Protein data for END4_MYCLE:

Description:
Probable endonuclease IV (EC 3.1.21.2) (Endodeoxyribonuclease IV).

Molecular weight: 26861

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-JUL-1993, integrated into UniProtKB/Swiss-Prot.
01-JUL-1993, sequence version 1.
07-MAR-2006, entry version 48.

Phylogenetic order:
Bacteria Actinobacteria Actinobacteridae Actinomycetales Corynebacterineae Mycobacteriaceae Mycobacterium.

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_MYCLE:

DatabasePointerAdd. info#1Add. info#2
EMBLZ14314CAA78670.1-
EMBLAL583923CAC30843.1-
PIRS31147S31147.
GenomeReviewsAL450380_GRML1889.1
LepromaML1889-.
BioCycMLEP1769:ML1889-MONOMER-.1
HAMAPMF_00152-1.
InterProIPR001719AP_endnuclease2.
InterProIPR012307Xylisom_TIMbarrl.
PfamPF01261AP_endonuc_21.
SMARTSM00518AP2Ec1.
TIGRFAMsTIGR00587nfo1.
PROSITEPS00729AP_NUCLEASE_F2_11.
PROSITEPS00730AP_NUCLEASE_F2_21.
PROSITEPS00731AP_NUCLEASE_F2_31.

General information about the databases mentioned above

Keywords:
Complete proteome; DNA damage; DNA repair; Endonuclease; Hydrolase; Metal-binding; Nuclease; Zinc.

References:
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX MEDLINE=93188701; PubMed=8446028;
RA Honore N.T., Bergh S., Chanteau S., Doucet-Populaire F., Eiglmeier K.,
RA Garnier T., Georges C., Launois P., Limpaiboon T., Newton S.,
RA Niang K., del Portillo P., Ramesh G.R., Reddi P., Ridel P.R.,
RA Sittisombut N., Wu-Hunter S., Cole S.T.;
RT "Nucleotide sequence of the first cosmid from the Mycobacterium leprae
RT genome project: structure and function of the Rif-Str regions.";
RL Mol. Microbiol. 7:207-214(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TN;
RX MEDLINE=21128732; PubMed=11234002; DOI=10.1038/35059006;
RA Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA Barrell B.G.;
RT "Massive gene decay in the leprosy bacillus.";
RL Nature 409:1007-1011(2001).

Feature:
CHAIN 1 252 Probable endonuclease IV.
/FTId=PRO_0000190854.
METAL 56 56 Zinc 1 (By similarity).
METAL 96 96 Zinc 1 (By similarity).
METAL 129 129 Zinc 1 (By similarity).
METAL 129 129 Zinc 2 (By similarity).
METAL 162 162 Zinc 2 (By similarity).
METAL 165 165 Zinc 3 (By similarity).
METAL 191 191 Zinc 2 (By similarity).
METAL 204 204 Zinc 3 (By similarity).
METAL 206 206 Zinc 3 (By similarity).
METAL 233 233 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: 252

     MLIGSHVSST DPLAAAEVEG ADVVQIFLGN PQSWKAPTLR SDADVLKATA LPVYVHAPYL
     INVASANSRV RIPSRKILQQ TCDAAADIGA AAVVVHGGYV ADDNDLEDGF QRWRKALDQL
     QTDVPVYLEN TAGGDHAMAR RFDTIARLWD VIGETGIGFC LDTCHAWAAG EGLIHVVDRI
     KAITGRIDLV HCNDSKDEAG SGRDRHANLG SGQIDAELLV AAVKVAGAPV ICETAEEGRK
     DDIAFLREKT SG