logo
sublogo
You are browsing environment: FUNGIDB
help

CAZyme Information: PGTG_03756-t26_1-p1

You are here: Home > Sequence: PGTG_03756-t26_1-p1

Basic Information | Genomic context | Full Sequence | Enzyme annotations |  CAZy signature domains |  CDD domains | CAZyme hits | PDB hits | Swiss-Prot hits | SignalP and Lipop annotations | TMHMM annotations

Basic Information help

Species Puccinia graminis
Lineage Basidiomycota; Pucciniomycetes; ; Pucciniaceae; Puccinia; Puccinia graminis
CAZyme ID PGTG_03756-t26_1-p1
CAZy Family CE8|CE8
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
674 DS178268|CGC5 73151.24 6.5437
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_PgraminisCRL75-36-700-3 16309 418459 509 15800
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in PGTG_03756-t26_1-p1.

CAZyme Signature Domains help

Family Start End Evalue family coverage
AA1 1 644 1e-91 0.9636871508379888

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
259953 CuRO_2_MCO_like_1 1.45e-72 113 275 1 163
The second cupredoxin domain of uncharacterized multicopper oxidase. Multicopper Oxidases (MCOs) are multi-domain enzymes that are able to couple oxidation of substrates with reduction of dioxygen to water. MCOs oxidise their substrate by accepting electrons at a mononuclear copper centre and transferring them to a trinuclear copper centre which binds a dioxygen. The dioxygen, following the transfer of four electrons, is reduced to two molecules of water. These MCOs are capable of oxidizing a vast range of substrates, varying from aromatic to inorganic compounds such as metals. This family of MCOs is composed of three cupredoxin domains that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 2 of 3-domain MCOs has lost the ability to bind copper.
259926 CuRO_1_Diphenol_Ox 4.11e-47 1 99 21 119
The first cupredoxin domain of fungal laccase, diphenol oxidase. Diphenol oxidase belongs to the laccase family. It catalyzes the initial steps in melanin biosynthesis from diphenols. Melanin is one of the virulence factors of infectious fungi. In the pathogenesis of C. neoformans, melanin pigments have been shown to protect the fungal cells from oxidative and microbicidal activities of host defense systems. Laccase is a blue multicopper oxidase (MCO) which catalyzes the oxidation of a variety aromatic - notably phenolic and inorganic substances coupled to the reduction of molecular oxygen to water. It has been implicated in a wide spectrum of biological activities and, in particular, plays a key role in morphogenesis, development and lignin metabolism. Although MCOs have diverse functions, majority of them have three cupredoxin domain repeats that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 1 of 3-domain MCOs contains part the trinuclear copper binding site, which is located at the interface of domains 1 and 3.
274555 ascorbase 1.56e-42 2 311 23 313
L-ascorbate oxidase, plant type. Members of this protein family are the copper-containing enzyme L-ascorbate oxidase (EC 1.10.3.3), also called ascorbase. This family is found in flowering plants, and shows greater sequence similarity to a family of laccases (EC 1.10.3.2) from plants than to other known ascorbate oxidases.
177843 PLN02191 6.04e-39 1 311 44 336
L-ascorbate oxidase
215324 PLN02604 3.75e-35 1 254 45 304
oxidoreductase

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
9.77e-91 1 412 136 550
9.86e-91 1 408 119 532
2.97e-89 1 412 124 544
5.41e-73 1 422 143 589
1.94e-64 1 407 132 572

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2.00e-40 2 399 26 408
Chain A, LACCASE 1 [Coprinopsis cinerea]
2.03e-40 2 399 26 408
Chain A, Laccase [Coprinopsis cinerea]
3.98e-39 2 399 25 407
Laccase from Antrodiella faginea [Antrodiella faginea]
9.61e-37 2 399 25 405
Crystal Structure of Laccase from Cerrena sp. RSD1 [Cerrena],5Z1X_B Crystal Structure of Laccase from Cerrena sp. RSD1 [Cerrena],5Z22_A Crystal Structure of Laccase from Cerrena sp. RSD1 [Cerrena]
1.36e-36 2 250 25 261
Chain A, Laccase [Lentinus tigrinus],2QT6_B Chain B, Laccase [Lentinus tigrinus]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1.32e-40 1 290 43 326
Laccase-4 OS=Thanatephorus cucumeris OX=107832 GN=LCC4 PE=1 SV=1
2.38e-40 2 252 43 292
Laccase-2 OS=Thanatephorus cucumeris OX=107832 GN=LCC2 PE=2 SV=1
1.40e-39 5 286 86 370
Laccase-2 OS=Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 / CBS 10515 / FGSC 9487) OX=235443 GN=LAC2 PE=3 SV=2
8.41e-39 2 399 47 430
Laccase-4 OS=Trametes villosa OX=47662 GN=LCC4 PE=3 SV=1
9.35e-39 1 417 49 456
Iron transport multicopper oxidase FET3 OS=Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) OX=284590 GN=FET3 PE=3 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI CS Position
1.000035 0.000001

TMHMM  Annotations      help

There is no transmembrane helices in PGTG_03756-t26_1-p1.