CAZyme Information: MGYG000002473_00934

Basic Information

• Species: Victivallis vadensis
• Lineage: Bacteria; Verrucomicrobiota; Lentisphaeria; Victivallales; Victivallaceae; Victivallis; Victivallis vadensis
• CAZyme ID: MGYG000002473_00934
• CAZy Family: CBM67
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1142		127947.26	8.4985

Genome Property

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

• Gene Location: Start: 20049; End: 23477 Strand: +

Full Sequence      

MKFSAIAMLLGLACMGMAGAPGWIWYPEKPQDNSVRAFRKTFEVDAPVKSAQLLVLADDG
AEIRVNGQPEKPFPGWLKFNRYDVTKFIRQGKNVIAVRARNGRGEAGLLCRFEIFTAKGV
IEVNTGADWKCSAELPANWEEPAFDDSGWKSAKRFGGANLSPWNKLVDVSPFLVAGAAKP
EPVPPEKKGRLMLDDFSDCSSWMGWLHSGMRPGHNVLPYQLGFGAGPEPSRDDGGSGMID
YDFIRPGGRIFFEKNAVYKSPAVAEAIEFDANPQGYECEVLFELMDRSDKTKFKTLPVKL
SGNAWKRYRLELNAKTVENFDALVFPVSIRGLWFVGGKPGKGRVLLDDLCFVVDQSDGTG
AITVHPEYRGLAHGVNRPVRQEYRIRNNWHRPVENTVSIDVYDIADRKLFSDRRKLKVGA
YGLGRIAFDVGRFPKKGSYRTEVTVRNPLAEQRFTGWFGVFEPNNKRLNTKPMWFGVEDQ
GLRNFRYEEELHIGWMKMLGIDIIRGNAIGRQLEEVPFTDFGYEQYRKMYQPHFDAGIDL
VFSYAGEVPGWTGKKFFASDREAFSRHMTRLAKFMGRNPGIRYFEWFNEPNLGYFRERNT
DEYLASQRIFYPIFKQYAPQVKVATGGVVINHARAKKDFARRMYQENQEFYDVACYHGHE
GYAAHVKSLETLDGWLAEAGVRKPFGNSEAGARSYYTHPDMFRLQAAELVKKITLTKSRN
SEFYIWFMLHDYGDKYINADDSFGLVTVDNQPKPSFLAYNELIRQLADTEPAEPVELDKR
LRNYRFTRGGEEIFVCWPQGSAFSFALRSSAPIVRTDIFGNETVIRPAGGIAFVDSGALP
FYLRAPEGALGAVDAPLQVVGVPVFAPGEMGTVELELVNPYREPFSYTLIAGGSERSGKL
RSGEAVRFRVPAAIPTDAQFGAAPFDCKLRLTGAGGAKLFDGSIALDSFVALPVSEKAGA
KVILDRADQVREMMFDPNSPRWSGPEDLSAEIRLGRRGATLVFDAVVTDDDHSAPGKDAY
VWQNDCIQVGIGTLAGDHYEFTVSGNGKGGATVWNHLRPRDNGNGAAWQVPASVKRQGDR
TFYHFEIPAALVGLKGTAGEVFRIAYLVNDNDKGRHMRFMEWNSGIQPSKNSNLFGWAKI
VR

Enzyme Prediction     

No EC number prediction in MGYG000002473_00934.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
CBM67	23	163	5.1e-33	0.9829545454545454

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd09621	CBM9_like_5	1.62e-57	960	1139	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 functional domains such as glycosyl hydrolases. The CBM9 module in these architectures may be involved in binding to carbohydrates.
pfam08531	Bac_rhamnosid_N	1.04e-11	46	155	1	153	Alpha-L-rhamnosidase N-terminal domain. This family consists of bacterial rhamnosidase A and B enzymes. This domain is probably involved in substrate recognition.
cd00241	DOMON_like	6.96e-07	975	1122	5	158	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	0.002	982	1137	30	180	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.
PRK10340	ebgA	0.002	27	98	102	176	cryptic beta-D-galactosidase subunit alpha; Reviewed

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AVM46501.1	0.0	5	1140	11	1153
AHF92778.1	4.44e-304	11	1140	27	1177
AVM46714.1	6.10e-196	190	1140	26	968
AVM46271.1	2.95e-168	190	1141	22	966
AVM46712.1	2.21e-162	172	1140	60	1011

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6T0Q_A	6.99e-12	23	163	200	344	PleurotusOstreatus Lectin (POL), apo form [Pleurotus ostreatus]
6T1D_A	7.16e-12	23	163	203	347	PleurotusOstreatus Lectin (POL), compelx with melibiose [Pleurotus ostreatus],6T1D_B Pleurotus Ostreatus Lectin (POL), compelx with melibiose [Pleurotus ostreatus],6T1D_C Pleurotus Ostreatus Lectin (POL), compelx with melibiose [Pleurotus ostreatus],6T1D_D Pleurotus Ostreatus Lectin (POL), compelx with melibiose [Pleurotus ostreatus],6T1D_E Pleurotus Ostreatus Lectin (POL), compelx with melibiose [Pleurotus ostreatus],6T1D_F Pleurotus Ostreatus Lectin (POL), compelx with melibiose [Pleurotus ostreatus]
6KBJ_A	8.09e-12	23	163	220	364	Structureof Lectin from Pleurotus ostreatus in complex with malonate [Pleurotus ostreatus],6KBQ_A Crystal Structure of Lectin from Pleurotus ostreatus in complex with Glycerol [Pleurotus ostreatus],6KC2_A Crystal Structure of Lectin from Pleurotus ostreatus in complex with Rhamnose [Pleurotus ostreatus],6LI7_A Crystal Structure of Lectin from Pleurotus ostreatus in complex with GalNAc [Pleurotus ostreatus],6LIK_A Crystal Structure of Lectin from Pleurotus ostreatus in complex with Galactose [Pleurotus ostreatus]

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
0.057395	0.733949	0.207378	0.000491	0.000349	0.000426

TMHMM  Annotations     

start	end
5	27