END4_BACAN
ID END4_BACAN Reviewed; 298 AA.
AC Q81LV1; Q6HTA3; Q6KMJ5;
DT 15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 131.
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};
GN OrderedLocusNames=BA_4508, GBAA_4508, BAS4186;
OS Bacillus anthracis.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=1392;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ames / isolate Porton;
RX PubMed=12721629; DOI=10.1038/nature01586;
RA Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T.,
RA Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R.,
RA Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M.,
RA Kolonay J.F., Beanan M.J., Dodson R.J., Brinkac L.M., Gwinn M.L.,
RA DeBoy R.T., Madpu R., Daugherty S.C., Durkin A.S., Haft D.H., Nelson W.C.,
RA Peterson J.D., Pop M., Khouri H.M., Radune D., Benton J.L., Mahamoud Y.,
RA Jiang L., Hance I.R., Weidman J.F., Berry K.J., Plaut R.D., Wolf A.M.,
RA Watkins K.L., Nierman W.C., Hazen A., Cline R.T., Redmond C., Thwaite J.E.,
RA White O., Salzberg S.L., Thomason B., Friedlander A.M., Koehler T.M.,
RA Hanna P.C., Kolstoe A.-B., Fraser C.M.;
RT "The genome sequence of Bacillus anthracis Ames and comparison to closely
RT related bacteria.";
RL Nature 423:81-86(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ames ancestor;
RX PubMed=18952800; DOI=10.1128/jb.01347-08;
RA Ravel J., Jiang L., Stanley S.T., Wilson M.R., Decker R.S., Read T.D.,
RA Worsham P., Keim P.S., Salzberg S.L., Fraser-Liggett C.M., Rasko D.A.;
RT "The complete genome sequence of Bacillus anthracis Ames 'Ancestor'.";
RL J. Bacteriol. 191:445-446(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sterne;
RA Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K.,
RA Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R.,
RA Richardson P., Rubin E., Tice H.;
RT "Complete genome sequence of Bacillus anthracis Sterne.";
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
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; AE016879; AAP28219.1; -; Genomic_DNA.
DR EMBL; AE017334; AAT33627.1; -; Genomic_DNA.
DR EMBL; AE017225; AAT56486.1; -; Genomic_DNA.
DR RefSeq; NP_846733.1; NC_003997.3.
DR RefSeq; WP_000912468.1; NZ_WXXJ01000027.1.
DR RefSeq; YP_030435.1; NC_005945.1.
DR PDB; 1XP3; X-ray; 2.57 A; A=1-298.
DR PDBsum; 1XP3; -.
DR AlphaFoldDB; Q81LV1; -.
DR SMR; Q81LV1; -.
DR STRING; 260799.BAS4186; -.
DR DNASU; 1088232; -.
DR EnsemblBacteria; AAP28219; AAP28219; BA_4508.
DR EnsemblBacteria; AAT33627; AAT33627; GBAA_4508.
DR GeneID; 45024164; -.
DR KEGG; ban:BA_4508; -.
DR KEGG; bar:GBAA_4508; -.
DR KEGG; bat:BAS4186; -.
DR PATRIC; fig|198094.11.peg.4476; -.
DR eggNOG; COG0648; Bacteria.
DR HOGENOM; CLU_025885_4_1_9; -.
DR OMA; HPGSHLK; -.
DR EvolutionaryTrace; Q81LV1; -.
DR Proteomes; UP000000427; Chromosome.
DR Proteomes; UP000000594; 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..298
FT /note="Probable endonuclease 4"
FT /id="PRO_0000190819"
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 111
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00152"
FT BINDING 146
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00152"
FT BINDING 146
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00152"
FT BINDING 180
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00152"
FT BINDING 183
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:1XP3"
FT STRAND 12..14
FT /evidence="ECO:0007829|PDB:1XP3"
FT HELIX 16..24
FT /evidence="ECO:0007829|PDB:1XP3"
FT TURN 25..27
FT /evidence="ECO:0007829|PDB:1XP3"
FT STRAND 29..33
FT /evidence="ECO:0007829|PDB:1XP3"
FT HELIX 46..49
FT /evidence="ECO:0007829|PDB:1XP3"
FT HELIX 51..60
FT /evidence="ECO:0007829|PDB:1XP3"
FT STRAND 66..69
FT /evidence="ECO:0007829|PDB:1XP3"
FT HELIX 82..101
FT /evidence="ECO:0007829|PDB:1XP3"
FT STRAND 102..104
FT /evidence="ECO:0007829|PDB:1XP3"
FT STRAND 107..110
FT /evidence="ECO:0007829|PDB:1XP3"
FT HELIX 120..134
FT /evidence="ECO:0007829|PDB:1XP3"
FT STRAND 140..146
FT /evidence="ECO:0007829|PDB:1XP3"
FT HELIX 159..168
FT /evidence="ECO:0007829|PDB:1XP3"
FT HELIX 172..174
FT /evidence="ECO:0007829|PDB:1XP3"
FT STRAND 175..180
FT /evidence="ECO:0007829|PDB:1XP3"
FT HELIX 181..186
FT /evidence="ECO:0007829|PDB:1XP3"
FT HELIX 191..205
FT /evidence="ECO:0007829|PDB:1XP3"
FT HELIX 208..210
FT /evidence="ECO:0007829|PDB:1XP3"
FT STRAND 211..216
FT /evidence="ECO:0007829|PDB:1XP3"
FT STRAND 218..221
FT /evidence="ECO:0007829|PDB:1XP3"
FT STRAND 235..238
FT /evidence="ECO:0007829|PDB:1XP3"
FT HELIX 240..247
FT /evidence="ECO:0007829|PDB:1XP3"
FT HELIX 250..252
FT /evidence="ECO:0007829|PDB:1XP3"
FT STRAND 257..259
FT /evidence="ECO:0007829|PDB:1XP3"
FT STRAND 267..269
FT /evidence="ECO:0007829|PDB:1XP3"
FT HELIX 275..284
FT /evidence="ECO:0007829|PDB:1XP3"
FT HELIX 291..296
FT /evidence="ECO:0007829|PDB:1XP3"
SQ SEQUENCE 298 AA; 32909 MW; C5178AB085784C8A CRC64;
MLKIGSHVSM SGKKMLLAAS EEAVSYGATT FMIYTGAPQN TRRKPIEELN IEAGRKHMEQ
NGIEEIIVHA PYIINVGNTT KPETFQLGVD FLRMEIERTS ALGVAKQIVL HPGAHVGAGA
DAGIQQIIKG LNEVLTPDQT VNIALETMAG KGTECGRSFE EIAKIIDGVK YNEKLSVCFD
TCHTHDAGYD IVNNFDGVLN EFDKIVGIDR LQVLHINDSK NVRGAGKDRH ENIGFGHIGY
KALHHIVHHP QLTHVPKILE TPYVGEDKKD KKPPYKLEIE MLKNGTFDEG LLEKIKAQ
