CAZyme Information: PWY74296.1

Basic Information

• Species: Aspergillus heteromorphus
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus heteromorphus
• CAZyme ID: PWY74296.1
• CAZy Family: CE8
• CAZyme Description: multicopper oxidase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
584	MSFL01000023|CGC1	64294.76	4.7163

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AheteromorphusCBS117.55	11436	1448321	306	11130

• Gene Location: location=MSFL01000023:80690-82647(-)

Full Sequence      

MVHLVPFLGMAGAAVASLSQLATNGHSTWGTLPSPNLPQFLTDGTSDLEPPWGNVDPAGP
PPTTGVTRHYNFTITRGFKFPDGFNKSVILVNDQFPGPLIEANWGDIISVAVTNNIDSQD
EGVTLHWHGLTQRNTPWNDGVPGVSQCPIAPRGASSFTYIFQADQYGTGWYHSHFSAQYD
DGLYGPMVIHGPLQSEITYDHDLGPVMISDYYRIGYSELLELSFSDPPRTVRADDNLING
KGVYDCNATEVDDQCLAGAGRARFQFQSGKLHRLRLINTGSLANQKFSIDGHELTVIAND
YVPLKPYTTRVVTLGPGQRTDIIVNATGSPTDVAWMRSDMDMACSENSTTTATHTALAAI
YYESANTTLLPRTNGTTWESNNYRNDPLDLTVPYYPLIPPEPETTQTVTITVSYNATTFA
MFMDGSSFQADYSEPALLSINEGNLSLPISRNIYNFGSNSTVRLILNNTDSTPHPMHLHG
HNFWVLAEGIGAWNGSITNPENPLRRDTHILQPGTVDAPSYLVLQWTQDNPGVWPLHCHM
ALHARAGMVMLVLERPDDFAAEFLSVPLATAETCRDWDVFRREV

Enzyme Prediction     

EC	1.10.3.2:2	-

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	62	378	4.5e-109	0.9583333333333334

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
274555	ascorbase	1.94e-73	67	548	1	517	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.
259923	CuRO_1_MaLCC_like	1.63e-66	65	190	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.
177843	PLN02191	4.84e-64	64	554	20	546	L-ascorbate oxidase
215324	PLN02604	2.79e-61	61	548	18	540	oxidoreductase
259968	CuRO_3_MaLCC_like	1.47e-56	397	553	1	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QKX63435.1|AA1_3	4.33e-290	22	580	15	571
CAK48652.1|AA1_3	3.24e-272	51	580	105	635
BCS07898.1|AA1_3	3.63e-238	24	580	27	589
BCR95349.1|AA1_3	1.20e-237	25	580	52	613
QGA18227.1|AA1_3	1.92e-226	1	580	3	572

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3V9E_A	1.22e-95	44	580	50	567	Structure of the L499M mutant of the laccase from B.aclada [Botrytis aclada]
3SQR_A	3.39e-95	44	580	50	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]
5LM8_A	1.88e-92	62	582	18	530	Crystal structure of a laccase-like multicopper oxidase McoG from from Aspergillus niger [Aspergillus niger]
5LWW_A	1.93e-92	62	582	19	531	Crystal structure of a laccase-like multicopper oxidase McoG from Aspergillus niger bound to zinc [Aspergillus niger]
5LWX_A	5.53e-92	62	582	46	558	Crystal structure of the H253D mutant of McoG from Aspergillus niger [Aspergillus niger]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|A0A067XMP2|PTAK_PESFW	3.90e-156	35	577	23	569	Oxydoreductase ptaK OS=Pestalotiopsis fici (strain W106-1 / CGMCC3.15140) OX=1229662 GN=ptaK PE=2 SV=2
sp|J5JH35|OPS5_BEAB2	1.36e-108	62	580	68	576	Oxidoreductase OpS5 OS=Beauveria bassiana (strain ARSEF 2860) OX=655819 GN=OpS5 PE=1 SV=1
sp|Q96WM9|LAC2_BOTFU	1.00e-97	62	580	63	568	Laccase-2 OS=Botryotinia fuckeliana OX=40559 GN=lcc2 PE=2 SV=1
sp|Q12570|LAC1_BOTFU	8.43e-89	52	577	47	545	Laccase-1 OS=Botryotinia fuckeliana OX=40559 GN=lcc1 PE=2 SV=3
sp|A0A067XMP0|PTAE_PESFW	5.20e-84	65	578	55	591	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 SP

Other	SP_Sec_SPI	CS Position
0.055131	0.944862	CS pos: 17-18. Pr: 0.6161

TMHMM  Annotations     

There is no transmembrane helices in PWY74296.1.