ID A0A076YQI9_9CAUD Unreviewed; 549 AA.
AC A0A076YQI9;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=DNA helicase/primase {ECO:0000256|HAMAP-Rule:MF_04154};
DE EC=2.7.7.- {ECO:0000256|HAMAP-Rule:MF_04154};
DE EC=3.6.4.12 {ECO:0000256|HAMAP-Rule:MF_04154};
GN ORFNames=Lo5R7ANS_31 {ECO:0000313|EMBL:AIK68501.1};
OS Mesorhizobium phage vB_MloP_Lo5R7ANS.
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Autographiviridae; Pairvirus; Pairvirus Lo5R7ANS.
OX NCBI_TaxID=1527771 {ECO:0000313|EMBL:AIK68501.1, ECO:0000313|Proteomes:UP000201609};
RN [1] {ECO:0000313|EMBL:AIK68501.1, ECO:0000313|Proteomes:UP000201609}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Halmillawewa A.P., Perry B., Gavard R., Yost C.K., Hynes M.F.;
RT "Genomic characterization of two T7-like Mesorhizobium loti phages
RT vB_MloP_Lo5R7ANS and vB_MloP_Cp1R7ANS-C2.";
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: ATP-dependent DNA helicase and primase essential for viral
CC DNA 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. ATP or dTTP hydrolysis propels
CC each helicase domain to translocate sequentially along DNA. Mediates
CC strand transfer when a joint molecule is available and participates in
CC recombinational DNA repair through its role in strand exchange. Primase
CC activity synthesizes short RNA primers at the sequence 5'-GTC-3' on the
CC lagging strand that the polymerase elongates using dNTPs and providing
CC the primase is still present. {ECO:0000256|HAMAP-Rule:MF_04154}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_04154};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_04154};
CC Note=Binds 2 Mg(2+), one of which is catalytic. {ECO:0000256|HAMAP-
CC Rule:MF_04154};
CC -!- SUBUNIT: Homohexamer. Assembles as a hexamer onto linear or circular
CC ssDNA in the presence of ATP or dTTP. Interacts (via C-terminus) with
CC the viral DNA polymerase that is bound to DNA; this interaction is
CC essential to initiate leading-strand DNA synthesis. The priming complex
CC consists of 2 DNA polymerases and 1 helicase-primase hexamer that
CC assemble on the DNA template. Interacts with the single-stranded DNA-
CC binding protein. Part of the replicase complex that includes the DNA
CC polymerase, the primase/helicase and the single-stranded DNA binding
CC protein. {ECO:0000256|HAMAP-Rule:MF_04154}.
CC -!- DOMAIN: The N-terminus zinc finger domain is essential for delivering
CC the primed DNA template to the DNA polymerase. The central core domain
CC contains the primase activity. The C-terminus region is responsible for
CC the helicase activity and binds 1 Mg(2+)-dTTP. {ECO:0000256|HAMAP-
CC Rule:MF_04154}.
CC -!- SIMILARITY: Belongs to the Teseptimavirus DNA helicase/primase family.
CC {ECO:0000256|HAMAP-Rule:MF_04154}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_04154}.
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DR EMBL; KM199771; AIK68501.1; -; Genomic_DNA.
DR RefSeq; YP_009100078.1; NC_025431.1.
DR GeneID; 22109838; -.
DR KEGG; vg:22109838; -.
DR OrthoDB; 615at10239; -.
DR Proteomes; UP000201609; Genome.
DR GO; GO:0043139; F:5'-3' DNA helicase activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003896; F:DNA primase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0003697; F:single-stranded DNA binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0039693; P:viral DNA genome replication; IEA:UniProtKB-UniRule.
DR CDD; cd19483; RecA-like_Gp4D_helicase; 1.
DR CDD; cd01029; TOPRIM_primases; 1.
DR Gene3D; 2.20.25.10; -; 1.
DR Gene3D; 2.20.25.180; -; 1.
DR Gene3D; 3.40.1360.10; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR HAMAP; MF_04154; Helic_Prim_T7; 1.
DR InterPro; IPR007694; DNA_helicase_DnaB-like_C.
DR InterPro; IPR048774; Helic-prim_T7_N.
DR InterPro; IPR046394; Helic_Prim_T7.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR013237; Phage_T7_Gp4_N.
DR InterPro; IPR034154; TOPRIM_DnaG/twinkle.
DR InterPro; IPR006171; TOPRIM_domain.
DR InterPro; IPR027032; Twinkle-like.
DR PANTHER; PTHR12873; T7-LIKE MITOCHONDRIAL DNA HELICASE; 1.
DR PANTHER; PTHR12873:SF0; TWINKLE MTDNA HELICASE; 1.
DR Pfam; PF03796; DnaB_C; 1.
DR Pfam; PF21268; Helic-prim_T7_N; 1.
DR Pfam; PF13155; Toprim_2; 1.
DR SMART; SM00778; Prim_Zn_Ribbon; 1.
DR SUPFAM; SSF56731; DNA primase core; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF57783; Zinc beta-ribbon; 1.
DR PROSITE; PS51199; SF4_HELICASE; 1.
DR PROSITE; PS50880; TOPRIM; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_04154};
KW DNA replication {ECO:0000256|HAMAP-Rule:MF_04154};
KW Helicase {ECO:0000256|HAMAP-Rule:MF_04154, ECO:0000313|EMBL:AIK68501.1};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_04154};
KW Magnesium {ECO:0000256|HAMAP-Rule:MF_04154};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_04154};
KW Multifunctional enzyme {ECO:0000256|HAMAP-Rule:MF_04154};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_04154,
KW ECO:0000313|EMBL:AIK68501.1};
KW Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_04154};
KW Primosome {ECO:0000256|HAMAP-Rule:MF_04154};
KW Reference proteome {ECO:0000313|Proteomes:UP000201609};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_04154};
KW Viral DNA replication {ECO:0000256|HAMAP-Rule:MF_04154};
KW Zinc {ECO:0000256|HAMAP-Rule:MF_04154};
KW Zinc-finger {ECO:0000256|HAMAP-Rule:MF_04154}.
FT DOMAIN 140..225
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT DOMAIN 266..527
FT /note="SF4 helicase"
FT /evidence="ECO:0000259|PROSITE:PS51199"
FT ZN_FING 14..36
FT /note="C4-like; zinc ribbon fold"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04154"
FT REGION 526..549
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 14
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04154"
FT BINDING 17
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04154"
FT BINDING 33
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04154"
FT BINDING 36
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04154"
FT BINDING 146
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04154"
FT BINDING 196
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04154"
FT BINDING 227
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04154"
FT BINDING 297..304
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04154"
FT SITE 441
FT /note="dTTP/dATP binding"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04154"
FT SITE 479
FT /note="dTTP/dATP binding"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04154"
FT SITE 500
FT /note="dTTP/dATP binding"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04154"
SQ SEQUENCE 549 AA; 61967 MW; 0FDAAB491D97270E CRC64;
MHETDSEFLR KEPCPKCGSR DNLARYTDGH AYCFGCRHYE PGDNELAEQT EAAEPRNVDF
VPLGEPSDWA SRGINLESAQ KWGFTRSSLN GQPVRLFNYR NSAQQLVWQK IRFQGKDFRS
KGSKEDMCLY GQWLWRDGGK RVVIVEGELD AISLSQMQGH KWPVVSIPNG CDGAAKALRK
NLQWLEQFEE IVLMFDQDEP GQKATDECKL IPFTPGKLKI ATLPLKDANE MLMAGRVKET
IDAIWGAKVY RPDGLVGVSD IMGDLLKPVE YGLPWCLEEL TKLTYGRRDG EVYGFGAGTG
IGKTDFLMQQ IAFDITELKQ HVGAIFLEQK PVETAKRVAG KLAGKMFHVP DAGWTPEELT
RAATELDGKL FFYDSFGQTD WELVKGHIRY MAVSLGIKLI YVDHLTAMAD TGDEKGTLEQ
IMKEMAGLAM ELGIIIHFVS HLSTPDGKPH EEGGRVMIRH FKGSRAIGFW SYFMFGLERD
QQNEDPIIAT TTVFRILKDR YTGRATGKTI MLGFKQETGR LYVREDDPFS DKDANDHGFK
NEDDDDLPF
//
