CAZyme Information: KEF56330.1

Basic Information

• Species: Exophiala aquamarina
• Lineage: Ascomycota; Eurotiomycetes; ; Herpotrichiellaceae; Exophiala; Exophiala aquamarina
• CAZyme ID: KEF56330.1
• CAZy Family: GH16
• CAZyme Description: unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
689	AMGV01000006|CGC6	76555.94	6.3488

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_EaquamarinaCBS119918	13118	1182545	0	13118

• Gene Location: location=AMGV01000006:1553669-1555904(+)

Full Sequence      

MDSGNEEGLARRNSTFTYKASEESTRPEFRHETAAAQDEDPLLSDEEQSPRQGFSESNSL
RIQSKGLTELPAWSTILLTLLILGLILFFQAFSYYANLLLRSHEHTTHDQAVGMLGIPCH
PGEHIHRKATTLNYNFTVSAAFERPDGVKKRVYLVNGAFPGPTIECRAGDTLSIHVTNAI
SDGEGISLHWHGLEMRNANQMDGAIGFTQAPIPVGSTFTYEFQIDQNQSGTFWWHAHSQV
QRGDGLYGGLIVHQPVVNQTEPRPSEALLLVGDWYHRTAQDVLAWFTSAAAIGNEPVPDS
ILINGKGIFDCSMAVTARPVECSSVESNHFLPIFDRHAREGNVRLRIVNAGSLAGFTLKF
SGAKVKPLAADGDNPIEADGHYNSVGVIYPGERVDLLLEWTGASILPPKVEIQLDPENFR
LPNPALSPNQDFVLLKPAIVSRTNRVIARSLDRHHLRLEQQNEEPVHFDLESATGITYGS
AAFELPEPSQEPIVVYTKTEKLARLSYHPKSFINRTSWSPQTDSDTGLRQPLISLPRHQW
DRNQLVPYIALPLTVDSNETMAGTGKNGTCIDIIINNLDDGAHPFHLHGHSFWVLRSYRA
EDRSWGSFNPYSSTPPDSDHASHFRLNTRTPIRKDTISVPRRGHVVLRLWTDNPGIWMLH
CHVLVHQASGMAMGLQIGGDLDSTRGLSF

Enzyme Prediction     

No EC number prediction in KEF56330.1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	148	672	1.6e-83	0.9804469273743017

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
274555	ascorbase	3.15e-64	134	671	4	517	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	2.30e-57	129	673	21	542	L-ascorbate oxidase
259977	CuRO_3_MCO_like_4	1.21e-53	493	677	1	166	The third 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 oxidize 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 subfamily of MCOs is composed of three cupredoxin domains. 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.
259926	CuRO_1_Diphenol_Ox	8.03e-51	134	253	3	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.
215324	PLN02604	8.22e-51	128	684	21	557	oxidoreductase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
UPK99837.1|AA1	2.38e-190	113	678	80	601
QKD61545.1|AA1	4.31e-186	109	678	69	597
AVI02163.1|AA1	1.22e-185	109	678	69	597
UNI22443.1|AA1	1.03e-184	115	687	85	618
QYT05468.1|AA1	9.80e-180	115	678	94	617

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1AOZ_A	3.82e-48	133	673	5	519	Refined Crystal Structure Of Ascorbate Oxidase At 1.9 Angstroms Resolution [Cucurbita pepo var. melopepo],1AOZ_B Refined Crystal Structure Of Ascorbate Oxidase At 1.9 Angstroms Resolution [Cucurbita pepo var. melopepo],1ASO_A X-Ray Structures And Mechanistic Implications Of Three Functional Derivatives Of Ascorbate Oxidase From Zucchini: Reduced-, Peroxide-, And Azide-Forms [Cucurbita pepo var. melopepo],1ASO_B X-Ray Structures And Mechanistic Implications Of Three Functional Derivatives Of Ascorbate Oxidase From Zucchini: Reduced-, Peroxide-, And Azide-Forms [Cucurbita pepo var. melopepo],1ASP_A X-ray Structures And Mechanistic Implications Of Three Functional Derivatives Of Ascorbate Oxidase From Zucchini: Reduced-, Peroxide-, And Azide-forms [Cucurbita pepo var. melopepo],1ASP_B X-ray Structures And Mechanistic Implications Of Three Functional Derivatives Of Ascorbate Oxidase From Zucchini: Reduced-, Peroxide-, And Azide-forms [Cucurbita pepo var. melopepo],1ASQ_A X-Ray Structures And Mechanistic Implications Of Three Functional Derivatives Of Ascorbate Oxidase From Zucchini: Reduced-, Peroxide-, And Azide-Forms [Cucurbita pepo var. melopepo],1ASQ_B X-Ray Structures And Mechanistic Implications Of Three Functional Derivatives Of Ascorbate Oxidase From Zucchini: Reduced-, Peroxide-, And Azide-Forms [Cucurbita pepo var. melopepo]
5LM8_A	1.49e-43	146	672	38	499	Crystal structure of a laccase-like multicopper oxidase McoG from from Aspergillus niger [Aspergillus niger]
5LWW_A	1.51e-43	146	672	39	500	Crystal structure of a laccase-like multicopper oxidase McoG from Aspergillus niger bound to zinc [Aspergillus niger]
5LWX_A	3.02e-43	146	672	66	527	Crystal structure of the H253D mutant of McoG from Aspergillus niger [Aspergillus niger]
3V9E_A	7.80e-41	131	673	67	538	Structure of the L499M mutant of the laccase from B.aclada [Botrytis aclada]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|J9VY90|LAC1_CRYNH	1.01e-55	130	670	60	553	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
sp|K7NCS2|FETC_EPIFE	4.46e-54	129	671	20	489	Iron transport multicopper oxidase fetC OS=Epichloe festucae (strain E2368) OX=696363 GN=fetC PE=2 SV=1
sp|Q55P57|LAC1_CRYNB	8.69e-54	130	670	60	553	Laccase-1 OS=Cryptococcus neoformans var. neoformans serotype D (strain B-3501A) OX=283643 GN=LAC1 PE=1 SV=1
sp|J9VQZ4|LAC2_CRYNH	3.56e-53	130	670	60	553	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
sp|I1RMG9|FET3_GIBZE	3.11e-50	128	671	21	490	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

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000052	0.000000

TMHMM  Annotations     

Start	End
70	92