ID A0A0L8V480_9BACT Unreviewed; 839 AA.
AC A0A0L8V480;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
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=NC99_40870 {ECO:0000313|EMBL:KOH43133.1};
OS Sunxiuqinia dokdonensis.
OC Bacteria; Bacteroidota; Bacteroidia; Marinilabiliales; Prolixibacteraceae;
OC Sunxiuqinia.
OX NCBI_TaxID=1409788 {ECO:0000313|EMBL:KOH43133.1, ECO:0000313|Proteomes:UP000036958};
RN [1] {ECO:0000313|Proteomes:UP000036958}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK {ECO:0000313|Proteomes:UP000036958};
RA Ahn S., Kim B.-C.;
RT "Genome sequencing of Sunxiuqinia dokdonensis strain SK.";
RL Submitted (JUL-2015) 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:KOH43133.1}.
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DR EMBL; LGIA01000199; KOH43133.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0L8V480; -.
DR STRING; 1409788.NC99_40870; -.
DR PATRIC; fig|1409788.3.peg.4176; -.
DR Proteomes; UP000036958; 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:UP000036958};
KW Zinc {ECO:0000256|HAMAP-Rule:MF_00983};
KW Zinc-finger {ECO:0000256|HAMAP-Rule:MF_00983}.
FT DOMAIN 313..483
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 559..738
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT ZN_FING 546..558
FT /note="C4-type"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00983"
FT ZN_FING 573..589
FT /note="C4-type"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00983"
SQ SEQUENCE 839 AA; 96152 MW; 90DD10D7BADEF56D CRC64;
MKESFFRTNK NSDVCIMSVQ MFADVILPLP LHDKFTYLVA PGFEPNMKVG IRVVVQFGAR
KFFSALVFRL HNQPPEGDFE LKEIEAVLDQ EPIVNHAQII AWEWVANYYC CSLGEVYKAA
LPSALKLESQ SNICVNPNFE TTGELNGEET ALLMMLQGKG QANIREINQF LGKKSSYATL
KILLEKNAIL MEEKLKESYK PKTVSMIRLA KEVSSPDEIQ LALESLKKAR KQSELLTYFL
SATIFHQEPK TSLLKKELLE QAGVSEAVLK ALIDKKILEN ESVEIGRLEM NHSADQYLYE
LNEVQEKTLL ELKQAFRSNR PVLLHGVTSS GKTEIYIKLI EEVLAEGKQV LYLVPEIGLT
SQLITRLKRA FGDRAGIYHS KFNDAERVEI WFNILHDKKD SYQVVVGARS AVFLPFKMLG
LIIVDEEHEN SYKQFDPAPR YNARDLAIVL GQIHKSPVLL GTATPSFESY YNVKLDKYAL
VELNERFQGI EMPEIVVADI RKATRQRQMK SLLTPSLFEE MKLALENNEQ VILFQNRRGF
APYVQCKTCG WIPKCKNCDV SLTYHKFRSG LVCHYCGHTS SLPANCGECH SEDIQTKGFG
TEQIEEELGL LFPEASIARM DLDTTRAKRS FEQMIYKFEN RQIDILVGTQ MVTKGLDFDH
VRVVGILNAD QLLNYPDFRS FERSFQLMAQ VSGRAGRKGK RGKVVIQSSQ ADHEVLQEVV
DNNFIQLFNR QMHERKLFRY PPYFRLIKLV VKHKNRDRLD LGANQLADLL RKHFRNQVLG
PEYPVVGRIQ NWYQKEIWLK LEKSKVLNQN KRMLMDAIDQ VKSLPNNGGL VIYADVDPM
//
