CAZyme Information: RAK77866.1

Basic Information

• Species: Aspergillus fijiensis
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus fijiensis
• CAZyme ID: RAK77866.1
• CAZy Family: GH3
• CAZyme Description: extracellular dihydrogeodin oxidase/laccase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
592	KZ824640|CGC2	66158.97	5.9472

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AfijiensisCBS313.89	12336	1448319	318	12018

• Gene Location: location=KZ824640:353894-355723(-)

Full Sequence      

MNFLLLLWLLASVALSSPIAHDLFPFKPTSQLEARAANQSQSLQNSQVPWKGFDINTNYY
KTAPDTGVVREYFFDIINTTRAPDGVERRVLLVNGQFPGPTIEANWGDTVKVHVTNRMQD
NGTAIHFHGVRQLNNNQMDGVTALTQCPVPPGSSYTYVWKAEQYGSSWYHSHFSLQAWEG
VYGGIVIHGPSTADYDQDLGVLFLSDWLHETYYSYYQEDLNSGRLPTMVTGLLNGTNIWV
PKHGPTVGQRFQTTFVPGRRYRIRLVNTAMHTQFKFSIDNHDLTVIAADFVPMVPFKTNH
VPIGMGQRYDIIVTANQRPDNYWIRAMPQSYCSNNTAADNIKGILRYRGSNPSSDPRSTK
WNYGGDVDCQDFPTSTLVPKLALNADLGEANTVTSDTGIGGIGKPPIYLWKMGGEIFNTS
WSDPTLLQTSDAPKKSSWEPGQGVIQASVADQWTVLIIQTTIPAVHPIHLHGHDFYILAQ
GLGTYDPSTVKLQTENPTRRDTLNLPAANGKGGYVVIGFEADNPGAWLIHCHIGFHAAEG
FAQQIIERQNEFEEFLDRDVLEETCNAWNEWAETNPYGFQHRGDHGPYESGI

Enzyme Prediction     

EC	1.10.3.2:1	-

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	57	363	1.4e-131	0.9807692307692307

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
274556	laccase	1.78e-77	69	542	3	514	laccase, plant. Members of this protein family include the copper-containing enzyme laccase (EC 1.10.3.2), often several from a single plant species, and additional, uncharacterized, closely related plant proteins termed laccase-like multicopper oxidases. This protein family shows considerable sequence similarity to the L-ascorbate oxidase (EC 1.10.3.3) family. Laccases are enzymes of rather broad specificity, and classification of all proteins scoring about the trusted cutoff of this model as laccases may be appropriate.
259923	CuRO_1_MaLCC_like	1.48e-72	67	188	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	8.91e-66	69	536	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.
259947	CuRO_2_MaLCC_like	3.51e-65	199	361	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.
225043	SufI	6.50e-63	84	546	48	447	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].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CAK40046.1|AA1_3|1.10.3.2	1.36e-300	3	592	4	594
BCS01335.1|AA1_3	2.60e-298	3	592	4	594
BCS13078.1|AA1_3	5.34e-296	39	592	2	558
BCR86101.1|AA1_3	1.13e-266	1	592	7	586
UDD65566.1|AA1_3	1.91e-244	13	592	10	580

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5LWX_A	1.30e-297	39	592	21	577	Crystal structure of the H253D mutant of McoG from Aspergillus niger [Aspergillus niger]
5LM8_A	1.32e-297	49	592	3	549	Crystal structure of a laccase-like multicopper oxidase McoG from from Aspergillus niger [Aspergillus niger]
5LWW_A	1.37e-297	49	592	4	550	Crystal structure of a laccase-like multicopper oxidase McoG from Aspergillus niger bound to zinc [Aspergillus niger]
3V9E_A	8.09e-146	28	574	31	570	Structure of the L499M mutant of the laccase from B.aclada [Botrytis aclada]
3SQR_A	8.09e-146	28	574	31	570	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	2.02e-160	28	577	22	554	Laccase-1 OS=Botryotinia fuckeliana OX=40559 GN=lcc1 PE=2 SV=3
sp|J5JH35|OPS5_BEAB2	4.24e-156	45	574	49	579	Oxidoreductase OpS5 OS=Beauveria bassiana (strain ARSEF 2860) OX=655819 GN=OpS5 PE=1 SV=1
sp|Q96WM9|LAC2_BOTFU	5.30e-149	25	574	28	571	Laccase-2 OS=Botryotinia fuckeliana OX=40559 GN=lcc2 PE=2 SV=1
sp|Q0CCX6|GEDJ_ASPTN	3.09e-117	29	571	21	585	Dihydrogeodin oxidase OS=Aspergillus terreus (strain NIH 2624 / FGSC A1156) OX=341663 GN=gedJ PE=1 SV=1
sp|Q96UM2|LAC3_BOTFU	4.52e-116	98	544	1	451	Laccase-3 (Fragment) OS=Botryotinia fuckeliana OX=40559 GN=lcc3 PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000289	0.999698	CS pos: 16-17. Pr: 0.9703

TMHMM  Annotations     

There is no transmembrane helices in RAK77866.1.