNCP NCGSNMFIDR GTGSEKVEKE
     LQQLFPSRNI GRIDAEIADT PEKLKKLLDY LREGKIDIVA GTKMITKGLD IYRIALIGVV
     DVDALISYPD INAPLRTFQL LVQVIGRAGR NEKGKAIIQT YKPTDPVITF ASNQDVEGFY
     ERELEIRKQL NYPPFASVVV LTYANLNQEI ARETIDTVAD EIENIEKKEK KVQEVYKYYL
     ELLGPSEHPI FKANNKYRYQ IFFKTNNVPE LVRLLKKIIS NYSGEWIIKV NPNEI
//
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