GenomeNet

Database: UniProt
Entry: A0A179D3C0_9BACT
LinkDB: A0A179D3C0_9BACT
Original site: A0A179D3C0_9BACT 
ID   A0A179D3C0_9BACT        Unreviewed;       451 AA.
AC   A0A179D3C0;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 28.
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=TDIS_1326 {ECO:0000313|EMBL:OAQ20557.1};
OS   Thermosulfurimonas dismutans.
OC   Bacteria; Thermodesulfobacteriota; Thermodesulfobacteria;
OC   Thermodesulfobacteriales; Thermodesulfobacteriaceae; Thermosulfurimonas.
OX   NCBI_TaxID=999894 {ECO:0000313|EMBL:OAQ20557.1, ECO:0000313|Proteomes:UP000078390};
RN   [1] {ECO:0000313|EMBL:OAQ20557.1, ECO:0000313|Proteomes:UP000078390}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S95 {ECO:0000313|EMBL:OAQ20557.1,
RC   ECO:0000313|Proteomes:UP000078390};
RA   Mardanov A.V., Beletsky A.V., Kadnikov V.V., Slobodkin A.I., Ravin N.V.;
RT   "Genome analysis of Thermosulfurimonas dismutans, the first thermophilic
RT   sulfur-disproportionating bacterium of the phylum Thermodesulfobacteria.";
RL   Submitted (APR-2016) 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|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:OAQ20557.1}.
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; LWLG01000009; OAQ20557.1; -; Genomic_DNA.
DR   RefSeq; WP_068670565.1; NZ_LWLG01000009.1.
DR   AlphaFoldDB; A0A179D3C0; -.
DR   STRING; 999894.TDIS_1326; -.
DR   PATRIC; fig|999894.6.peg.1324; -.
DR   Proteomes; UP000078390; 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:OAQ20557.1};
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}.
FT   DOMAIN          185..450
FT                   /note="SF4 helicase"
FT                   /evidence="ECO:0000259|PROSITE:PS51199"
SQ   SEQUENCE   451 AA;  50454 MW;  B42CC063A60B573F CRC64;
     MARRKEAPAL LLDRLPPQNL EAERGVLGSI FLEPSVILKV VEILSPEDFY REAHAEIYRA
     MLSLFERNEP IDLITVHDEL VSRGTLEEVG GATYLAELAG LLPTSAHAVH YAQIVKEKAL
     LRRLIRVATE IAARAYEAAE PVEDILEAAE KSIFELRSYS ERDGFRNIKE LIKEAIRQLE
     KLHQRPELIT GVPTGFTEFD HMTAGLQPGD LIIVAGRPSM GKTSLALNIA CYAAAEAGIP
     VGIFSLEMSR EQLAARMLCA EARVNLQSLR TGRISESEWQ RLTFAANKLS RAPIFVDDTP
     ALSILDLRAK ARRLMSEHGL GLIIIDYLQL LQSRERRERR EQEISDISSS LKAMAKEFNV
     PVVALSQLNR RVEERPDKRP QLADLRESGA IEQDADLIVF IYRDEVYNKD TPHKGVAEII
     IGKQRNGPTG TVKLAFQAPY SSFANLSDIQ E
//
DBGET integrated database retrieval system