END4_THEMA
ID END4_THEMA Reviewed; 287 AA.
AC Q9WYJ7;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Probable endonuclease 4 {ECO:0000255|HAMAP-Rule:MF_00152};
DE EC=3.1.21.2 {ECO:0000255|HAMAP-Rule:MF_00152};
DE AltName: Full=Endodeoxyribonuclease IV {ECO:0000255|HAMAP-Rule:MF_00152};
DE AltName: Full=Endonuclease IV {ECO:0000255|HAMAP-Rule:MF_00152};
GN Name=nfo {ECO:0000255|HAMAP-Rule:MF_00152}; OrderedLocusNames=TM_0362;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
CC -!- FUNCTION: Endonuclease IV plays a role in DNA repair. It cleaves
CC phosphodiester bonds at apurinic or apyrimidinic (AP) sites, generating
CC a 3'-hydroxyl group and a 5'-terminal sugar phosphate.
CC {ECO:0000255|HAMAP-Rule:MF_00152}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endonucleolytic cleavage to 5'-phosphooligonucleotide end-
CC products.; EC=3.1.21.2; Evidence={ECO:0000255|HAMAP-Rule:MF_00152};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00152};
CC Note=Binds 3 Zn(2+) ions. {ECO:0000255|HAMAP-Rule:MF_00152};
CC -!- SIMILARITY: Belongs to the AP endonuclease 2 family.
CC {ECO:0000255|HAMAP-Rule:MF_00152}.
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DR EMBL; AE000512; AAD35449.1; -; Genomic_DNA.
DR PIR; B72387; B72387.
DR RefSeq; NP_228173.1; NC_000853.1.
DR RefSeq; WP_010865102.1; NZ_CP011107.1.
DR PDB; 2X7V; X-ray; 2.30 A; A=1-287.
DR PDB; 2X7W; X-ray; 2.36 A; A=1-287.
DR PDB; 4HNO; X-ray; 0.92 A; A=2-285.
DR PDBsum; 2X7V; -.
DR PDBsum; 2X7W; -.
DR PDBsum; 4HNO; -.
DR AlphaFoldDB; Q9WYJ7; -.
DR SMR; Q9WYJ7; -.
DR STRING; 243274.THEMA_02905; -.
DR EnsemblBacteria; AAD35449; AAD35449; TM_0362.
DR KEGG; tma:TM0362; -.
DR eggNOG; COG0648; Bacteria.
DR InParanoid; Q9WYJ7; -.
DR OMA; HPGSHLK; -.
DR OrthoDB; 1088517at2; -.
DR BRENDA; 3.1.21.2; 6331.
DR EvolutionaryTrace; Q9WYJ7; -.
DR Proteomes; UP000008183; Chromosome.
DR GO; GO:0008833; F:deoxyribonuclease IV (phage-T4-induced) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003906; F:DNA-(apurinic or apyrimidinic site) endonuclease activity; IBA:GO_Central.
DR GO; GO:0008081; F:phosphoric diester hydrolase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006284; P:base-excision repair; IBA:GO_Central.
DR CDD; cd00019; AP2Ec; 1.
DR HAMAP; MF_00152; Nfo; 1.
DR InterPro; IPR001719; AP_endonuc_2.
DR InterPro; IPR018246; AP_endonuc_F2_Zn_BS.
DR InterPro; IPR036237; Xyl_isomerase-like_sf.
DR InterPro; IPR013022; Xyl_isomerase-like_TIM-brl.
DR PANTHER; PTHR21445; PTHR21445; 1.
DR Pfam; PF01261; AP_endonuc_2; 1.
DR SMART; SM00518; AP2Ec; 1.
DR SUPFAM; SSF51658; SSF51658; 1.
DR TIGRFAMs; TIGR00587; nfo; 1.
DR PROSITE; PS00729; AP_NUCLEASE_F2_1; 1.
DR PROSITE; PS00730; AP_NUCLEASE_F2_2; 1.
DR PROSITE; PS00731; AP_NUCLEASE_F2_3; 1.
DR PROSITE; PS51432; AP_NUCLEASE_F2_4; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA damage; DNA repair; Endonuclease; Hydrolase;
KW Metal-binding; Nuclease; Reference proteome; Zinc.
FT CHAIN 1..287
FT /note="Probable endonuclease 4"
FT /id="PRO_0000190880"
FT BINDING 69
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00152"
FT BINDING 109
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00152"
FT BINDING 144
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00152"
FT BINDING 144
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00152"
FT BINDING 178
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00152"
FT BINDING 181
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00152"
FT BINDING 215
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00152"
FT BINDING 228
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00152"
FT BINDING 230
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00152"
FT BINDING 260
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00152"
FT STRAND 4..7
FT /evidence="ECO:0007829|PDB:4HNO"
FT HELIX 14..16
FT /evidence="ECO:0007829|PDB:4HNO"
FT HELIX 17..23
FT /evidence="ECO:0007829|PDB:4HNO"
FT STRAND 27..31
FT /evidence="ECO:0007829|PDB:4HNO"
FT STRAND 37..39
FT /evidence="ECO:0007829|PDB:4HNO"
FT HELIX 46..58
FT /evidence="ECO:0007829|PDB:4HNO"
FT HELIX 63..65
FT /evidence="ECO:0007829|PDB:4HNO"
FT STRAND 66..69
FT /evidence="ECO:0007829|PDB:4HNO"
FT HELIX 81..101
FT /evidence="ECO:0007829|PDB:4HNO"
FT STRAND 105..108
FT /evidence="ECO:0007829|PDB:4HNO"
FT HELIX 118..133
FT /evidence="ECO:0007829|PDB:4HNO"
FT STRAND 140..144
FT /evidence="ECO:0007829|PDB:4HNO"
FT HELIX 157..166
FT /evidence="ECO:0007829|PDB:4HNO"
FT HELIX 170..172
FT /evidence="ECO:0007829|PDB:4HNO"
FT STRAND 173..178
FT /evidence="ECO:0007829|PDB:4HNO"
FT HELIX 179..184
FT /evidence="ECO:0007829|PDB:4HNO"
FT HELIX 192..205
FT /evidence="ECO:0007829|PDB:4HNO"
FT HELIX 208..210
FT /evidence="ECO:0007829|PDB:4HNO"
FT STRAND 211..216
FT /evidence="ECO:0007829|PDB:4HNO"
FT STRAND 218..221
FT /evidence="ECO:0007829|PDB:4HNO"
FT STRAND 235..238
FT /evidence="ECO:0007829|PDB:4HNO"
FT HELIX 239..247
FT /evidence="ECO:0007829|PDB:4HNO"
FT HELIX 250..253
FT /evidence="ECO:0007829|PDB:4HNO"
FT STRAND 257..259
FT /evidence="ECO:0007829|PDB:4HNO"
FT HELIX 265..281
FT /evidence="ECO:0007829|PDB:4HNO"
SQ SEQUENCE 287 AA; 32435 MW; A2BEE00CE7AE4A5A CRC64;
MIKIGAHMPI SKGFDRVPQD TVNIGGNSFQ IFPHNARSWS AKLPSDEAAT KFKREMKKHG
IDWENAFCHS GYLINLASPK DDIWQKSVEL LKKEVEICRK LGIRYLNIHP GSHLGTGEEE
GIDRIVRGLN EVLNNTEGVV ILLENVSQKG GNIGYKLEQL KKIRDLVDQR DRVAITYDTC
HGFDSGYDIT KKEGVEALLN EIESLFGLER LKMIHLNDSK YPLGAAKDRH ERIGSGFIGE
EGFAVFFSFK EIQEVPWILE TPGGNEEHAE DIKKVFEIIE KFGIEVD
