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CAZyme Information: MGYG000004157_01662

You are here: Home > Sequence: MGYG000004157_01662

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 HGM11514 sp900757255
Lineage Bacteria; Firmicutes_A; Clostridia; HGM11514; HGM11514; HGM11514; HGM11514 sp900757255
CAZyme ID MGYG000004157_01662
CAZy Family GH16
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1731 186823.76 4.3168
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000004157 2480742 MAG United Kingdom Europe
Gene Location Start: 2339;  End: 7534  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000004157_01662.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH16 1040 1264 2.3e-17 0.8521739130434782

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
NF033190 inl_like_NEAT_1 1.17e-20 1554 1721 580 743
NEAT domain-containing leucine-rich repeat protein. Members of this family have an N-terminal NEAT (near transporter) domain often associated with iron transport, followed by a leucine-rich repeat region with significant sequence similarity to the internalins of Listeria monocytogenes. However, since Bacillus cereus (from which this protein was described, in PMID:16978259) is not considered an intracellular pathogen, and the function may be iron transport rather than internalization, applying the name "internalin" to this family probably would be misleading.
cd08023 GH16_laminarinase_like 1.16e-17 1004 1264 1 235
Laminarinase, member of the glycosyl hydrolase family 16. Laminarinase, also known as glucan endo-1,3-beta-D-glucosidase, is a glycosyl hydrolase family 16 member that hydrolyzes 1,3-beta-D-glucosidic linkages in 1,3-beta-D-glucans such as laminarins, curdlans, paramylons, and pachymans, with very limited action on mixed-link (1,3-1,4-)-beta-D-glucans.
cd02178 GH16_beta_agarase 1.77e-15 1006 1264 27 257
Beta-agarase, member of glycosyl hydrolase family 16. Beta-agarase is a glycosyl hydrolase family 16 (GH16) member that hydrolyzes the internal beta-1,4-linkage of agarose, a hydrophilic polysaccharide found in the cell wall of Rhodophyceaea, marine red algae. Agarose is a linear chain of galactose units linked by alternating L-alpha-1,3- and D-beta-1,4-linkages that are additionally modified by a 3,6-anhydro-bridge. Agarose forms thermo-reversible gels that are widely used in the food industry or as a laboratory medium. While beta-agarases are also found in two other families derived from the sequence-based classification of glycosyl hydrolases (GH50, and GH86) the GH16 members are most abundant. This domain adopts a curved beta-sandwich conformation, with a tunnel-shaped active site cavity, referred to as a jellyroll fold.
cd00413 Glyco_hydrolase_16 6.85e-13 1006 1264 1 210
glycosyl hydrolase family 16. The O-Glycosyl hydrolases are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. A glycosyl hydrolase classification system based on sequence similarity has led to the definition of more than 95 different families inlcuding glycosyl hydrolase family 16. Family 16 includes lichenase, xyloglucan endotransglycosylase (XET), beta-agarase, kappa-carrageenase, endo-beta-1,3-glucanase, endo-beta-1,3-1,4-glucanase, and endo-beta-galactosidase, all of which have a conserved jelly roll fold with a deep active site channel harboring the catalytic residues.
NF033190 inl_like_NEAT_1 4.15e-12 1553 1663 640 751
NEAT domain-containing leucine-rich repeat protein. Members of this family have an N-terminal NEAT (near transporter) domain often associated with iron transport, followed by a leucine-rich repeat region with significant sequence similarity to the internalins of Listeria monocytogenes. However, since Bacillus cereus (from which this protein was described, in PMID:16978259) is not considered an intracellular pathogen, and the function may be iron transport rather than internalization, applying the name "internalin" to this family probably would be misleading.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QUI25357.1 7.09e-108 672 1269 662 1285
QHI71623.1 7.00e-69 871 1267 34 410
QKS72634.1 8.60e-31 1555 1730 2061 2236
AFK87257.1 6.30e-30 1555 1730 968 1142
AZK45712.1 1.41e-29 1548 1730 559 742

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4AQ1_A 1.45e-12 1555 1730 3 168
Structureof the SbsB S-layer protein of Geobacillus stearothermophilus PV72p2 in complex with nanobody KB6 [Geobacillus stearothermophilus]
4AQ1_C 1.45e-12 1555 1730 3 168
Structureof the SbsB S-layer protein of Geobacillus stearothermophilus PV72p2 in complex with nanobody KB6 [Geobacillus stearothermophilus]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P38535 1.80e-29 1546 1731 897 1082
Exoglucanase XynX OS=Acetivibrio thermocellus OX=1515 GN=xynX PE=3 SV=1
P38536 4.01e-28 1556 1731 1682 1856
Amylopullulanase OS=Thermoanaerobacterium thermosulfurigenes OX=33950 GN=amyB PE=3 SV=2
P19424 1.66e-23 1541 1730 23 214
Endoglucanase OS=Bacillus sp. (strain KSM-635) OX=1415 PE=1 SV=1
C6CRV0 1.00e-17 1563 1729 1291 1458
Endo-1,4-beta-xylanase A OS=Paenibacillus sp. (strain JDR-2) OX=324057 GN=xynA1 PE=1 SV=1
P36917 1.54e-17 1546 1658 1045 1157
Endo-1,4-beta-xylanase A OS=Thermoanaerobacterium saccharolyticum OX=28896 GN=xynA PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
0.647563 0.345090 0.003676 0.000782 0.000572 0.002325

TMHMM  Annotations      download full data without filtering help

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