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CAZyme Information: KFA56552.1

You are here: Home > Sequence: KFA56552.1

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 Stachybotrys chartarum
Lineage Ascomycota; Sordariomycetes; ; Stachybotryaceae; Stachybotrys; Stachybotrys chartarum
CAZyme ID KFA56552.1
CAZy Family GT90
CAZyme Description unspecified product
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
195 KL650185|CGC7 21752.94 4.6613
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_SchartarumIBT40293 11453 1280524 0 11453
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.78:1

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH134 35 195 3.2e-87 0.9937106918238994

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
381622 mannanase_GH134 6.75e-88 33 195 2 162
glycosyl hydrolase family 134 inverting endo-beta-1,4-mannanase. glycosyl hydrolase family 134 beta-mannanase (E.C. 3.2.1.78) differs from other mannanases in as it has a hen egg white lysozyme fold and cleaves beta-1,4-mannans with inversion of sterochemistry. Beta-mannosidases are enzymes involved in seed germination and the degradation of the hemicellulose fraction of soft- and hardwoods.
381610 chitinase-like 1.24e-04 57 156 1 96
chitinase-like domain. This family includes proteins such as chitinases, chitosanase, pesticin, and endolysin, which are involved in the degradation of 1,4-N-acetyl D-glucosamine linkages in chitin polymers and related activities. Chitinases are enzymes that catalyze the hydrolysis of the beta-1,4-N-acetyl-D-glucosamine linkages in chitin polymers. Chitosanase enzymes hydrolyze chitosan, a biopolymer of beta (1,4)-linked-D-glucosamine (GlcN) residues produced by partial or full deacetylation of chitin. Pesticin (Pst) is a anti-bacterial toxin produced by Yersinia pestis that acts through uptake by the target related bacteria and the hydrolysis of peptidoglycan in the periplasm. The dsDNA phages of eubacteria use endolysins or muralytic enzymes in conjunction with hollin, a small membrane protein, to degrade the peptidoglycan found in bacterial cell walls. Similarly, bacteria produce autolysins to facilitate the biosynthesis of its cell wall heteropolymer peptidoglycan and cell division.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
6.56e-143 1 195 1 195
6.30e-141 1 195 1 195
3.65e-140 1 195 1 195
2.29e-116 1 195 1 196
1.87e-110 1 195 1 194

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1.50e-68 33 195 2 162
Mannanase(RmMan134A) [Rhizopus microsporus],5XTJ_B Mannanase(RmMan134A) [Rhizopus microsporus],5XTT_A Crystal structure of RmMan134A-M3 complex [Rhizopus microsporus],5XTT_B Crystal structure of RmMan134A-M3 complex [Rhizopus microsporus],5XU5_A Complex structure of RmMan134A-M4 [Rhizopus microsporus],5XU5_B Complex structure of RmMan134A-M4 [Rhizopus microsporus],5XUG_A Complex structure(RmMan134A-M5). [Rhizopus microsporus],5XUG_B Complex structure(RmMan134A-M5). [Rhizopus microsporus],5XUL_A Complex structure (RmMan134A-M6). [Rhizopus microsporus],5XUL_B Complex structure (RmMan134A-M6). [Rhizopus microsporus]
9.99e-67 33 195 2 162
beta-1,4-mannanase-SeMet-RmMan134A [Rhizopus microsporus],5XXA_B beta-1,4-mannanase-SeMet-RmMan134A [Rhizopus microsporus]
1.32e-63 35 195 10 168
Structure of a beta-1,4-mannanase, SsGH134, in complex with Man3. [Streptomyces sp. NRRL B-24361]
1.56e-63 35 195 15 173
Structure of a beta-1,4-mannanase, SsGH134. [Streptomyces sp.]
3.78e-63 35 195 10 168
Structure of an inactive (E45Q) variant of a beta-1,4-mannanase, SsGH134, in complex with Man5 [Streptomyces sp. NRRL B-16215]

Swiss-Prot Hits      help

KFA56552.1 has no Swissprot hit.

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI CS Position
0.000280 0.999707 CS pos: 18-19. Pr: 0.9776

TMHMM  Annotations      help

There is no transmembrane helices in KFA56552.1.