ID A0A1H6USZ3_9FLAO Unreviewed; 813 AA.
AC A0A1H6USZ3;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
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=SAMN05660918_2015 {ECO:0000313|EMBL:SEI94816.1};
OS Flavobacterium terrigena.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=402734 {ECO:0000313|EMBL:SEI94816.1, ECO:0000313|Proteomes:UP000199702};
RN [1] {ECO:0000313|EMBL:SEI94816.1, ECO:0000313|Proteomes:UP000199702}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17934 {ECO:0000313|EMBL:SEI94816.1,
RC ECO:0000313|Proteomes:UP000199702};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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}.
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DR EMBL; FNYA01000004; SEI94816.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H6USZ3; -.
DR STRING; 402734.SAMN05660918_2015; -.
DR OrthoDB; 9759544at2; -.
DR Proteomes; UP000199702; 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 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; 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 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 289..458
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 534..711
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT ZN_FING 521..533
FT /note="C4-type"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00983"
FT ZN_FING 548..564
FT /note="C4-type"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00983"
SQ SEQUENCE 813 AA; 93766 MW; AC15BCBBB20BA112 CRC64;
MHFINVILPL NLDKTFTYSV NVEEYKFLQP GMRVTVPFGK TKVYTALVVD KHTNPPELYE
AKEISQIIDE VPIVNEIQLK HWSWIASYYM CSIGEVFKSA LPSGLILESE TIISSSHTES
DKTLATDEEF LVLEALENKS SITISEISQI LNKKNVIPII QNLLAKGLLT MQEEVQENYK
PKLVKYIKLQ DEFLQPEQLQ ELLEILGKAK KQKEIVLSYF QLQATEKKPI TSKLLIETSG
VSAAVIKSLV DKQIFEEYYI NTDRVSFEKE DDYEIQLSES QTIVLESIKE KFTQFDVNLL
HGVTASGKTE VYIKLIEEFI EQDKQVLFLL PEIALTTQLV QRLSAYFGNQ IAVFHSKYNS
NERVEVYNHV LQNSDKAKVV LGVRSALFLP FSNLGLIVVD EEHEATYKQQ DPAPRYHARD
AAIVLAKFHN AKVLLGSATP SLESYHNAKT NKYGLIELFT RFNNVVLPEI HLIDLKDKYF
RKRMDGHFSD ELLERMHETL ANNEQIMLFQ NRRGYSPYIE CATCGHVPQC PSCDVSLTYY
KYKNHLKCHY CGHSMAKPTH CHACNSLDIS AKGFGTEQVE LELIKLFPNK RIARMDQDTT
RGKFAFEKMI DAFKNQEIDI LVGTQMLAKG LDFENVTLVG ILNADNLLNQ PYYRAYERAY
QMMVQVAGRS GRKAKKGSVV IQTYNPMHNT IQQVVNNNYL GMFNEQLYER RNFQYPPYFR
LLQIRLKHRD YEKLREGSTW LYNVLKQAIQ VPILGPEEPA INRIRNEYIR TILIKIPNNT
NLIQTKKLIK KVLISFEATS QYRSIKTTIN VDY
//
