CAZyme Information: SPSK_01702-t39_1-p1

Basic Information

• Species: Sporothrix schenckii
• Lineage: Ascomycota; Sordariomycetes; ; Ophiostomataceae; Sporothrix; Sporothrix schenckii
• CAZyme ID: SPSK_01702-t39_1-p1
• CAZy Family: AA9
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
496	AXCR01000005|CGC4	51372.11	6.9337

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=AXCR01000005:1913227-1914717(-)

Full Sequence      

MHASLFLVALAAVAGPVAAWPGMGPGGHGAAAGHAHHARFHHSDMYKEIRRAAADAETKN
AAKTVAVAANNGDDHHEQHKRSVEMLGDLVYLPDDSLSASGKEIKLILAGKMSPHAPLPV
NKRESAPEHKQVRRNNPCRPQAPSSTAKSESAPASSSSSSAVPASSEPVSSAPVSSQPVS
SPPASSTPVSSAPASSAPASSAPVSSAPLSSALSESSSTQSSSTQSTASPSPIPSPASCD
VWSQVAKAIVPTFQDGKNGCSRLARGAIRLGFHDAGAWNRTSAWGGADGSIALNPSELAR
AENRGLQDIVAQTLVWYDAWHSRGVGMADLIQFSAIVATVTCPLGPRIKFFAGRPDDARA
APDGLLPSVDGTAPALIDLFQAKTFSPADLVALLGAHSTSQQFFADPAQAGAPQDSTPGV
WDTKFYAETAARTAPKGVYRFPSDVALATYQGTSATWQHMSSQFAWDGAYANAYFRLSLL
GVNNINDLVDCSESVP

Enzyme Prediction     

No EC number prediction in SPSK_01702-t39_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA2	244	482	3e-55	0.984313725490196

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
173826	ligninase	1.49e-90	239	496	14	288	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	2.69e-27	248	478	2	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	6.91e-23	262	398	14	150	Peroxidase.
173825	ascorbate_peroxidase	2.79e-20	268	483	34	251	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.
178218	PLN02608	7.59e-16	268	447	35	208	L-ascorbate peroxidase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CCF45286.1|AA2	1.73e-86	238	496	103	364
AEO59029.1|AA2	2.17e-86	238	496	99	359
QBZ59830.1|AA2	8.70e-84	238	496	153	417
VBB71993.1|AA2	2.24e-83	238	496	96	358
CDP22930.1|AA2	1.41e-81	238	496	155	417

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1LY8_A	5.16e-35	235	496	18	297	Chain A, Peroxidase [Coprinopsis cinerea],1LY8_B Chain B, Peroxidase [Coprinopsis cinerea]
5FNB_A	7.28e-34	237	496	12	283	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]
1LYK_A	1.28e-33	235	496	18	297	Chain A, Peroxidase [Coprinopsis cinerea],1LYK_B Chain B, Peroxidase [Coprinopsis cinerea]
1LY9_A	1.77e-33	235	496	18	297	Chain A, Peroxidase [Coprinopsis cinerea],1LY9_B Chain B, Peroxidase [Coprinopsis cinerea],1LYC_A Chain A, Peroxidase [Coprinopsis cinerea],1LYC_B Chain B, Peroxidase [Coprinopsis cinerea]
1ARP_A	1.80e-33	235	496	19	298	Crystal structure of the fungal peroxidase from Arthromyces ramosus at 1.9 angstroms resolution: structural comparisons with the lignin and cytochrome C peroxidases [Penicillium janthinellum],1ARU_A Crystal Structures Of Cyanide-And Triiodide-Bound Forms Of Arthromyces Ramosus Peroxidase At Different Ph Values. Perturbations Of Active Site Residues And Their Implication In Enzyme Catalysis [Agaricales sp. 'Arthromyces ramosus'],1ARV_A Crystal Structures Of Cyanide-And Triiodide-Bound Forms Of Arthromyces Ramosus Peroxidase At Different Ph Values. Perturbations Of Active Site Residues And Their Implication In Enzyme Catalysis [Agaricales sp. 'Arthromyces ramosus'],1ARW_A Crystal Structures Of Cyanide-And Triiodide-Bound Forms Of Arthromyces Ramosus Peroxidase At Different Ph Values. Perturbations Of Active Site Residues And Their Implication In Enzyme Catalysis [Agaricales sp. 'Arthromyces ramosus'],1ARX_A Crystal Structures Of Cyanide-And Triiodide-Bound Forms Of Arthromyces Ramosus Peroxidase At Different Ph Values. Perturbations Of Active Site Residues And Their Implication In Enzyme Catalysis [Agaricales sp. 'Arthromyces ramosus'],1ARY_A Crystal Structures Of Cyanide-And Triiodide-Bound Forms Of Arthromyces Ramosus Peroxidase At Different Ph Values. Perturbations Of Active Site Residues And Their Implication In Enzyme Catalysis [Agaricales sp. 'Arthromyces ramosus'],1C8I_A BINDING MODE OF HYDROXYLAMINE TO ARTHROMYCES RAMOSUS PEROXIDASE [Agaricales sp. 'Arthromyces ramosus'],1CK6_A BINDING MODE OF SALICYLHYDROXAMIC ACID TO ARTHROMYCES RAMOSUS PEROXIDASE [Agaricales sp. 'Arthromyces ramosus'],1GZA_A PEROXIDASE [Agaricales sp. 'Arthromyces ramosus'],1GZB_A PEROXIDASE [Agaricales sp. 'Arthromyces ramosus'],1HSR_A BINDING MODE OF BENZHYDROXAMIC ACID TO ARTHROMYCES RAMOSUS PEROXIDASE [Agaricales sp. 'Arthromyces ramosus'],2E39_A Crystal structure of the CN-bound form of Arthromyces ramosus peroxidase at 1.3 Angstroms resolution [Agaricales sp. 'Arthromyces ramosus'],2E3A_A Crystal structure of the NO-bound form of Arthromyces ramosus peroxidase at 1.3 Angstroms resolution [Agaricales sp. 'Arthromyces ramosus'],2E3B_A Crystal structure of the HA-bound form of Arthromyces ramosus peroxidase at 1.3 Angstroms resolution [Agaricales sp. 'Arthromyces ramosus']

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|P28314|PER_COPCI	9.72e-33	235	496	38	317	Peroxidase OS=Coprinopsis cinerea OX=5346 GN=CIP1 PE=1 SV=2
sp|P28313|PER_ARTRA	1.36e-32	235	496	39	318	Peroxidase OS=Arthromyces ramosus OX=5451 PE=1 SV=3
sp|Q70LM3|PEM2_PHLRA	2.99e-32	260	496	57	318	Manganese peroxidase 2 OS=Phlebia radiata OX=5308 GN=mnp2 PE=1 SV=1
sp|Q9UR19|VPL1_PLEER	4.62e-32	237	496	42	313	Versatile peroxidase VPL1 OS=Pleurotus eryngii OX=5323 GN=vpl1 PE=1 SV=1
sp|A8NK72|PER_COPC7	9.05e-32	235	496	38	317	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
0.000230	0.999746	CS pos: 19-20. Pr: 0.9748

TMHMM  Annotations     

There is no transmembrane helices in SPSK_01702-t39_1-p1.