{PDOC52005}
{PS52005; CBM56}
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* CBM56 (carbohydrate binding type-56) domain profile *
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Carbohydrate binding  modules  (CBMs)  are  independent  domains  existing  in
carbohydrate active enzymes. The majority of such domains exhibit carbohydrate
binding activity,  which  enhances  the  catalytic  efficiency of carbohydrate
active enzymes.  The  non-catalytic  CBMs  are classified into families, which
currently number  >70  and  are based on amino acid sequence identity. The CBM
family 56  (CBM56) domain is an ~95-amino acid module, which selectively binds
insoluble beta-1,3-glucans,  probably by binding domains in the polysaccharide
with triple-helical quaternary structure [1,2,3,4,E1].

The CBM56  domain  adopts  a  beta-sandwich  fold  comprising  two opposing 4-
stranded beta-sheets  with  the very last beta-strand in the fold being broken
up by a bulge in its middle (see <PDB:5T7A>) [1].

Some proteins known to contain a CBM56 domain are listed below:

 - Bacillus halodurans BH0236, a multimodular beta-1,3-glucanase comprising an
   N-terminal family 81 glycoside hydrolase (GH) catalytic module, an internal
   family 6 carbohydrate-binding module (CBM) (see <PDOC51175>) that binds the
   nonreducing end  of  beta-1,3-glucan  chains, and a C-terminal CBM56 domain
   [1].
 - Paenibacillus  barengoltzii  GH  family 64 beta-1,3-glucanase (PbBgl64A), a
   multi-domain protein  that  belongs  to  the  GH64-TLP  superfamily,  which
   consists of an N-terminal CBM56 domain and a C-terminal family 64 GH domain
   [2,3].
 - Clostridium  beijerinckii  glucanallin,  composed of a BetaGamma-crystallin
   domain (see <PDOC00197>), a GH64 domain, and a CBM56 domain [4].

The profile we developed covers the whole CBM56 domain.

-Sequences known to belong to this class detected by the profile: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.
-Last update: September 2022 / First entry.

[ 1] Hettle A., Fillo A., Abe K., Massel P., Pluvinage B., Langelaan D.N.,
     Smith S.P., Boraston A.B.
     "Properties of a family 56 carbohydrate-binding module and its role in
     the recognition and hydrolysis of beta-1,3-glucan."
     J. Biol. Chem. 292:16955-16968(2017).
     PubMed=28827308; DOI=10.1074/jbc.M117.806711
[ 2] Qin Z., Yang D., You X., Liu Y., Hu S., Yan Q., Yang S., Jiang Z.
     "The recognition mechanism of triple-helical beta-1,3-glucan by a
     beta-1,3-glucanase."
     Chem. Commun. (Camb). 53:9368-9371(2017).
     PubMed=28787048; DOI=10.1039/c7cc03330c
[ 3] Lin S., Qin Z., Chen Q., Fan L., Zhou J., Zhao L.
     "Efficient Immobilization of Bacterial GH Family 46 Chitosanase by
     Carbohydrate-Binding Module Fusion for the Controllable Preparation of
     Chitooligosaccharides."
     J. Agric. Food. Chem. 67:6847-6855(2019).
     PubMed=31132258; DOI=10.1021/acs.jafc.9b01608
[ 4] Krishnan B., Srivastava S.S., Sankeshi V., Garg R., Srivastava S.,
     Sankaranarayanan R., Sharma Y.
     "betagamma-Crystallination Endows a Novel Bacterial Glycoside
     Hydrolase 64 with Ca(2+)-Dependent Activity Modulation."
     J. Bacteriol. 201:0-0(2019).
     PubMed=31527113; DOI=10.1128/JB.00392-19
[E1] http://www.cazy.org/CBM56.html

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