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Description:
Probable endonuclease IV (EC 3.1.21.2) (Endodeoxyribonuclease IV).
Molecular weight: 32998
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:
31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
01-OCT-2000, sequence version 1.
07-MAR-2006, entry version 35.
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_BACHD:
| Database | Pointer | Add. info#1 | Add. info#2 |
| EMBL | BA000004 | BAB05105.1 | - |
| PIR | B83823 | B83823. | |
| HSSP | P12638 | 1QTW | |
| SMR | Q9KD33 | 3-298.1 | |
| GenomeReviews | BA000004_GR | BH1386.1 | |
| BioCyc | BHAL86665:BH1386-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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=C-125 / JCM 9153;
RX MEDLINE=20512582; PubMed=11058132; DOI=10.1093/nar/28.21.4317;
RA Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N.,
RA Fuji F., Hirama C., Nakamura Y., Ogasawara N., Kuhara S.,
RA Horikoshi K.;
RT "Complete genome sequence of the alkaliphilic bacterium Bacillus
RT halodurans and genomic sequence comparison with Bacillus subtilis.";
RL Nucleic Acids Res. 28:4317-4331(2000).
Feature:
CHAIN 1 298 Probable endonuclease IV.
/FTId=PRO_0000190822.
METAL 70 70 Zinc 1 (By similarity).
METAL 111 111 Zinc 1 (By similarity).
METAL 146 146 Zinc 1 (By similarity).
METAL 146 146 Zinc 2 (By similarity).
METAL 180 180 Zinc 2 (By similarity).
METAL 183 183 Zinc 3 (By similarity).
METAL 215 215 Zinc 2 (By similarity).
METAL 228 228 Zinc 3 (By similarity).
METAL 230 230 Zinc 3 (By similarity).
METAL 260 260 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: 298
MTLHLGSHVS MNGKKMLLGS SEEAISYGAN TFMVYTGAPQ NTRRKPIEEL NIEAGRAHMK
ENGIDHIIVH APYIINIGNS EKPATFKLGV DFLQSEIERT QALGADQIVL HPGAHVGAGV
DKGIEKIIEG LNEVLTENDG VQIALETMAG KGSECGRTFE EIARIINGVT HNDRLSVCFD
TCHTHDAGYN IVEDFDGVLN EFDKIIGVER IKVLHINDSK NPRGAAKDRH ENIGFGHIGF
KALHYIVHHP QLQDIPKILE TPYVGEDKKN KKPPYKFEID MIRNGTFHEG LLEKIVAQ