ID A0A2V3ZVS2_9BACT Unreviewed; 824 AA.
AC A0A2V3ZVS2;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
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 ECO:0000313|EMBL:PXY00755.1};
GN ORFNames=DF185_12675 {ECO:0000313|EMBL:PXY00755.1};
OS Marinifilum breve.
OC Bacteria; Bacteroidota; Bacteroidia; Marinilabiliales; Marinifilaceae.
OX NCBI_TaxID=2184082 {ECO:0000313|EMBL:PXY00755.1, ECO:0000313|Proteomes:UP000248079};
RN [1] {ECO:0000313|EMBL:PXY00755.1, ECO:0000313|Proteomes:UP000248079}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JC075 {ECO:0000313|EMBL:PXY00755.1,
RC ECO:0000313|Proteomes:UP000248079};
RA Fu T.;
RT "Marinifilum breve JC075T sp. nov., a marine bacterium isolated from Yongle
RT Blue Hole in the South China Sea.";
RL Submitted (MAY-2018) 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:PXY00755.1}.
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DR EMBL; QFLI01000005; PXY00755.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2V3ZVS2; -.
DR OrthoDB; 9759544at2; -.
DR Proteomes; UP000248079; 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; 2.
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 297..468
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 566..732
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT ZN_FING 531..543
FT /note="C4-type"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00983"
FT ZN_FING 558..574
FT /note="C4-type"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00983"
SQ SEQUENCE 824 AA; 94439 MW; 8063391FD2999732 CRC64;
MNNNLNFADI ILPLPLAGVY TYSIPDEFKN QMAIGKRVVV PLGTKKLYTG IVQALHNNAP
ADYKVKDILS CLDDFPVINN FQLKFWDWIS QYYQSVLGDV YKAAIPSGLK LESQTKIILN
EEFVADNALS KTEDQILNIL SKSKDVSIAS LNQATGLKNT LPQIKSLLDK GAVVIEEHIS
SGYKEKKQEF VSLHSNFTEE EIGEILNGLK RAKKQQELLY SYLNLSKHYF EEKPEKVSSN
ELLKSVDCSR AILKSLVDKN ILKFYFEKLD RLDLSSINTT GLKELNPHQE IAINEIRDNF
EHKNCVLLHG VTSSGKTEIY IHLIEEQLKL GKQVLYLLPE IALTTQIINR LKSVFGNKVG
VYHSKFNDSE RVEIYNNVLE NKTDKAYQVI LGVRSSVFLP FNNLGLIIID EEHENTYKQF
DPAPRYHARD AALYLANLHG AKTLLGTATP AVESYYNAQT GKYGLVELFK RYQEIEMPEI
IVADIKEARR RKMMKSIFSP ELMSHMTESL ENKEQIILFQ NRRGYAPYLE CKSCGWVPHC
PNCSVSLTYH RHNNLLVCHY CGHGMTPPNN CEHCGSSGLE DRGFGTEKIE EELLSYFPEA
KVGRMDLDTT RKKNAYEKLI YQFEKHELDI LVGTQMVSKG LDFDNVGLVG ILNADSMLNY
PDFRAYERSF QMMAQVSGRA GRKKKRGKVL IQTYTPEHEI IKNVVKNDYF EMYSSQIAER
KEYIYPPFYR LINISLKHKN QRLVNEAANY FANSLRKIFG IRVFGPQSPV INRIQNSFIV
NILLKIEKKS SPAKAKWILN QQANFLKEIE KFKSIQINFD VDPM
//
