ID A0A0W1QI63_9SPHN Unreviewed; 721 AA.
AC A0A0W1QI63;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
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=ATB93_01455 {ECO:0000313|EMBL:KTF68220.1};
OS Sphingomonas sp. WG.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1592629 {ECO:0000313|EMBL:KTF68220.1, ECO:0000313|Proteomes:UP000052965};
RN [1] {ECO:0000313|EMBL:KTF68220.1, ECO:0000313|Proteomes:UP000052965}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WG {ECO:0000313|EMBL:KTF68220.1,
RC ECO:0000313|Proteomes:UP000052965};
RA Li H., Feng Z., Sun Y., Jiao X., Zhou W., Zhu H.;
RT "Draft Genome Sequence of Sphingomonas sp. WG, a welan gum producing
RT strain.";
RL Submitted (NOV-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:KTF68220.1}.
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DR EMBL; LNOS01000064; KTF68220.1; -; Genomic_DNA.
DR RefSeq; WP_019368998.1; NZ_LNOS01000064.1.
DR AlphaFoldDB; A0A0W1QI63; -.
DR Proteomes; UP000052965; 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 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; 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; PF17764; PriA_3primeBD; 1.
DR Pfam; PF18074; PriA_C; 1.
DR Pfam; PF18319; PriA_CRR; 1.
DR SMART; SM00487; DEXDc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 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:UP000052965};
KW Zinc {ECO:0000256|HAMAP-Rule:MF_00983};
KW Zinc-finger {ECO:0000256|HAMAP-Rule:MF_00983}.
FT DOMAIN 203..369
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT ZN_FING 430..442
FT /note="C4-type"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00983"
FT ZN_FING 457..473
FT /note="C4-type"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00983"
SQ SEQUENCE 721 AA; 78652 MW; FBA31BBD535D1300 CRC64;
MSRARILVLH PALGPLDYRV PSSMEVAPGS IVIVPIGPRQ FAGVVWEPER LPTEEIGDNR
LRAILAVADA PPIPAPVRRL IEWTADYYLA PPSSVLAMTL RTSAAFEAAP TITEYRATGQ
VPDRLTPQRA QALERIGERQ GLVRELAAIA EVSDAVIRGL VKTGAIEAVT VDTQAPYPLP
DPAFAPPELN PAQAAVAGGL RTAVETAAFQ PFLLDGVTGS GKTEVYFEAV AEAIAAGKQT
LVLLPEIALT EPFLTRFARR FGCEPVAWHS GLRSSERRRA WRAIAGGEAL VTVGARSALF
LPYPKLGLIV VDEAHETSFK QEEGVHYHAR DVAVMRGMFE RCPVVLASAT PAIETRHQVE
VGRYAELKLP GRYGAAELPR IEAIDLIREP PERGRWLAPR LVAAIEETLK RGEQSLLFLN
RRGYAPLTLC RHCGHRFQCP NCTAWMVEHR LLHRLSCHHC GHTMPTPSMC PECKSDDTLV
ACGPGVERIA DEVAALWPEA RTAIVTSDTL WSPAKAAEFV SRMEHGAIDI VVGTQLVTKG
YHFPNLTLVG VVDADLGLDG GDLRASERTF QQIMQVSGRA GRGEKPGTVF IQTHAPEARV
MQALVSGDAE AFYAAETESR READAPPFGR YAAIIVSSED KAAAEETARM IGRAAPELAE
MHVYGPAPAP LAMLRGRHRF RLLVHARRSF AVQEVIRDWL GGLSWSQRVR VAVDVDPYSF
V
//
