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Description:
Probable endonuclease IV (EC 3.1.21.2) (Endodeoxyribonuclease IV).
Molecular weight: 30555
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:
15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
01-MAR-2003, sequence version 1.
07-MAR-2006, entry version 22.
Phylogenetic order:
Bacteria Actinobacteria Actinobacteridae Bifidobacteriales Bifidobacteriaceae Bifidobacterium.
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_BIFLO:
| Database | Pointer | Add. info#1 | Add. info#2 |
| EMBL | AE014295 | AAN24574.1 | - |
| HSSP | P12638 | 1QTW | |
| GenomeReviews | AE014295_GR | BL0757.1 | |
| BioCyc | BLON206672:BL0757-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 | FALSE_NEG. |
| PROSITE | PS00730 | AP_NUCLEASE_F2_2 | FALSE_NEG. |
| 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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCC 2705;
RX MEDLINE=22294977; PubMed=12381787; DOI=10.1073/pnas.212527599;
RA Schell M.A., Karmirantzou M., Snel B., Vilanova D., Berger B.,
RA Pessi G., Zwahlen M.-C., Desiere F., Bork P., Delley M.,
RA Pridmore R.D., Arigoni F.;
RT "The genome sequence of Bifidobacterium longum reflects its adaptation
RT to the human gastrointestinal tract.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:14422-14427(2002).
Feature:
CHAIN 1 283 Probable endonuclease IV.
/FTId=PRO_0000190827.
METAL 69 69 Zinc 1 (By similarity).
METAL 113 113 Zinc 1 (By similarity).
METAL 148 148 Zinc 1 (By similarity).
METAL 148 148 Zinc 2 (By similarity).
METAL 182 182 Zinc 2 (By similarity).
METAL 185 185 Zinc 3 (By similarity).
METAL 217 217 Zinc 2 (By similarity).
METAL 230 230 Zinc 3 (By similarity).
METAL 232 232 Zinc 3 (By similarity).
METAL 262 262 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: 283
MMELYIGSHL STAGGWNALL ERSHEEGGTA FAFFPRSPYG KRSKALDPAG AAAFGARLKA
EGYGPLVVHA PYVYNLAGKD EAKRAFAIEA LAEDIELLTA IRAAGQEVYI NIHPGAHVGQ
GAETGCRLIS EGLNQVFERA DGVMVLLETM AGKGTECGRN FDELATIMDG VENKANVGVT
FDTCHVLDAG YDLENDYDGV MRQLDEAIGL ARVKAIHVND SQFGLGSHKD RHANIGEGQL
GIPFFTRLVN DPTMAKLPMI LETKEQTPTT HRDEIALLRG LVD