ID A0A1G3CSH8_9BURK Unreviewed; 831 AA.
AC A0A1G3CSH8;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
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=A2X74_00925 {ECO:0000313|EMBL:OHC10437.1};
OS Polynucleobacter sp. GWA2_45_21.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Polynucleobacter.
OX NCBI_TaxID=1801989 {ECO:0000313|EMBL:OHC10437.1, ECO:0000313|Proteomes:UP000176957};
RN [1] {ECO:0000313|EMBL:OHC10437.1, ECO:0000313|Proteomes:UP000176957}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OHC10437.1}.
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DR EMBL; MHZG01000001; OHC10437.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G3CSH8; -.
DR STRING; 1801989.A2X74_00925; -.
DR Proteomes; UP000176957; 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:0004519; F:endonuclease activity; IEA:InterPro.
DR GO; GO:0006269; P:DNA replication, synthesis of RNA primer; IEA:UniProtKB-UniRule.
DR CDD; cd00984; DnaB_C; 1.
DR Gene3D; 3.10.28.10; Homing endonucleases; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
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; IPR036844; Hint_dom_sf.
DR InterPro; IPR027434; Homing_endonucl.
DR InterPro; IPR004042; Intein_endonuc.
DR InterPro; IPR004860; LAGLIDADG_2.
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; 2.
DR Pfam; PF14528; LAGLIDADG_3; 1.
DR SUPFAM; SSF51294; Hedgehog/intein (Hint) domain; 1.
DR SUPFAM; SSF55608; Homing endonucleases; 1.
DR SUPFAM; SSF48024; N-terminal domain of DnaB helicase; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS50819; INTEIN_ENDONUCLEASE; 1.
DR PROSITE; PS51199; SF4_HELICASE; 2.
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 Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 201..238
FT /note="SF4 helicase"
FT /evidence="ECO:0000259|PROSITE:PS51199"
FT DOMAIN 356..499
FT /note="DOD-type homing endonuclease"
FT /evidence="ECO:0000259|PROSITE:PS50819"
FT DOMAIN 591..820
FT /note="SF4 helicase"
FT /evidence="ECO:0000259|PROSITE:PS51199"
SQ SEQUENCE 831 AA; 92022 MW; E316B5F266603888 CRC64;
MAESRSRSLM SNPGMMGSGD AALQALKVPP HSVEAEQSLL GGLLIDNTAW DRLGGVLTDK
DFYRPEHALI YKVIQRLVGD NHPADVITVH EAVKSEQGGD LVGIDYLNSL AQSTPSAANI
KGYADIVRDR SILRRLIEVS DNIVNSAFVP EGRSVRTLLD EAESRILQIG EEGSRKADYL
EIEPLLKTVV ARIDELYNRQ GGSDITGIAT GFIDLDKQTS GLQKGDLVIV AGRPSMGKAQ
PLDAKVKTVD GWKLMGDLRF GDRLASVDGQ HSMVTGIYPQ GIKQIYKVTF SDGREAECCY
EHLWRVMYRD WDAPKVINTA RLMEMLSCVR YKNRLWIDPV SGDFGHSNKL PINPWVLGAL
LGDGTLALSH GSVMFSTKSP ELIERMNALA GYEMELVHAN AYDWRLVSKT RIAANGQRQS
VPTNYFRSAL QDLGVLGCRS FDKYIPATYL EANKTSRLAL FQGLMDTDGW IEKWGSIRFC
TASKQLSEDV ASLARSLGGF CSIAHKQTSY TYKGEKKQGR LSYVLNMSFG PGFQAFTLPE
KKERLRSTWD RQRRLTFKSI EPSRVSEAQC ISVSHPDRTY VTNEYVVTHN TAFALNIAEN
VALAEGLPVV VFSMEMSGEQ LAARLLGSVG RVDQGRMRTG KLQDDEWPRV TDAIARLSNT
QILIDETGAL SSLELRARAR RIARNFGGTL GLVVIDYLQL MSGSGSENRA TEISEISRSL
KSLAKELQCP VVALSQLNRG LEQRPNKRPI MSDLRESGAI EQDADLIMFI YRDEVYHPDT
TTDKGMAEII IGKQRNGPIG TVRLSWQGPY TKFDNLAMGS VGYSSGGYEP F
//