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Description:
Probable endonuclease IV (EC 3.1.21.2) (Endodeoxyribonuclease IV).
Molecular weight: 33069
View which proteins in this organism that is involved with DNA Repair;
classified after biological processes (using data from the GOA project):
DNA repair( GO:0006281 )
Important dates:
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 1.
07-MAR-2006, entry version 48.
Phylogenetic order:
Bacteria Firmicutes Bacillales Bacillaceae Bacillus.
To calculate the pI (Isoelectric point - the pH where a protein has a neutral charge),
go to this page and enter the protein ID (e.g 3MG_ECOLI): http://us.expasy.org/tools/pi_tool.html
Links to references in other databases for protein END4_BACSU:
| Database | Pointer | Add. info#1 | Add. info#2 |
| EMBL | D84432 | BAA12496.1 | - |
| EMBL | Z99116 | CAB14443.1 | - |
| PIR | E69954 | E69954. | |
| HSSP | P12638 | 1QTW | |
| SMR | P54476 | 2-297.1 | |
| GenomeReviews | AL009126_GR | BSU25130.1 | |
| SubtiList | BG11665 | nfo. | |
| BioCyc | BSUB1423:BSU2510-MONOMER | -.1 | |
| HAMAP | MF_00152 | - | 1. |
| InterPro | IPR001719 | AP_endnuclease2. | |
| InterPro | IPR012307 | Xylisom_TIMbarrl. | |
| Pfam | PF01261 | AP_endonuc_2 | 1. |
| SMART | SM00518 | AP2Ec | 1. |
| TIGRFAMs | TIGR00587 | nfo | 1. |
| PROSITE | PS00729 | AP_NUCLEASE_F2_1 | 1. |
| PROSITE | PS00730 | AP_NUCLEASE_F2_2 | 1. |
| PROSITE | PS00731 | AP_NUCLEASE_F2_3 | 1. |
Keywords:
Complete proteome; DNA damage; DNA repair; Endonuclease; Hydrolase; Metal-binding; Nuclease; Zinc.
References:
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168 / JH642;
RX MEDLINE=97124195; PubMed=8969508;
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
RT the Bacillus subtilis genome containing the skin element and many
RT sporulation genes.";
RL Microbiology 142:3103-3111(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX MEDLINE=98044033; PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G.,
RA Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S.,
RA Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S.,
RA Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M.,
RA Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A.,
RA Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T.,
RA Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D.,
RA Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N.,
RA Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G.,
RA Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A.,
RA Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M.,
RA Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M.,
RA Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S.,
RA 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.,
RA Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B.,
RA Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R.,
RA Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P.,
RA Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H.,
RA Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P.,
RA Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F.,
RA Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H.,
RA 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).
Feature:
CHAIN 1 297 Probable endonuclease IV.
/FTId=PRO_0000190825.
METAL 69 69 Zinc 1 (By similarity).
METAL 110 110 Zinc 1 (By similarity).
METAL 145 145 Zinc 1 (By similarity).
METAL 145 145 Zinc 2 (By similarity).
METAL 179 179 Zinc 2 (By similarity).
METAL 182 182 Zinc 3 (By similarity).
METAL 214 214 Zinc 2 (By similarity).
METAL 227 227 Zinc 3 (By similarity).
METAL 229 229 Zinc 3 (By similarity).
METAL 259 259 Zinc 2 (By similarity).
Comments:
-!- FUNCTION: Endonuclease IV plays a role in DNA repair. It cleaves
phosphodiester bonds at apurinic or apyrimidinic sites (AP sites)
to produce new 5' ends that are base-free deoxyribose 5-phosphate
residues. It preferentially attacks modified AP sites created by
bleomycin and neocarzinostatin (By similarity).
-!- CATALYTIC ACTIVITY: Endonucleolytic cleavage to 5'-
phosphooligonucleotide end-products.
-!- COFACTOR: Binds 3 zinc ions (By similarity).
-!- SIMILARITY: Belongs to the AP endonuclease 2 family.
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Sequence length: 297
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