CAZyme Information: RL4_JR_09294-RA-p1

Basic Information

• Species: Raffaelea lauricola
• Lineage: Ascomycota; Sordariomycetes; ; Ophiostomataceae; Raffaelea; Raffaelea lauricola
• CAZyme ID: RL4_JR_09294-RA-p1
• CAZy Family: GT20
• CAZyme Description: unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
612		67334.11	4.6129

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=JACBXF010000071:367352-369190(-)

Full Sequence      

MLFMTASVVAMAAAAAAKTVTYEWDLSWVKANPDGLFERDVVGINGAWPLPIVNVTKGDR
LVVTMNNKLDVSSSIHWHGMFQNGTNYMDGPSMVTQCPVPPGSSFTYNFTVDQNGTYWYH
CHTDFCYPDGYRQALLVQDDQAPFKYDKEISITLSDWYHDLQKVLSKQFMSLYNPTGAEP
VPNSFLLNEGLNQKIAVEPGKTYLLRIINIAAFVSQFFWIEGVNMTIVEVDGVYVEPKSA
DKIYLSVAQRYSVLLTTPNTTAANLAMVMVADSDLLDTIPSDLQLNSTHWLVLNESAPMD
QVAMTVDLSNELIPVDDIDLVPTDGQALFENPDIVVNVTVFMINLINGYNYAFFNNITYT
APKVPSLYSVLSAPDNATASSSVVYGEYTNPFVLKKNQVVEIVINNGDTGTHPFHLHGHT
FQVINRSPPYGADYNAYKDGDPVYYDASNHSDFPTIPVRRDTVVLPPQGYVVLRFIADNP
GVWIFHCHIDWHLSSGLALIFVEAPDELRAQTTIPDQHYSVCAAASVPTVGNAAANSANF
LDLKGQNKQQKSIPGGFTPRGETAMAFCVLSAVLGITALVFYGLADLKHRPTDPPTPQQH
NGSDDVVAAKSG

Enzyme Prediction     

EC	1.10.3.2:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	38	374	3.4e-140	0.9910979228486647

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
274555	ascorbase	8.31e-88	22	517	4	534	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	5.58e-85	27	505	43	450	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	5.19e-83	333	505	1	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	1.56e-72	22	517	26	557	L-ascorbate oxidase
259945	CuRO_2_Fet3p_like	1.54e-70	149	295	2	148	The second 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 2 of 3-domain MCOs has lost the ability to bind copper.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
UKZ96021.1|AA1_2	3.83e-282	17	607	16	605
QKX63715.1|AA1_2	6.08e-277	7	611	13	617
UKZ71088.1|AA1_2	1.68e-273	10	607	8	604
AYD59708.1|AA1_2	1.64e-271	17	602	16	601
QYT00246.1|AA1_2	2.70e-270	17	602	16	601

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1ZPU_A	1.10e-185	18	556	1	534	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]
3KW7_A	4.71e-75	26	522	10	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]
1GYC_A	4.00e-69	32	522	16	488	Chain A, LACCASE 2 [Trametes versicolor]
5LDU_A	1.12e-67	32	522	16	488	Recombinant high-redox potential laccase from Basidiomycete Trametes hirsuta [Trametes hirsuta]
1V10_A	1.35e-67	7	503	9	489	Chain A, Laccase [Rigidoporus microporus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|E9R598|FETC_ASPFU	6.48e-219	2	605	6	591	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	6.77e-211	4	585	7	577	Iron transport multicopper oxidase fetC OS=Epichloe festucae (strain E2368) OX=696363 GN=fetC PE=2 SV=1
sp|I1RMG9|FET3_GIBZE	3.00e-199	15	585	20	578	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|P78591|FET3_CANAX	4.79e-196	11	589	15	584	Iron transport multicopper oxidase FET3 OS=Candida albicans OX=5476 GN=FET3 PE=3 SV=1
sp|P38993|FET3_YEAST	5.77e-195	11	588	15	587	Iron transport multicopper oxidase FET3 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=FET3 PE=1 SV=2

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.216054	0.783926	CS pos: 17-18. Pr: 0.4189

TMHMM  Annotations     

Start	End
563	585