dbCAN-seq: a database of CAZyme sequence and annotation

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CAZyme Information: RL4_JR_03810-RA-p1

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Basic Information help

Species

Raffaelea lauricola

Lineage

Ascomycota; Sordariomycetes; ; Ophiostomataceae; Raffaelea; Raffaelea lauricola

CAZyme ID

RL4_JR_03810-RA-p1

CAZy Family

GH13

CAZyme Description

unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
547	JACBXF010000149\|CGC2	59862.79	4.6425

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_RlauricolaRL4	10461	N/A	146	10315

Gene Location

Full Sequence Download help

Enzyme Prediction help

EC	1.10.3.2:1

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
AA1	35	373	1.1e-115	0.9910979228486647

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
274555	ascorbase	8.48e-78	20	495	4	531	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.
215324	PLN02604	1.79e-70	20	495	27	554	oxidoreductase
225043	SufI	5.35e-67	32	481	48	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].
259920	CuRO_1_Fet3p	9.23e-65	18	136	1	121	The first Cupredoxin domain of multicopper oxidase Fet3P. Fet3p catalyzes the ferroxidase reaction, which couples the oxidation of Fe(II) to Fe(III) and a four-electron reduction of molecular oxygen to water. Fet3p is a type I membrane protein with the amino-terminal oxidase domain in the exocellular space and the carboxyl terminus in the cytoplasm. The periplamic produced Fe(III) is transferred to the permease Ftr1p for import into the cytosol. The four copper ions are inserted post-translationally and are essential for catalytic activity, thus linking copper and iron homeostasis. Like other related multicopper oxidases (MCOs), Fet3p 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 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	6.77e-64	18	492	24	551	L-ascorbate oxidase

CAZyme Hits help

Hit ID	E-Value	Query Start	Query End	Hit Start
1.37e-254	6	541	13	543
1.04e-253	9	542	14	544
8.69e-252	15	542	20	552
1.23e-251	15	542	20	552
2.00e-251	15	544	20	547

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
3.32e-107	19	528	4	523	Crystal Structure of Fet3p, a Multicopper Oxidase that Functions in Iron Import [Saccharomyces cerevisiae],1ZPU_B Crystal Structure of Fet3p, a Multicopper Oxidase that Functions in Iron Import [Saccharomyces cerevisiae],1ZPU_C Crystal Structure of Fet3p, a Multicopper Oxidase that Functions in Iron Import [Saccharomyces cerevisiae],1ZPU_D Crystal Structure of Fet3p, a Multicopper Oxidase that Functions in Iron Import [Saccharomyces cerevisiae],1ZPU_E Crystal Structure of Fet3p, a Multicopper Oxidase that Functions in Iron Import [Saccharomyces cerevisiae],1ZPU_F Crystal Structure of Fet3p, a Multicopper Oxidase that Functions in Iron Import [Saccharomyces cerevisiae]
1.26e-76	21	505	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]
1.30e-73	28	505	14	485	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]
1.33e-73	28	505	14	485	Coriolopsis gallica laccase collected at 12.65 keV [Coriolopsis gallica]
2.55e-73	30	525	16	495	T2-depleted laccase from Coriolopsis caperata soaked with CuCl [Coriolopsis caperata],4JHV_A T2-depleted laccase from Coriolopsis caperata [Coriolopsis caperata]

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
7.91e-221	12	542	17	544	Multicopper oxidase PfmaD OS=Pestalotiopsis fici (strain W106-1 / CGMCC3.15140) OX=1229662 GN=PfmaD PE=2 SV=1
7.15e-167	13	534	18	543	Iron transport multicopper oxidase fetC OS=Epichloe festucae (strain E2368) OX=696363 GN=fetC PE=2 SV=1
2.02e-155	13	528	20	538	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
8.88e-155	15	533	20	539	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
1.59e-126	15	514	18	527	Multicopper oxidase abr1 OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=abr1 PE=2 SV=2

SignalP and Lipop Annotations help

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000338	0.999649	CS pos: 15-16. Pr: 0.9658

TMHMM Annotations help

There is no transmembrane helices in RL4_JR_03810-RA-p1.