CAZyme Information: MGYG000002407_00474

Basic Information

• Species: Cohnella sp900169535
• Lineage: Bacteria; Firmicutes; Bacilli; Paenibacillales; Paenibacillaceae; Cohnella; Cohnella sp900169535
• CAZyme ID: MGYG000002407_00474
• CAZy Family: CBM9
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
2133	MGYG000002407_13|CGC1	230716.46	4.4245

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002407	6325359	Isolate	not provided	not provided

• Gene Location: Start: 108295; End: 114696 Strand: -

Full Sequence      

MRRKTAMRVAAWALAIVTALGGLPLPGASTAPAAAASETWFEDDFDSPALAQERWKEVPG
QWDVKTEDGVSFFHGFHANTRTFLRLEEAAGWTDYEVNVRARFAANVTGRAEFFVRADDS
GNFYSVEAQLTQDGASAATFKIHRWAGTVYQGNLTANVTHAYDPTQWHDYTVTVEGSTIS
LRLDGEPIISATDPNSHYPSGGIGFRSQNVGLQIDRVAVSGEGGRAQELQIHHSPITEAD
TGQGIDISADIVGPASVTATVYYRYGHADEGRIFESASMSKGSGDSHSVRLPAPPSGDED
TLNYYIEASDAAGSRKSTGYADDFADAARTAEHWTKTPEEWIVADDGDERVMKATAGNTR
NYLTGAGSETWTDYDVEFRAKFARKANGRGEFFVRANDQGDYYAVEAQTSEGTNDVLLKI
HYWDNTVYQQNLTANVNATFDASAWNDYRIEVRGNRITFYVNGTGLISATDSNNRYPSGG
IGFRSNNVDLEIADLTVSHPVKLIASGPLAVEHSPVASVPYNADIPVAFTVRGDAGSAVT
AAVRYRYGDEPEREVAAARGTDGIYRATIPGTNRSSAVGYHIAVRDEAGNAARYPASGDA
SVAVGAFEPYANDFESLAVGSVPAGWTVRGDAKIAALPEGGKALRLNGRVGTVYPSATLS
NPAYGSIDNFILKFRAKYVRTSDEYYNVWRLRYRTQNDNNNYSMEWGTHNWRYFIMRKTD
LGGNYYLGTYNEALDNRWVDYEIRASGITHELYIDGEKVIGVDDFDTLRMDKGYIQFGTV
NGIELLIDSFEIVPLEPEPIYNVEPAGNYTGIYGPGEAPGLNVFVSGGAEAHTYKVAYKV
RRADGERELVASGEREYELAAYGELNEELTFEPGIGDIGTYDVEVELYVDGVRSDASTKT
MRMAVVREIPETPEIDADIESKFGFNTHYKENWRDDIMDAVRKTGARHHRSTLNIADSFT
GQYGADGKPVFDFAKTDAYLNKIASFGLNSIPVFGVIEDTATAASYEGLRLLERFAYESA
NRYRGLIRTFETSNEPELFVDPYIPYEIVQQWKRLYLGTKKANPGSALIAGGHTSSVRSV
LPRELELGAYNFADAFSWHPYVYNAMPDGAIESFVDDIGGMIDAYGGWKDFYLTEGGWPT
AKGGYPNVSEEVQRDYIARAFLIYMTEPKVRAWEYYNFKNDGTDENYYEIFWGITDVDGR
PKLAYGAVNNLMTTLAGAAYAGRLEVPDGKVRAYVFLKDGKPIIAAWRSVDHKDDPASNP
ATSQLAIDVGTDEVVVRSIEGRDRTVAATNGQAEVTVSGSPIFILNASADALYEAAIALQ
GDYREDAAGKIAKLETADNAAAVAELLGRLEGIGQRLETAMREPALADKAAGLEQGIGSL
YGLMSDMASAIEAGQAERKQAFVVMEALYYYAEAAAQALIQAKSEQGAGAGAGSAVPDYA
AAVAAARSALEARAGDDYVLPVGNAAVMRAERYGRLAENNRERGADAASYAYGLLAREFA
AVALRMTAADAPVYVGAWLNVTPVKRNAEAGYASELAGTVANDTAESVSAAVRIVPPEGW
GEAETLTATIAPGGTYRFEHTLAIPADAPEGVYEPKVELVVGGAVVDEAAIELTVESAIA
AGILPVGKPIAELDEIQVRLQGRSAAPKSGKVTVYGPDGEPLAPVSGDTFADLGKDETVT
LAFRWDYREARDFNEYSNRITVTESASGRVIFDDAQVPLDFLLIEKTGTVAVDGRLDDWT
AAYPVHLRGAGRNNTGVYDPGNLDATAYAMWDDGHLYLAAKVSDDIHKNSEDAANMWKND
SLQFAIDPLADSPAAYNQDDMEWGFARHDDGRLLANIFFSRPPNPNGSAGELLPFAIARD
EEAKETTYEIKIPRGLIHGLALAEGTKLGMNYAVNDADFQMGRDNFIQWTRGLADGKNPG
GYDRFALADTAEDPDPVSGTSIALAADKPIVEVGEKVAVTVAAEEADDLYAVELTFRYDP
SLFRLNRAELAEAFAPGGDGYLRYEDDGGTVRVAASRTGAVPGAFGSADLIRLEFAALSE
DGAADFAVPGPVAVSNSGGQAAVVPQGGELRVAVADTAAVTGGKPNPKAIETIARSFGKR
EGETGYKAVYDMNKDGIIDIIDLAYVASRYLRS

Enzyme Prediction     

No EC number prediction in MGYG000002407_00474.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
CBM9	1732	1911	1.2e-24	0.9010989010989011

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd09621	CBM9_like_5	2.44e-36	1733	1922	2	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 functional domains such as glycosyl hydrolases. The CBM9 module in these architectures may be involved in binding to carbohydrates.
cd09619	CBM9_like_4	5.42e-16	1729	1923	1	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.
cd08547	Type_II_cohesin	7.25e-16	1941	2076	2	136	Type II cohesin domain, interaction partner of dockerin. Bacterial cohesin domains bind to a complementary protein domain named dockerin, and this interaction is required for the formation of the cellulosome, a cellulose-degrading complex. The cellulosome consists of scaffoldin, a noncatalytic scaffolding polypeptide, that comprises repeating cohesion modules and a single carbohydrate-binding module (CBM). Specific calcium-dependent interactions between cohesins and dockerins appear to be essential for cellulosome assembly. This subfamily represents type II cohesins; their interactions with dockerin mediate attachment of the cellulosome complex to the bacterial cell wall.
pfam06452	CBM9_1	5.74e-12	1732	1910	1	163	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.
cd00241	DOMON_like	5.32e-11	1756	1898	11	148	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
QTH41073.1	0.0	370	1929	86	1636
CQR57727.1	0.0	341	1929	53	1636
ACZ43011.1	3.75e-77	968	1927	345	1274
QUL56627.1	5.05e-64	869	1933	339	1371
AIQ40299.1	4.89e-61	873	1933	343	1371

PDB Hits     

has no PDB hit.

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P38535	1.44e-07	1693	1909	686	875	Exoglucanase XynX OS=Acetivibrio thermocellus OX=1515 GN=xynX PE=3 SV=1
P36917	1.66e-06	1693	1909	834	1023	Endo-1,4-beta-xylanase A OS=Thermoanaerobacterium saccharolyticum OX=28896 GN=xynA PE=1 SV=1

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
0.003408	0.991004	0.002754	0.002203	0.000316	0.000276

TMHMM  Annotations     

start	end
9	31