Species | UMGS755 sp900545185 | |||||||||||
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Lineage | Bacteria; Firmicutes_A; Clostridia; Monoglobales_A; UBA9506; UMGS755; UMGS755 sp900545185 | |||||||||||
CAZyme ID | MGYG000004064_01820 | |||||||||||
CAZy Family | PL21 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 16566; End: 21365 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
PL21 | 554 | 632 | 9.9e-17 | 0.9305555555555556 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
pfam07833 | Cu_amine_oxidN1 | 8.89e-11 | 968 | 1058 | 1 | 92 | Copper amine oxidase N-terminal domain. Copper amine oxidases catalyze the oxidative deamination of primary amines to the corresponding aldehydes, while reducing molecular oxygen to hydrogen peroxide. These enzymes are dimers of identical subunits, each comprising four domains. The N-terminal domain, which is absent in some amine oxidases, consists of a five-stranded antiparallel beta sheet twisted around an alpha helix. The D1 domains from the two subunits comprise the 'stalk' of the mushroom-shaped dimer, and interact with each other but do not pack tightly against each other. |
pfam00754 | F5_F8_type_C | 7.41e-09 | 1086 | 1202 | 2 | 125 | F5/8 type C domain. This domain is also known as the discoidin (DS) domain family. |
pfam18675 | HepII_C | 1.79e-08 | 845 | 929 | 3 | 88 | Heparinase II C-terminal domain. Heparinase II (HepII) is an 85-kDa dimeric enzyme that depolymerizes both heparin and heparan sulfate glycosaminoglycans. The protein is composed of three domains: an N-terminal alpha-helical domain, a central two-layered beta-sheet domain, and a C-terminal domain forming a two-layered beta-sheet. The C-terminal domain contains nine beta-strands packed together in a manner resembling a beta-barrel. |
cd00057 | FA58C | 6.31e-05 | 1078 | 1195 | 7 | 134 | Substituted updates: Jan 31, 2002 |
cd04080 | CBM6_cellulase-like | 9.88e-05 | 48 | 160 | 38 | 144 | Carbohydrate Binding Module 6 (CBM6); appended to glycoside hydrolase (GH) domains, including GH5 (cellulase). This family includes carbohydrate binding module 6 (CBM6) domains that are appended to several glycoside hydrolase (GH) domains, including GH5 (cellulase) and GH16, as well as to coagulation factor 5/8 carbohydrate-binding domains. CBM6s are non-catalytic carbohydrate binding domains that facilitate the strong binding of the GH catalytic modules with their dedicated, insoluble substrates. The CBM6s are appended to GHs that display a diversity of substrate specificities. For some members of this family information is available about the specific substrates of the appended GH domains. It includes the CBM domains of various enzymes involved in cell wall degradation including, an extracellular beta-1,3-glucanase from Lysobacter enzymogenes encoded by the gluC gene (its catalytic domain belongs to the GH16 family), the tandem CBM domains of Pseudomonas sp. PE2 beta-1,3(4)-glucanase A (its catalytic domain also belongs to GH16), and a family 6 CBM from Cellvibrio mixtus Endoglucanase 5A (CmCBM6) which binds to the beta1,4-beta1,3-mixed linked glucans lichenan, and barley beta-glucan, cello-oligosaccharides, insoluble forms of cellulose, the beta1,3-glucan laminarin, and xylooligosaccharides, and the CBM6 of Fibrobacter succinogenes S85 XynD xylanase, appended to a GH10 domain, and Cellvibrio japonicas Cel5G appended to a GH5 (cellulase) domain. GH5 (cellulase) family includes enzymes with several known activities such as endoglucanase, beta-mannanase, and xylanase, which are involved in the degradation of cellulose and xylans. GH16 family includes enzymes with lichenase, xyloglucan endotransglycosylase (XET), and beta-agarase activities. CBM6 is an unusual CBM as it represents a chimera of two distinct binding sites with different modes of binding: binding site I within the loop regions and binding site II on the concave face of the beta-sandwich fold. For CmCBM6 it has been shown that these two binding sites have different ligand specificities. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
BBH20141.1 | 1.82e-155 | 186 | 1205 | 231 | 1225 |
QOU74174.1 | 7.48e-140 | 55 | 930 | 58 | 941 |
AYM77060.1 | 1.92e-138 | 55 | 930 | 58 | 941 |
QHW00380.1 | 7.53e-138 | 172 | 929 | 53 | 800 |
QDG70382.1 | 2.84e-137 | 55 | 930 | 78 | 961 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
2FUQ_A | 3.64e-133 | 190 | 929 | 19 | 747 | ChainA, heparinase II protein [Pedobacter heparinus],2FUQ_B Chain B, heparinase II protein [Pedobacter heparinus] |
3E80_A | 3.85e-133 | 190 | 929 | 21 | 749 | Structureof Heparinase II complexed with heparan sulfate degradation disaccharide product [Pedobacter heparinus],3E80_B Structure of Heparinase II complexed with heparan sulfate degradation disaccharide product [Pedobacter heparinus],3E80_C Structure of Heparinase II complexed with heparan sulfate degradation disaccharide product [Pedobacter heparinus] |
3E7J_A | 9.51e-131 | 190 | 929 | 21 | 749 | ChainA, Heparinase II protein [Pedobacter heparinus],3E7J_B Chain B, Heparinase II protein [Pedobacter heparinus] |
2FUT_A | 5.93e-128 | 190 | 929 | 20 | 748 | ChainA, heparinase II protein [Pedobacter heparinus],2FUT_B Chain B, heparinase II protein [Pedobacter heparinus] |
7D29_A | 9.75e-17 | 1100 | 1216 | 26 | 139 | CBM32of AlyQ [Persicobacter sp. CCB-QB2],7D2A_A CBM32 of AlyQ in complex with 4,5-unsaturated mannuronic acid [Persicobacter sp. CCB-QB2] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
C6XZB6 | 4.01e-132 | 190 | 929 | 44 | 772 | Heparin and heparin-sulfate lyase OS=Pedobacter heparinus (strain ATCC 13125 / DSM 2366 / CIP 104194 / JCM 7457 / NBRC 12017 / NCIMB 9290 / NRRL B-14731 / HIM 762-3) OX=485917 GN=hepB PE=1 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.000296 | 0.999113 | 0.000185 | 0.000141 | 0.000130 | 0.000132 |
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