ID G8EY64_9CAUD Unreviewed; 461 AA.
AC G8EY64;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 08-NOV-2023, entry version 36.
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=P29A0810_153 {ECO:0000313|EMBL:AOV60089.1}, SXCG_00136
GN {ECO:0000313|EMBL:AGN33992.1}, SXFG_00206
GN {ECO:0000313|EMBL:AET72754.1};
OS Synechococcus phage S-CAM8.
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Kyanoviridae; Neritesvirus; Neritesvirus scam8.
OX NCBI_TaxID=754038 {ECO:0000313|EMBL:AET72754.1, ECO:0000313|Proteomes:UP000297591};
RN [1] {ECO:0000313|EMBL:AGN33992.1, ECO:0000313|Proteomes:UP000014318}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S-CAM8 06008BI06 {ECO:0000313|EMBL:AGN33992.1};
RG The Broad Institute Genome Sequencing Platform;
RA Henn M.R., Martiny J., Weihe C., Levin J., Malboeuf C., Casali M., Russ C.,
RA Lennon N., Chapman S.B., Erlich R., Young S.K., Yandava C., Zeng Q.,
RA Alvarado L., Anderson S., Berlin A., Chen Z., Freedman E., Gellesch M.,
RA Goldberg J., Green L., Griggs A., Gujja S., Heilman E.R., Heiman D.,
RA Hollinger A., Howarth C., Larson L., Mehta T., Pearson M., Roberts A.,
RA Ryan E., Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S.,
RA White J., Haas B., Nusbaum C., Birren B.;
RT "The Genome Sequence of Synechococcus phage S-CAM8 0608BI06.";
RL Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AET72754.1, ECO:0000313|Proteomes:UP000297591}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0608SB47 {ECO:0000313|EMBL:AET72754.1,
RC ECO:0000313|Proteomes:UP000297591};
RG The Broad Institute Genome Sequencing Platform;
RA Henn M.R., Martiny J., Weihe C., Levin J., Malboeuf C., Casali M., Russ C.,
RA Lennon N., Chapman S.B., Erlich R., Young S.K., Yandava C., Zeng Q.,
RA Alvarado L., Anderson S., Berlin A., Chen Z., Freedman E., Gellesch M.,
RA Goldberg J., Green L., Griggs A., Gujja S., Heilman E.R., Heiman D.,
RA Hollinger A., Howarth C., Larson L., Mehta T., Pearson M., Roberts A.,
RA Ryan E., Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S.,
RA White J., Haas B., Nusbaum C., Birren B.;
RT "The Genome Sequence of Synechococcus phage S-CAM8 0608SB47.";
RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:AOV60089.1, ECO:0000313|Proteomes:UP000224839}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0810PA29 {ECO:0000313|EMBL:AOV60089.1};
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JF974299; AET72754.1; -; Genomic_DNA.
DR EMBL; HQ634178; AGN33992.1; -; Genomic_DNA.
DR EMBL; KU686203; AOV60089.1; -; Genomic_DNA.
DR RefSeq; YP_008125685.1; NC_021530.1.
DR GeneID; 16045287; -.
DR KEGG; vg:16045287; -.
DR OrthoDB; 2035at10239; -.
DR Proteomes; UP000014318; Genome.
DR Proteomes; UP000224839; Genome.
DR Proteomes; UP000297591; Segment.
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; IPR036185; DNA_heli_DnaB-like_N_sf.
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; SSF48024; N-terminal domain of DnaB helicase; 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:AGN33992.1};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_04155};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_04155};
KW Reference proteome {ECO:0000313|Proteomes:UP000014318};
KW Viral DNA replication {ECO:0000256|HAMAP-Rule:MF_04155}.
FT DOMAIN 160..427
FT /note="SF4 helicase"
FT /evidence="ECO:0000259|PROSITE:PS51199"
FT BINDING 192..199
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04155"
SQ SEQUENCE 461 AA; 52212 MW; 974E0A75C5005ABB CRC64;
MNLEVTILSN LIYNEKYARK VLPFLKYDYF TAREHKIIFL EIHEYISQYD ACPSLNAIGI
ECQERTDLTE DQFKEIIQVL NVLSDDPADY DWLVDTTEKW CQERAIYLSL MESVKIADGQ
DTKRDKGAIP SILSEALGVS FDQHVGHDYV SDAQERFDFY HRKEDKIPFD LSLFNKITKG
GLPNKTLNIA LAGTGVGKSL FMCHCAAAAL LQGKNVLYIT MEMAEEKIAE RIDANLLNVP
IQQLGDLPQV MFEKKIANLS KKTQGKLIIK EYPTASAHVG HFKSLVSDLA LKRSIKPDII
FVDYLNICAS ERYKGSIVNS YTYVKAIAEE LRGFAVECNV PIISATQTTR SGYGSTDVDL
TDTSESFGLP ATADLMFALI STEELEGMNQ IMVKQLKNRY NDTTTFKRFC IGIDRAKMRL
YDVEESAQDD LINSGQETEP QQIDLVKKFT SKKTFQDLKY D
//
