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Description:
Probable endonuclease IV (EC 3.1.21.2) (Endodeoxyribonuclease IV).
Molecular weight: 32843
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-NOV-2002, integrated into UniProtKB/Swiss-Prot.
01-DEC-2001, sequence version 1.
07-MAR-2006, entry version 28.
Phylogenetic order:
Bacteria Firmicutes Bacillales Listeriaceae Listeria.
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_LISIN:
| Database | Pointer | Add. info#1 | Add. info#2 |
| EMBL | AL596168 | CAC96718.1 | - |
| PIR | AF1618 | AF1618. | |
| HSSP | P12638 | 1QTW | |
| SMR | Q92BR0 | 2-295.1 | |
| GenomeReviews | AL592022_GR | lin1487.1 | |
| ListiList | LIN01487 | -.1 | |
| BioCyc | LINN1642:LIN1487-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 | 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=CLIP 11262 / Serovar 6a;
RX MEDLINE=21537279; PubMed=11679669; DOI=10.1126/science.1063447;
RA Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A.,
RA Baquero F., Berche P., Bloecker H., Brandt P., Chakraborty T.,
RA Charbit A., Chetouani F., Couve E., de Daruvar A., Dehoux P.,
RA Domann E., Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O.,
RA Entian K.-D., Fsihi H., Garcia-del Portillo F., Garrido P.,
RA Gautier L., Goebel W., Gomez-Lopez N., Hain T., Hauf J., Jackson D.,
RA Jones L.-M., Kaerst U., Kreft J., Kuhn M., Kunst F., Kurapkat G.,
RA Madueno E., Maitournam A., Mata Vicente J., Ng E., Nedjari H.,
RA Nordsiek G., Novella S., de Pablos B., Perez-Diaz J.-C., Purcell R.,
RA Remmel B., Rose M., Schlueter T., Simoes N., Tierrez A.,
RA Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
RT "Comparative genomics of Listeria species.";
RL Science 294:849-852(2001).
Feature:
CHAIN 1 297 Probable endonuclease IV.
/FTId=PRO_0000190846.
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
MLRLGSHVSM SGKKMLLGAS EEAASYGSNT FMIYTGAPQN TRRKPIEELN IEAGLEHMKA
HDMADIVVHA PYIINIGNSV KPETFELGVN FLQSEIERTR ALGAKQIVLH PGAHVGEGAD
KGIKQIIQGL NEALIHDQDV QIALETMAGK GSECGRTFEE LAQIIDGVTH NELLSVTFDT
CHTHDAGYDI VNDFDGVLNE FDKIIGIDRL KVLHINDSKN ERGAHKDRHA NIGFGHIGFD
ALHYIVHHPQ LSNIPKILET PYVGEDKASK KAPYKWEIAM LRNGEFDPDL LNKIQNS