ID M4QRW5_9CAUD Unreviewed; 468 AA.
AC M4QRW5;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 22-FEB-2023, entry version 31.
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=SWZG_00102 {ECO:0000313|EMBL:AGH31613.1};
OS Synechococcus phage S-SKS1.
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Llyrvirus; Llyrvirus SSKS1.
OX NCBI_TaxID=754042 {ECO:0000313|EMBL:AGH31613.1, ECO:0000313|Proteomes:UP000201252};
RN [1] {ECO:0000313|EMBL:AGH31613.1, ECO:0000313|Proteomes:UP000201252}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG The Broad Institute Genome Sequencing Platform;
RA Henn M.R., Clokie M., Levin J., Malboeuf C., Casali M., Russ C., Lennon N.,
RA Chapman S.B., Erlich R., Young S.K., Yandava C., Zeng Q., Alvarado L.,
RA Anderson S., Berlin A., Chen Z., Freedman E., Gellesch M., Goldberg J.,
RA Green L., Griggs A., Gujja S., Heilman E.R., Heiman D., Hollinger A.,
RA Howarth C., Larson L., Mehta T., Pearson M., Roberts A., Ryan E., Saif S.,
RA Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., White J., Haas B.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Synechococcus phage S-SKS1.";
RL Submitted (OCT-2010) 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; HQ633071; AGH31613.1; -; Genomic_DNA.
DR RefSeq; YP_007674465.1; NC_020851.1.
DR GeneID; 15011013; -.
DR KEGG; vg:15011013; -.
DR OrthoDB; 2035at10239; -.
DR Proteomes; UP000201252; 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:AGH31613.1};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_04155};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_04155};
KW Reference proteome {ECO:0000313|Proteomes:UP000201252};
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 REGION 443..468
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 450..468
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 203..210
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04155"
SQ SEQUENCE 468 AA; 53092 MW; 2DA51AF47D3123CD CRC64;
MMLPRRKFSL MERIETTILR NLICNENYSR KVIPFIEPTY FEQRGEKVIF EEITQFIVKY
GSAITAEALN IEVENRTDLN ESEIKETRDI CNSFTDLPVD NEWLLDTTEK WCRDRAIYLA
LMESIHIADG NDEKKSRDAI PSILSDALAV SFDNNIGHDY LENYQERYEY YHRKEEKVSF
DLEYLNKITS GGISNKTLTI ALAGTGVGKS LFMCHVASSV LLQGKNVLYI TMEMAEEKIA
ERIDANLLDV AIQNIVDLPK STFENKVTKL AAKTQGTLII KEYPTASAHS GHFKALLSEL
ALKKSFRPDI IFIDYLNICA SSRYKSGMSV NSYSYIKSIA EELRGLAGEA EVPIVSATQT
TRSGFGSSDV DLTDTSESFG LPATADLMFA LISTEELEQI GQIMVKQLKN RYNDTVVNKR
FVIGIDRSKM RLYDCEQSAQ DNILDSGQEE EYNNEDRPKK SFEGFKFS
//
