CAZyme Information: EPrPIT00000024225-p1

Basic Information

• Species: Globisporangium irregulare
• Lineage: Oomycota; NA; ; Pythiaceae; Globisporangium; Globisporangium irregulare
• CAZyme ID: EPrPIT00000024225-p1
• CAZy Family: PL1
• CAZyme Description: Cytochrome c peroxidase, mitochondrial

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
288		32036.68	8.0211

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_GirregulareDAOMBR486	13869	1223557	65	13804

• Gene Location: location=PirrDAOMBR486_SC1629:3693-4926(-)

Full Sequence      

MLRRVAIQAAKQAGAVSKTRTFASVASSGAKGANAGKKQPSAVLLAAAGVAVAGGFAMTD
LVNAREKKPDLEQIKKEIVEIFDENNYMGPTLINHGGNAGLHLAVKALEKVKKNHPEITY
ADLYILAGVAIIEEMGGPSVPFRLGRPDAVSGEECTPDGRLPDADKGSKSKNINHVRDVF
YRMGFNDREIWTWSNEFFRQLVENKWTVKKWNGPMQFEDPTGELMMLPADIAMIEDPEFK
KYVELYAKDEELWFSDFSKAFVKLTENGVKFPEKTGWRKYIFFGPRGE

Enzyme Prediction     

EC	1.11.1.11:1

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
173825	ascorbate_peroxidase	5.43e-94	62	272	4	253	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	2.34e-49	95	272	66	247	L-ascorbate peroxidase
178467	PLN02879	2.29e-37	90	268	64	246	L-ascorbate peroxidase
173823	plant_peroxidase_like	1.46e-35	91	266	50	255	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.
166005	PLN02364	5.38e-34	95	268	68	246	L-ascorbate peroxidase 1

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
UIZ22874.1|AA2	3.17e-130	1	284	1	340
BCS12828.1|AA2	8.18e-59	94	282	153	360
BCS01074.1|AA2	8.18e-59	94	282	153	360
QGI58483.1|AA2	9.84e-59	94	282	142	352
QGI89392.1|AA2	9.84e-59	94	282	142	352

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3RIV_A	7.91e-49	63	270	1	261	The Crystal Structure of Leishmania major Peroxidase [Leishmania major strain Friedlin],3RIV_B The Crystal Structure of Leishmania major Peroxidase [Leishmania major strain Friedlin]
3RIW_A	7.91e-49	63	270	1	261	The Crystal Structure of Leishmania major Peroxidase mutant C197T [Leishmania major strain Friedlin],3RIW_B The Crystal Structure of Leishmania major Peroxidase mutant C197T [Leishmania major strain Friedlin]
4GED_A	1.03e-48	95	270	62	260	Crystal Structure of the Leishmania Major Peroxidase-Cytochrome C Complex [Leishmania major]
5AL9_A	1.08e-48	95	270	62	260	Structure of Leishmania major peroxidase D211R mutant (high res) [Leishmania major],5ALA_A Structure of Leishmania major peroxidase D211R mutant (low res) [Leishmania major],5ALA_B Structure of Leishmania major peroxidase D211R mutant (low res) [Leishmania major]
5AMM_A	1.08e-48	95	270	62	260	Structure of Leishmania major peroxidase D211N mutant [Leishmania major],5AMM_B Structure of Leishmania major peroxidase D211N mutant [Leishmania major]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q4WPF8|CCPR_ASPFU	1.53e-59	33	282	50	362	Cytochrome c peroxidase, mitochondrial OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=ccp1 PE=3 SV=1
sp|Q4ING3|CCPR_GIBZE	1.68e-56	94	282	142	352	Cytochrome c peroxidase, mitochondrial OS=Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1) OX=229533 GN=CCP1 PE=3 SV=1
sp|Q7SDV9|CCPR_NEUCR	3.67e-55	94	282	145	353	Cytochrome c peroxidase, mitochondrial OS=Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) OX=367110 GN=ccp-1 PE=3 SV=1
sp|Q4PBY6|CCPR_USTMA	4.99e-55	95	269	172	368	Cytochrome c peroxidase, mitochondrial OS=Ustilago maydis (strain 521 / FGSC 9021) OX=237631 GN=CCP1 PE=3 SV=1
sp|P0C0V3|CCPR_EMENI	5.58e-55	94	282	148	357	Cytochrome c peroxidase, mitochondrial OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=ccp1 PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
0.999282	0.000742

TMHMM  Annotations     

There is no transmembrane helices in EPrPIT00000024225-p1.