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CAZyme Information: MGYG000000514_00452

You are here: Home > Sequence: MGYG000000514_00452

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 CAG-590 sp900769115
Lineage Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; CAG-590; CAG-590 sp900769115
CAZyme ID MGYG000000514_00452
CAZy Family GH26
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1313 MGYG000000514_5|CGC3 144747.36 4.7879
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000514 3147233 MAG Fiji Oceania
Gene Location Start: 57210;  End: 61151  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000000514_00452.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH26 424 770 4.1e-53 0.900990099009901
CBM23 940 1095 3.8e-29 0.8888888888888888

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam02156 Glyco_hydro_26 6.69e-29 424 713 1 252
Glycosyl hydrolase family 26.
COG4124 ManB2 1.38e-21 582 726 157 296
Beta-mannanase [Carbohydrate transport and metabolism].
pfam13306 LRR_5 5.18e-05 1203 1253 12 53
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 0.003 1202 1253 37 79
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 0.005 1221 1253 1 33
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
QQQ93186.1 5.43e-246 177 1122 187 1115
ASU28432.1 2.23e-245 177 1122 234 1162
ANU75629.1 2.23e-245 177 1122 234 1162
QJU14275.1 1.19e-244 177 1122 187 1115
AEY67866.1 1.69e-226 78 1114 254 1248

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4YN5_A 6.62e-49 423 829 51 433
Catalyticdomain of Bacillus sp. JAMB-750 GH26 Endo-beta-1,4-mannanase [Bacillus sp. JAMB750]
2BVT_A 3.76e-44 421 883 6 415
Thestructure of a modular endo-beta-1,4-mannanase from Cellulomonas fimi explains the product specificity of glycoside hydrolase family 26 mannanases. [Cellulomonas fimi],2BVT_B The structure of a modular endo-beta-1,4-mannanase from Cellulomonas fimi explains the product specificity of glycoside hydrolase family 26 mannanases. [Cellulomonas fimi],2BVY_A The structure and characterization of a modular endo-beta-1,4-mannanase from Cellulomonas fimi [Cellulomonas fimi]
2X2Y_A 1.38e-42 421 883 6 415
Cellulomonasfimi endo-beta-1,4-mannanase double mutant [Cellulomonas fimi],2X2Y_B Cellulomonas fimi endo-beta-1,4-mannanase double mutant [Cellulomonas fimi]
1J9Y_A 1.53e-38 421 821 9 378
Crystalstructure of mannanase 26A from Pseudomonas cellulosa [Cellvibrio japonicus]
1R7O_A 1.89e-38 421 821 19 388
CrystalStructure of apo-mannanase 26A from Psudomonas cellulosa [Cellvibrio japonicus]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
A1A278 3.09e-52 421 1038 40 624
Mannan endo-1,4-beta-mannosidase OS=Bifidobacterium adolescentis (strain ATCC 15703 / DSM 20083 / NCTC 11814 / E194a) OX=367928 GN=BAD_1030 PE=1 SV=1
P49424 1.83e-37 421 821 47 416
Mannan endo-1,4-beta-mannosidase OS=Cellvibrio japonicus (strain Ueda107) OX=498211 GN=manA PE=1 SV=2
P16699 2.55e-16 422 690 33 274
Mannan endo-1,4-beta-mannosidase A and B OS=Caldalkalibacillus mannanilyticus (strain DSM 16130 / CIP 109019 / JCM 10596 / AM-001) OX=1236954 PE=1 SV=1
P49425 6.01e-14 601 726 300 408
Mannan endo-1,4-beta-mannosidase OS=Rhodothermus marinus (strain ATCC 43812 / DSM 4252 / R-10) OX=518766 GN=manA PE=1 SV=3
P55278 6.37e-13 528 690 119 270
Mannan endo-1,4-beta-mannosidase OS=Bacillus subtilis OX=1423 PE=3 SV=1

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
0.001090 0.995241 0.002729 0.000476 0.000245 0.000196

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000514_00452.