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Database: UniProt
Entry: A0A2I2KN21_9ACTN
LinkDB: A0A2I2KN21_9ACTN
Original site: A0A2I2KN21_9ACTN 
ID   A0A2I2KN21_9ACTN        Unreviewed;       442 AA.
AC   A0A2I2KN21;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   27-MAR-2024, entry version 19.
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   Name=dnaB {ECO:0000313|EMBL:SNQ47056.1};
GN   ORFNames=FRACA_170016 {ECO:0000313|EMBL:SNQ47056.1};
OS   Frankia canadensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Frankiales; Frankiaceae; Frankia.
OX   NCBI_TaxID=1836972 {ECO:0000313|EMBL:SNQ47056.1, ECO:0000313|Proteomes:UP000234331};
RN   [1] {ECO:0000313|EMBL:SNQ47056.1, ECO:0000313|Proteomes:UP000234331}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FRACA_ARgP5 {ECO:0000313|EMBL:SNQ47056.1};
RA   Kim H.J., Triplett B.A.;
RL   Submitted (JUN-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; FZMO01000079; SNQ47056.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2I2KN21; -.
DR   Proteomes; UP000234331; 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:InterPro.
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; IPR003593; AAA+_ATPase.
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   SMART; SM00382; AAA; 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:SNQ47056.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU362085};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU362085};
KW   Primosome {ECO:0000256|ARBA:ARBA00022515, ECO:0000256|RuleBase:RU362085};
KW   Reference proteome {ECO:0000313|Proteomes:UP000234331}.
FT   DOMAIN          179..442
FT                   /note="SF4 helicase"
FT                   /evidence="ECO:0000259|PROSITE:PS51199"
SQ   SEQUENCE   442 AA;  47674 MW;  713B2058914DE2C6 CRC64;
     MSDETITTPP HDLPAEQAVL GAMLMSREAR GDISEILQPS DFYRPAHSSI FEAVMRLDGQ
     GEPADALTVA ADLLRRGHLD RVGGPEYLHT LIAAVPTAAN GGYYARIVAE KAVFRRLLEA
     GGRIAQIGQT AAGAATDAQE LADQTLHAAL NGPDTGNGPV LLGADSAAFL DELEALQRGD
     VTPAGVLTGF SDLDEVTRGF QPGQLVIIAA RPSVGKTTLA LDVARAAAIK ARRPTLFVSL
     EMTDKELRQK IRAAEARISL RNIQTGQLTE DDWSRLTRVL ADTVDAPLRI DTSPGLGVAA
     IRTRARRMQR RHGLDLLIVD YLQLLVTAKK EENRQQEVAG ISRSLKLLAG ELGVPVVALS
     QLNRAVEQRA VKRPQLSDLR DSGAIEQDAD MVIMIHREDA HDENSARAGE ADLIIEKNRS
     GPKGTFTVAF QGHYSRFVDM GC
//
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