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Database: UniProt
Entry: A0A1T0AVH6_9PAST
LinkDB: A0A1T0AVH6_9PAST
Original site: A0A1T0AVH6_9PAST 
ID   A0A1T0AVH6_9PAST        Unreviewed;       464 AA.
AC   A0A1T0AVH6;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   24-JAN-2024, entry version 21.
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=B0187_00705 {ECO:0000313|EMBL:OOS00845.1};
OS   Haemophilus paracuniculus.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=734 {ECO:0000313|EMBL:OOS00845.1, ECO:0000313|Proteomes:UP000190867};
RN   [1] {ECO:0000313|EMBL:OOS00845.1, ECO:0000313|Proteomes:UP000190867}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCUG 43573 {ECO:0000313|EMBL:OOS00845.1,
RC   ECO:0000313|Proteomes:UP000190867};
RA   Engstrom-Jakobsson H., Salva-Serra F., Thorell K., Gonzales-Siles L.,
RA   Karlsson R., Boulund F., Engstrand L., Kristiansson E., Moore E.;
RT   "Draft genome sequence of Haemophilus paracuniculus CCUG 43573 type
RT   strain.";
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 and contains
CC       distinct active sites for ATP binding, DNA binding, and interaction
CC       with DnaC protein, primase, and other prepriming proteins.
CC       {ECO:0000256|ARBA:ARBA00003574, 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}.
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:OOS00845.1}.
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DR   EMBL; MUYA01000001; OOS00845.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1T0AVH6; -.
DR   STRING; 734.B0187_00705; -.
DR   OrthoDB; 9773982at2; -.
DR   Proteomes; UP000190867; 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|ARBA:ARBA00022806, ECO:0000256|RuleBase:RU362085};
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:UP000190867}.
FT   DOMAIN          184..457
FT                   /note="SF4 helicase"
FT                   /evidence="ECO:0000259|PROSITE:PS51199"
SQ   SEQUENCE   464 AA;  52133 MW;  0D9D6C622AEC8438 CRC64;
     MAHQTQSQPI NTHYSIEAEQ AVLGGLLLDN EKWDEVSQIL APSNFYVHAH QQIFSTIQAM
     CEANSPVDLL TLERKLAEKA ILEEVGGLAY LAELSQNTPS VANIATYAEI VRRDSQAREL
     FALGQHLRTE AVKVNSQTSL DTLLEHTERR LTDLAFNHQQ QESIVSLPDV LAQVIQQMNS
     SCEQNKATTG TAFGIERLDR ATSGAQNGEL IILAARPSMG KTALSLTFAE SALESQPDKP
     IQYYSLEMPA DQILQRFLSM RSQVAINKIR QPTEMSDEDW ARFSEAFNYI HSHWNNRLLI
     DDSSYLSPQS LRIRARRNAR KYGEPSVIIV DYLQLMSVPE QKNSSNRNLE IAEISRSLKS
     LAKEMNCPVI ALSQLNRNLE LRSDKRPMPS DLRDSGSLEQ DADLLLFIYR DEVYHQNTDL
     PGIAEILIGK QRNGPTGTIL TQFRGEFGLF ANIPDDEYEK LGSA
//
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