CAZyme Information: MGYG000003099_00379

Basic Information

• Species: Barnesiella sp900538555
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Barnesiellaceae; Barnesiella; Barnesiella sp900538555
• CAZyme ID: MGYG000003099_00379
• CAZy Family: CBM9
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
334	MGYG000003099_2|CGC4	36882.42	4.2465

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003099	3270064	MAG	Spain	Europe

• Gene Location: Start: 188603; End: 189607 Strand: -

Full Sequence      

MGLLAMCCMGAPNLAAEVTADLVIKKGTPIYVDGKADDPVWAAIEPVAIDRPFQTEEPSL
TAYFKMYYTDESIFLLVDVDDDVHYPLWRNPADKKQNYMYDKVEVYFDVNDVLKDGNSPA
HNGKNDPPIAPGHAQLAFDFDDEGGYDQDRYMPSDVVYNFLDNQVYVAYSKKENGGYTVE
YDFPINAYINDKNQALDVEAFKALPNGMGFDITIVDNDNDGKGRKRMVWCSDKTEAYQNM
DGCGVVVFSSEELPVGGGIHAASVPAVRFYPNPVKETLTVEGDFDTVVLVNLLGQQVKKS
AGRQMNVADLAAGVYVIKTYKDGACSGVSKITKE

Enzyme Prediction     

No EC number prediction in MGYG000003099_00379.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
CBM9	32	246	6.4e-23	0.9835164835164835

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam06452	CBM9_1	1.42e-14	32	247	1	180	Carbohydrate family 9 binding domain-like. CBM9_1 is a C-terminal domain on bacterial xylanase proteins, and it is tandemly repeated in a number of family-members. The CBM9 module binds to amorphous and crystalline cellulose and a range of soluble di- and monosaccharides as well as to cello- and xylo- oligomers of different degrees of polymerization. Comparison of the glucose and cellobiose complexes during crystallisation reveals surprising differences in binding of these two substrates by CBM9-2. Cellobiose was found to bind in a distinct orientation from glucose, while still maintaining optimal stacking and electrostatic interactions with the reducing end sugar.
cd09619	CBM9_like_4	1.14e-10	29	239	1	182	DOMON-like type 9 carbohydrate binding module. Family 9 carbohydrate-binding modules (CBM9) play a role in the microbial degradation of cellulose and hemicellulose (materials found in plants). The domain has previously been called cellulose-binding domain. The polysaccharide binding sites of CBMs with available 3D structure have been found to be either flat surfaces with interactions formed by predominantly aromatic residues (tryptophan and tyrosine), or extended shallow grooves. CBM9 domains found in this uncharacterized heterogeneous subfamily are often located at the C-terminus of longer proteins and may co-occur with various other domains.
cd00005	CBM9_like_1	1.54e-09	23	248	3	184	DOMON-like type 9 carbohydrate binding module of xylanases. Family 9 carbohydrate-binding modules (CBM9) play a role in the microbial degradation of cellulose and hemicellulose (materials found in plants). The domain has previously been called cellulose-binding domain. The polysaccharide binding sites of CBMs with available 3D structure have been found to be either flat surfaces with interactions formed by predominantly aromatic residues (tryptophan and tyrosine), or extended shallow grooves. The CBM9 domain frequently occurs in tandem repeats; members found in this subfamily typically co-occur with glycosyl hydrolase family 10 domains and are annotated as endo-1,4-beta-xylanases. CBM9 from Thermotoga maritima xylanase 10A is reported to have specificity for polysaccharide reducing ends.
pfam18962	Por_Secre_tail	4.06e-08	270	331	2	70	Secretion system C-terminal sorting domain. Species that include Porphyromonas gingivalis, Fibrobacter succinogenes, Flavobacterium johnsoniae, Cytophaga hutchinsonii, Gramella forsetii, Prevotella intermedia, and Salinibacter ruber have on average twenty or more copies of this C-terminal domain, associated with sorting to the outer membrane and covalent modification. This domain targets proteins to type IX secretion systems and is secreted then cleaved off by a C-terminal signal peptidease. Based on similarity to other families it is likely that this domain adopts an immunoglobulin like fold.
TIGR04183	Por_Secre_tail	4.88e-07	270	334	2	72	Por secretion system C-terminal sorting domain. Species that include Porphyromonas gingivalis, Fibrobacter succinogenes, Flavobacterium johnsoniae, Cytophaga hutchinsonii, Gramella forsetii, Prevotella intermedia, and Salinibacter ruber average twenty or more copies of a C-terminal domain, represented by this model, associated with sorting to the outer membrane and covalent modification.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BCI63366.1	4.00e-110	21	334	25	352
APD07227.1	3.42e-08	25	242	44	242

PDB Hits     

has no PDB hit.

Swiss-Prot Hits     

has no Swissprot hit.

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.105746	0.837959	0.054617	0.000939	0.000380	0.000334

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003099_00379.