PROSITE logo

PROSITE documentation PDOC00575

View entry in NiceDoc format
View entry in raw text format (no links)
{PDOC00575}
{PS00680; MAP_1}
{PS01202; MAP_2}
{BEGIN}
****************************************
* Methionine aminopeptidase signatures *
****************************************

Methionine aminopeptidase  (EC 3.4.11.18) (MAP) is responsible for the removal
of the amino-terminal (initiator) methionine from nascent eukaryotic cytosolic
and cytoplasmic  prokaryotic  proteins  if the penultimate amino acid is small
and uncharged.  All  MAP  studied  to date are monomeric proteins that require
cobalt ions for activity.

Two subfamilies  of  MAP  enzymes  are  known  to  exist  [1,2].  While  being
evolutionary related,  they only share a limited amount of sequence similarity
mostly clustered  around  the residues shown, in the Escherichia coli MAP [3],
to be involved in cobalt-binding.

The first  family  consists  of enzymes from prokaryotes as well as eukaryotic
MAP-1, while  the second group is made up of archebacterial MAP and eukaryotic
MAP-2. The  second  subfamily  also  includes proteins which do not seem to be
MAP, but  that  are  clearly evolutionary related such as mouse proliferation-
associated protein 1 and fission yeast curved DNA-binding protein.

For each  of these subfamilies, we developed a specific signature pattern that
includes residues known to be involved in colbalt-binding.

-Consensus pattern: [MFY]-x-G-H-G-[LIVMC]-[GSHN]-x(3)-H-x(4)-[LIVM]-x(1,2)-
                    [HN]-[YWVHF]
                    [H is a cobalt ligand]
-Sequences known to belong to this class detected by the pattern: ALL MAP from
 family 1.
-Other sequence(s) detected in Swiss-Prot: NONE.

-Consensus pattern: [DA]-[LIVMY]-x-K-[LIVM]-D-x-G-x-[HQ]-[LIVMS]-[DNS]-G-x(3)-
                    [DN]
                    [The second D and the last D/N are cobalt ligands]
-Sequences known to belong to this class detected by the pattern: ALL MAP from
 family 2. Does not detect fission yeast curved DNA-binding protein.
-Other sequence(s) detected in Swiss-Prot: NONE.

-Note: These proteins belong to family M24A and M24C in the classification  of
 peptidases [4,E1].

-Last update: April 2006 / Patterns revised.

[ 1] Arfin S.M., Kendall R.L., Hall L., Weaver L.H., Stewart A.E.,
     Matthews B.W., Bradshaw R.A.
     "Eukaryotic methionyl aminopeptidases: two classes of cobalt-dependent
     enzymes."
     Proc. Natl. Acad. Sci. U.S.A. 92:7714-7718(1995).
     PubMed=7644482
[ 2] Keeling P.J., Doolittle W.F.
     "Methionine aminopeptidase-1: the MAP of the mitochondrion?"
     Trends Biochem. Sci. 21:285-286(1996).
     PubMed=8772380
[ 3] Roderick S.L., Matthews B.W.
     "Structure of the cobalt-dependent methionine aminopeptidase from
     Escherichia coli: a new type of proteolytic enzyme."
     Biochemistry 32:3907-3912(1993).
     PubMed=8471602
[ 4] Rawlings N.D., Barrett A.J.
     "Evolutionary families of metallopeptidases."
     Methods Enzymol. 248:183-228(1995).
     PubMed=7674922
[E1] https://www.uniprot.org/docs/peptidas

--------------------------------------------------------------------------------
PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and
distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives
(CC BY-NC-ND 4.0) License, see https://prosite.expasy.org/prosite_license.html
--------------------------------------------------------------------------------

{END}