ID A0A1D8KL50_9CAUD Unreviewed; 462 AA.
AC A0A1D8KL50;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 22-FEB-2023, entry version 27.
DE RecName: Full=DnaB-like replicative helicase {ECO:0000256|HAMAP-Rule:MF_04155};
DE EC=3.6.4.- {ECO:0000256|HAMAP-Rule:MF_04155};
GN ORFNames=C440309_163 {ECO:0000313|EMBL:AOV59386.1}, N231010_163
GN {ECO:0000313|EMBL:AOV59862.1}, S330809_163
GN {ECO:0000313|EMBL:AOV59624.1};
OS Synechococcus phage S-CAM4.
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Kyanoviridae; Potamoivirus; Potamoivirus cam4.
OX NCBI_TaxID=1883367 {ECO:0000313|EMBL:AOV59386.1, ECO:0000313|Proteomes:UP000241987};
RN [1] {ECO:0000313|Proteomes:UP000217816, ECO:0000313|Proteomes:UP000240822}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0309CC44 {ECO:0000313|EMBL:AOV59386.1}, 0809SB33
RC {ECO:0000313|EMBL:AOV59624.1}, and 1010NB23
RC {ECO:0000313|EMBL:AOV59862.1};
RX PubMed=27693926; DOI=10.1016/j.virol.2016.09.016;
RA Crummett L.T., Puxty R.J., Weihe C., Marston M.F., Martiny J.B.;
RT "The genomic content and context of auxiliary metabolic genes in marine
RT cyanomyoviruses.";
RL Virology 499:219-229(2016).
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; KU686200; AOV59386.1; -; Genomic_DNA.
DR EMBL; KU686201; AOV59624.1; -; Genomic_DNA.
DR EMBL; KU686202; AOV59862.1; -; Genomic_DNA.
DR RefSeq; YP_009320596.1; NC_031900.1.
DR GeneID; 30305866; -.
DR KEGG; vg:30305866; -.
DR Proteomes; UP000217816; Genome.
DR Proteomes; UP000240822; Genome.
DR Proteomes; UP000241987; 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:0016779; F:nucleotidyltransferase 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:AOV59386.1};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_04155, ECO:0000313|EMBL:AOV59386.1};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_04155};
KW Nucleotidyltransferase {ECO:0000313|EMBL:AOV59386.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000217816};
KW Transferase {ECO:0000313|EMBL:AOV59386.1};
KW Viral DNA replication {ECO:0000256|HAMAP-Rule:MF_04155}.
FT DOMAIN 163..430
FT /note="SF4 helicase"
FT /evidence="ECO:0000259|PROSITE:PS51199"
FT BINDING 195..202
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04155"
SQ SEQUENCE 462 AA; 52541 MW; CA2F33F482B5EE24 CRC64;
MATERIQQTI LRNLIFTEEY YRKVVPFLRA DYFEEYHEKV IFEEIADFAG KYDKVPTQEV
LSINLQNRND LTDETFRDSL STIRGLTDEW VDYEWLLDAT EKWCQDRAIY LALMSSIKIA
DGGDKKISKD AIPGILQEAL AVSFDEHIGH DYIEQAKDRY EFYHRKEEKV PFDLEKFNYI
TKGGISNKTL SVALAGTGVG KSLFMCHCAG AALTQGRNVL YITCEMAEEK IAERIDANLL
NVSIKDIAEL PEVIFNSKVQ EISRKTRGKL IIKEYPTASA HAGHFKSLIS DLSLKRDFKP
DIIYIDYLNI CASARYKGAI VNSYTYVKAI AEELRGLAVE CNVPIVTATQ TTRSGYGNSD
PDLTDTSESF GLPATADFMF ALISTDELEQ QGRIMVKQLK NRYNETAASR KFMVGIDRSK
MRLYDVAEDA SDININEEDP GEEFSQFAQT QNRLSKFAEW NV
//
