CAZyme Information: SPSK_07949-t39_1-p1

Basic Information

• Species: Sporothrix schenckii
• Lineage: Ascomycota; Sordariomycetes; ; Ophiostomataceae; Sporothrix; Sporothrix schenckii
• CAZyme ID: SPSK_07949-t39_1-p1
• CAZy Family: GH76
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
238		25147.42	6.6027

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_Sschenckii1099-18	10434	1397361	141	10293

• Gene Location: location=AXCR01000004:316789-317505(-)

Full Sequence      

MGPGNGGADGSILLADGELQRRENRGLADIAHLIMSWHSEFGRYSPHPPSVADLIQIGAI
VAAVTCPGGPRIRSFVGRPDFNAGSTPPPPQPPHELIPKPTDDAQTILRKMAAKTFTAVD
LVALLGAHSVSHQYFTDLALAGAPQDTTDGVFDTKFYAETRAPRAPLGVYRIASDVAVAR
DPATHALWRTYSGADAATQDRWTAAYASAYVRLSLLGVADLNALTDCSGVLPQAKALP

Enzyme Prediction     

No EC number prediction in SPSK_07949-t39_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA2	4	218	9.6e-42	0.8352941176470589

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
173826	ligninase	9.99e-66	4	237	62	293	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	2.18e-21	2	214	36	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	3.18e-20	4	145	28	176	Peroxidase.
173827	secretory_peroxidase	1.26e-14	50	218	95	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.
173825	ascorbate_peroxidase	4.46e-11	4	218	49	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QLI65955.1|AA2	1.18e-54	5	232	136	351
AEO59029.1|AA2	2.44e-54	4	232	144	359
UQC76336.1|AA2	2.02e-52	4	235	144	364
UNI21317.1|AA2	3.70e-52	6	232	135	349
CAE7175176.1|AA2	5.25e-52	6	235	145	361

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4BLK_A	1.41e-31	4	237	58	289	CRYSTAL STRUCTURE OF FUNGAL VERSATILE PEROXIDASE I FROM PLEUROTUS OSTREATUS - CRYSTAL FORM I [Pleurotus ostreatus],4BLL_A CRYSTAL STRUCTURE OF FUNGAL VERSATILE PEROXIDASE I FROM PLEUROTUS OSTREATUS - CRYSTAL FORM II [Pleurotus ostreatus],4BLN_A CRYSTAL STRUCTURE OF FUNGAL VERSATILE PEROXIDASE I FROM PLEUROTUS OSTREATUS - CRYSTAL FORM III [Pleurotus ostreatus],4BLX_A CRYSTAL STRUCTURE OF FUNGAL VERSATILE PEROXIDASE I FROM PLEUROTUS OSTREATUS - CRYSTAL FORM IV [Pleurotus ostreatus],4BLY_A Crystal Structure Of Fungal Versatile Peroxidase I From Pleurotus Ostreatus - Crystal Form V [Pleurotus ostreatus],4BLZ_A Crystal Structure Of Fungal Versatile Peroxidase I From Pleurotus Ostreatus - Crystal Form Vi [Pleurotus ostreatus],4BLZ_B Crystal Structure Of Fungal Versatile Peroxidase I From Pleurotus Ostreatus - Crystal Form Vi [Pleurotus ostreatus],4BM0_A Crystal Structure Of Fungal Versatile Peroxidase I From Pleurotus Ostreatus - Crystal Form Vii [Pleurotus ostreatus]
2VKA_A	4.08e-31	4	237	57	288	Site-Directed Mutagenesis of the Catalytic Tryptophan Environment in Pleurotus eryngii Versatile Peroxidase [Pleurotus eryngii]
3FMU_A	5.29e-31	4	237	57	288	Chain A, Versatile peroxidase VPL2 [Pleurotus eryngii]
2W23_A	1.09e-30	4	237	57	288	Structure of mutant W169Y of Pleurotus eryngii versatile peroxidase (VP) [Pleurotus eryngii]
3FM4_A	1.44e-30	4	237	57	288	Chain A, Versatile peroxidase VPL2 [Pleurotus eryngii]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|C0IW58|LNP_TAICA	2.57e-31	4	232	66	290	Low-redox potential peroxidase OS=Taiwanofungus camphoratus OX=2696576 GN=LnP PE=1 SV=1
sp|Q9UR19|VPL1_PLEER	1.24e-29	4	237	87	318	Versatile peroxidase VPL1 OS=Pleurotus eryngii OX=5323 GN=vpl1 PE=1 SV=1
sp|O94753|VPL2_PLEER	1.72e-29	4	237	87	318	Versatile peroxidase VPL2 OS=Pleurotus eryngii OX=5323 GN=vpl2 PE=1 SV=1
sp|P28314|PER_COPCI	1.31e-26	4	234	91	319	Peroxidase OS=Coprinopsis cinerea OX=5346 GN=CIP1 PE=1 SV=2
sp|P28313|PER_ARTRA	1.84e-26	4	234	92	320	Peroxidase OS=Arthromyces ramosus OX=5451 PE=1 SV=3

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
0.999957	0.000099

TMHMM  Annotations     

There is no transmembrane helices in SPSK_07949-t39_1-p1.