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CAZyme Information: CNG01250-t26_2-p1

You are here: Home > Sequence: CNG01250-t26_2-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 Cryptococcus neoformans
Lineage Arthropoda; Insecta; ; Eriococcidae; Cryptococcus; Cryptococcus neoformans
CAZyme ID CNG01250-t26_2-p1
CAZy Family GH33
CAZyme Description Laccase 2
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
507 55482.22 5.7248
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_CneoformansJEC21 7004 214684 372 6632
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in CNG01250-t26_2-p1.

CAZyme Signature Domains help

Family Start End Evalue family coverage
AA1 2 466 7e-100 0.9441340782122905

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
259950 CuRO_2_Diphenol_Ox 1.77e-80 109 269 1 164
The second 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 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. Laccase is a multicopper oxidase (MCO) 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.
259971 CuRO_3_Diphenol_Ox 9.34e-78 318 473 1 158
The third 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 3 of 3-domain MCOs contains the Type 1 (T1) copper binding site and part the trinuclear copper binding site, which is located at the interface of domains 1 and 3.
274555 ascorbase 1.04e-75 3 471 30 520
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 4.60e-71 2 474 51 546
L-ascorbate oxidase
215324 PLN02604 1.14e-60 3 471 53 543
oxidoreductase

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
0.0 1 507 1 507
0.0 1 507 1 507
0.0 1 505 88 592
0.0 1 505 88 592
1.57e-310 1 505 88 592

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1.81e-62 2 503 95 571
Structure of the L499M mutant of the laccase from B.aclada [Botrytis aclada]
2.63e-62 3 498 52 529
Crystal structure of a laccase-like multicopper oxidase McoG from from Aspergillus niger [Aspergillus niger]
2.68e-62 3 498 53 530
Crystal structure of a laccase-like multicopper oxidase McoG from Aspergillus niger bound to zinc [Aspergillus niger]
4.90e-62 2 503 95 571
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]
8.43e-62 3 495 33 492
Crystal Structure of Laccase from Steccherinum ochraceum [Steccherinum ochraceum],3T6V_B Crystal Structure of Laccase from Steccherinum ochraceum [Steccherinum ochraceum],3T6V_C Crystal Structure of Laccase from Steccherinum ochraceum [Steccherinum ochraceum],3T6W_A Crystal Structure of Steccherinum ochraceum Laccase obtained by multi-crystals composite data collection technique (10% dose) [Steccherinum ochraceum],3T6W_B Crystal Structure of Steccherinum ochraceum Laccase obtained by multi-crystals composite data collection technique (10% dose) [Steccherinum ochraceum],3T6W_C Crystal Structure of Steccherinum ochraceum Laccase obtained by multi-crystals composite data collection technique (10% dose) [Steccherinum ochraceum],3T6X_A Crystal Structure of Steccherinum ochraceum Laccase obtained by multi-crystals composite data collection technique (20% dose) [Steccherinum ochraceum],3T6X_B Crystal Structure of Steccherinum ochraceum Laccase obtained by multi-crystals composite data collection technique (20% dose) [Steccherinum ochraceum],3T6X_C Crystal Structure of Steccherinum ochraceum Laccase obtained by multi-crystals composite data collection technique (20% dose) [Steccherinum ochraceum],3T6Z_A Crystal Structure of Steccherinum ochraceum Laccase obtained by multi-crystals composite data collection technique (60% dose) [Steccherinum ochraceum],3T6Z_B Crystal Structure of Steccherinum ochraceum Laccase obtained by multi-crystals composite data collection technique (60% dose) [Steccherinum ochraceum],3T6Z_C Crystal Structure of Steccherinum ochraceum Laccase obtained by multi-crystals composite data collection technique (60% dose) [Steccherinum ochraceum],3T71_A Crystal Structure of Steccherinum ochraceum Laccase obtained by multi-crystals composite data collection technique (90% dose) [Steccherinum ochraceum],3T71_B Crystal Structure of Steccherinum ochraceum Laccase obtained by multi-crystals composite data collection technique (90% dose) [Steccherinum ochraceum],3T71_C Crystal Structure of Steccherinum ochraceum Laccase obtained by multi-crystals composite data collection technique (90% dose) [Steccherinum ochraceum]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
0.0 1 505 88 592
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
2.65e-309 1 505 88 592
Laccase-1 OS=Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 / CBS 10515 / FGSC 9487) OX=235443 GN=LAC1 PE=1 SV=1
6.21e-308 1 505 88 592
Laccase-1 OS=Cryptococcus neoformans var. neoformans serotype D (strain B-3501A) OX=283643 GN=LAC1 PE=1 SV=1
2.73e-62 3 480 93 555
Oxydoreductase ptaK OS=Pestalotiopsis fici (strain W106-1 / CGMCC3.15140) OX=1229662 GN=ptaK PE=2 SV=2
8.52e-62 3 466 1 447
Laccase-3 (Fragment) OS=Botryotinia fuckeliana OX=40559 GN=lcc3 PE=3 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI CS Position
0.958995 0.041023

TMHMM  Annotations      help

There is no transmembrane helices in CNG01250-t26_2-p1.