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Database: UniProt
Entry: A0A0M8WT57_9ACTN
LinkDB: A0A0M8WT57_9ACTN
Original site: A0A0M8WT57_9ACTN 
ID   A0A0M8WT57_9ACTN        Unreviewed;       486 AA.
AC   A0A0M8WT57;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 31.
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=ADL04_31805 {ECO:0000313|EMBL:KOV91850.1};
OS   Streptomyces sp. NRRL B-3648.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1519493 {ECO:0000313|EMBL:KOV91850.1, ECO:0000313|Proteomes:UP000037702};
RN   [1] {ECO:0000313|EMBL:KOV91850.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL B-3648 {ECO:0000313|EMBL:KOV91850.1};
RA   Noorani M.;
RL   Submitted (JUL-2015) 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, 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:KOV91850.1}.
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DR   EMBL; LGDZ01000220; KOV91850.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0M8WT57; -.
DR   PATRIC; fig|1519493.3.peg.6783; -.
DR   Proteomes; UP000037702; 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:KOV91850.1};
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000037702}.
FT   DOMAIN          220..486
FT                   /note="SF4 helicase"
FT                   /evidence="ECO:0000259|PROSITE:PS51199"
FT   REGION          1..51
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        13..38
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   486 AA;  53461 MW;  A29D9DB59D682A6F CRC64;
     MDDPWADSGP SDRLPASRRR SDGGRGRDEQ HDRGRDNGTW DGGGSSFERI PPQDLDAEQS
     VLGGMLLSKD AIADVVEILK GHDFYKPAHE TIYTAILDVY AKGEPADPIT IAAELTKRGE
     INKVGGAAYL HSLVQTVPTA ANAEYYAEIV HERAVLRRLV EAGTRITQMG YAADGDVDEI
     VNSAQAEIYA VTEQRTSEDY LPLGDIMEGA LDEIEAIGSR SGEMTGVPTG FTDFDSLTNG
     LHPGQMIVIA ARPAMGKSTL ALDFARAASI KNNLPSVIFS LEMGRNEIAM RLLSAEARVA
     LHHMRSGTMT DEDWTRLARR MPDVSAAPLY IDDSPNLSMM EIRAKCRRLK QRNDLKLVVI
     DYLQLMQSGG SKRAESRQQE VSDMSRNLKL LAKELEIPVI ALSQLNRGPE QRTDKKPMVS
     DLRESGSIEQ DADMVILLHR EDAYEKESPR AGEADLIVAK HRNGPTATIT VAFQGHYSRF
     VDMAQT
//
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