CAZyme Information: RL4_JR_04109-RA-p1

Basic Information

• Species: Raffaelea lauricola
• Lineage: Ascomycota; Sordariomycetes; ; Ophiostomataceae; Raffaelea; Raffaelea lauricola
• CAZyme ID: RL4_JR_04109-RA-p1
• CAZy Family: GH16
• CAZyme Description: unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
929	JACBXF010000067|CGC13	99368.52	6.0706

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: location=JACBXF010000067:298511-302723(-)

Full Sequence      

MRFLSVLPVLAALLPGRRAASTSDSLQDADAPQSGYLPHHNIDPAKLSSYTMNWTAQFIT
SEMFYAKPLTFTPTGSSVERVVVVSNMNYIRVLDSFTGKVLLQRQVRPPFNTSDITCGDM
PNNVGIAGTPVIDAATEIVYFYSKGYKGDVAGPQGVANGEYKLYALNLADLTDVPGFPVT
VDGRYANNDNARYFLGGTSLQRPGLVMLGDSIVAGFGSHCNNYNVTGFLITASKTAGVGI
TNIQAMVASPGAPVPQALDITNQGNGKSGIWMSGTGLALDEANSRVFIVTGNGGGPGQLK
GSNGVPTSGSTYLSTVEDTAASYRIAANGSLVQNDWFAPYNYDNWNGGDRDFGSAGISLL
DPATFSGGGVNRVAIAGGKTGKASAHVSSYVSPTPTRTNIVSLRWNISWVNAAPDGHARP
YIGINGQWPIPPLVAKLGDELKIQVTNSLGNQTTSMHFHGLFMKGYTYADGAAFVSQCPI
PPGQTIVQQFVLTQVGTYWFHSHDHAQYMDGLRGVLVVKDPSAPYGKVDNDVVLSLSDLY
HDEAPNLIHHYLSSNNSDATGGAEPSPDSTLINDAQNVQIAMAPGNTTLFRVVNMGAAAA
QYLTLEGHDMTVVEIDGQYVTPYTVSQLFVAVSQRYAVIVHSKDDATANYRFTAVLQTRM
FVDGSLPSGSVSSATGYLVYDSTKTLPSSPFTPATSAWDDSVFTPLDRESLYGPVTLTIS
IGVTMATNEQNQIRGLINGVTYLAQKIPTLYTVLTAPASVVNNSAIYGANSVPFILPYGA
VVEVTIDNHDDRAHPFHLHGHYFQVISRSDGGSLFPGMDSTPTVPMKRDTVVVYAQGSTT
IRFVADNPGVWLFHCHTEWHMESGMAATFIEAPAELQAAKPYIPVSHRDICDRQGISRKG
NAGGNWKSWLDLTNANTKPPTEAWGALIT

Enzyme Prediction     

EC	1.10.3.2:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	419	756	1.1e-113	0.9851632047477745

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
274555	ascorbase	1.15e-76	400	872	1	524	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.
225043	SufI	3.08e-72	423	874	56	451	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].
259966	CuRO_3_Fet3p	4.37e-69	718	873	3	160	The third Cupredoxin domain of multicopper oxidase Fet3p. Fet3p catalyzes the ferroxidase reaction, which couples the oxidation of Fe(II) to Fe(III) with the four-electron reduction of molecular oxygen to water. Fet3p is a type I membrane protein with the amino-terminal oxidase domain in the extracellular space and the carboxyl terminus in the cytoplasm. The periplasmic 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 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.
177843	PLN02191	2.90e-67	400	871	23	546	L-ascorbate oxidase
215324	PLN02604	8.95e-61	404	871	28	546	oxidoreductase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ATZ46936.1|AA1_2	2.00e-150	396	919	22	545
AEO71107.1|AA1_2	3.87e-150	401	920	35	555
AHZ65140.1|AA1_2	6.70e-150	401	920	10	526
QKD56481.1|AA1_2	1.48e-149	390	920	14	542
AUS45841.1|AA1_2	6.27e-149	401	920	28	548

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1ZPU_A	1.15e-118	402	918	4	527	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]
4JHU_A	2.09e-65	413	891	16	485	T2-depleted laccase from Coriolopsis caperata soaked with CuCl [Coriolopsis caperata],4JHV_A T2-depleted laccase from Coriolopsis caperata [Coriolopsis caperata]
5ANH_A	5.05e-64	413	891	16	485	Crystal Structure Of Laccase From Basidiomycete Pm1 (cect 2971) [basidiomycete PM1],5ANH_B Crystal Structure Of Laccase From Basidiomycete Pm1 (cect 2971) [basidiomycete PM1],5ANH_C Crystal Structure Of Laccase From Basidiomycete Pm1 (cect 2971) [basidiomycete PM1]
5A7E_A	1.31e-63	413	891	16	485	Chain A, CORIOLOPSIS GALLICA LACCASE [Coriolopsis gallica]
4A2D_A	1.80e-63	413	891	16	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|E9R598|FETC_ASPFU	4.11e-149	405	919	27	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
sp|K7NCS2|FETC_EPIFE	2.53e-142	405	919	27	542	Iron transport multicopper oxidase fetC OS=Epichloe festucae (strain E2368) OX=696363 GN=fetC PE=2 SV=1
sp|I1RMG9|FET3_GIBZE	1.04e-132	405	920	29	548	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
sp|W3X7K0|PFMAD_PESFW	6.92e-123	396	926	18	542	Multicopper oxidase PfmaD OS=Pestalotiopsis fici (strain W106-1 / CGMCC3.15140) OX=1229662 GN=PfmaD PE=2 SV=1
sp|Q6CII3|FET3_KLULA	3.53e-118	402	918	29	553	Iron transport multicopper oxidase FET3 OS=Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) OX=284590 GN=FET3 PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000210	0.999758	CS pos: 19-20. Pr: 0.9722

TMHMM  Annotations     

There is no transmembrane helices in RL4_JR_04109-RA-p1.