CAZyme Information: PWY83987.1

Basic Information

• Species: Aspergillus eucalypticola
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus eucalypticola
• CAZyme ID: PWY83987.1
• CAZy Family: GT2|GT2
• CAZyme Description: unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
618		69293.09	6.5579

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AeucalypticolaCBS122712	12207	1448314	274	11933

• Gene Location: location=MSFU01000002:190292-192499(-)

Full Sequence      

MQNNLPYCQEMKEQGSILLDSQQSPSLRLRRLPWGIVLYPSTICGLILLLFVAQISQPSP
LQRLVPSRVLNSQIHPTVHEPDASRPLIELHPEDHVYRNPSTQHHDWVVTADHRRPDGVL
KRVYLINDLFPGPTVEARSGDRLIVNVTNFLDDEPISIHWHGVHIENAMDGAVGVTQRAI
PPGSTFTYNFKIPTDQSGTFWYHAHSGLLRADGLYGGLIVHEPSPKPTVRGLLARADQQE
LGSYDKDILLLIGDWYHRSADQVYSWYMRAGSFGNEPVPDSLLINGVVDCILQHLSASYL
DAKGDAAYRVRVVNTGSVAGFTLGFQNREFTLIQVDSIDVEQQDSNSAGVLYPGQRMDII
LRPSPDKTPSSLTIDLDKECFRYPNPALASVQTFDITNSPNNLSSSISSLNNTISLSEVA
TRKSLLSGLPAKAHQTHVVYTKIEKLSINHNVPYGFFNRTSWRPQIDTPLIDLPREKWDE
NQLVFSTGSTTSRPLSSEQDQDLWIDLVVNNLDDSGHPFHMHGHHFYILRTYQAPVGWGA
YNPFTDAHPPGLAPHPASSSRTDSPYDLSQARLRDTVYIPSRGHAVLRFRADNPGIWLFH
CHIIWHQASGMAMLLHIE

Enzyme Prediction     

No EC number prediction in PWY83987.1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	119	612	4.9e-89	0.9804469273743017

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
274555	ascorbase	6.51e-59	102	611	1	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.
225043	SufI	2.33e-58	107	612	38	443	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].
259977	CuRO_3_MCO_like_4	4.73e-58	438	617	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.
259869	CuRO_1_LCC_like	4.08e-52	103	221	1	120	Cupredoxin domain 1 of laccase-like multicopper oxidases; including laccase, CueO, spore coat protein A, ascorbate oxidase and similar proteins. Laccase-like multicopper oxidases (MCOs) in this family contain three cupredoxin domains. They are able to couple oxidation of substrates with reduction of dioxygen to water. MCOs are capable of oxidizing a vast range of substrates, varying from aromatic to inorganic compounds such as metals. Although the members of this family have diverse functions, majority of them have three cupredoxin domain repeats. 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. Also included in this family are cupredoxin domains 1, 3, and 5 of the 6-domain MCO ceruloplasmin and similar proteins.
177843	PLN02191	3.38e-51	107	615	28	544	L-ascorbate oxidase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CAK44017.1|AA1	0.0	22	617	2	586
BCS06095.1|AA1	3.03e-310	169	618	1	460
BCR93452.1|AA1	3.03e-310	169	618	1	460
QMW37919.1|AA1	7.14e-257	21	617	8	598
QRD88142.1|AA1	9.23e-257	21	617	25	615

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1ZPU_A	3.47e-52	106	615	6	477	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]
3V9E_A	1.51e-47	116	613	81	538	Structure of the L499M mutant of the laccase from B.aclada [Botrytis aclada]
3SQR_A	3.90e-47	116	613	81	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]
5LM8_A	3.46e-44	117	612	38	499	Crystal structure of a laccase-like multicopper oxidase McoG from from Aspergillus niger [Aspergillus niger]
5LWW_A	3.52e-44	117	612	39	500	Crystal structure of a laccase-like multicopper oxidase McoG from Aspergillus niger bound to zinc [Aspergillus niger]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|I1RMG9|FET3_GIBZE	4.60e-60	101	611	23	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|K7NCS2|FETC_EPIFE	6.19e-59	101	612	21	490	Iron transport multicopper oxidase fetC OS=Epichloe festucae (strain E2368) OX=696363 GN=fetC PE=2 SV=1
sp|P43561|FET5_YEAST	5.76e-57	109	612	30	508	Iron transport multicopper oxidase FET5 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=FET5 PE=1 SV=1
sp|Q6CII3|FET3_KLULA	1.77e-56	101	615	26	503	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
sp|P78591|FET3_CANAX	5.71e-56	116	615	37	496	Iron transport multicopper oxidase FET3 OS=Candida albicans OX=5476 GN=FET3 PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000039	0.000010

TMHMM  Annotations     

Start	End
32	54