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trunc25like

Trunc25like refers to a family of protein sequences that share a conserved motif or domain similarity to a notional trunc25 domain. In public sequence databases, trunc25like is used as a classification for proteins or protein fragments that display a recognizable, but often modest, similarity to trunc25. It is not a single gene or strictly defined protein, but rather a set of related sequences that can occur as standalone proteins or as parts of larger, multidomain proteins.

Discovery and classification of trunc25like arose through comparative genomics and automated domain predictions. The category encompasses

Structure and function are not yet well characterized for trunc25like. No widely accepted three-dimensional structure has

Genomic context often provides additional clues. In some organisms, trunc25like-containing proteins are found near genes associated

See also: protein domain families, Pfam, UniProt annotations, RNA processing factors. Further reading includes comparative genomics

diverse
taxa,
including
bacteria,
archaea,
and
some
eukaryotes,
and
most
members
are
annotated
on
the
basis
of
sequence
similarity
rather
than
experimentally
confirmed
function.
Because
the
exact
role
of
the
trunc25like
domain
remains
unclear,
annotations
are
typically
cautious,
identifying
a
putative
domain
without
asserting
a
specific
biochemical
activity.
been
solved,
and
the
majority
of
members
lack
experimental
functional
validation.
Consequently,
hypotheses
about
trunc25like
function
vary;
proposed
roles
include
involvement
in
RNA-related
processes,
mediating
protein-protein
interactions,
or
acting
as
a
small
accessory
module
within
larger
enzymes.
The
diversity
of
contexts
in
which
trunc25like
appears
suggests
it
may
participate
in
multiple,
lineage-specific
functions.
with
RNA
processing
or
stress
response,
implying
a
possible
regulatory
or
modular
role.
Evolutionarily,
the
family
shows
diversification
through
lineage-specific
expansions
and
domain
shuffling.
studies
and
database
annotations
that
discuss
trunc25like
in
the
context
of
conserved
motifs
and
domain
architecture.