(data stored in SCRATCH zone)

SWISSPROT: END4_BACSU

ID   END4_BACSU              Reviewed;         297 AA.
AC   P54476;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   11-DEC-2019, entry version 129.
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}; Synonyms=yqfS;
GN   OrderedLocusNames=BSU25130;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168 / JH642;
RX   PubMed=8969508; DOI=10.1099/13500872-142-11-3103;
RA   Mizuno M., Masuda S., Takemaru K., Hosono S., Sato T., Takeuchi M.,
RA   Kobayashi Y.;
RT   "Systematic sequencing of the 283 kb 210 degrees-232 degrees region of the
RT   Bacillus subtilis genome containing the skin element and many sporulation
RT   genes.";
RL   Microbiology 142:3103-3111(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
CC   -!- FUNCTION: Endonuclease IV plays a role in DNA repair. It cleaves
CC       phosphodiester bonds at apurinic or apyrimidinic sites (AP sites) to
CC       produce new 5'-ends that are base-free deoxyribose 5-phosphate
CC       residues. It preferentially attacks modified AP sites created by
CC       bleomycin and neocarzinostatin. {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}.
DR   EMBL; D84432; BAA12496.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB14443.1; -; Genomic_DNA.
DR   PIR; E69954; E69954.
DR   RefSeq; NP_390392.1; NC_000964.3.
DR   RefSeq; WP_009967756.1; NZ_JNCM01000036.1.
DR   SMR; P54476; -.
DR   STRING; 224308.BSU25130; -.
DR   jPOST; P54476; -.
DR   PaxDb; P54476; -.
DR   PRIDE; P54476; -.
DR   EnsemblBacteria; CAB14443; CAB14443; BSU25130.
DR   GeneID; 937922; -.
DR   KEGG; bsu:BSU25130; -.
DR   PATRIC; fig|224308.179.peg.2732; -.
DR   eggNOG; ENOG4105EFU; Bacteria.
DR   eggNOG; COG0648; LUCA.
DR   HOGENOM; HOG000224895; -.
DR   InParanoid; P54476; -.
DR   KO; K01151; -.
DR   OMA; HPGSHLK; -.
DR   PhylomeDB; P54476; -.
DR   BioCyc; BSUB:BSU25130-MONOMER; -.
DR   Proteomes; UP000001570; 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   3: Inferred from homology;
DR   PRODOM; P54476.
DR   SWISS-2DPAGE; P54476.
KW   DNA damage; DNA repair; Endonuclease; Hydrolase; Metal-binding; Nuclease;
KW   Reference proteome; Zinc.
FT   CHAIN           1..297
FT                   /note="Probable endonuclease 4"
FT                   /id="PRO_0000190825"
FT   METAL           69
FT                   /note="Zinc 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00152"
FT   METAL           110
FT                   /note="Zinc 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00152"
FT   METAL           145
FT                   /note="Zinc 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00152"
FT   METAL           145
FT                   /note="Zinc 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00152"
FT   METAL           179
FT                   /note="Zinc 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00152"
FT   METAL           182
FT                   /note="Zinc 3"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00152"
FT   METAL           214
FT                   /note="Zinc 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00152"
FT   METAL           227
FT                   /note="Zinc 3"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00152"
FT   METAL           229
FT                   /note="Zinc 3"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00152"
FT   METAL           259
FT                   /note="Zinc 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00152"
SQ   SEQUENCE   297 AA;  33069 MW;  49A54AF24B61EB84 CRC64;
     MLRIGSHVSM SGKHMLLAAS QEAVSYGANT FMIYTGAPQN TRRKKIEDLN IEAGRAHMQE
     NGIDEIIVHA PYIINIGNTT NPSTFELGVD FLRSEIERTA AIGAKQIVLH PGAHVGAGAE
     AGIKKIIEGL NEVIDPNQNV QIALETMAGK GSECGRSFEE LAQIIEGVTH NEQLSVCFDT
     CHTHDAGYNI VEDFDGVLNE FDKIIGIDRI KVLHINDSKN VKGARKDRHE NIGFGEIGFD
     ALQYVVHHEQ LKDIPKILET PYVGEDKKNK KPPYRFEIEM LKEKQFDDTL LEKILQQ
//

If you have problems or comments...

PBIL Back to PBIL home page