CAZyme Information: MGYG000001995_03676

Basic Information

• Species: Parabacteroides sp900541965
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Tannerellaceae; Parabacteroides; Parabacteroides sp900541965
• CAZyme ID: MGYG000001995_03676
• CAZy Family: CBM9
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
369	MGYG000001995_90|CGC1	42562.13	4.7674

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001995	4648473	MAG	Spain	Europe

• Gene Location: Start: 4198; End: 5307 Strand: -

Full Sequence      

MSKSILLSLSLATLTLLSCGNKQASKEQAISYPEQFPFNPPTYVCYKAPGQIKVDGILSP
GEWDAIPWTSDFVDIEGDKRPKPYLNTRAKMAYDEKGMYFAALLEEPHVWATLMQHDTVI
YYDNDFEIFLNPTNDTHNYLEYEINAKGTDWDLFLSRPYRDNPQVLNNLELAGMQSAVHI
NGTLNNPNDIDKSWSVEVFMPWTAIYEVMRGKGKPEAGEQMRVNFSRVQWTTEVQNGQYV
KVPIKGEDKIREYNWVWAPTGVINIHMPEYWGYVQFSDKVAGTGETPFVTNPAEEVKWLL
RNLYYRQNLYAATFGQYATTVNELKPEEICTPEQAKQIRLYTTPSMYEISMPAPDGTLWH
IRQDGWVWK

Enzyme Prediction     

No EC number prediction in MGYG000001995_03676.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
CBM9	54	255	4.3e-36	0.967032967032967

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd09620	CBM9_like_3	9.64e-66	54	273	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	1.72e-14	42	228	1	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.
cd00241	DOMON_like	8.26e-05	71	215	4	137	Domon-like ligand-binding domains. DOMON-like domains can be found in all three kindgoms of life and are a diverse group of ligand binding domains that have been shown to interact with sugars and hemes. DOMON domains were initially thought to confer protein-protein interactions. They were subsequently found as a heme-binding motif in cellobiose dehydrogenase, an extracellular fungal oxidoreductase that degrades both lignin and cellulose, and in ethylbenzene dehydrogenase, an enzyme that aids in the anaerobic degradation of hydrocarbons. The domain interacts with sugars in the type 9 carbohydrate binding modules (CBM9), which are present in a variety of glycosyl hydrolases, and it can also be found at the N-terminus of sensor histidine kinases.
cd09619	CBM9_like_4	0.009	51	227	1	157	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QUT94008.1	7.64e-215	1	368	1	368
QUR47585.1	1.79e-213	1	368	1	368
QXD16319.1	1.87e-110	40	368	32	361
QOS77319.1	1.85e-104	38	369	13	339
QLG42346.1	3.70e-104	38	369	13	339

PDB Hits     

has no PDB hit.

Swiss-Prot Hits     

has no Swissprot hit.

SignalP and Lipop Annotations

This protein is predicted as LIPO

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000000	0.000030	1.000013	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001995_03676.