CAZyme Information: ASPCADRAFT_519260-t33_1-p1

Basic Information

• Species: Aspergillus carbonarius
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus carbonarius
• CAZyme ID: ASPCADRAFT_519260-t33_1-p1
• CAZy Family: GT45
• CAZyme Description: multicopper oxidase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
653	KV907534|CGC1	73602.68	4.5819

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AcarbonariusITEM5010	11735	602072	260	11475

• Gene Location: location=KV907534:11995-14383(-)

Full Sequence      

MLLESCFTAIINFFGFASLVPFQQQPLPPHGAAPSDSDDLEFTPIGSSITCDYTGLSKYY
TGPDTHGNWSVWFESKDESQNKSITIDTDYEDYIPPGIDRHFYVDVGMDEADPKTPDGRD
YRQGKYFNNSYPGPYIEACWGDTIHVHVTNSLEHNGTAIHMHGIRMFNDSLADGVPGVSQ
CPIAPGETFTYKFRAVQYGTTWYHSHYSLQYTDGLLGPLTIHGPASAFEDWNWATVEGMV
QGPISMDSIIINGNGSYQGRYPDNRYRQRVKPNKRILLRLINASTDTAYIFSIDDHELEV
IGADLVPVHPYNKTHLYIGIGQRYHVILRTKPEVLHEPSYWIRTEPAQHCENFACEPNER
QGILLYDDNVTRDPTTGKHDYDPMCQDENHTDIKPILEWQVPRPSPEQLKNVRFLFEVKR
EANFTLPPEPEGNIPAGPDISVWKIMDDDPAWVDYTDPTVNHTDRPEDDWPPTAALFEIN
QTTYGGWAYMLVDGGHQKELPPSKPGDSVIPAAHPIHLHGHDFALLKQSYDPFNHSLIGN
DTAMNSFIDTFTLDNPARRDVVLLPLNGYIVIAFKVDNPGAWLLHCHIAWHASGGLALQI
LEDKEQLSPDIIGSPASDASDQLQEGCDSWKTWYDNWGNHADPTGRFQDDSGV

Enzyme Prediction     

EC	1.10.3.2:4	1.10.3.-:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	88	385	9.2e-103	0.9935897435897436

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
259923	CuRO_1_MaLCC_like	6.49e-60	97	222	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	5.59e-51	422	601	4	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.
274555	ascorbase	1.53e-48	128	591	26	512	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.
259947	CuRO_2_MaLCC_like	2.48e-48	216	381	1	164	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	4.39e-48	128	638	48	572	L-ascorbate oxidase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CAK46289.1|AA1_3	4.26e-255	1	653	1	672
QKX62792.1|AA1_3	2.61e-189	1	653	1	661
BCS03291.1|AA1_3	3.74e-186	1	653	1	671
BCS14922.1|AA1_3	3.74e-186	1	653	1	671
BCS14352.1|AA1_3	1.40e-185	107	653	8	554

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3SQR_A	6.64e-102	85	653	53	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	1.31e-101	85	653	53	580	Structure of the L499M mutant of the laccase from B.aclada [Botrytis aclada]
5LWX_A	3.22e-92	86	630	37	553	Crystal structure of the H253D mutant of McoG from Aspergillus niger [Aspergillus niger]
5LM8_A	1.64e-91	86	630	9	525	Crystal structure of a laccase-like multicopper oxidase McoG from from Aspergillus niger [Aspergillus niger]
5LWW_A	1.68e-91	86	630	10	526	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	1.10e-155	28	653	23	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	1.39e-108	115	653	72	605	Dihydrogeodin oxidase OS=Aspergillus terreus (strain NIH 2624 / FGSC A1156) OX=341663 GN=gedJ PE=1 SV=1
sp|Q96WM9|LAC2_BOTFU	4.56e-102	85	653	53	581	Laccase-2 OS=Botryotinia fuckeliana OX=40559 GN=lcc2 PE=2 SV=1
sp|Q12570|LAC1_BOTFU	1.40e-97	127	653	86	561	Laccase-1 OS=Botryotinia fuckeliana OX=40559 GN=lcc1 PE=2 SV=3
sp|J5JH35|OPS5_BEAB2	9.08e-96	62	653	47	590	Oxidoreductase OpS5 OS=Beauveria bassiana (strain ARSEF 2860) OX=655819 GN=OpS5 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
0.777579	0.222428

TMHMM  Annotations     

There is no transmembrane helices in ASPCADRAFT_519260-t33_1-p1.