GenomeNet

Database: UniProt
Entry: A0A2A4CTT8_9RHOB
LinkDB: A0A2A4CTT8_9RHOB
Original site: A0A2A4CTT8_9RHOB 
ID   A0A2A4CTT8_9RHOB        Unreviewed;       495 AA.
AC   A0A2A4CTT8;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-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   ORFNames=CLN94_04150 {ECO:0000313|EMBL:PCD77698.1};
OS   Pseudothioclava arenosa.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Pseudothioclava.
OX   NCBI_TaxID=1795308 {ECO:0000313|EMBL:PCD77698.1, ECO:0000313|Proteomes:UP000243507};
RN   [1] {ECO:0000313|EMBL:PCD77698.1, ECO:0000313|Proteomes:UP000243507}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CAU 1312 {ECO:0000313|EMBL:PCD77698.1,
RC   ECO:0000313|Proteomes:UP000243507};
RA   Liu Y., Shao Z.;
RT   "A multilocus sequence analysis scheme for characterization of bacteria in
RT   the genus Thioclava.";
RL   Submitted (SEP-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:PCD77698.1}.
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; NTJD01000002; PCD77698.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2A4CTT8; -.
DR   OrthoDB; 9773982at2; -.
DR   Proteomes; UP000243507; 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:UP000243507}.
FT   DOMAIN          190..487
FT                   /note="SF4 helicase"
FT                   /evidence="ECO:0000259|PROSITE:PS51199"
SQ   SEQUENCE   495 AA;  54262 MW;  B101411FF223662D CRC64;
     MNDATLPQGA EPANIDALPH NIEAEQQLLG AILTNNDIFD RIAAVVKPEH FFEPVHQRIY
     EVAIARIQKN ALASPVTLKA FLEEDEGLKA LGGPAYLARL AGSAIAAYAA RDYAQMIYEL
     AIRRELIRLG GDISARAQTM VVEDDPKEQI TAAEQKLYNL AEQGQADKGF VSFLKAVTEA
     VSSANAAYQR DGGLAGVSTG LRDLDKKLGG LHPSDLLILA GRPSMGKTSL ATNIAFNIAK
     AYKRGIRHDG SEGAVEGGVV GFFSLEMSAE QLAARVLSEA SEVPSEQIRR GDMTETEFRR
     FVEAAKALET CPLYIDDTPA LPISQVAARC RRLKRTHGLD VVMVDYLQLL RGTGKGENRV
     QEIAEISMGL KAIAKELNIP VVALSQLSRT VESREDKRPQ LSDLRESGSI EQDADVVMFV
     YRDEYYRERE KPSDHELDKM AEWQAVMEKV HGKAEVIIGK QRHGPIGAVE LAFEGRFTRF
     SDLAQPWQGD GSDGF
//
DBGET integrated database retrieval system