CAZyme Information: MGYG000004182_00813

Basic Information

• Species: Phocaeicola sp900551445
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Phocaeicola; Phocaeicola sp900551445
• CAZyme ID: MGYG000004182_00813
• CAZy Family: CBM9
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
682	MGYG000004182_11|CGC2	79638.5	5.5177

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004182	3344512	MAG	United Kingdom	Europe

• Gene Location: Start: 56364; End: 58412 Strand: -

Full Sequence      

MRKQVICSLFALLVVGQLWAQNLYTRYERMLTLPEGYVCYRTNGKIKIDGKLDEADWQKA
QPTSSFVDISGKGFAKPCYDTSAKMLWDDHYLYVAATLQEEDIKAKLSQRDTIIYYDNDF
EVFLDPDGDGQNYFEIETNAKGVIFDLMLDKPYRSGGNFLVQWDCSGLQLAVHREGTLNK
SNDKDKRWTVEMAIPHKALTVNFSNLAEAGKYWRINFSRVQWLKPGQREENWVWMPTGRI
DMHMPDRWGFLYLSDKVVGKGTDAFKYPYNLAAYKLLWAMFYAQLDYYAKEKNYLRAKEN
FFLTDAELQDLSVGSEISVEATSRTFCMSVTVPEEKVRYVVDQNGRFTCEAITPRQVKNW
VWMRINKEKGDEFYKNYFALMKECGISGVMFEGYDENTYRMCKDAGLEAHYWKWTMNRRE
VLSTHPDWFAVNRKGESCYDRPAYVDYYRFLCPNHEGVAEYLAADYLKEANLPYVDGVHL
DYVRFPDVVLPVSLWKNYGIEQTAELPEYDYCYCEVCRRMFKEQTGKDPLDLKYPMEDQS
WINFRLDAITRVVDKITQTLKAEGKQISAAVFPGPSMARKMVRQDWGEWSLDAYFPMIYN
GFYYEGPKWIGRSVKESVETVHGKARIYAGLMFPDIKNTFEQALDEAFNNGASGVSFFDG
PDEEYLHKFKAYLEKRGFEVVK

Enzyme Prediction     

No EC number prediction in MGYG000004182_00813.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
CBM9	48	251	2.1e-41	0.9835164835164835

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd09620	CBM9_like_3	8.49e-74	48	250	1	200	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 may co-occur with various other domains.
cd09618	CBM9_like_2	2.05e-33	37	220	2	170	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 subfamily are typically found at the N-terminus of longer proteins that lack additional annotation with domain footprints.
COG1649	YddW	3.29e-13	406	659	128	368	Uncharacterized lipoprotein YddW, UPF0748 family [Function unknown].
pfam06452	CBM9_1	1.94e-11	48	205	1	138	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.
cd00005	CBM9_like_1	1.74e-07	44	135	7	89	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CUA18365.1	0.0	20	680	27	687
QCQ32632.1	0.0	20	680	26	686
QRP90424.1	0.0	20	680	27	687
AKA51642.1	0.0	20	680	27	687
AUI46257.1	0.0	20	680	26	686

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
0.000666	0.998504	0.000241	0.000186	0.000187	0.000177

TMHMM  Annotations     

There is no transmembrane helices in MGYG000004182_00813.