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CAZyme Information: KIX04862.1

You are here: Home > Sequence: KIX04862.1

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 Rhinocladiella mackenziei
Lineage Ascomycota; Eurotiomycetes; ; Herpotrichiellaceae; Rhinocladiella; Rhinocladiella mackenziei
CAZyme ID KIX04862.1
CAZy Family GH20
CAZyme Description Rhinocladiella mackenziei CBS 650.93 unplaced genomic scaffold supercont1.4, whole genome shotgun sequence [Source:UniProtKB/TrEMBL;Acc:A0A0D2FRR9]
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
651 KN847478|CGC11 71325.53 4.9095
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_RmackenzieiCBS650.93 11418 1442369 36 11382
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in KIX04862.1.

CAZyme Signature Domains help

Family Start End Evalue family coverage
AA1 145 624 1.4e-119 0.9776536312849162

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
274555 ascorbase 7.59e-91 128 624 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.
259953 CuRO_2_MCO_like_1 7.17e-77 262 425 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.
215324 PLN02604 7.20e-77 141 644 37 558
oxidoreductase
177843 PLN02191 3.26e-76 123 628 18 544
L-ascorbate oxidase
259977 CuRO_3_MCO_like_4 1.08e-65 468 630 1 166
The third 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 oxidize 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 subfamily of MCOs is composed of three cupredoxin domains. 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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
4.15e-214 74 648 69 655
3.98e-202 79 648 68 658
3.01e-201 104 609 82 589
5.21e-175 98 648 157 722
1.12e-151 102 648 98 655

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4.33e-87 133 650 8 493
Crystal structure of LacB from Trametes sp. AH28-2 [Trametes sp. AH28-2],3KW7_B Crystal structure of LacB from Trametes sp. AH28-2 [Trametes sp. AH28-2]
5.96e-86 130 648 5 488
Crystal structure of laccase from Coriolus zonatus at 2.6 A resolution [Trametes ochracea]
1.61e-84 133 650 8 487
Chain A, CORIOLOPSIS GALLICA LACCASE [Coriolopsis gallica]
6.22e-84 133 650 8 487
Coriolopsis gallica Laccase T2 Copper Depleted at pH 4.5 [Coriolopsis gallica],4A2E_A Crystal Structure of a Coriolopsis gallica Laccase at 1.7 A Resolution pH 5.5 [Coriolopsis gallica],4A2G_A Coriolopsis gallica laccase collected at 8.98 keV [Coriolopsis gallica],4A2H_A Crystal Structure of Laccase from Coriolopsis gallica pH 7.0 [Coriolopsis gallica]
6.39e-84 133 650 8 487
Coriolopsis gallica laccase collected at 12.65 keV [Coriolopsis gallica]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2.08e-95 119 649 52 579
Laccase-1 OS=Cryptococcus neoformans var. neoformans serotype D (strain B-3501A) OX=283643 GN=LAC1 PE=1 SV=1
4.64e-93 119 649 52 579
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
7.15e-90 119 649 52 579
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
2.93e-87 109 650 9 518
Laccase-5 OS=Trametes villosa OX=47662 GN=LCC5 PE=3 SV=2
2.21e-86 125 651 19 514
Iron transport multicopper oxidase fetC OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=fetC PE=2 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI CS Position
0.999829 0.000200

TMHMM  Annotations      download full data without filtering help

Start End
44 66