ID C9MRK2_9BACT Unreviewed; 769 AA.
AC C9MRK2;
DT 24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 24-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 68.
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:EEX17952.1};
GN ORFNames=HMPREF0973_02259 {ECO:0000313|EMBL:EEX17952.1};
OS Prevotella veroralis F0319.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Prevotella.
OX NCBI_TaxID=649761 {ECO:0000313|EMBL:EEX17952.1, ECO:0000313|Proteomes:UP000003327};
RN [1] {ECO:0000313|EMBL:EEX17952.1, ECO:0000313|Proteomes:UP000003327}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0319 {ECO:0000313|EMBL:EEX17952.1,
RC ECO:0000313|Proteomes:UP000003327};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA Mardis E.R., Wilson R.K.;
RL Submitted (SEP-2009) 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:EEX17952.1}.
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DR EMBL; ACVA01000049; EEX17952.1; -; Genomic_DNA.
DR RefSeq; WP_004383944.1; NZ_GG698715.1.
DR AlphaFoldDB; C9MRK2; -.
DR STRING; 649761.HMPREF0973_02259; -.
DR eggNOG; COG1198; Bacteria.
DR HOGENOM; CLU_013353_3_1_10; -.
DR OrthoDB; 9759544at2; -.
DR Proteomes; UP000003327; 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:UP000003327};
KW Zinc {ECO:0000256|HAMAP-Rule:MF_00983};
KW Zinc-finger {ECO:0000256|HAMAP-Rule:MF_00983}.
FT DOMAIN 244..413
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 511..665
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT ZN_FING 476..488
FT /note="C4-type"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00983"
FT ZN_FING 503..519
FT /note="C4-type"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00983"
SQ SEQUENCE 769 AA; 87623 MW; F170356424419BFB CRC64;
MTYANIILPL PLEGYFTYAV SEGLAPQIQV GVRVTVPLGK SKTYVGIVAE YPVDVPKPAK
EVAQQGKKKI VYKNIADVLD DTPILLPQQL RLWKWIADYY MSPIGDVYKA ALPSGLKAED
GFRPRTELFI RLADKYRDEQ TLTLLISSMK RAAKQLDVLM TYLRLTGVDN IEHILPETEL
REVTREELMN ESHASIAVIR SLQEKMILVT YEKEVGRLNH NIAPHPEKIK PLNEAQTEAY
NHILVQMMGH PVTLLHGVTS SGKTEIYIHL IQKAINEHKQ VLYLLPEIAL TVQITERLKA
VFGNRLGIYH SKYSDAERVE IWKKQLSSNP YDVILGARSA VFLPFHRLGL VIIDEEHEQS
FKQQDPAPRY HARSAAIVLA QMYAGAKTLL GTATPSMESY YNAKQGKYGL VELSRRYKDI
HLPSIEVVDM KDLYRRKMVS GPFSPRLLAA VRGALERGEQ AILFQNRRGF APMIECRQCG
WVPKCPNCDI SLTYHKSMNY LSCHYCGYTM KVPEVCPCCE SKDIRGRGYG TEKIEDEIRS
IFPEARIARM DLDTTHTRNA YERLINDFST GKNNLLIGTQ MVTKGLDFGK VSVVGILNAD
SMLNYPDFRA YEQAFMMMSQ VSGRAGRMGK RGEVILQTKT PDLPVIQYVV HNDYPTFFKE
LLDERCEFHY PPFYHLVYVY LKHRDENIVN TAGVELGSRL RDIFGARVLG PDKPAVARVK
TLSIRKIVLK LENGIDYPRV RQYLRGALEA MMKDKRYGAL QVYYDVDPL
//
