CAZyme Information: ASPCADRAFT_135012-t33_1-p1

Basic Information

• Species: Aspergillus carbonarius
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus carbonarius
• CAZyme ID: ASPCADRAFT_135012-t33_1-p1
• CAZy Family: AA3
• CAZyme Description: multicopper oxidase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
577	KV907515|CGC1	64230.39	4.8238

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=KV907515:283437-285278(-)

Full Sequence      

MRLSFPLILSSLSCVLGASSPNISQPVGCVNSPTSRACWRDGYNLSTNYYEEVPDTGVVR
EYWFNVENTTAAPDGVELPVQLINGSFPGPTIIADWGDTVVVHVTNSLQTNGTGLHFHGI
RQNWTDQMDGVPSITQCPIAPGQSYTYKWRAVEYGSGWYHSHFYVQAWDGVFGGIVINGP
ATANYDVDLGHLFLNDWYHVWPYSSPNSIWREPLELTRQKTADELVLQASTNGPPTPPNG
LINGTNTYGSFGSRFETTFDAGTKYRIRLVNAAADNHFRFMIDNHTMEVIAADFVPIHPY
NTTQLSIGMGQRYDIIVTGKERTSGNFWLRAIPQEACSETDALNNIKGIIRYDNSSTADP
TTSAYSYTDSCADEAATNLVPYLAINASDRYAYSTEEEVAVQVTDNALLWTMNKTSFHTA
WDYPTLMQVADNNQTWSAKERVIHLPYPDKWVYMAVHSPFAQDHPMHLHGHDFWILASGY
GNFDPSQTDGLTLVNAPRRDVAMMPASGYLVIALKTTNPGAWLMHCHIAWHTSEGFAVQL
LERASEITYDYETLNSTCASWTSYVAAQDVTQHDSGV

Enzyme Prediction     

EC	1.10.3.2:4	1.10.3.-:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	47	371	9.1e-126	0.9935897435897436

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
259947	CuRO_2_MaLCC_like	8.27e-68	189	370	1	167	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.
259968	CuRO_3_MaLCC_like	2.31e-66	405	541	21	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.
259923	CuRO_1_MaLCC_like	8.47e-66	57	178	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.
274555	ascorbase	1.19e-62	59	547	1	531	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	4.03e-58	56	547	20	551	L-ascorbate oxidase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CAK44895.1|AA1_3	0.0	1	577	1	559
BCR82613.1|AA1_3	0.0	9	577	9	557
UQC73404.1|AA1_3	1.79e-294	29	521	64	536
AVO20570.1|AA1_3	2.75e-245	18	577	22	561
QGA14113.1|AA1_3	2.59e-235	5	577	4	568

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5LWX_A	3.82e-180	31	564	24	556	Crystal structure of the H253D mutant of McoG from Aspergillus niger [Aspergillus niger]
5LM8_A	2.42e-179	42	564	6	528	Crystal structure of a laccase-like multicopper oxidase McoG from from Aspergillus niger [Aspergillus niger]
5LWW_A	2.50e-179	42	564	7	529	Crystal structure of a laccase-like multicopper oxidase McoG from Aspergillus niger bound to zinc [Aspergillus niger]
3V9E_A	4.62e-166	10	577	20	580	Structure of the L499M mutant of the laccase from B.aclada [Botrytis aclada]
3SQR_A	4.62e-166	10	577	20	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q12570|LAC1_BOTFU	4.87e-176	23	577	31	561	Laccase-1 OS=Botryotinia fuckeliana OX=40559 GN=lcc1 PE=2 SV=3
sp|Q96WM9|LAC2_BOTFU	2.94e-169	10	577	20	581	Laccase-2 OS=Botryotinia fuckeliana OX=40559 GN=lcc2 PE=2 SV=1
sp|J5JH35|OPS5_BEAB2	4.48e-168	7	577	16	590	Oxidoreductase OpS5 OS=Beauveria bassiana (strain ARSEF 2860) OX=655819 GN=OpS5 PE=1 SV=1
sp|Q96UM2|LAC3_BOTFU	1.41e-128	88	539	1	451	Laccase-3 (Fragment) OS=Botryotinia fuckeliana OX=40559 GN=lcc3 PE=3 SV=1
sp|Q0CCX6|GEDJ_ASPTN	1.05e-123	26	577	25	605	Dihydrogeodin oxidase OS=Aspergillus terreus (strain NIH 2624 / FGSC A1156) OX=341663 GN=gedJ PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000214	0.999738	CS pos: 17-18. Pr: 0.9794

TMHMM  Annotations     

There is no transmembrane helices in ASPCADRAFT_135012-t33_1-p1.