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CAZyme Information: MGYG000001770_00932

You are here: Home > Sequence: MGYG000001770_00932

Basic Information | Genomic context | Full Sequence | Enzyme annotations |  CAZy signature domains |  CDD domains | CAZyme hits | PDB hits | Swiss-Prot hits | SignalP and Lipop annotations | TMHMM annotations

Basic Information help

Species Prevotella sp900313215
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotella; Prevotella sp900313215
CAZyme ID MGYG000001770_00932
CAZy Family GH87
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1347 MGYG000001770_18|CGC1 146531.67 4.6053
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001770 3003526 MAG Denmark Europe
Gene Location Start: 11520;  End: 15563  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.59

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH87 44 602 8e-155 0.8458961474036851

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd14490 CBM6-CBM35-CBM36_like_1 1.02e-40 45 209 1 156
uncharacterized members of the carbohydrate binding module 6 (CBM6) and CBM35_like superfamily. Carbohydrate binding module family 6 (CBM6, family 6 CBM), also known as cellulose binding domain family VI (CBD VI), and related CBMs (CBM35 and CBM36). These are non-catalytic carbohydrate binding domains found in a range of enzymes that display activities against a diverse range of carbohydrate targets, including mannan, xylan, beta-glucans, cellulose, agarose, and arabinans. These domains facilitate the strong binding of the appended catalytic modules to their dedicated, insoluble substrates. Many of these CBMs are associated with glycoside hydrolase (GH) domains. 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. CBM36s are calcium-dependent xylan binding domains. CBM35s display conserved specificity through extensive sequence similarity, but divergent function through their appended catalytic modules.
pfam13306 LRR_5 9.05e-21 1008 1120 4 114
Leucine rich repeats (6 copies). This family includes a number of leucine rich repeats. This family contains a large number of BSPA-like surface antigens from Trichomonas vaginalis.
pfam13306 LRR_5 1.12e-20 1008 1108 26 127
Leucine rich repeats (6 copies). This family includes a number of leucine rich repeats. This family contains a large number of BSPA-like surface antigens from Trichomonas vaginalis.
sd00036 LRR_3 1.08e-19 1008 1120 6 119
leucine-rich repeats. A leucine-rich repeat (LRR) is a structural protein motif of 20-30 amino acids that is unusually rich in the hydrophobic amino acid leucine. The conserved eleven-residue sequence motif (LxxLxLxxN/CxL) within the LRRs corresponds to the beta-strand and adjacent loop regions, whereas the remaining parts of the repeats are variable. LRRs fold together to form a solenoid protein domain, termed leucine-rich repeat domain. Leucine-rich repeats are usually involved in protein-protein interactions.
sd00036 LRR_3 6.83e-19 1011 1112 32 136
leucine-rich repeats. A leucine-rich repeat (LRR) is a structural protein motif of 20-30 amino acids that is unusually rich in the hydrophobic amino acid leucine. The conserved eleven-residue sequence motif (LxxLxLxxN/CxL) within the LRRs corresponds to the beta-strand and adjacent loop regions, whereas the remaining parts of the repeats are variable. LRRs fold together to form a solenoid protein domain, termed leucine-rich repeat domain. Leucine-rich repeats are usually involved in protein-protein interactions.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QUB45559.1 0.0 11 993 8 964
ANR73273.1 0.0 11 993 7 963
BBA29482.1 0.0 11 954 7 939
AUI55285.1 0.0 11 993 8 964
QUB58650.1 0.0 11 984 8 955

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5ZRU_A 1.31e-157 45 561 13 527
ChainA, Alpha-1,3-glucanase [Niallia circulans],5ZRU_C Chain C, Alpha-1,3-glucanase [Niallia circulans]
7C7D_A 8.27e-32 44 543 53 507
Crystalstructure of the catalytic unit of thermostable GH87 alpha-1,3-glucanase from Streptomyces thermodiastaticus strain HF3-3 [Streptomyces thermodiastaticus],7C7D_B Crystal structure of the catalytic unit of thermostable GH87 alpha-1,3-glucanase from Streptomyces thermodiastaticus strain HF3-3 [Streptomyces thermodiastaticus]
6K0M_A 4.29e-20 45 487 14 423
Catalyticdomain of GH87 alpha-1,3-glucanase from Paenibacillus glycanilyticus FH11 [Paenibacillus glycanilyticus],6K0N_A Catalytic domain of GH87 alpha-1,3-glucanase in complex with nigerose [Paenibacillus glycanilyticus]
6K0P_A 4.03e-19 45 487 14 423
Catalyticdomain of GH87 alpha-1,3-glucanase D1045A in complex with nigerose [Paenibacillus glycanilyticus]
6K0S_A 4.03e-19 45 487 14 423
Catalyticdomain of GH87 alpha-1,3-glucanase D1069A in complex with nigerose [Paenibacillus glycanilyticus],6K0V_A Catalytic domain of GH87 alpha-1,3-glucanase D1069A in complex with tetrasaccharides [Paenibacillus glycanilyticus],6K0V_B Catalytic domain of GH87 alpha-1,3-glucanase D1069A in complex with tetrasaccharides [Paenibacillus glycanilyticus],6K0V_C Catalytic domain of GH87 alpha-1,3-glucanase D1069A in complex with tetrasaccharides [Paenibacillus glycanilyticus],6K0V_D Catalytic domain of GH87 alpha-1,3-glucanase D1069A in complex with tetrasaccharides [Paenibacillus glycanilyticus]

Swiss-Prot Hits      help

has no Swissprot hit.

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
0.000341 0.998868 0.000246 0.000186 0.000179 0.000158

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001770_00932.