GenomeNet

Database: UniProt
Entry: A0A2A2Y6G7_9BACT
LinkDB: A0A2A2Y6G7_9BACT
Original site: A0A2A2Y6G7_9BACT 
ID   A0A2A2Y6G7_9BACT        Unreviewed;       479 AA.
AC   A0A2A2Y6G7;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-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=CAK88_12065 {ECO:0000313|EMBL:PAZ04255.1};
OS   Verrucomicrobiae bacterium AMD-G2.
OC   Bacteria; Verrucomicrobiota; Verrucomicrobiae.
OX   NCBI_TaxID=1982328 {ECO:0000313|EMBL:PAZ04255.1, ECO:0000313|Proteomes:UP000217571};
RN   [1] {ECO:0000313|EMBL:PAZ04255.1, ECO:0000313|Proteomes:UP000217571}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AMD-G2 {ECO:0000313|EMBL:PAZ04255.1};
RA   Cabello-Yeves P.J., Ghai R., Mehrshad M., Picazo A., Camacho A.,
RA   Rodriguez-Valera F.;
RT   "Genome diversity of Verrucomicrobia from freshwater lakes.";
RL   Submitted (APR-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|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:PAZ04255.1}.
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; NEUM01000026; PAZ04255.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2A2Y6G7; -.
DR   Proteomes; UP000217571; 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:PAZ04255.1};
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}.
FT   DOMAIN          203..475
FT                   /note="SF4 helicase"
FT                   /evidence="ECO:0000259|PROSITE:PS51199"
SQ   SEQUENCE   479 AA;  53088 MW;  7F0BF3C3A637B7AC CRC64;
     MIAVEEKKSF EKNAPSLQQG SEGKMDDVMR AMPHALGPEK SILSSMLQNP QEYISTAIEE
     KLTKEHFYLP AHSMIFDVLM ECFEKGQDVE LVSLVQKLID KSLLENIGGP AALTELYSYA
     PNAGHFLTHL GYVKDKFILR SVINSCNDAI TQAYDNPEDV PQLLDGVETA VLAIRENAEV
     NRAVTIKSSV KDVMEYFAAL CAGEKEAQGF PTGYEVLDRM SSGLKPGEMF VIAARPSMGK
     TSLMMNIVEH ICIDQEKPAM VFSCEMSSFQ IVQRLVFSRA RFKLSDLHKG LIPQKKDLLS
     IKRAAEEIGN AKLFIDDTPG ITINDLRAKA RRKKRDEDIQ LIAIDYLQLM RSLSKQAANS
     REREIAEISA GLKGLAKELG IPIIVLAQLN RGPESRSGGT PKMSDLRESG SIEQDADLIG
     LLYRSAYYAE NEEERKEEEG RAELLLAKNR NGETGPVPLT FIAPLMRFET GAPAQEPSA
//
DBGET integrated database retrieval system