CAZyme Information: KFA55153.1

Basic Information

• Species: Stachybotrys chartarum
• Lineage: Ascomycota; Sordariomycetes; ; Stachybotryaceae; Stachybotrys; Stachybotrys chartarum
• CAZyme ID: KFA55153.1
• CAZy Family: GT1
• CAZyme Description: unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
379		41753.74	4.5906

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: location=KL650561:5369-6564(+)

Full Sequence      

MGQQLEELSKIDKRQLNNELIGDLLTLTDDELTPTGAEIKLILTNQVPPQHHNIAYEDPV
PEKDTPACAQDTCCIWWYIAQEMAEAMVGNAPRCNKLARASARLGFHDAGSWSKSTGPTG
GADGSIVFAHECEDRIENNGLQEVCAQMRTWYSKYQSYGVSMADLIQMGANVATVVCPNG
PRIRSFVGRIDNPNPAPTGNLPEITHSVDHLLALFQDKTITPNQLVALVGAHTTAQQRFV
DTTRAGDPLDRTPGVWDGGFYGEVVNPNSPPRVFKFPTDIALSTDPRTSSEWQNFVPRSP
AWNGAYARAYVRVSLLGVYNINDLTECTKVLPFPNSSFFPIPDDVEMEDFLRSAPNQEAS
DALERGDLLPGFEAHHKTE

Enzyme Prediction     

No EC number prediction in KFA55153.1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA2	78	317	1.2e-55	0.9803921568627451

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
173826	ligninase	4.41e-112	73	346	14	309	Ligninase and other manganese-dependent fungal peroxidases. Ligninases and related extracellular fungal peroxidases belong to class II of the plant heme-dependent peroxidase superfamily. All members of the superfamily share a heme prosthetic group and catalyze a multistep oxidative reaction involving hydrogen peroxide as the electron acceptor. Class II peroxidases are fungal glycoproteins that have been implicated in the oxidative breakdown of lignin, the main cell wall component of woody plants. They contain four conserved disulphide bridges and two conserved calcium binding sites.
173823	plant_peroxidase_like	6.04e-36	81	314	1	254	Heme-dependent peroxidases similar to plant peroxidases. Along with animal peroxidases, these enzymes belong to a group of peroxidases containing a heme prosthetic group (ferriprotoporphyrin IX), which catalyzes a multistep oxidative reaction involving hydrogen peroxide as the electron acceptor. The plant peroxidase-like superfamily is found in all three kingdoms of life and carries out a variety of biosynthetic and degradative functions. Several sub-families can be identified. Class I includes intracellular peroxidases present in fungi, plants, archaea and bacteria, called catalase-peroxidases, that can exhibit both catalase and broad-spectrum peroxidase activities depending on the steady-state concentration of hydrogen peroxide. Catalase-peroxidases are typically comprised of two homologous domains that probably arose via a single gene duplication event. Class II includes ligninase and other extracellular fungal peroxidases, while class III is comprised of classic extracellular plant peroxidases, like horseradish peroxidase.
173825	ascorbate_peroxidase	2.10e-25	103	318	35	250	Ascorbate peroxidases and cytochrome C peroxidases. Ascorbate peroxidases are a subgroup of heme-dependent peroxidases of the plant superfamily that share a heme prosthetic group and catalyze a multistep oxidative reaction involving hydrogen peroxide as the electron acceptor. Along with related catalase-peroxidases, ascorbate peroxidases belong to class I of the plant superfamily. Ascorbate peroxidases are found in the chloroplasts and/or cytosol of algae and plants, where they have been shown to control the concentration of lethal hydrogen peroxide molecules. The yeast cytochrome c peroxidase is a divergent member of the family; it forms a complex with cytochrome c to catalyze the reduction of hydrogen peroxide to water.
395089	peroxidase	6.47e-22	103	233	21	150	Peroxidase.
178218	PLN02608	1.02e-16	103	286	36	212	L-ascorbate peroxidase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QLI65955.1|AA2	1.70e-130	4	369	22	386
UNI21317.1|AA2	1.01e-128	9	369	24	384
UQC76336.1|AA2	6.01e-127	9	370	30	399
CCF45286.1|AA2	2.10e-119	17	351	44	383
QRD06638.1|AA2	1.20e-115	4	371	31	400

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3Q3U_A	1.59e-37	73	334	15	291	Trametes cervina lignin peroxidase [Trametopsis cervina]
4BM1_A	4.30e-37	69	334	11	292	CRYSTAL STRUCTURE OF MANGANESE PEROXIDASE 4 FROM PLEUROTUS OSTREATUS - CRYSTAL FORM I [Pleurotus ostreatus],4BM1_B CRYSTAL STRUCTURE OF MANGANESE PEROXIDASE 4 FROM PLEUROTUS OSTREATUS - CRYSTAL FORM I [Pleurotus ostreatus],4BM2_A Crystal Structure Of Manganese Peroxidase 4 From Pleurotus Ostreatus - Crystal Form Ii [Pleurotus ostreatus],4BM3_A Crystal Structure Of Manganese Peroxidase 4 From Pleurotus Ostreatus - Crystal Form Iii [Pleurotus ostreatus],4BM4_A Crystal Structure Of Manganese Peroxidase 4 From Pleurotus Ostreatus - Crystal Form Iv [Pleurotus ostreatus]
7OO5_A	2.76e-34	69	341	11	293	Chain A, lignin peroxidase [Agrocybe pediades]
2VKA_A	7.72e-34	69	334	10	285	Site-Directed Mutagenesis of the Catalytic Tryptophan Environment in Pleurotus eryngii Versatile Peroxidase [Pleurotus eryngii]
5FNE_A	1.03e-33	69	334	10	285	Crystal Structure Of Fungal Versatile Peroxidase From Pleurotus Eryngii Triple Mutant E37k, H39r & G330r [Pleurotus eryngii]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|P11543|LIG5_PHACH	1.57e-32	72	346	40	341	Ligninase LG5 OS=Phanerodontia chrysosporium OX=2822231 GN=GLG5 PE=2 SV=1
sp|Q9UR19|VPL1_PLEER	4.86e-32	69	334	40	315	Versatile peroxidase VPL1 OS=Pleurotus eryngii OX=5323 GN=vpl1 PE=1 SV=1
sp|P20013|LIGC_TRAVE	5.91e-32	69	334	36	321	Ligninase C OS=Trametes versicolor OX=5325 PE=1 SV=2
sp|O94753|VPL2_PLEER	6.73e-32	69	334	40	315	Versatile peroxidase VPL2 OS=Pleurotus eryngii OX=5323 GN=vpl2 PE=1 SV=1
sp|Q02567|PEM1_PHACH	1.26e-31	73	347	35	338	Manganese peroxidase 1 OS=Phanerodontia chrysosporium OX=2822231 GN=MNP1 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000054	0.000000

TMHMM  Annotations     

There is no transmembrane helices in KFA55153.1.