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CAZyme Information: MGYG000002817_02922

You are here: Home > Sequence: MGYG000002817_02922

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 Paenibacillus_B sp900539405
Lineage Bacteria; Firmicutes; Bacilli; Paenibacillales; Paenibacillaceae; Paenibacillus_B; Paenibacillus_B sp900539405
CAZyme ID MGYG000002817_02922
CAZy Family GH18
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
422 MGYG000002817_14|CGC2 45790.68 6.8859
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000002817 6425839 MAG United States North America
Gene Location Start: 105910;  End: 107178  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000002817_02922.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH18 187 374 7.1e-18 0.5033783783783784

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam07833 Cu_amine_oxidN1 1.62e-31 56 152 1 93
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.
cd02874 GH18_CFLE_spore_hydrolase 2.76e-24 158 404 1 304
Cortical fragment-lytic enzyme (CFLE) is a peptidoglycan hydrolase involved in bacterial endospore germination. CFLE is expressed as an inactive preprotein (called SleB) in the forespore compartment of sporulating cells. SleB translocates across the forespore inner membrane and is deposited as a mature enzyme in the cortex layer of the spore. As part of a sensory mechanism capable of initiating germination, CFLE degrades a spore-specific peptidoglycan constituent called muramic-acid delta-lactam that comprises the outer cortex. CFLE has a C-terminal glycosyl hydrolase family 18 (GH18) catalytic domain as well as two N-terminal LysM peptidoglycan-binding domains. In addition to SleB, this family includes YaaH, YdhD, and YvbX from Bacillus subtilis.
COG3858 YaaH 6.67e-14 151 404 79 409
Spore germination protein YaaH [Cell cycle control, cell division, chromosome partitioning].
cd00598 GH18_chitinase-like 1.45e-10 176 403 21 208
The GH18 (glycosyl hydrolase, family 18) type II chitinases hydrolyze chitin, an abundant polymer of beta-1,4-linked N-acetylglucosamine (GlcNAc) which is a major component of the cell wall of fungi and the exoskeleton of arthropods. Chitinases have been identified in viruses, bacteria, fungi, protozoan parasites, insects, and plants. The structure of the GH18 domain is an eight-stranded beta/alpha barrel with a pronounced active-site cleft at the C-terminal end of the beta-barrel. The GH18 family includes chitotriosidase, chitobiase, hevamine, zymocin-alpha, narbonin, SI-CLP (stabilin-1 interacting chitinase-like protein), IDGF (imaginal disc growth factor), CFLE (cortical fragment-lytic enzyme) spore hydrolase, the type III and type V plant chitinases, the endo-beta-N-acetylglucosaminidases, and the chitolectins. The GH85 (glycosyl hydrolase, family 85) ENGases (endo-beta-N-acetylglucosaminidases) are closely related to the GH18 chitinases and are included in this alignment model.
pfam07833 Cu_amine_oxidN1 1.91e-09 38 84 45 91
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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QDM45581.1 6.95e-283 1 422 1 422
SYX87256.1 1.66e-207 1 421 1 422
QYR22488.1 1.21e-158 4 418 2 418
QUO42548.1 3.35e-156 38 417 31 410
QQE75522.1 3.35e-156 38 417 31 410

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4Q6T_A 3.59e-07 212 372 54 233
Thecrystal structure of a class V chitininase from Pseudomonas fluorescens Pf-5 [Pseudomonas protegens Pf-5]
4S3K_A 1.37e-06 228 394 170 359
ChainA, Spore germination protein YaaH [Priestia megaterium QM B1551]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P37531 1.88e-07 243 374 186 322
Cortical fragment-lytic enzyme OS=Bacillus subtilis (strain 168) OX=224308 GN=sleL PE=1 SV=2

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
0.000257 0.999054 0.000209 0.000175 0.000160 0.000141

TMHMM  Annotations      download full data without filtering help

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