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PR01813

Identifier
ANNEXINFUNGI  [View Relations]  [View Alignment]  
Accession
PR01813
No. of Motifs
5
Creation Date
15-JAN-2003
Title
Fungal annexin type XIV signature
Database References
PRINTS; PR00196 ANNEXIN
Literature References
1. BARTON, G.J., NEWMAN, R.H., FREEMONT, P.S. AND CRUMPTON, M.J.
Amino acid sequence analysis of the annexin super-gene family of proteins.
EUR.J.BIOCHEM. 198 749-760 (1991).
 
2. BRAUN, E.L., KANG, S., NELSON, M.A. AND NATVIG, D.O.
Identification of the first fungal annexin: analysis of annexin gene
duplications and implications for eukaryotic evolution.
J.MOL.EVOL. 47 531-543 (1998).
 
3. BENZ, J. AND HOFMANN, A.
Annexins: from structure to function.
BIOL.CHEM. 378 177-183 (1997).
 
4. GEISOW, M.J.
Annexins-forms without function but not without fun.
TRENDS BIOTECHNOL. 9 180-181 (1991).

Documentation
The annexins (or lipocortins) are a family of proteins that bind to
phospholipids in a calcium-dependent manner [1]. They are distributed
ubiquitously in different tissues and cell types of higher and lower
eukaryotes, including mammals, fish, birds, Drosophila melanogaster, Xenopus
laevis, Caenorhabtidis elegans, Dictyostelium discoideum and Neurospora 
crassa [2,3]. The plant annexins are somewhat distinct from those found in
other taxa [3].
 
Several distinct annexin subtypes exist, each of which has an amino acid
sequence consisting of an N-terminal 'arm' followed by 4 or 8 copies of a
conserved domain of 61 residues (only one of these residues, an arginine,
is conserved between all copies). The calcium binding sites are found within
the repeated domains [4]. Individual repeats (sometimes referred to as 
endonexin folds) consist of 5 alpha-helices wound into a right-handed
superhelix. The biological roles of some annexin subtypes is unclear; the
family has been linked with inhibition of phospholipase activity,
exocytosis and endoctyosis, signal transduction, organisation of the
extracellular matrix, resistance to reactive oxygen species and DNA
replication [2].
 
The first fungal annexin was reported in 1998, encoded by the anx14
gene of the filamentous ascomycete Neurospora crassa [2]. Phylogenetic
analyses clustered the fungal annexin with homologous proteins from a
number of animal species; this is consistent with the existence of an
animal-fungal clade.
 
ANNEXINFUNGI is a 5-element fingerprint that provides a signature for the
type XIV fungal annexins. The fingerprint was derived from an initial
alignment of 2 sequences: the motifs were drawn from conserved regions
spanning the C-terminal half of the alignment, focusing on those sections
that characterise fungal type XIV annexins but distinguish them from other
closely related annexin subtypes - motifs 1 and 2 lie within the first core
repeat; motif 3 resides within the third repeat; and motifs 4 and 5 lie
within repeat 4. A single iteration on SPTR40_20f was required to reach
convergence, no further sequences being identified beyond the starting set.
Summary Information
2 codes involving  5 elements
0 codes involving 4 elements
0 codes involving 3 elements
0 codes involving 2 elements
Composite Feature Index
522222
400000
300000
200000
12345
True Positives
O59907        Q96UP4        
Sequence Titles
O59907      ANNEXIN XIV - Neurospora crassa.              
Q96UP4 ANNEXIN XIV-LIKE PROTEIN - Aspergillus niger.
Scan History
SPTR40_20f 1  300  NSINGLE    
Initial Motifs
Motif 1  width=10
Element Seqn Id St Int Rpt
PSPGYGPAMN O59907 152 152 -
PSPGYDPTFL Q96UP4 189 189 -

Motif 2 width=10
Element Seqn Id St Int Rpt
IPWNPDPDAD O59907 162 0 -
APGTASNEAE Q96UP4 199 0 -

Motif 3 width=13
Element Seqn Id St Int Rpt
GELSMKTERHFMI O59907 292 120 -
GELSGKTERFFEM Q96UP4 330 121 -

Motif 4 width=15
Element Seqn Id St Int Rpt
HMKDALLIQLRHGTD O59907 382 77 -
HLEDALVTMLRVARD Q96UP4 420 77 -

Motif 5 width=10
Element Seqn Id St Int Rpt
VRAHWDRNNM O59907 424 27 -
VRLHWNPEYF Q96UP4 463 28 -
Final Motifs
Motif 1  width=10
Element Seqn Id St Int Rpt
PSPGYGPAMN O59907 152 152 -
PSPGYDPTFL Q96UP4 189 189 -

Motif 2 width=10
Element Seqn Id St Int Rpt
IPWNPDPDAD O59907 162 0 -
APGTASNEAE Q96UP4 199 0 -

Motif 3 width=13
Element Seqn Id St Int Rpt
GELSMKTERHFMI O59907 292 120 -
GELSGKTERFFEM Q96UP4 330 121 -

Motif 4 width=15
Element Seqn Id St Int Rpt
HMKDALLIQLRHGTD O59907 382 77 -
HLEDALVTMLRVARD Q96UP4 420 77 -

Motif 5 width=10
Element Seqn Id St Int Rpt
VRAHWDRNNM O59907 424 27 -
VRLHWNPEYF Q96UP4 463 28 -