ID L1QFA6_9CLOT Unreviewed; 735 AA.
AC L1QFA6;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 50.
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=HMPREF0216_01821 {ECO:0000313|EMBL:EKY26636.1};
OS Clostridium celatum DSM 1785.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=545697 {ECO:0000313|EMBL:EKY26636.1, ECO:0000313|Proteomes:UP000010420};
RN [1] {ECO:0000313|EMBL:EKY26636.1, ECO:0000313|Proteomes:UP000010420}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 1785 {ECO:0000313|EMBL:EKY26636.1,
RC ECO:0000313|Proteomes:UP000010420};
RA Weinstock G., Sodergren E., Lobos E.A., Fulton L., Fulton R., Courtney L.,
RA Fronick C., O'Laughlin M., Godfrey J., Wilson R.M., Miner T., Farmer C.,
RA Delehaunty K., Cordes M., Minx P., Tomlinson C., Chen J., Wollam A.,
RA Pepin K.H., Bhonagiri V., Zhang X., Suruliraj S., Warren W., Mitreva M.,
RA Mardis E.R., Wilson R.K.;
RL Submitted (MAY-2012) 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:EKY26636.1}.
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DR EMBL; AMEZ01000053; EKY26636.1; -; Genomic_DNA.
DR RefSeq; WP_005213519.1; NZ_KB291645.1.
DR AlphaFoldDB; L1QFA6; -.
DR STRING; 545697.HMPREF0216_01821; -.
DR GeneID; 85156539; -.
DR PATRIC; fig|545697.3.peg.1791; -.
DR eggNOG; COG1198; Bacteria.
DR HOGENOM; CLU_013353_3_1_9; -.
DR OrthoDB; 9759544at2; -.
DR Proteomes; UP000010420; 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:UP000010420};
KW Zinc {ECO:0000256|HAMAP-Rule:MF_00983};
KW Zinc-finger {ECO:0000256|HAMAP-Rule:MF_00983}.
FT DOMAIN 212..378
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 474..631
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT ZN_FING 440..452
FT /note="C4-type"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00983"
FT ZN_FING 466..482
FT /note="C4-type"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00983"
SQ SEQUENCE 735 AA; 85155 MW; 57F87A03766D1806 CRC64;
MKLYAEIIVN SDALEIDRPF TYKVPHELEE DIKIGQIVKV PFGFGNRYSE GFVLSIKKEE
EACLNFKVKE ISSIENKEPI ITEADIELIN FLRTKYLCKY IDAFRLLIPT GILKGAKSKS
KKVIAFIDDD LSKFKSKDGY TEIIDFIKSN SGVYTKAELT KNHSISLYKL NKLIENGNLL
VEEETVYRYN DRIYIKDNEK ELTFEQKNVI EEFLNSKKNI FLLKGVTGSG KTEVYMRLVE
KTLSENKSAI ILVPEISLTP QMIERFKGRF GRDVALFHSK LSDGERFDEW YRVRQGKARL
IVGARSAIFL PAKNLGLIII DEEHENTYKS EQNPKYQTKE VAEFISNQRG CKVILGSATP
SIENYYRAIT GEIELLELKN RVDNKEMPPM QVIDMREELR SGNKSLFSRE LYKSINETLS
KGEQVILFLN RRGFSTFVSC RSCGYVFKCE ECDISMTYHK NGFLVCHYCG KTKREPKVCP
KCDSKYVKFF GAGTQRVEEE VRKYFKDARV LRMDVDTTRE KNSHEKIYNA FKEKKANILI
GTQMVSKGLD FKDVTLVGIL AADMSINIPD YRSGEKTFQI ITQVAGRAGR GEKQGKVIIQ
TYTPEHYSLN YAINYDYEGF YEKEFTIRAL MKYPPFGKIF LINGISKNEE LLKEFMHKIF
NIIEPLVKKE YDLEILGPIP CMISKIKENY RWQIIIKGEF NDEFAKNIKE LLYEENKNVY
NDIRISIDIN PNNLN
//
