ID A0A066ZR63_HYDMR Unreviewed; 748 AA.
AC A0A066ZR63;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
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=EI16_08375 {ECO:0000313|EMBL:KDN96283.1};
OS Hydrogenovibrio marinus.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC Piscirickettsiaceae; Hydrogenovibrio.
OX NCBI_TaxID=28885 {ECO:0000313|EMBL:KDN96283.1, ECO:0000313|Proteomes:UP000027341};
RN [1] {ECO:0000313|EMBL:KDN96283.1, ECO:0000313|Proteomes:UP000027341}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MH-110 {ECO:0000313|EMBL:KDN96283.1,
RC ECO:0000313|Proteomes:UP000027341};
RA Cha H.J., Jo B.H., Hwang B.H.;
RT "Draft genome sequence of Hydrogenovibrio marinus MH-110, a model organism
RT for aerobic H2 metabolism.";
RL Submitted (APR-2014) 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:KDN96283.1}.
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DR EMBL; JMIU01000001; KDN96283.1; -; Genomic_DNA.
DR RefSeq; WP_029912134.1; NZ_JMIU01000001.1.
DR AlphaFoldDB; A0A066ZR63; -.
DR STRING; 28885.EI16_08375; -.
DR Proteomes; UP000027341; 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:UP000027341};
KW Zinc {ECO:0000256|HAMAP-Rule:MF_00983};
KW Zinc-finger {ECO:0000256|HAMAP-Rule:MF_00983}.
FT DOMAIN 215..381
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 478..645
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT ZN_FING 443..455
FT /note="C4-type"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00983"
FT ZN_FING 470..486
FT /note="C4-type"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00983"
SQ SEQUENCE 748 AA; 84290 MW; 9FEE3A65716724B2 CRC64;
MFIQVAVPGP FLTPLDYQYV YDEKQILPVV GGRVWVPFRN RKLIGVVMSI KETTDLDVKK
IRLISEVVDA APIFSERDLQ FLQWAAHYYH EPIGNVMQTA LPKRLKEGEA VALEGVTAWQ
LNDTGRAEAA DKIRSNAIQQ LNVLEFLKSH PYPVTESTLT ACLSGWRTPM KRFHEMGWVD
KTEKNCLHAW QQAEDPNHSL NEEQQAAVDA VLDKALQTED FHAFLLEGVT GSGKTETYLG
MIESTIAQGK QVLVLVPEIG LTPQTVERFE RFLNQPVAVM HSDLTDRERH CAWYMVQSNQ
VKVLLGTRSA LFTPFANLGL CILDEEHDLS FKQQDNFRYS ARDALVRRAQ LEKVPVVLGS
ATPSLETLHN AMSGRYGYLK LTQRAGGASM PEMRLLDVRG DKSVQQHEGV SSALREMITN
HLEQQGQVLL FLNRRGFAPV LMCHSCGWQA ACPSCDANMT YHHQFRELRC HHCGYQQKAP
QACPSCGEQE FVNVGQGTEK LETIIQSWFP NYKTLRIDRD TTRNKGQMAE ATQLAREGKA
DILIGTQMLA KGHHFPKVTL VALLDIDQGL FSCDFRAAER MAQLVVQVAG RAGRAEREGE
VVIQTHHPDH PLLKTLVEHG YDAFAKEALD ERKAGELPPF SYQILLRAES IDPHSAWQFL
LDIESALQLK AVDQTKSARL GSAPLEAFGP VSAPMLRRQG RFRYQLLLQS SHRGLLHHWL
GSLESNIYAH PLVNKVRWSI DVDPQEMS
//