CAZyme Information: ASPZODRAFT_55640-t33_1-p1

Basic Information

• Species: Penicilliopsis zonata
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Penicilliopsis; Penicilliopsis zonata
• CAZyme ID: ASPZODRAFT_55640-t33_1-p1
• CAZy Family: GH71
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
591	KV878336|CGC3	65824.50	5.9289

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_PzonataCBS506.65	10027	1073090	158	9869

• Gene Location: location=KV878336:3254095-3256271(-)

Full Sequence      

MAWSHAFSLAGSLLILSTALLIVQTFWTGPGVPTLVAEHAVSAAERRIEILLHPQDHVLR
PADSLRHVWNITSGRKVPDGVAKDVFLINGQFPGPTIEARSGDVLEVEVWNSLADEEVSI
HWHGLLMRGANHMDGATGITQCAIPPGASYTYRFRIEQEGTFWYEYHAHSDVQRSDGLYG
GLVVHPPGAIQQDEEILLLAGDWYHRPAGEVLDAFMDAKSDGSEPCPDSLLINGLGHFDC
SRALPAFPVDCSPSDMPWIQMDTRKTYRVRVANVGALTGISITIPNAQIQVTHFDGQRIT
ASPPVNSVGVLYPGERVDFILSWNRPEETSQLIIDLDKENFQTPNLALSPTQSFAISDPK
GQFSSSNQTEITSFNLQTAQGLLLPHPLPEPKSFVVLYSAIQILVHEHNIPMGFINRTHW
KKQPQPLLSLGREDWNSYQLVPWTGPEPAWIDIVINNMDVTGHPFHLHGTTFYVLSSYRG
KSGWDYFNPFDTSKPPKGGAYNVINPLEKDTVYVPPLGYVVLRFRADNEGIWMLHCHVLW
HQASGMSMAVQVLGDEHAGFRDHRMGEVTREYCSGTYSPSHLREVDKKLAI

Enzyme Prediction     

No EC number prediction in ASPZODRAFT_55640-t33_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	81	546	9.8e-90	0.9776536312849162

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
274555	ascorbase	1.70e-71	66	546	3	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.
215324	PLN02604	2.12e-64	66	546	26	540	oxidoreductase
177843	PLN02191	1.20e-62	69	548	28	542	L-ascorbate oxidase
259977	CuRO_3_MCO_like_4	4.42e-56	396	552	2	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.
225043	SufI	5.80e-54	54	556	22	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].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
UPK99837.1|AA1	1.37e-157	47	552	81	600
QLI63445.1|AA1	1.20e-150	52	552	72	610
QKD61545.1|AA1	1.76e-150	52	568	79	615
QPC80252.1|AA1	1.88e-150	52	552	87	600
AVI02163.1|AA1	4.97e-150	52	568	79	615

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1AOZ_A	1.28e-56	65	548	3	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]
3V9E_A	7.69e-55	61	548	63	538	Structure of the L499M mutant of the laccase from B.aclada [Botrytis aclada]
3SQR_A	2.03e-54	61	548	63	538	Crystal structure of laccase from Botrytis aclada at 1.67 A resolution [Botrytis aclada],4X4K_A Structure of laccase from Botrytis aclada with full copper content [Botrytis aclada]
1ZPU_A	6.94e-49	67	572	3	496	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]
5LM8_A	3.85e-46	54	550	18	502	Crystal structure of a laccase-like multicopper oxidase McoG from from Aspergillus niger [Aspergillus niger]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|K7NCS2|FETC_EPIFE	2.75e-66	59	546	17	489	Iron transport multicopper oxidase fetC OS=Epichloe festucae (strain E2368) OX=696363 GN=fetC PE=2 SV=1
sp|P14133|ASO_CUCSA	1.39e-62	69	548	43	555	L-ascorbate oxidase OS=Cucumis sativus OX=3659 PE=1 SV=1
sp|J9VY90|LAC1_CRYNH	2.04e-62	67	553	64	560	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|I1RMG9|FET3_GIBZE	1.88e-59	75	546	35	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
sp|Q55P57|LAC1_CRYNB	5.18e-59	33	552	27	560	Laccase-1 OS=Cryptococcus neoformans var. neoformans serotype D (strain B-3501A) OX=283643 GN=LAC1 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000001	0.000055

TMHMM  Annotations     

Start	End
7	29