ID A0A1F6PJK3_9BACT Unreviewed; 843 AA.
AC A0A1F6PJK3;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
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=A2039_04250 {ECO:0000313|EMBL:OGH96260.1};
OS Candidatus Melainabacteria bacterium GWA2_34_9.
OC Bacteria; Candidatus Melainabacteria.
OX NCBI_TaxID=1801604 {ECO:0000313|EMBL:OGH96260.1, ECO:0000313|Proteomes:UP000198266};
RN [1] {ECO:0000313|EMBL:OGH96260.1, ECO:0000313|Proteomes:UP000198266}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OGH96260.1}.
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DR EMBL; MFRJ01000096; OGH96260.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F6PJK3; -.
DR STRING; 1801604.A2039_04250; -.
DR Proteomes; UP000198266; 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; 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 InterPro; IPR036390; WH_DNA-bd_sf.
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; PF13412; HTH_24; 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 SUPFAM; SSF46785; Winged helix' DNA-binding domain; 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 Zinc {ECO:0000256|HAMAP-Rule:MF_00983};
KW Zinc-finger {ECO:0000256|HAMAP-Rule:MF_00983}.
FT DOMAIN 317..485
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 577..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"
FT REGION 207..230
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 207..222
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 843 AA; 95405 MW; 29D5123E3B348B11 CRC64;
MIPINKYAQV IVDIQNLDTR TFSYLIPEEL QEIVKIGLPV LVPFGNQGVV NAFVVGFSNY
LPAEIKAKYI YEILDTEPFF DLDYLQFAEW VANYYCCNLQ NVLECAIPSN FFSKSKRIVS
LVKENFSDVK FNANQEKVIA VLKEKPEISV FSLQKKTKIS SSAFYEALRK LRAANIIEIN
TLIEAKSAKP KLEKFVRFLC HSEGVSPKNL SNSENSQPDR SFARPADSGD MLRMTDKQNK
IIEQLEKLGG EYKLNEFLKE AKTTVPTVKK IAETGKIEIF DKEIYRNPLK IFENQTKDEF
LTLSEHQKEA LSKITDSMET NNSEPLLLYG ITGSGKTEVY LHAAKTALEK GTSVIILAPE
ILLASQLAKR ISARFGVDKV ALWHSNISEG ERFDVWERIR SGEVKIIVGA RSAIFAPVKN
LGLIIIDEEH ESSYKQTSPS PRYNAKTLAF ERTKRTRSAL VLGSATPDVV SYYRAKNTDR
ILHLPERFGS GELAGVTVFD MREEFNTGNK SIFSRALRHN LKKNLEEGKQ SILLINRRGF
STYGQCVNCG FVAECESCSI PLILHKTTNK LRCHYCNFER DFINTCPECG SGAFKYSGLG
TQKVEELFNK NFPEARAARI DSDIMTKKNA HIEIIEAFTQ GEIDVLIGTQ MIAKGLDIAN
VTLVGVLSAD SLFNMPDFRA GERGFQLLTQ VAGRAGRGDF KGKVYFQTYS PEYFAIQHAK
EQDFVSFYNY EMQGRNDLSY PPFSYLIRLI ISSKNETKAR KISEEVAYKL KVLTELRGID
ERLEVLGPSP CIISRLKDEY RFHIIIKNTM GENGHFMITN YLKTLNIPAD VKFLIDVDPS
DML
//
