CAZyme Information: KFA53786.1

Basic Information

• Species: Stachybotrys chartarum
• Lineage: Ascomycota; Sordariomycetes; ; Stachybotryaceae; Stachybotrys; Stachybotrys chartarum
• CAZyme ID: KFA53786.1
• CAZy Family: GH47
• CAZyme Description: unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
396	KL650837|CGC2	42838.37	4.2686

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=KL650837:363899-365139(-)

Full Sequence      

MRSLTILVVALASLDLTLAYPGMGAKLEEMKKLRSRQSSEMIGDLETLDDSELTPTGRAI
KDILLGDALAEDLVNITLIVPPRDSAACAQDTCCIWKHIADDMRDAMIGSALRCNDAARQ
AIRLGFHDAGTWSRSTGSGGGADGSIVLTDECEDRAENNGLEEICAQMRIWHAEYQSYGV
SMADLIQMAANVATVTCPLGPRVRTFVGRVDNSSPAPAGLLPSPFDSVDDLLDLFADKTI
DAEDLVALVGAHSTSQQRFVDPSRAGDPQDKTPGVWDVQFYAETTSANSPQRIFKFQSDV
LLSQDSRTAPTWQQFSGQLQGQIPWNLAYARAYVRLSLLGVYNINDLTECTSVLPPIVVG
TFLNPDQLLLNAFLNGPRNTAASDALFNGDLLSLLP

Enzyme Prediction     

No EC number prediction in KFA53786.1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA2	96	340	1.6e-62	0.9882352941176471

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
173826	ligninase	1.24e-129	82	356	4	289	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	6.71e-35	122	337	22	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.
395089	peroxidase	3.98e-24	122	316	20	185	Peroxidase.
173825	ascorbate_peroxidase	4.28e-20	122	341	34	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.
173827	secretory_peroxidase	9.16e-19	95	341	22	283	Horseradish peroxidase and related secretory plant peroxidases. Secretory peroxidases belong to class III 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 III peroxidases are found in the extracellular space or in the vacuole in plants where they have been implicated in hydrogen peroxide detoxification, auxin catabolism and lignin biosynthesis, and stress response. Class III peroxidases contain four conserved disulphide bridges and two conserved calcium binding sites.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
UNI21317.1|AA2	1.48e-152	19	376	15	369
QLI65955.1|AA2	1.77e-149	9	392	6	386
UQC76336.1|AA2	3.00e-139	1	390	1	396
CAE7175176.1|AA2	3.11e-133	11	376	12	378
CCF45286.1|AA2	1.34e-132	5	395	4	405

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4BM1_A	4.82e-45	89	355	11	290	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]
2VKA_A	2.48e-41	84	360	5	290	Site-Directed Mutagenesis of the Catalytic Tryptophan Environment in Pleurotus eryngii Versatile Peroxidase [Pleurotus eryngii]
5FNB_A	3.44e-41	84	360	5	290	Crystal Structure Of Fungal Versatile Peroxidase From Pleurotus Eryngii Septuple Mutant E37k, H39r, V160a, T184m, Q202l, D213a & G330r [Pleurotus eryngii],5FNB_B Crystal Structure Of Fungal Versatile Peroxidase From Pleurotus Eryngii Septuple Mutant E37k, H39r, V160a, T184m, Q202l, D213a & G330r [Pleurotus eryngii]
5FNE_A	4.81e-41	84	360	5	290	Crystal Structure Of Fungal Versatile Peroxidase From Pleurotus Eryngii Triple Mutant E37k, H39r & G330r [Pleurotus eryngii]
3FMU_A	6.71e-41	84	360	5	290	Chain A, Versatile peroxidase VPL2 [Pleurotus eryngii]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q9UR19|VPL1_PLEER	2.54e-39	84	360	35	320	Versatile peroxidase VPL1 OS=Pleurotus eryngii OX=5323 GN=vpl1 PE=1 SV=1
sp|O94753|VPL2_PLEER	2.54e-39	84	360	35	320	Versatile peroxidase VPL2 OS=Pleurotus eryngii OX=5323 GN=vpl2 PE=1 SV=1
sp|P28314|PER_COPCI	1.93e-38	93	358	42	320	Peroxidase OS=Coprinopsis cinerea OX=5346 GN=CIP1 PE=1 SV=2
sp|P28313|PER_ARTRA	1.97e-38	93	358	43	321	Peroxidase OS=Arthromyces ramosus OX=5451 PE=1 SV=3
sp|A8NK72|PER_COPC7	5.21e-38	93	358	42	320	Peroxidase OS=Coprinopsis cinerea (strain Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003) OX=240176 GN=CIP1 PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000198	0.999757	CS pos: 19-20. Pr: 0.9806

TMHMM  Annotations     

There is no transmembrane helices in KFA53786.1.