END4_GEOKA
ID END4_GEOKA Reviewed; 299 AA.
AC Q5KX27;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 95.
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=GK2474;
OS Geobacillus kaustophilus (strain HTA426).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus;
OC Geobacillus thermoleovorans group.
OX NCBI_TaxID=235909;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HTA426;
RX PubMed=15576355; DOI=10.1093/nar/gkh970;
RA Takami H., Takaki Y., Chee G.-J., Nishi S., Shimamura S., Suzuki H.,
RA Matsui S., Uchiyama I.;
RT "Thermoadaptation trait revealed by the genome sequence of thermophilic
RT Geobacillus kaustophilus.";
RL Nucleic Acids Res. 32:6292-6303(2004).
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; BA000043; BAD76759.1; -; Genomic_DNA.
DR RefSeq; WP_011231954.1; NC_006510.1.
DR PDB; 3AAL; X-ray; 1.60 A; A=1-299.
DR PDBsum; 3AAL; -.
DR AlphaFoldDB; Q5KX27; -.
DR SMR; Q5KX27; -.
DR STRING; 235909.GK2474; -.
DR EnsemblBacteria; BAD76759; BAD76759; GK2474.
DR KEGG; gka:GK2474; -.
DR PATRIC; fig|235909.7.peg.2649; -.
DR eggNOG; COG0648; Bacteria.
DR HOGENOM; CLU_025885_4_1_9; -.
DR OMA; HPGSHLK; -.
DR BRENDA; 4.2.99.18; 8138.
DR Proteomes; UP000001172; 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:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
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..299
FT /note="Probable endonuclease 4"
FT /id="PRO_1000011307"
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 110
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00152"
FT BINDING 145
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00152"
FT BINDING 145
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00152"
FT BINDING 179
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00152"
FT BINDING 182
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00152"
FT BINDING 214
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00152"
FT BINDING 227
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00152"
FT BINDING 229
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00152"
FT BINDING 259
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:3AAL"
FT TURN 12..15
FT /evidence="ECO:0007829|PDB:3AAL"
FT HELIX 16..25
FT /evidence="ECO:0007829|PDB:3AAL"
FT STRAND 29..36
FT /evidence="ECO:0007829|PDB:3AAL"
FT HELIX 47..49
FT /evidence="ECO:0007829|PDB:3AAL"
FT HELIX 51..60
FT /evidence="ECO:0007829|PDB:3AAL"
FT STRAND 65..69
FT /evidence="ECO:0007829|PDB:3AAL"
FT HELIX 82..102
FT /evidence="ECO:0007829|PDB:3AAL"
FT STRAND 105..109
FT /evidence="ECO:0007829|PDB:3AAL"
FT HELIX 119..133
FT /evidence="ECO:0007829|PDB:3AAL"
FT STRAND 141..145
FT /evidence="ECO:0007829|PDB:3AAL"
FT HELIX 158..167
FT /evidence="ECO:0007829|PDB:3AAL"
FT HELIX 171..173
FT /evidence="ECO:0007829|PDB:3AAL"
FT STRAND 174..179
FT /evidence="ECO:0007829|PDB:3AAL"
FT HELIX 180..186
FT /evidence="ECO:0007829|PDB:3AAL"
FT HELIX 190..204
FT /evidence="ECO:0007829|PDB:3AAL"
FT HELIX 207..209
FT /evidence="ECO:0007829|PDB:3AAL"
FT STRAND 210..215
FT /evidence="ECO:0007829|PDB:3AAL"
FT STRAND 217..220
FT /evidence="ECO:0007829|PDB:3AAL"
FT STRAND 234..237
FT /evidence="ECO:0007829|PDB:3AAL"
FT HELIX 239..246
FT /evidence="ECO:0007829|PDB:3AAL"
FT STRAND 256..258
FT /evidence="ECO:0007829|PDB:3AAL"
FT HELIX 274..283
FT /evidence="ECO:0007829|PDB:3AAL"
FT HELIX 290..294
FT /evidence="ECO:0007829|PDB:3AAL"
SQ SEQUENCE 299 AA; 33040 MW; CA79F0CC75E1703C CRC64;
MLKIGSHVSM SGKKMLLAAS EEAASYGANT FMIYTGAPQN TKRKSIEELN IEAGRQHMQA
HGIEEIVVHA PYIINIGNTT NLDTFSLGVD FLRAEIERTE AIGAKQLVLH PGAHVGAGVE
AGLRQIIRGL NEVLTREQNV QIALETMAGK GSECGRTFEE LAYIIDGVAY NDKLSVCFDT
CHTHDAGYDI VNDFDGVLEE FDRIIGLGRL KVLHINDSKN PRGSRKDRHE NIGFGHIGFA
ALNYIVHHPQ LEDIPKILET PYVGEDKNNK KPPYKHEIAM LRAQSFDDQL LEKINAGAE
