dbCAN-seq: a database of CAZyme sequence and annotation

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CAZyme Information: HVAS_10026760.1-p1

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Basic Information help

Species

Hemileia vastatrix

Lineage

Basidiomycota; Pucciniomycetes; ; Zaghouaniaceae; Hemileia; Hemileia vastatrix

CAZyme ID

HVAS_10026760.1-p1

CAZy Family

CE4

CAZyme Description

unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
362	PHNK01002676\|CGC1	40841.49	6.3850

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_HvastatrixRaceXXXIII	12854	N/A	284	12570

Gene Location

Full Sequence Download help

Enzyme Prediction help

No EC number prediction in HVAS_10026760.1-p1.

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
AA1	82	337	2e-84	0.6815642458100558

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
259926	CuRO_1_Diphenol_Ox	4.36e-64	66	184	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.
274555	ascorbase	1.87e-59	65	327	1	277	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.
259923	CuRO_1_MaLCC_like	1.18e-50	64	184	2	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.
177843	PLN02191	1.84e-48	66	327	24	300	L-ascorbate oxidase
215324	PLN02604	2.96e-47	62	327	21	298	oxidoreductase

CAZyme Hits help

Hit ID	E-Value	Query Start	Query End	Hit Start
5.47e-93	52	337	102	384
1.34e-90	45	337	77	368
5.15e-78	56	337	94	381
2.47e-66	60	337	143	426
2.47e-66	60	337	143	426

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
2.14e-51	63	327	18	278	Crystal structure of a laccase-like multicopper oxidase McoG from from Aspergillus niger [Aspergillus niger]
2.18e-51	63	327	19	279	Crystal structure of a laccase-like multicopper oxidase McoG from Aspergillus niger bound to zinc [Aspergillus niger]
6.52e-50	63	327	46	306	Crystal structure of the H253D mutant of McoG from Aspergillus niger [Aspergillus niger]
3.93e-47	78	330	17	261	Chain A, LACCASE 1 [Coprinopsis cinerea]
4.00e-47	78	330	17	261	Chain A, Laccase [Coprinopsis cinerea]

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
1.23e-53	78	328	34	289	Laccase-2 OS=Thanatephorus cucumeris OX=107832 GN=LCC2 PE=2 SV=1
6.66e-51	63	327	59	332	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
1.78e-50	63	327	59	332	Laccase-1 OS=Cryptococcus neoformans var. neoformans serotype D (strain B-3501A) OX=283643 GN=LAC1 PE=1 SV=1
5.66e-50	65	327	73	333	Oxidoreductase OpS5 OS=Beauveria bassiana (strain ARSEF 2860) OX=655819 GN=OpS5 PE=1 SV=1
9.52e-50	52	331	11	287	Laccase-1 OS=Agaricus bisporus OX=5341 GN=lcc1 PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
0.559675	0.440315

TMHMM Annotations download full data without filtering help

Start	End
2	24