ID G0VRU1_MEGEL Unreviewed; 785 AA.
AC G0VRU1;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 61.
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=MELS_1762 {ECO:0000313|EMBL:CCC73981.1};
OS Megasphaera elsdenii DSM 20460.
OC Bacteria; Bacillota; Negativicutes; Veillonellales; Veillonellaceae;
OC Megasphaera.
OX NCBI_TaxID=1064535 {ECO:0000313|EMBL:CCC73981.1, ECO:0000313|Proteomes:UP000010111};
RN [1] {ECO:0000313|EMBL:CCC73981.1, ECO:0000313|Proteomes:UP000010111}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20460 {ECO:0000313|EMBL:CCC73981.1,
RC ECO:0000313|Proteomes:UP000010111};
RX PubMed=21914887; DOI=10.1128/JB.05861-11;
RA Marx H., Graf A.B., Tatto N., Thallinger G.G., Mattanovich D., Sauer M.;
RT "Genome Sequence of the Ruminal Bacterium Megasphaera elsdenii.";
RL J. Bacteriol. 193:5578-5579(2011).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; HE576794; CCC73981.1; -; Genomic_DNA.
DR RefSeq; WP_014016708.1; NZ_CP027570.1.
DR AlphaFoldDB; G0VRU1; -.
DR STRING; 1064535.MELS_1762; -.
DR KEGG; med:MELS_1762; -.
DR eggNOG; COG1198; Bacteria.
DR HOGENOM; CLU_013353_3_1_9; -.
DR Proteomes; UP000010111; Chromosome.
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:UP000010111};
KW Zinc {ECO:0000256|HAMAP-Rule:MF_00983};
KW Zinc-finger {ECO:0000256|HAMAP-Rule:MF_00983}.
FT DOMAIN 269..435
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 532..691
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT ZN_FING 497..509
FT /note="C4-type"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00983"
FT ZN_FING 524..540
FT /note="C4-type"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00983"
SQ SEQUENCE 785 AA; 87974 MW; 817843684C5225F4 CRC64;
MFAEIIINTT AKRLQQTFSY IVPEGMAVRV GSRVLVPFGH RREEGIVVAL QEHLAEPADF
TLKPIEGLLS TQTGFQEEMI RTALWIRDYY VCNLSDALRL FMIDKKGLVR RDVVSAGPAQ
PQTADEARLQ TYVAGKGRCE KGALSRRFGQ DLVEKALASQ VLTSRICYKN QIADKMEDWL
SFAADDTEAI LHGRRRQQEL LQALKAKGEG PVSYWQGQGY SRNLMRRLCA TGLACWSQRP
ARTTNVLPSL ARDEAFSLTA EQQQALKVIG SDEHGKTYVL HGITSSGKTE IYMQLTSQAL
KKGKQVVVLV PEIALTGQIV RRFLRRFGDD VVVMHSQLSQ GEKRNNWLRM QNGTSHICIG
ARSAVFAAAQ SIGLFIVDEA HDSSYKQDEA PRYHAVAVAR QRAAYYGCPV VLGSATPALA
DYYRALQGEY VLVELKERVG HRPLPAVQVV DMRDELARGN YRVVSDALLT LLEETLAARQ
QAIILLNRRG FSTFVMCRKC GYVVKCDTCD VAMVYHRQAA HLRCHYCDAE KPIPTVCPSC
GSKYIKFFGS GTEKVEAQLH ELLPTARIIR LDQDTTSRKH SGDRIIEAFR RHEYDILLGT
QMVAKGHDFP GVSAVGILSA DSLLNIPAYW AGERTFQLLT QAAGRAGRGD IPGRVIMQTY
APDHYVIQCA ARQDYRAFYD QEVQFRKELG YPPFQEMAKI LVQDESEEQV WRKANDVAAA
LNSWNQDHGD EVAVIGPYED VIKKIRNKYR VVLSLTGKDL TAIKKAMQHL PACWQTGVII
DIDPM
//
