GenomeNet

Database: UniProt
Entry: A0A1I5FBZ5_PARPN
LinkDB: A0A1I5FBZ5_PARPN
Original site: A0A1I5FBZ5_PARPN 
ID   A0A1I5FBZ5_PARPN        Unreviewed;       499 AA.
AC   A0A1I5FBZ5;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 30.
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=BDE18_2520 {ECO:0000313|EMBL:RKS43704.1}, HYQ43_00890
GN   {ECO:0000313|EMBL:QLH12905.1};
OS   Paracoccus pantotrophus (Thiosphaera pantotropha).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Paracoccus.
OX   NCBI_TaxID=82367 {ECO:0000313|EMBL:RKS43704.1, ECO:0000313|Proteomes:UP000273626};
RN   [1] {ECO:0000313|EMBL:RKS43704.1, ECO:0000313|Proteomes:UP000273626}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35512 / DSM 2944 / CIP 106514 / LMD 82.5 / NBRC 102493 /
RC   NCCB 82005 / GB17 {ECO:0000313|Proteomes:UP000273626}, and DSM 2944
RC   {ECO:0000313|EMBL:RKS43704.1};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT   (KMG-II): from individual species to whole genera.";
RL   Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:QLH12905.1, ECO:0000313|Proteomes:UP000509322}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ACCC10489 {ECO:0000313|EMBL:QLH12905.1,
RC   ECO:0000313|Proteomes:UP000509322};
RA   Si Y.;
RT   "The complete genome of Paracoccus pantotrophus ACCC 10489.";
RL   Submitted (JUL-2020) 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   ---------------------------------------------------------------------------
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; CP058689; QLH12905.1; -; Genomic_DNA.
DR   EMBL; RBLI01000002; RKS43704.1; -; Genomic_DNA.
DR   RefSeq; WP_024843749.1; NZ_RIAQ01000034.1.
DR   AlphaFoldDB; A0A1I5FBZ5; -.
DR   GeneID; 51368987; -.
DR   OrthoDB; 9773982at2; -.
DR   Proteomes; UP000273626; Unassembled WGS sequence.
DR   Proteomes; UP000509322; Chromosome 1.
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}.
FT   DOMAIN          196..493
FT                   /note="SF4 helicase"
FT                   /evidence="ECO:0000259|PROSITE:PS51199"
SQ   SEQUENCE   499 AA;  54571 MW;  14434886AF0000E4 CRC64;
     MSELRAVEIR KPGEIAEAAA AQAVPFSIEA EQQLLGALLT NNEVYDHVSR IIQAGHFYDP
     VHRRIYEICA ERIARNALAS PVTIKAFMEH DAGLKELGGP AYLARLAGAA ISSHAARDYA
     QMIREFALRR ELIGLGQDIA ARAATVTVSD SAEEQIKEAE QVLYKLGEQG VAERGFQSFL
     AAVTGALNAA NAAFSRGGGL SGISTGLVDL DGKMGGLNRS DLIILAGRPS MGKTSLATNI
     AFNVAKAHRL GELPDGTHGT VAGGVVGFFS LEMSAEQLAA RILSEAAEVP SEAIRRGDMT
     EDEFRRFVKA AHDLQNCPLY IDDTPALPIN QLAARARKLK RTMGLDLLIV DYLQLLRAAS
     AKDSRVNEVS EITQGLKAVA KELDIPVIAL SQLSRQVESR EDKRPQLSDL RESGSIEQDA
     DIVMFVFREE YYREREKPAD HDLDKMATWQ QVMESCHGKA EVIIGKQRHG PIGTVELSFE
     GRFTRFGNLE KHRSWDRAE
//
DBGET integrated database retrieval system