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CAZyme Information: OTA23364.1

You are here: Home > Sequence: OTA23364.1

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 Hortaea werneckii
Lineage Ascomycota; Dothideomycetes; ; Teratosphaeriaceae; Hortaea; Hortaea werneckii
CAZyme ID OTA23364.1
CAZy Family AA7
CAZyme Description unspecified product
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
677 74729.14 4.7039
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_HwerneckiiEXF-2000 15649 1157616 29 15620
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

EC 1.10.3.2:2 -

CAZyme Signature Domains help

Family Start End Evalue family coverage
AA1 136 457 1.5e-118 0.9807692307692307

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
259923 CuRO_1_MaLCC_like 8.26e-72 146 267 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.
274555 ascorbase 1.08e-66 148 633 1 517
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 6.05e-61 148 633 3 513
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.
225043 SufI 1.46e-59 169 633 54 442
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and spore coat protein CotA) [Cell cycle control, cell division, chromosome partitioning, Inorganic ion transport and metabolism, Cell wall/membrane/envelope biogenesis].
215324 PLN02604 1.36e-58 148 633 24 540
oxidoreductase

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
1.42e-316 52 677 60 685
2.61e-314 39 677 26 665
7.21e-292 54 677 38 663
2.17e-239 78 677 20 594
6.02e-230 69 677 90 698

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1.43e-112 128 677 49 580
Crystal structure of laccase from Botrytis aclada at 1.67 A resolution [Botrytis aclada],4X4K_A Structure of laccase from Botrytis aclada with full copper content [Botrytis aclada]
2.84e-112 128 677 49 580
Structure of the L499M mutant of the laccase from B.aclada [Botrytis aclada]
3.46e-100 118 668 22 560
Crystal structure of the H253D mutant of McoG from Aspergillus niger [Aspergillus niger]
2.42e-99 136 668 11 532
Crystal structure of a laccase-like multicopper oxidase McoG from from Aspergillus niger [Aspergillus niger]
2.49e-99 136 668 12 533
Crystal structure of a laccase-like multicopper oxidase McoG from Aspergillus niger bound to zinc [Aspergillus niger]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
6.93e-179 120 677 37 585
Oxydoreductase ptaK OS=Pestalotiopsis fici (strain W106-1 / CGMCC3.15140) OX=1229662 GN=ptaK PE=2 SV=2
7.34e-119 128 677 54 590
Oxidoreductase OpS5 OS=Beauveria bassiana (strain ARSEF 2860) OX=655819 GN=OpS5 PE=1 SV=1
1.35e-116 128 677 49 581
Laccase-2 OS=Botryotinia fuckeliana OX=40559 GN=lcc2 PE=2 SV=1
3.28e-103 128 677 47 561
Laccase-1 OS=Botryotinia fuckeliana OX=40559 GN=lcc1 PE=2 SV=3
1.36e-94 133 677 46 605
Dihydrogeodin oxidase OS=Aspergillus terreus (strain NIH 2624 / FGSC A1156) OX=341663 GN=gedJ PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI CS Position
0.006053 0.993937 CS pos: 25-26. Pr: 0.5727

TMHMM  Annotations      help

There is no transmembrane helices in OTA23364.1.