Protein data for END3_RICPR:

Description:
Endonuclease III (EC 4.2.99.18) (DNA-(apurinic or apyrimidinic site)lyase).

Molecular weight: 24174

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 ) base-excision repair( GO:0006284 )


Important dates:
15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
01-JUL-1997, sequence version 1.
07-MAR-2006, entry version 38.

Phylogenetic order:
Bacteria Proteobacteria Alphaproteobacteria Rickettsiales Rickettsiaceae Rickettsieae Rickettsia typhus group.

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 END3_RICPR:

DatabasePointerAdd. info#1Add. info#2
EMBLY11778CAA72458.1-
EMBLAJ235273CAA15174.1-
PIRF71634F71634.
HSSPP206252ABK
GenomeReviewsAJ235269_GRRP746.1
BioCycRPRO782:RP746-MONOMER-.1
InterProIPR003265Endo_3c.
InterProIPR004035EndoIII_FCL.
InterProIPR004036EndoIII_HhH.
InterProIPR003651FeS_bind.
InterProIPR000445HhH.
InterProIPR005759Nth.
PfamPF00633HHH1.
PfamPF00730HhH-GPD1.
SMARTSM00478ENDO3c1.
SMARTSM00525FES1.
TIGRFAMsTIGR01083nth1.
PROSITEPS00764ENDONUCLEASE_III_11.
PROSITEPS01155ENDONUCLEASE_III_21.

General information about the databases mentioned above

Keywords:
4Fe-4S; Complete proteome; DNA damage; DNA repair; Glycosidase; Hydrolase; Iron; Iron-sulfur; Lyase; Metal-binding; Multifunctional enzyme.

References:
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Madrid E;
RX MEDLINE=97419517; PubMed=9274032;
RA Andersson J.O., Andersson S.G.E.;
RT "Genomic rearrangements during evolution of the obligate intracellular
RT parasite Rickettsia prowazekii as inferred from an analysis of 52015
RT bp nucleotide sequence.";
RL Microbiology 143:2783-2795(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Madrid E;
RX MEDLINE=99039499; PubMed=9823893; DOI=10.1038/24094;
RA Andersson S.G.E., Zomorodipour A., Andersson J.O.,
RA Sicheritz-Ponten T., Alsmark U.C.M., Podowski R.M., Naeslund A.K.,
RA Eriksson A.-S., Winkler H.H., Kurland C.G.;
RT "The genome sequence of Rickettsia prowazekii and the origin of
RT mitochondria.";
RL Nature 396:133-140(1998).

Feature:
CHAIN 1 212 Endonuclease III.
/FTId=PRO_0000102221.
METAL 187 187 Iron-sulfur (4Fe-4S) (By similarity).
METAL 194 194 Iron-sulfur (4Fe-4S) (By similarity).
METAL 197 197 Iron-sulfur (4Fe-4S) (By similarity).
METAL 203 203 Iron-sulfur (4Fe-4S) (By similarity).

Comments:
-!- FUNCTION: Has both an apurinic and/or apyrimidinic endonuclease
activity and a DNA N-glycosylase activity. Incises damaged DNA at
cytosines, thymines and guanines. Acts on a damaged strand, 5'
from the damaged site (By similarity).
-!- CATALYTIC ACTIVITY: The C-O-P bond 3' to the apurinic or
apyrimidinic site in DNA is broken by a beta-elimination reaction,
leaving a 3'-terminal unsaturated sugar and a product with a
terminal 5'-phosphate.
-!- COFACTOR: Binds 1 4Fe-4S cluster which is not important for the
catalytic activity, but which is probably involved in the proper
positioning of the enzyme along the DNA strand (By similarity).
-!- SIMILARITY: Belongs to the nth/mutY family.
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Sequence length: 212

     MQAQIMNKIF EIFSKNNPKP QTELIYKNDF TLLVAVILSA RATDISVNLA TKHLFETYNT
     PEKFLELGEE GLKKYIKSIG LFNSKAKNII ALCQILIKNY QTSIPNNFKE LVKLPGVGRK
     TANVVLNCLF AMPTMAVDTH VFRVSKRIGL AKGNTAAIVE KELLQIIDEK WLTYAHHWLI
     LHGRYICKAR KPGCNICPIK EYCEYYINTF SS