PROSITE output appended by default
Note: comments marked by "## COMMENT: "
Note 2: this example contains only the ProSite related output of PredictProtein!
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):
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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}
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