ID A0A411BI76_9CAUD Unreviewed; 522 AA.
AC A0A411BI76;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 13-SEP-2023, entry version 12.
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=ASwh1_153 {ECO:0000313|EMBL:QAY01218.1};
OS Aeromonas phage Aswh_1.
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Straboviridae; Emmerichvirinae; Ishigurovirus.
OX NCBI_TaxID=2419740 {ECO:0000313|EMBL:QAY01218.1, ECO:0000313|Proteomes:UP000289392};
RN [1] {ECO:0000313|EMBL:QAY01218.1, ECO:0000313|Proteomes:UP000289392}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Yuan S., Ma Y., Liu Q.;
RT "ASwh_1, Complete genome sequences of 3 novel enterobacteria, Pakpunavirus
RT like phages.";
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
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; MH791414; QAY01218.1; -; Genomic_DNA.
DR Proteomes; UP000289392; 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:QAY01218.1};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_04155};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_04155};
KW Reference proteome {ECO:0000313|Proteomes:UP000289392};
KW Viral DNA replication {ECO:0000256|HAMAP-Rule:MF_04155}.
FT DOMAIN 171..439
FT /note="SF4 helicase"
FT /evidence="ECO:0000259|PROSITE:PS51199"
FT BINDING 202..209
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04155"
SQ SEQUENCE 522 AA; 58998 MW; B91DF7E651E5DA42 CRC64;
MSVSMSQIII NNLVYNSEFF GKVYPFLKPE YFARGPYRIA FEMIHEYAKK HNKAPSVNAL
GVMIEKKQNI SQVEYDQSKV LISRIEQIPE DPKWLVEETE KFCQERAMDI AISECIQIRE
NFSKPLDEQD KKIKDIGAIP EIMKTALSVG FTFDIGHDYM AQAEDRWESY NKKTNKIPFL
NHMLNRITKG GVELGTLNVI LAGTGVGKSI GLCHLATEYL QLGLNVLYVS FEMSEETVGK
RIDANLMDIS LDDLDSGLVQ KSEFMNRFNK KVLGKKLGKL FVKQFPTSGA NVNHIRNLMD
ELEMKKGFKP DVIMVDYLGI MASSRMKFSD NSYSFIKAIS EEVRGLAIEK KIVAWSGAQT
NRGSSGSLEI DKADIADSYA LLHGCDFVLA ISEDEDLISL GQQLFKQLKS RYGDINTHNK
FCMVVEKGKM RWSDLDDTAP YTVVYERKDL EERSDISADS IVVRKGDDVT SVAVEIEPEI
ADIIDTKPLG PVLFKRNLSK VQIDFNEDIA GMIDEDSAPW DD
//
