Example for output from PROSITE

Sequence: 1ppt (PDB)

PROSITE output appended by default


OUTPUT

Note: comments marked by "## COMMENT: "

Note 2: this example contains only the ProSite related output of PredictProtein!

Quick guide through output



The following information has been received by the server:

~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~

________________________________________________________________________________

return concise
phdacc
test seq from phd people
run prodom
#1ppt.pir ( 1ppt.hssp from:    1 to:   36 )
MPPRWASLLL LACSLLLLAV PPGTAGPSQP TYPGDDAPVE DLIRFYNDLQ
QYLNVVTRHR YGRRSSSRVL CEEPMGAAGC

________________________________________________________________________________



Result of PROSITE search (Amos Bairoch):
~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~

________________________________________________________________________________


Prosite Database -- Copyright: Amos Bairoch
ProSearch Software -- Release 1.2 -- Copyright: Lee Kolakowski
The following patterns are in < /home/phd/server/work/t-normal-32487.seqGCG >:

Access#	    From->To	Name                	Doc#
_______	    ________	____________________	_________
PS00004	    186->190	CAMP_PHOSPHO_SITE   	PDOC00004
PS00005	    189->192	PKC_PHOSPHO_SITE    	PDOC00005
PS00009	    184->188	AMIDATION           	PDOC00009
{PDOC00004}
{PS00004; CAMP_PHOSPHO_SITE}
{BEGIN}

cAMP- and cGMP-dependent protein kinase phosphorylation site


There has been a  number of studies  relative to the  specificity of cAMP- and
cGMP-dependent protein kinases [1,2,3].  Both types of kinases appear to share
a preference  for  the  phosphorylation  of serine or threonine residues found
close to at least  two consecutive N-terminal  basic residues. It is important
to note that there are quite a number of exceptions to this rule.

-Consensus pattern: [RK](2)-x-[ST]
                    [S or T is the phosphorylation site]
-Last update: June 1988 / First entry.

[ 1] Fremisco J.R., Glass D.B., Krebs E.G.
     J. Biol. Chem. 255:4240-4245(1980).
[ 2] Glass D.B., Smith S.B.
     J. Biol. Chem. 258:14797-14803(1983).
[ 3] Glass D.B., El-Maghrabi M.R., Pilkis S.J.
     J. Biol. Chem. 261:2987-2993(1986).
{END}
{PDOC00005}
{PS00005; PKC_PHOSPHO_SITE}
{BEGIN}

Protein kinase C phosphorylation site


In vivo, protein kinase C  exhibits  a  preference  for the phosphorylation of
serine or  threonine residues found close to a C-terminal basic residue [1,2].
The presence  of  additional   basic residues at the  N- or C-terminal of  the
target amino acid enhances the Vmax and Km of the phosphorylation reaction.

-Consensus pattern: [ST]-x-[RK]
                    [S or T is the phosphorylation site]
-Last update: June 1988 / First entry.

[ 1] Woodget J.R., Gould K.L., Hunter T.
     Eur. J. Biochem. 161:177-184(1986).
[ 2] Kishimoto A., Nishiyama K., Nakanishi H., Uratsuji Y., Nomura H.,
     Takeyama Y., Nishizuka Y.
     J. Biol. Chem. 260:12492-12499(1985).
{END}
{PDOC00009}
{PS00009; AMIDATION}
{BEGIN}

Amidation site


The precursor of  hormones  and other active  peptides  which are C-terminally
amidated is always directly followed [1,2] by a glycine residue which provides
the amide group, and  most often by at  least two  consecutive  basic residues
(Arg or Lys) which generally function as an active peptide  precursor cleavage
site.  Although all amino acids can be amidated,  neutral hydrophobic residues
such as Val or Phe are good substrates, while  charged residues such as Asp or
Arg  are much less reactive.  C-terminal  amidation has not  yet been shown to
occur in unicellular organisms or in plants.

-Consensus pattern: x-G-[RK]-[RK]
                    [x is the amidation site]
-Last update: June 1988 / First entry.

[ 1] Kreil G.
     Meth. Enzymol. 106:218-223(1984).
[ 2] Bradbury A.F., Smyth D.G.
     Biosci. Rep. 7:907-916(1987).
{END}

________________________________________________________________________________