dbCAN-seq: a database of CAZyme sequence and annotation

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CAZyme Information: Z517_01079-t43_1-p1

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Basic Information help

Species

Fonsecaea pedrosoi

Lineage

Ascomycota; Eurotiomycetes; ; Herpotrichiellaceae; Fonsecaea; Fonsecaea pedrosoi

CAZyme ID

Z517_01079-t43_1-p1

CAZy Family

AA3

CAZyme Description

hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
643	KN846969\|CGC1	70500.52	4.5602

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_FpedrosoiCBS271-37	12573	1442368	46	12527

Gene Location

Full Sequence Download help

Enzyme Prediction help

No EC number prediction in Z517_01079-t43_1-p1.

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
AA1	139	617	3.7e-121	0.9776536312849162

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
274555	ascorbase	4.71e-95	122	639	1	537	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	8.59e-81	117	639	18	560	L-ascorbate oxidase
215324	PLN02604	6.06e-79	122	639	24	560	oxidoreductase
259953	CuRO_2_MCO_like_1	2.82e-76	256	418	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	6.04e-69	123	241	1	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.

CAZyme Hits help

Hit ID	E-Value	Query Start	Query End	Hit Start
6.40e-219	91	641	92	655
2.95e-214	86	602	69	589
6.76e-209	87	643	77	660
5.52e-178	100	643	165	724
3.58e-161	99	642	108	661

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
3.01e-87	126	641	7	485	T2-depleted laccase from Coriolopsis caperata soaked with CuCl [Coriolopsis caperata],4JHV_A T2-depleted laccase from Coriolopsis caperata [Coriolopsis caperata]
3.55e-87	126	641	7	491	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]
3.22e-86	134	621	35	487	Chain A, Laccase [Rigidoporus microporus]
3.73e-85	128	641	9	488	Crystal structure of laccase from Cerrena maxima at 1.76A resolution [Cerrena]
6.75e-85	126	641	7	485	PM1 mutant, 7D5 [Aspergillus oryzae],6H5Y_B PM1 mutant, 7D5 [Aspergillus oryzae]

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
5.20e-103	120	642	59	579	Laccase-1 OS=Cryptococcus neoformans var. neoformans serotype D (strain B-3501A) OX=283643 GN=LAC1 PE=1 SV=1
2.35e-100	120	642	59	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
3.66e-97	120	642	59	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
9.61e-97	122	643	22	513	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
2.06e-91	118	643	20	517	Iron transport multicopper oxidase FET3 OS=Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1) OX=229533 GN=FET3 PE=2 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
0.999996	0.000042

TMHMM Annotations download full data without filtering help

Start	End
40	62