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Database: UniProt
Entry: A0A1R4FAE1_9ACTO
LinkDB: A0A1R4FAE1_9ACTO
Original site: A0A1R4FAE1_9ACTO 
ID   A0A1R4FAE1_9ACTO        Unreviewed;       455 AA.
AC   A0A1R4FAE1;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=Replicative DNA helicase {ECO:0000256|ARBA:ARBA00021957, ECO:0000256|RuleBase:RU362085};
DE            EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551, ECO:0000256|RuleBase:RU362085};
GN   ORFNames=CZ771_05845 {ECO:0000313|EMBL:SJM52772.1};
OS   Actinomycetales bacterium JB111.
OC   Bacteria; Actinomycetota; Actinomycetes; Actinomycetales.
OX   NCBI_TaxID=1434822 {ECO:0000313|EMBL:SJM52772.1, ECO:0000313|Proteomes:UP000196124};
RN   [1] {ECO:0000313|EMBL:SJM52772.1, ECO:0000313|Proteomes:UP000196124}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JB111 {ECO:0000313|EMBL:SJM52772.1,
RC   ECO:0000313|Proteomes:UP000196124};
RA   Peterson S.W.;
RL   Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Participates in initiation and elongation during chromosome
CC       replication; it exhibits DNA-dependent ATPase activity.
CC       {ECO:0000256|ARBA:ARBA00002835, ECO:0000256|RuleBase:RU362085}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC         Evidence={ECO:0000256|ARBA:ARBA00001665,
CC         ECO:0000256|RuleBase:RU362085};
CC   -!- SIMILARITY: Belongs to the helicase family. DnaB subfamily.
CC       {ECO:0000256|ARBA:ARBA00008428, ECO:0000256|RuleBase:RU362085}.
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DR   EMBL; FUHX01000026; SJM52772.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1R4FAE1; -.
DR   OrthoDB; 9773982at2; -.
DR   Proteomes; UP000196124; 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:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006269; P:DNA replication, synthesis of RNA primer; IEA:UniProtKB-UniRule.
DR   CDD; cd00984; DnaB_C; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR036185; DNA_heli_DnaB-like_N_sf.
DR   InterPro; IPR007692; DNA_helicase_DnaB.
DR   InterPro; IPR007694; DNA_helicase_DnaB-like_C.
DR   InterPro; IPR007693; DNA_helicase_DnaB-like_N.
DR   InterPro; IPR016136; DNA_helicase_N/primase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   NCBIfam; TIGR00665; DnaB; 1.
DR   PANTHER; PTHR30153:SF2; REPLICATIVE DNA HELICASE; 1.
DR   PANTHER; PTHR30153; REPLICATIVE DNA HELICASE DNAB; 1.
DR   Pfam; PF00772; DnaB; 1.
DR   Pfam; PF03796; DnaB_C; 1.
DR   SUPFAM; SSF48024; N-terminal domain of DnaB helicase; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51199; SF4_HELICASE; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU362085};
KW   DNA replication {ECO:0000256|ARBA:ARBA00022705,
KW   ECO:0000256|RuleBase:RU362085};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU362085};
KW   Helicase {ECO:0000256|RuleBase:RU362085, ECO:0000313|EMBL:SJM52772.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU362085};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU362085}; Primosome {ECO:0000256|RuleBase:RU362085};
KW   Reference proteome {ECO:0000313|Proteomes:UP000196124}.
FT   DOMAIN          192..455
FT                   /note="SF4 helicase"
FT                   /evidence="ECO:0000259|PROSITE:PS51199"
FT   REGION          378..397
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        379..397
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   455 AA;  49593 MW;  45F50A202E09975A CRC64;
     MIVAVSVAEE QSAGRGEFDR TPPQDLSAEQ SVLGGMLMSK DAIADVVEEL RGVDFYKPAH
     EMVYEAIIDL FGRGEPADPV TVAAELTKRG ELARVGGAPY LHTLVASVPT AANAGYYARI
     VAELAILRRL VQAGTRIVQL GYATDGGDVE EIVNSAQAEV YAVADQRSSE DYLPLRDLVG
     PTIDELQRIE SKTGDDGAVP TGFTDLDALT NGLHPGQMVI IAARPAIGKS TIALDICRNA
     ALRNNQAAVI FSLEMGRTEI TMRMLSAEAG VSLKHMREGS LRDDEWQRIV GASGRAHDAP
     LFIDDSPNMS MMEIRAKCRR LKQNNDLKLV AVDYLQLMTS GKRVESRQQE VSEFSRALKL
     LAKEIEVPVI AVAQLNRGPE QRGDKKPMMS DLRESGSLEQ DADVVMLLHR EDAYEKEHPR
     AGEADIIVAK QRSGPTGTVT VAFQGHYSRF VDMGH
//
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