ID A0A143QEA2_9NOCA Unreviewed; 212 AA.
AC A0A143QEA2;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=Replicative DNA helicase {ECO:0000313|EMBL:AMY20737.1};
DE EC=3.6.4.12 {ECO:0000313|EMBL:AMY20737.1};
GN Name=dnaB_1 {ECO:0000313|EMBL:AMY20737.1};
GN ORFNames=A3Q40_03376 {ECO:0000313|EMBL:AMY20737.1};
OS Rhodococcus sp. PBTS 1.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=1653478 {ECO:0000313|EMBL:AMY20737.1, ECO:0000313|Proteomes:UP000076180};
RN [1] {ECO:0000313|EMBL:AMY20737.1, ECO:0000313|Proteomes:UP000076180}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PBTS 1 {ECO:0000313|EMBL:AMY20737.1,
RC ECO:0000313|Proteomes:UP000076180};
RX PubMed=27284129;
RA Stamler R.A., Vereecke D., Zhang Y., Schilkey F., Devitt N., Randall J.J.;
RT "Complete Genome and Plasmid Sequences for Rhodococcus fascians D188 and
RT Draft Sequences for Rhodococcus Isolates PBTS 1 and PBTS 2.";
RL Genome Announc. 4:0-0(2016).
RN [2] {ECO:0000313|Proteomes:UP000076180}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PBTS 1 {ECO:0000313|Proteomes:UP000076180};
RA Stamer R., Vereecke D., Zhang Y., Schilkey F., Devitt N., Randall J.;
RT "Complete Genome and Plasmid Sequences for Rhodococcus fascians D188 and
RT Draft Sequences for Rhodococcus spp. Isolates PBTS 1 and PBTS 2.";
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|ARBA:ARBA00002835}.
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DR EMBL; CP015219; AMY20737.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A143QEA2; -.
DR STRING; 1653478.A3Q40_03376; -.
DR KEGG; rhu:A3Q40_03376; -.
DR PATRIC; fig|1653478.3.peg.3427; -.
DR Proteomes; UP000076180; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR InterPro; IPR036185; DNA_heli_DnaB-like_N_sf.
DR InterPro; IPR007693; DNA_helicase_DnaB-like_N.
DR InterPro; IPR016136; DNA_helicase_N/primase_C.
DR Pfam; PF00772; DnaB; 1.
DR SUPFAM; SSF48024; N-terminal domain of DnaB helicase; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000313|EMBL:AMY20737.1};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Helicase {ECO:0000313|EMBL:AMY20737.1};
KW Hydrolase {ECO:0000313|EMBL:AMY20737.1};
KW Nucleotide-binding {ECO:0000313|EMBL:AMY20737.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000076180}.
FT DOMAIN 54..150
FT /note="DNA helicase DnaB-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00772"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 212 AA; 22433 MW; 736F05F004796599 CRC64;
MSALRAVPTE GPDEHPAGHD AAVLDLAPDT APVAAPAGDP TAQELDELDP RTDPESLTLC
ALMWSAESAD TTRVATALTP GDFANPAHAE LFTIIAALIT ENRPHDPASV AAVIHRAGGG
QKDAPLRRVL ADVVTADAPA VSAAHYADIV LSQSYRRSFH IAGQRITQAA EQGPEEELFD
YMVQLGRQQR AAWNRLNTFR SGGAVQGEGE RS
//
