{PDOC51784}
{PS51784; EXOI_SH3}
{PS51785; EXOI_C}
{BEGIN}
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* Exonuclease I (ExoI) SH3-like and C-terminal domains profiles *
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In bacteria,  exonuclease I (ExoI) is a monomeric processive 3'-5' exonuclease
that degrades single-stranded DNA. The enzyme has been implicated as primarily
being involved  in  repairing  frameshift  mutations.  ExoI  consists of three
domains: an  N-terminal  nuclease  domain  with  homology  to the proofreading
domain of  E.  coli  DNA  polymereae  I  and other DnaQ superfamily enzymes, a
central domain  with  a  portion  that  resembles  an SH3 domain fold and a C-
terminal alpha-helical  domain.  While  a  typical SH3-like domain consists of
five or  six  antiparallel beta-strands that form a compact beta-sandwich, the
beta-sandwich of  the  SH3-like domain in ExoI is surrounded by alpha-helices,
resulting in a substantially elaborated fold (see <PDB:1FXX>) [1,2,3].

The profile  we  developed  covers  the  entire  ExoI  SH3-like and C-terminal
domains.

-Sequences known to belong to this class detected by the profile: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.

-Sequences known to belong to this class detected by the profile: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.

-Last update: December 2015 / First entry.

[ 1] Breyer W.A., Matthews B.W.
     "Structure of Escherichia coli exonuclease I suggests how processivity
     is achieved."
     Nat. Struct. Biol. 7:1125-1128(2000).
     PubMed=11101894; DOI=10.1038/81978
[ 2] Busam R.D.
     "Structure of Escherichia coli exonuclease I in complex with thymidine
     5'-monophosphate."
     Acta Crystallogr. D 64:206-210(2008).
     PubMed=18219121; DOI=10.1107/S090744490706012X
[ 3] Korada S.K.C., Johns T.D., Smith C.E., Jones N.D., McCabe K.A.,
     Bell C.E.
     "Crystal structures of Escherichia coli exonuclease I in complex with
     single-stranded DNA provide insights into the mechanism of processive
     digestion."
     Nucleic Acids Res. 41:5887-5897(2013).
     PubMed=23609540; DOI=10.1093/nar/gkt278

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