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Entry: J7KI59_9CAUD
LinkDB: J7KI59_9CAUD
Original site: J7KI59_9CAUD 
ID   J7KI59_9CAUD            Unreviewed;       471 AA.
AC   J7KI59;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 1.
DT   24-JAN-2024, entry version 37.
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=Aesp030 {ECO:0000313|EMBL:AFQ97112.1};
OS   Aeromonas phage Aes508.
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC   Straboviridae; Tulanevirus; Tulanevirus aes508.
OX   NCBI_TaxID=1198013 {ECO:0000313|EMBL:AFQ97112.1, ECO:0000313|Proteomes:UP000003289};
RN   [1] {ECO:0000313|EMBL:AFQ97112.1, ECO:0000313|Proteomes:UP000003289}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Petrov V.M., Ratnayaka S., Karam J.D.;
RT   "Aeromonas salmonicida phage Aes508 complete genome.";
RL   Submitted (JUL-2011) 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; JN377894; AFQ97112.1; -; Genomic_DNA.
DR   RefSeq; YP_007010719.1; NC_019543.1.
DR   GeneID; 14016897; -.
DR   KEGG; vg:14016897; -.
DR   Proteomes; UP000003289; 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:AFQ97112.1};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_04155};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_04155};
KW   Viral DNA replication {ECO:0000256|HAMAP-Rule:MF_04155}.
FT   DOMAIN          166..435
FT                   /note="SF4 helicase"
FT                   /evidence="ECO:0000259|PROSITE:PS51199"
FT   REGION          431..462
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        436..462
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         198..205
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_04155"
SQ   SEQUENCE   471 AA;  53128 MW;  99D1307E5FF224DB CRC64;
     MMPETILENL LFNNTYFISA YPYIKEDYFD RGPYREIFKL IQKHVNEYNT IPTKTALAIA
     LDKKSIDQVT HDGVKEVLAR LSSKPEDHAW LIKETESYCK DQAMYNALSK AIEIQENAAK
     PFEERNKKLP DVGAIEDLMK EALAISFDGS VGHDWFEDYE RRYMLYQSKA NKVPFISNVL
     NKITKGGAEL GTLNVIMAGV NVGKSLGLCS LAADYLQTGK NVVYFSMEMA EHVVAKRIDA
     NLLDVTLDEI DDGNMSFAEY KARMERLKSR NMGRLIIKQY PTSGANANHF NAFLNELKLK
     KNFKADVVIV DYLGICASTR IRGGSENSYT LVKAIAEELR GLAVQHQVVL WTGAQTTRSA
     WDSTDIDMSD VAESAGLPAT ADFMLAVMET EELAQMGLQL MKQIKSRYGD KNWINKFKMG
     VKKGNQRWYD VEEEQQSRPG TPNAPSPRQA DNTKGNNSRQ HLDELAATMN F
//
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