ID A0A2H4N7R6_9CAUD Unreviewed; 463 AA.
AC A0A2H4N7R6;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 28-JUN-2023, entry version 16.
DE RecName: Full=DnaB-like replicative helicase {ECO:0000256|HAMAP-Rule:MF_04155};
DE EC=3.6.4.- {ECO:0000256|HAMAP-Rule:MF_04155};
OS Lake Baikal phage Baikal-20-5m-C28.
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes.
OX NCBI_TaxID=2047876 {ECO:0000313|EMBL:ATV46301.1, ECO:0000313|Proteomes:UP000252964};
RN [1] {ECO:0000313|EMBL:ATV46301.1, ECO:0000313|Proteomes:UP000252964}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=29079621;
RA Cabello-Yeves P.J., Zemskaya T.I., Rosselli R., Coutinho F.H.,
RA Zakharenko A.S., Blinov V.V., Rodriguez-Valera F.;
RT "Genomes of novel microbial lineages assembled from the sub-ice waters of
RT Lake Baikal.";
RL Appl. Environ. Microbiol. 0:0-0(2017).
CC -!- FUNCTION: ATP-dependent DNA helicase essential for viral DNA
CC replication and recombination. The helicase moves 5' -> 3' on the
CC lagging strand template, unwinding the DNA duplex ahead of the leading
CC strand polymerase at the replication fork and generating ssDNA for both
CC leading and lagging strand synthesis. Interaction with the primase
CC allows the primase to initiate lagging strand synthesis and fully
CC activates the helicase. Loaded by the helicase assembly factor on
CC replication forks that begin at discrete replication origin sequences,
CC as well as on forks that are created during recombination.
CC {ECO:0000256|HAMAP-Rule:MF_04155}.
CC -!- SUBUNIT: Homohexamer. The homohexamer is a trimer of asymmetric dimers.
CC Interacts with the DNA primase; this interaction forms the active
CC primosome complex, which is composed of 6 helicase and 1 primase
CC subunits and expresses full helicase and primase activities. Interacts
CC (via C-terminus) with the helicase assembly factor; this interaction
CC brings about the rapid assembly of the helicase onto ssDNA. Part of the
CC replicase complex that includes the DNA polymerase, the polymerase
CC clamp, the clamp loader complex, the single-stranded DNA binding
CC protein, the primase, the DnaB-like replicative helicase and the
CC helicase assembly factor. {ECO:0000256|HAMAP-Rule:MF_04155}.
CC -!- SIMILARITY: Belongs to the helicase family. DnaB subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_04155}.
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DR EMBL; MG198570; ATV46301.1; -; Genomic_DNA.
DR Proteomes; UP000252964; Genome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR GO; GO:0039693; P:viral DNA genome replication; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR HAMAP; MF_04155; Helic_T4; 1.
DR InterPro; IPR007694; DNA_helicase_DnaB-like_C.
DR InterPro; IPR046393; Helic_T4.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR30153:SF2; REPLICATIVE DNA HELICASE; 1.
DR PANTHER; PTHR30153; REPLICATIVE DNA HELICASE DNAB; 1.
DR Pfam; PF03796; DnaB_C; 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|HAMAP-Rule:MF_04155};
KW DNA replication {ECO:0000256|HAMAP-Rule:MF_04155};
KW DNA-binding {ECO:0000256|HAMAP-Rule:MF_04155};
KW Helicase {ECO:0000256|HAMAP-Rule:MF_04155, ECO:0000313|EMBL:ATV46301.1};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_04155};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_04155};
KW Reference proteome {ECO:0000313|Proteomes:UP000252964};
KW Viral DNA replication {ECO:0000256|HAMAP-Rule:MF_04155}.
FT DOMAIN 155..424
FT /note="SF4 helicase"
FT /evidence="ECO:0000259|PROSITE:PS51199"
FT REGION 439..463
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 444..463
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 187..194
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04155"
SQ SEQUENCE 463 AA; 52396 MW; F69CFF8C5C6DA8EA CRC64;
MISQLILNQL CTNEEYTRRA LPFLKDEYFE RGERLLFAVL SHFVNKYNTV PTEGALKLEL
QKIPNVPNEI VELVAQAYVA DPVDIAWVLD ETERFCQDRS IYLAIMESIQ IIDGKHKELS
NNAIPDILSK ALAVSFDTNI GHDYIDSSDL RYEYYHKTEE RLPFDLDYFN KITKGGLPNK
TLNIILAGTG VGKSLFMCHM AGASLMQGKN VLYITMEMAE ERIAERIDAN LMNIPIDQLE
QLPKQVYDQK IQKIGQKNIG KLIIKEYPTG AAHTGHFRAL LNELKLKKNF KPDIIFIDYL
NICASSRIRG LGGSINTYSY IKTIAEEMRG LAVENNLPIV SATQTTRSGF SNTDVGLEDT
SESFGLPATA DFMFAVISTE ELEKLGQLMV KQLKNRYNDL TFHKRFIVGV DRSRMKLYDV
EPSAQSLIND GAHVAVKPEA DKPLNTFGSK ERSNKDFGDF TYE
//
