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CAZyme Information: KLU93056.1

You are here: Home > Sequence: KLU93056.1

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 Magnaporthiopsis poae
Lineage Ascomycota; Sordariomycetes; ; Magnaporthaceae; Magnaporthiopsis; Magnaporthiopsis poae
CAZyme ID KLU93056.1
CAZy Family GT62
CAZyme Description Uncharacterized protein (Fragment) [Source:UniProtKB/TrEMBL;Acc:A0A0H2UD14]
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
358 38843.77 7.5021
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_MpoaeATCC64411 12363 644358 200 12163
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

EC 1.10.3.2:4 1.10.3.-:1

CAZyme Signature Domains help

Family Start End Evalue family coverage
AA1 59 356 1.1e-113 0.9230769230769231

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
259923 CuRO_1_MaLCC_like 2.16e-71 69 193 1 122
The first cupredoxin domain of the fungal laccases similar to Ma-LCC from Melanocarpus albomyces. The subfamily of fungal laccases includes Ma-LCC and similar proteins. Ma-LCC is a multicopper oxidase (MCO) from Melanocarpus albomyces. Its crystal structure contains all four coppers at the mono- and trinuclear copper centers. Laccase is a blue multi-copper enzyme that 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 in fungi and plants. 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.
259947 CuRO_2_MaLCC_like 4.25e-51 204 358 1 148
The second cupredoxin domain of the fungal laccases similar to Ma-LCC from Melanocarpus albomyces. The subfamily of fungal laccases includes Ma-LCC and similar proteins. Ma-LCC is a multicopper oxidase (MCO) from Melanocarpus albomyces. Its crystal structure contains all four coppers at the mono- and trinuclear copper centers. Laccase is a blue multi-copper enzyme that 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 in fungi and plants. Laccase 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.
274555 ascorbase 1.34e-45 80 354 7 291
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.
274556 laccase 7.97e-45 71 343 3 269
laccase, plant. Members of this protein family include the copper-containing enzyme laccase (EC 1.10.3.2), often several from a single plant species, and additional, uncharacterized, closely related plant proteins termed laccase-like multicopper oxidases. This protein family shows considerable sequence similarity to the L-ascorbate oxidase (EC 1.10.3.3) family. Laccases are enzymes of rather broad specificity, and classification of all proteins scoring about the trusted cutoff of this model as laccases may be appropriate.
400195 Cu-oxidase_3 8.53e-45 88 197 10 119
Multicopper oxidase. This entry contains many divergent copper oxidase-like domains that are not recognized by the pfam00394 model.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
4.56e-135 41 358 23 339
2.69e-130 24 357 20 344
2.69e-130 24 357 20 344
4.72e-126 41 356 48 349
1.50e-125 25 351 42 369

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2.08e-128 38 356 1 309
Crystal structure of laccase from Myceliophthora thermophila [Thermothelomyces thermophilus]
4.86e-124 41 356 4 309
Crystal Structure of Laccase from Melanocarpus albomyces in Four Copper Form [Melanocarpus albomyces],1GW0_B Crystal Structure of Laccase from Melanocarpus albomyces in Four Copper Form [Melanocarpus albomyces],2IH8_A A low-dose crystal structure of a recombinant Melanocarpus albomyces laccase [Melanocarpus albomyces],2IH8_B A low-dose crystal structure of a recombinant Melanocarpus albomyces laccase [Melanocarpus albomyces],2IH9_A A high-dose crystal structure of a recombinant Melanocarbus albomyces laccase [Melanocarpus albomyces],2IH9_B A high-dose crystal structure of a recombinant Melanocarbus albomyces laccase [Melanocarpus albomyces],3FU7_B Melanocarpus albomyces laccase crystal soaked (4 sec) with 2,6-dimethoxyphenol [Melanocarpus albomyces],3FU9_A Melanocarpus albomyces laccase crystal soaked (20 min) with 2,6-dimethoxyphenol [Melanocarpus albomyces],3FU9_B Melanocarpus albomyces laccase crystal soaked (20 min) with 2,6-dimethoxyphenol [Melanocarpus albomyces],3QPK_A Probing oxygen channels in Melanocarpus albomyces laccase [Melanocarpus albomyces],3QPK_B Probing oxygen channels in Melanocarpus albomyces laccase [Melanocarpus albomyces]
4.86e-124 41 356 4 309
L559A mutant of Melanocarpus albomyces laccase [Melanocarpus albomyces],3DKH_B L559A mutant of Melanocarpus albomyces laccase [Melanocarpus albomyces]
6.87e-124 41 356 4 309
Near-atomic resolution structure of a Melanocarpus albomyces laccase [Melanocarpus albomyces],2Q9O_B Near-atomic resolution structure of a Melanocarpus albomyces laccase [Melanocarpus albomyces],3FU7_A Melanocarpus albomyces laccase crystal soaked (4 sec) with 2,6-dimethoxyphenol [Melanocarpus albomyces],3FU8_A Melanocarpus albomyces laccase crystal soaked (10 sec) with 2,6-dimethoxyphenol [Melanocarpus albomyces],3FU8_B Melanocarpus albomyces laccase crystal soaked (10 sec) with 2,6-dimethoxyphenol [Melanocarpus albomyces]
8.17e-122 9 356 6 349
Crystal structure of an ascomycete fungal laccase from Thielavia arenaria [Canariomyces arenarius],3PPS_B Crystal structure of an ascomycete fungal laccase from Thielavia arenaria [Canariomyces arenarius],3PPS_C Crystal structure of an ascomycete fungal laccase from Thielavia arenaria [Canariomyces arenarius],3PPS_D Crystal structure of an ascomycete fungal laccase from Thielavia arenaria [Canariomyces arenarius]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4.77e-131 24 357 20 344
Laccase OS=Cryphonectria parasitica OX=5116 GN=LAC-1 PE=3 SV=1
4.03e-123 37 356 50 359
Laccase-1 OS=Melanocarpus albomyces OX=204285 GN=LAC1 PE=1 SV=1
1.52e-122 37 356 45 354
Laccase-2 OS=Podospora anserina OX=2587412 GN=LAC2 PE=2 SV=1
2.04e-119 41 356 55 360
Laccase OS=Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) OX=367110 GN=lacc PE=1 SV=3
8.58e-87 103 350 1 239
Laccase-3 (Fragment) OS=Botryotinia fuckeliana OX=40559 GN=lcc3 PE=3 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI CS Position
0.000350 0.999619 CS pos: 22-23. Pr: 0.9744

TMHMM  Annotations      help

There is no transmembrane helices in KLU93056.1.