CAZyme Information: MGYG000003249_01654

Basic Information

• Species: Victivallis sp900761715
• Lineage: Bacteria; Verrucomicrobiota; Lentisphaeria; Victivallales; Victivallaceae; Victivallis; Victivallis sp900761715
• CAZyme ID: MGYG000003249_01654
• CAZy Family: CBM9
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
864		93831.26	5.1248

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003249	2933905	MAG	United States	North America

• Gene Location: Start: 2322; End: 4916 Strand: -

Full Sequence      

MHRWLILVAGLILAFSSSAAEWVHSGSGSEALPLIRVTNPGREPRTLRVESVLRDTEGLA
VATAAMTREAAPGESVTLAPFPEVASVSGEIRLLESTVTGEGDDPVVLSTVVGTPRPVRA
AGLVGMNVHLGRYTPAVRWRLMRLLRDAGVVHVRVDAGFGIASNPEEVSRALAALREEVL
GLEAFGLRPLILLGYYPPEFYDSPRKSQLACEWAYAMAAGLRGRADFHYGNETNSGWAGF
GAAADLAVVNKAFALGTLAADPSAKRGSFGIAEGLADYVKEFCRTDADSYLDALAVHPYC
GTPEAGVAKSAAAKALLRSRNRNCEVWATEIGFQVDDGPGKLNALTRELTGIAGFSLEHQ
RQLLPRLFLLAAQQGIDRVYWYDFFGGNDPETFWLVDENERPRPAYFALKECARRLNGAT
AVDGTSLSSLIQKQLFRNADGSLFLACWALQSGVTADFLLPPGVTLRDDCGNELPLPADR
RLTLGHGVVYVDGFDPAEVPSILERGVLLSSLDQTTFNRPAHRFTVKPGETFEVPLAAFN
SLDRAVTLSPRLERGVPGWRITLPPDFAVDAKAGNTRPVKVKVPADAVPGVEQRLVFGGR
LDGGVREVLPFEVRVEVTGDFPYRAIRAAAARGDAPQWSSFHEDRAGTGNPWLEAAPGIA
LPDGRLDEWSAAEFYPIDQKFQWILRDPGVPDSADWSGRVAFRWDAKNLYVAFLIDDEDL
SCRDFLSRDWRDSDNLRVMLSAVADPARRPKQITETDLLTILTPTGMTGSEPPMVSVAAL
GGLSRPGAEQRIQTAAQLWHGGYALEAVIPFSLIGFTPSSGAVLGLNVMADDVDDGYRQH
VAMTRYENQNYWNSPAATGNLRLR

Enzyme Prediction     

No EC number prediction in MGYG000003249_01654.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
CBM9	663	863	6.5e-18	0.989010989010989

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd09619	CBM9_like_4	2.92e-20	662	855	4	183	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	5.36e-14	663	863	2	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	1.66e-06	789	863	111	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	9.45e-06	682	840	1	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.
cd09621	CBM9_like_5	3.40e-04	662	840	1	166	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 functional domains such as glycosyl hydrolases. The CBM9 module in these architectures may be involved in binding to carbohydrates.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
SDU11835.1	8.58e-232	1	863	1	869
AHF90983.1	2.32e-209	15	863	20	906
AHF92009.1	1.87e-200	49	863	28	866
AIQ58724.1	4.38e-09	278	834	648	1251
QHC72302.1	1.73e-08	195	429	1207	1434

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
0.000508	0.998719	0.000235	0.000171	0.000165	0.000167

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003249_01654.