CAZyme Information: KAF7626700.1

Basic Information

• Species: Aspergillus flavus
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus flavus
• CAZyme ID: KAF7626700.1
• CAZy Family: GH62
• CAZyme Description: Extracellular dihydrogeodin oxidase/laccase, putative [Source:UniProtKB/TrEMBL;Acc:B8NWQ2]

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
581	AAIH03000077|CGC15	64526.47	5.0263

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AflavusNRRL3357	14313	332952	0	14313

• Gene Location: location=AAIH03000077:1336944-1338760(+)

Full Sequence      

MMNLLLPLIFVVLAASIQHTTPPFESPLSSGTGLLSRGVLHNQQFNVNTNYYSRTPDTGV
VREYWFDITNATAAPDGVDRPMMLVNGQYPGPTVEADWGDTVKVHVKNNLENNGTSIHFH
GIRQFLNNQMDGTVSVTQCPIAPGTSYTYAWRAEQYGTGFYHSHFSLQAWEGVFGGIVIH
GPATAEYDEDLGVLFLNDWPHRTFNEMYMNQIRNPATPVIDTGLINMTNVCVNGDGDTAG
QRFKTEFVRGKKYRIRLVNVAMHAHFRFSIDDHNLTVIASDFVPIVPFTTNNIAIGMGQR
YDIIIQADQSVDNYWIRSVPQSACSNIPTGDNIKGIVHYMGADDDGDPMTVKWDYGDDTQ
CLDRPMSDLVPWVSLDAMISNAINISDAVAPIAAENSGIFLWTIGGQAFNVSWRDPTLQH
SPTTGINNTISDPKAIELPEANQWVIFVITTTQGVPHPIHLHGHDFYILAQGVGPFSKSI
PLQTRNPPRRDVALLPAQSDGGYLVIAFPTDNPGAWLLHCHMGFHSSAGFVQQIVEQKTE
FWRFLNPELLRDTCDAWDDYAAVNPYGVQYRGTNGPYESGM

Enzyme Prediction     

EC	1.10.3.2:1	-

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	49	357	3.7e-132	0.9871794871794872

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
259923	CuRO_1_MaLCC_like	1.09e-72	59	180	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	9.33e-67	61	525	1	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.
177843	PLN02191	1.49e-64	58	529	20	539	L-ascorbate oxidase
259968	CuRO_3_MaLCC_like	3.54e-64	396	535	20	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	1.01e-58	191	353	1	163	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QRD92702.1|AA1_3	0.0	1	581	1	581
QMW36304.1|AA1_3	0.0	1	581	1	581
UDD65566.1|AA1_3	0.0	2	581	1	580
BAE66440.1|AA1_3	0.0	2	580	1	579
QMW48360.1|AA1_3	0.0	1	581	1	555

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5LM8_A	2.17e-260	43	581	5	549	Crystal structure of a laccase-like multicopper oxidase McoG from from Aspergillus niger [Aspergillus niger]
5LWW_A	2.25e-260	43	581	6	550	Crystal structure of a laccase-like multicopper oxidase McoG from Aspergillus niger bound to zinc [Aspergillus niger]
5LWX_A	1.39e-258	43	581	33	577	Crystal structure of the H253D mutant of McoG from Aspergillus niger [Aspergillus niger]
3SQR_A	1.41e-146	44	560	51	567	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	1.41e-146	44	560	51	567	Structure of the L499M mutant of the laccase from B.aclada [Botrytis aclada]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q96WM9|LAC2_BOTFU	4.61e-150	44	560	51	568	Laccase-2 OS=Botryotinia fuckeliana OX=40559 GN=lcc2 PE=2 SV=1
sp|Q12570|LAC1_BOTFU	5.51e-149	44	566	49	554	Laccase-1 OS=Botryotinia fuckeliana OX=40559 GN=lcc1 PE=2 SV=3
sp|J5JH35|OPS5_BEAB2	1.38e-148	45	560	57	576	Oxidoreductase OpS5 OS=Beauveria bassiana (strain ARSEF 2860) OX=655819 GN=OpS5 PE=1 SV=1
sp|Q96UM2|LAC3_BOTFU	6.45e-116	90	533	1	451	Laccase-3 (Fragment) OS=Botryotinia fuckeliana OX=40559 GN=lcc3 PE=3 SV=1
sp|Q70KY3|LAC1_MELAO	1.76e-114	45	566	67	602	Laccase-1 OS=Melanocarpus albomyces OX=204285 GN=LAC1 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000415	0.999544	CS pos: 16-17. Pr: 0.8774

TMHMM  Annotations     

There is no transmembrane helices in KAF7626700.1.