ID A0A2K8H5Z7_9CAUD Unreviewed; 291 AA.
AC A0A2K8H5Z7;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Flap endonuclease {ECO:0000256|HAMAP-Rule:MF_04140};
DE Short=FEN {ECO:0000256|HAMAP-Rule:MF_04140};
DE EC=3.1.11.- {ECO:0000256|HAMAP-Rule:MF_04140};
DE AltName: Full=5'-3' exonuclease {ECO:0000256|HAMAP-Rule:MF_04140};
DE AltName: Full=Exodeoxyribonuclease {ECO:0000256|HAMAP-Rule:MF_04140};
DE EC=3.1.11.3 {ECO:0000256|HAMAP-Rule:MF_04140};
GN ORFNames=P24_0125 {ECO:0000313|EMBL:ASU01578.1};
OS Escherichia phage chee24.
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Demerecviridae; Markadamsvirinae; Tequintavirus; Tequintavirus chee24.
OX NCBI_TaxID=2024330 {ECO:0000313|EMBL:ASU01578.1, ECO:0000313|Proteomes:UP000240516};
RN [1] {ECO:0000313|Proteomes:UP000240516}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=29487585; DOI=10.3389/fmicb.2018.00202;
RA Svab D., Falgenhauer L., Rohde M., Szabo J., Chakraborty T., Toth I.;
RT "Identification and Characterization of T5-Like Bacteriophages Representing
RT Two Novel Subgroups from Food Products.";
RL Front. Microbiol. 9:202-202(2018).
CC -!- FUNCTION: Catalyzes both the 5'-exonucleolytic and structure-specific
CC endonucleolytic hydrolysis of DNA branched nucleic acid molecules and
CC probably plays a role in viral genome replication. Active on flap
CC (branched duplex DNA containing a free single-stranded 5'-end),
CC 5'overhangs and pseudo-Y structures. The substrates require a free,
CC single-stranded 5' end, with endonucleolytic hydrolysis occurring at
CC the junction of double- and single-stranded DNA. This function may be
CC used for example to trim such branched molecules generated by Okazaki
CC fragments synthesis during replication. {ECO:0000256|HAMAP-
CC Rule:MF_04140}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Exonucleolytic cleavage in the 5'- to 3'-direction to yield
CC nucleoside 5'-phosphates.; EC=3.1.11.3; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_04140};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_04140};
CC Name=K(+); Xref=ChEBI:CHEBI:29103;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_04140};
CC Note=Binds divalent metal cations, probably Mg(2+). In vitro low metal
CC concentrations selectively stimulate the endonuclease reaction.
CC Endonuclease activity is suggested to require only the first cation,
CC whereas exonuclease activity is suggested to require binding of both.
CC High pH favors the exonuclase activity whereas low pH favors the
CC endonuclease activity. Metal ions enhance substrate binding. K(+) is
CC bound to the H3TH region. {ECO:0000256|HAMAP-Rule:MF_04140};
CC -!- DOMAIN: Three alpha-helices form a helical arch which forms a hole in
CC the protein and through which the 5' flap of the scissile ssDNA is
CC threaded. {ECO:0000256|HAMAP-Rule:MF_04140}.
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DR EMBL; MF431730; ASU01578.1; -; Genomic_DNA.
DR Proteomes; UP000240516; Genome.
DR GO; GO:0008409; F:5'-3' exonuclease activity; IEA:UniProtKB-UniRule.
DR GO; GO:0017108; F:5'-flap endonuclease activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0033567; P:DNA replication, Okazaki fragment processing; IEA:UniProtKB-UniRule.
DR GO; GO:0039693; P:viral DNA genome replication; IEA:UniProtKB-UniRule.
DR CDD; cd09899; H3TH_T4-like; 1.
DR CDD; cd00008; PIN_53EXO-like; 1.
DR Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR Gene3D; 3.40.50.1010; 5'-nuclease; 1.
DR HAMAP; MF_04140; FEN_T5; 1.
DR InterPro; IPR020046; 5-3_exonucl_a-hlix_arch_N.
DR InterPro; IPR002421; 5-3_exonuclease.
DR InterPro; IPR036279; 5-3_exonuclease_C_sf.
DR InterPro; IPR020045; DNA_polI_H3TH.
DR InterPro; IPR038969; FEN.
DR InterPro; IPR043666; FEN_D15-like.
DR InterPro; IPR008918; HhH2.
DR InterPro; IPR029060; PIN-like_dom_sf.
DR PANTHER; PTHR42646:SF4; 5'-3' EXONUCLEASE FAMILY PROTEIN; 1.
DR PANTHER; PTHR42646; FLAP ENDONUCLEASE XNI; 1.
DR Pfam; PF01367; 5_3_exonuc; 1.
DR Pfam; PF02739; 5_3_exonuc_N; 1.
DR SMART; SM00475; 53EXOc; 1.
DR SMART; SM00279; HhH2; 1.
DR SUPFAM; SSF47807; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR SUPFAM; SSF88723; PIN domain-like; 1.
PE 3: Inferred from homology;
KW DNA replication {ECO:0000256|HAMAP-Rule:MF_04140};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW Rule:MF_04140}; Early protein {ECO:0000256|HAMAP-Rule:MF_04140};
KW Endonuclease {ECO:0000256|HAMAP-Rule:MF_04140};
KW Exonuclease {ECO:0000256|HAMAP-Rule:MF_04140};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_04140, ECO:0000313|EMBL:ASU01578.1};
KW Magnesium {ECO:0000256|HAMAP-Rule:MF_04140};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_04140};
KW Nuclease {ECO:0000256|HAMAP-Rule:MF_04140};
KW Potassium {ECO:0000256|HAMAP-Rule:MF_04140};
KW Viral DNA replication {ECO:0000256|HAMAP-Rule:MF_04140}.
FT CHAIN 1..291
FT /note="Flap endonuclease"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04140"
FT /id="PRO_5026407590"
FT DOMAIN 20..274
FT /note="5'-3' exonuclease"
FT /evidence="ECO:0000259|SMART:SM00475"
FT REGION 82..116
FT /note="Helical arch"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04140"
FT REGION 188..224
FT /note="DNA-binding; H3TH"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04140"
FT BINDING 83
FT /ligand="DNA"
FT /ligand_id="ChEBI:CHEBI:16991"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04140"
FT BINDING 130
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04140"
FT BINDING 130
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_04140"
FT BINDING 153
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04140"
FT BINDING 155
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04140"
FT BINDING 155
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04140"
FT BINDING 201
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04140"
FT BINDING 209
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04140"
FT BINDING 212
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04140"
SQ SEQUENCE 291 AA; 33349 MW; 934B497DBE3B14EE CRC64;
MSKSWGKFIE EEEAEMASRR NLMIVDGTNL GFRFKHNNSK KPFASSYVST IQSLAKSYSA
RTTIVLGDKG KSVFRLEHLP EYKGNRDEKY AQRTEEEKAL DEQFFEYLKD AFELCETTFP
TFTIRGVEAD DMAAYIVKLI GHLYDHVWLI STDGDWDTLL TDKVSRFSFT TRREYHLRDM
YEHHNVDDVE QFISLKAIMG DLGDNIRGVE GIGAKRGYNI IREFGNVLDI IDQLPLPGKQ
KYIQNLNASE ELLFRNLILV DLPTYCVDAI AAAGQDVLDK FTKDILEIAG Q
//
