CAZyme Information: MGYG000002473_03353

Basic Information

• Species: Victivallis vadensis
• Lineage: Bacteria; Verrucomicrobiota; Lentisphaeria; Victivallales; Victivallaceae; Victivallis; Victivallis vadensis
• CAZyme ID: MGYG000002473_03353
• CAZy Family: CBM9
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
769		84376.87	7.138

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002473	4576885	Isolate	not provided	not provided

• Gene Location: Start: 1635; End: 3944 Strand: -

Full Sequence      

MFTAEIADAAGRTTRISGIFGEAAPVGPEKADVFGMNVHFGRYDADQRWKLYPLLKKAGV
STVRTDSSFRNFKTREEARETLLRLKEAILGQEAFGFESMVLVGYFPPGFHRSAEKLVTA
REWMELLARELKGRASFHYGNETNSGWGAFGAAADMAQLNNAMAIGTEAGDPGARRGSFG
IAEGDIAYLDRFLGAGAGDRLDAICLHPYGGTPEASVAKLLAARGVIRKHGGNQQIWATE
VGFHTDEAGKRNELTGNLTGVSGFTMLHQRQLLARLFVLALSHGIERIYWYDFYGLKDPE
TFYLVNPDLTLRDSYHALAECARQLKGARPLGGTAPHELIQRHYFRRADGTTVMAAWALA
GGVRADFRLPANAEATDDLGRPVALPPDRVPVLGDGVLYVTGLKLPEFTARKVIAGTLDE
RNFNRPMSRFTVRPGGTVQIPWSVWNGSAAPVEAAPAVLRRLPGWKIGLPGNIAVEPGKQ
HNGKILLTAPTDAVPGVEYEFTFAANIDGLQRTLPYTVRVAAEGEFPYRAIQQTASGSCP
MWNPMDESKAGTGNPELTARRGSAKIDGDLAEWKPEEFFPIDQKFQWILRDSGIPSAEDW
SGWIAFRWDEKKLYAAVLVRDDELFFGDFLSRDWRDSDNMRLFLSSVADPAKRAKTITGD
DLLLIMTPTGVARTEGPMLNIASLGGLVRSGMESQVEMKSRVWKNGYVLEAAIPFSLFNA
KPAEGTVLGLNVMADDCDGNFRQHVGMTYYKSPNYWNSPAALGNLKLGK

Enzyme Prediction     

No EC number prediction in MGYG000002473_03353.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
CBM9	566	767	2.2e-17	0.9945054945054945

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd09619	CBM9_like_4	6.66e-24	566	763	4	187	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.
pfam06452	CBM9_1	5.42e-11	566	767	1	181	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	3.37e-07	558	767	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.
cd00241	DOMON_like	8.21e-06	604	744	22	154	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AHF90983.1	6.01e-221	17	767	145	906
SDU11835.1	1.12e-211	6	767	102	869
AHF92009.1	2.62e-206	17	767	89	866
ACZ43418.1	2.97e-15	141	743	464	1010
SDS28907.1	2.73e-13	141	758	301	856

PDB Hits     

has no PDB hit.

Swiss-Prot Hits     

has no Swissprot hit.

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
1.000053	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002473_03353.