CAZyme Information: PWY75666.1

Basic Information

• Species: Aspergillus eucalypticola
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus eucalypticola
• CAZyme ID: PWY75666.1
• CAZy Family: GH47
• CAZyme Description: unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
673		75749.30	4.5004

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=MSFU01000009:327548-330047(+)

Full Sequence      

MLLESCWTALVHFFGFQSLFSSQQYPLPPNGAIEYPSSPTAAAGQADPTDVLEFQPLGAS
KNFKCQYPGLKDKYLATPNGNQSLWLQPSQQTSQDEVYDIDTDYEIKAPTGITRDIYVDV
SKLDSNDALAPDGVSFPEGKYINGSYPGPRIEACWGDTVRVHVTNKVDKNGTAIHMHGIR
MFNSSYSDGVPGVTQCPIAVNDTFTYEFQAIQYGTTWYHSHYSLQYTDGMLGPLTIYGPA
SSAFAKWTYGVVEGNSPVIQMDSILINNKGSWAGKYPDNRYKTDQLKPGKKYLLRLINAA
TDTAFIFSIDEHKMKVIGADLVPVHPYDMDSLYIGIGQRYHVIVETKSDPEDINRNYWIR
TWPASGCHNFACEPNERQGIFQYNTTDLEDPISTPYRPPYGGQCRDEDHDKLIPVFPWMI
PKPTPDQLQQVRFPFDLLKQDKFTMPAEDGWNGTDETIGAWQVNGAPAWVNYQDLTVNHL
DGNYTWPENAALFELNSDPDTDEPTWAYMVIDGGHQDEEEKPPGEKVVPAAHPMHLHGHD
FALLKQSYDPFDDDIGNDPNAMQGFIDSLSYDNPARRDVVLLPKNGYIVIAFKLDNPGTW
LLHCHIAWHASGGLALQILEDKDKIKELLDKDINPGQTARDQIDDGCTGWKEWWDNKENR
WNASARFQDDSGV

Enzyme Prediction     

EC	1.10.3.2:4	1.10.3.-:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	102	397	3.1e-106	0.9775641025641025

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
259923	CuRO_1_MaLCC_like	1.13e-63	111	237	1	122	The first cupredoxin domain of the fungal laccases similar to Ma-LCC from Melanocarpus albomyces. The subfamily of fungal laccases includes Ma-LCC and similar proteins. Ma-LCC is a multicopper oxidase (MCO) from Melanocarpus albomyces. Its crystal structure contains all four coppers at the mono- and trinuclear copper centers. Laccase is a blue multi-copper enzyme that 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 in fungi and plants. 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.
259968	CuRO_3_MaLCC_like	2.02e-57	444	619	11	157	The third cupredoxin domain of the fungal laccases similar to Ma-LCC from Melanocarpus albomyces. The subfamily of fungal laccases includes Ma-LCC and similar proteins. Ma-LCC is a multicopper oxidase (MCO) from Melanocarpus albomyces. Its crystal structure contains all four coppers at the mono- and trinuclear copper centers. Laccase is a blue multi-copper enzyme that 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 in fungi and plants. 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 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.
259947	CuRO_2_MaLCC_like	1.90e-56	242	399	13	165	The second cupredoxin domain of the fungal laccases similar to Ma-LCC from Melanocarpus albomyces. The subfamily of fungal laccases includes Ma-LCC and similar proteins. Ma-LCC is a multicopper oxidase (MCO) from Melanocarpus albomyces. Its crystal structure contains all four coppers at the mono- and trinuclear copper centers. Laccase is a blue multi-copper enzyme that 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 in fungi and plants. Laccase 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.
177843	PLN02191	3.88e-53	142	640	47	566	L-ascorbate oxidase
274555	ascorbase	6.13e-53	142	638	25	541	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CAK46289.1|AA1_3	0.0	1	673	1	672
BCS14352.1|AA1_3	1.11e-245	121	673	7	554
BCS02695.1|AA1_3	1.37e-212	176	607	1	450
BCS03291.1|AA1_3	3.93e-191	1	673	1	671
BCS14922.1|AA1_3	3.93e-191	1	673	1	671

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3SQR_A	3.80e-103	98	673	52	580	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]
3V9E_A	7.49e-103	98	673	52	580	Structure of the L499M mutant of the laccase from B.aclada [Botrytis aclada]
5LWX_A	2.10e-96	98	653	35	556	Crystal structure of the H253D mutant of McoG from Aspergillus niger [Aspergillus niger]
5LM8_A	1.05e-95	98	653	7	528	Crystal structure of a laccase-like multicopper oxidase McoG from from Aspergillus niger [Aspergillus niger]
5LWW_A	1.08e-95	98	653	8	529	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|D4APX3|LAC1_ARTBC	1.18e-154	50	673	32	633	Laccase ARB_05828 OS=Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) OX=663331 GN=ARB_05828 PE=1 SV=1
sp|Q0CCX6|GEDJ_ASPTN	1.11e-105	88	673	32	605	Dihydrogeodin oxidase OS=Aspergillus terreus (strain NIH 2624 / FGSC A1156) OX=341663 GN=gedJ PE=1 SV=1
sp|Q96WM9|LAC2_BOTFU	3.39e-104	98	673	52	581	Laccase-2 OS=Botryotinia fuckeliana OX=40559 GN=lcc2 PE=2 SV=1
sp|J5JH35|OPS5_BEAB2	6.11e-104	98	673	57	590	Oxidoreductase OpS5 OS=Beauveria bassiana (strain ARSEF 2860) OX=655819 GN=OpS5 PE=1 SV=1
sp|A0A067XMP0|PTAE_PESFW	2.41e-101	98	673	40	610	Oxidoreductase ptaE OS=Pestalotiopsis fici (strain W106-1 / CGMCC3.15140) OX=1229662 GN=ptaE PE=2 SV=2

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
0.854541	0.145463

TMHMM  Annotations     

There is no transmembrane helices in PWY75666.1.