ID A0A0A2MIT3_9FLAO Unreviewed; 816 AA.
AC A0A0A2MIT3;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 36.
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=Q766_12260 {ECO:0000313|EMBL:KGO92547.1};
OS Flavobacterium subsaxonicum WB 4.1-42 = DSM 21790.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=1121898 {ECO:0000313|EMBL:KGO92547.1, ECO:0000313|Proteomes:UP000030111};
RN [1] {ECO:0000313|EMBL:KGO92547.1, ECO:0000313|Proteomes:UP000030111}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WB 4.1-42 {ECO:0000313|EMBL:KGO92547.1,
RC ECO:0000313|Proteomes:UP000030111};
RA Zeng Z., Chen C.;
RL Submitted (SEP-2013) 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:KGO92547.1}.
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; JRLY01000009; KGO92547.1; -; Genomic_DNA.
DR RefSeq; WP_026991421.1; NZ_JRLY01000009.1.
DR AlphaFoldDB; A0A0A2MIT3; -.
DR STRING; 1121898.GCA_000422725_03452; -.
DR eggNOG; COG1198; Bacteria.
DR OrthoDB; 9759544at2; -.
DR Proteomes; UP000030111; 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; 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:UP000030111};
KW Zinc {ECO:0000256|HAMAP-Rule:MF_00983};
KW Zinc-finger {ECO:0000256|HAMAP-Rule:MF_00983}.
FT DOMAIN 290..459
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 546..712
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT ZN_FING 522..534
FT /note="C4-type"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00983"
FT ZN_FING 549..565
FT /note="C4-type"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00983"
SQ SEQUENCE 816 AA; 93220 MW; 0E45B9E85A084D8A CRC64;
MPYFTQVILP LALPKSFTYS VNEAEYAYLK SGMRVAVPFG KNKIYTGLVI ELHQNPPQLY
QAKEIHQILD DNPIVTETQL QHWNWIAEYY MCTIGEVYKS ALPGGFILES ETIITSQKDF
NPLEIALTDE EYLVYEALQT QSALKVQEVV SILNKKTILP VINRLIAKNA VSLQEEISEK
YKPKTTRYIR LQPEFLQESQ LSELMELLSR AQKQREAVLQ YFQLHAAEKK PVTVKKLTEA
GTTAAVIKSL IDKGVFEEYF LEEDRVQFTG SGNAAFNLSE KQQGAFDEIK ASFDKHAVTL
LHGITSSGKT EIYIRLIEEF INSGKQVLYL LPEIALTTQL VVRLTAYFGN KVAVFHSKYT
NNERVETWQQ VLEASAKAQV VIGARSALFL PFQKLGLIII DEEHEQTFKQ QDPAPRYHAR
DAAIVLANMF GAKVLLGSAT PSIESYSNVN AGKYGYVALK ERFGKVLPPE IILVDIKDKY
KRKRMTGHFS DTMTEAIAET LALGKQVILF QNRRGFSPWI ECMTCGHVPQ CPQCDVSLTY
YKYKNQLRCH YCAYHIANPT HCHQCHSTDI SSKGFGTEQI ELELKTLFPD KNSWRMDQDT
TRGKHGYEKI IDSFKNREID ILVGTQMLAK GLHFDNVGLV GILNADNMLF QPDFRAFERA
YQMMVQVAGR AGRKEDRGTV LIQTYNPLHN VIRQVTENDY EGMFKEQIYE RHNFKYPPYF
RLVRIILKHK DYEKLKNASL WLHNVLMQHL NNIPVLGPEE PGISRIRNEY IRAIMIKIPP
GAALGNTKRT IGKILESLDA VPQYRSVKVT VNVDPY
//
