CAZyme Information: EKG09647.1

Basic Information

• Species: Macrophomina phaseolina
• Lineage: Ascomycota; Dothideomycetes; ; Botryosphaeriaceae; Macrophomina; Macrophomina phaseolina
• CAZyme ID: EKG09647.1
• CAZy Family: AA1
• CAZyme Description: Multicopper oxidase type 1

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
617		67856.65	4.8682

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_MphaseolinaMS6	14712	1126212	906	13806

• Gene Location: location=AHHD01000582:88154-90200(-)

Full Sequence      

MPFSPRLSICLLAFCSHIVFALSIPNVKDRTPHLSPRNYGFRFGNLSWGGAEPSDPLAQG
AERLDDISLPAPEDGCLFSKDARNCWRDNFNIDTDFDERFPTTGKTVTYNLEITNTTMAP
DGIERVVMAVNGQYPGPTLIADWGDTMVINVKNSLDHNGTGLHFHGLRQYKSNGADGANG
ITECPIAPGETKTYTFQCTQHGSSWYHSHYSVQYSDGVLGGIIINGPADAHYDHDLGVYM
LSDWYHTPMFELAEAARHSTRGPPKADNGLINGTMKSPDGSLGAYGQIHVKKGLRYRIRV
MNVGTNDHYLFSVDGHNLTVIASDFVPVVPFSASSISLGVGQRYDVILIADQDIDNYWIR
SDPDSACSVNGNAGNIKAILSYDTAPADAQPNSTRHSISSGCKDMAVVPRVANTVPSDRF
ADAVQSLAMSVNITQQNGPLVQWYINGSAMEVDWSYPTVQYVLDGNTSYPRELNLVQLDE
ADQWYYFVIQTVQGLRVNLPHPIHLHGHDFYILGAGPGEWDGNIDGLQFDNPPRRDTAML
PAGGYLILAFPADNPGAWLMHCHIPFHVQQGFGLQFLERPDEIEGVMGDTSPFYNECAAW
KDYYGGGQAFQQSDSGL

Enzyme Prediction     

EC	1.10.3.2:4	1.10.3.-:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	94	402	9.8e-126	0.9935897435897436

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
274555	ascorbase	3.09e-81	109	583	4	528	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	5.89e-78	103	583	20	551	L-ascorbate oxidase
259968	CuRO_3_MaLCC_like	3.21e-75	421	577	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.
259923	CuRO_1_MaLCC_like	1.08e-69	104	225	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.
259947	CuRO_2_MaLCC_like	7.04e-69	236	400	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ATZ47489.1|AA1_3	4.20e-208	67	617	102	663
CCD50266.1|AA1_3	4.20e-208	67	617	102	663
QQP64015.1|AA1_3	1.10e-205	67	617	102	663
ALR81978.1|AA1_3	1.64e-204	67	617	111	671
QSZ31194.1|AA1_3	1.74e-204	67	617	60	621

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3V9E_A	8.80e-155	76	617	39	580	Structure of the L499M mutant of the laccase from B.aclada [Botrytis aclada]
3SQR_A	8.80e-155	76	617	39	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]
6F5K_A	3.65e-151	83	617	10	559	Crystal structure of laccase from Myceliophthora thermophila [Thermothelomyces thermophilus]
5LWX_A	5.83e-149	68	603	13	556	Crystal structure of the H253D mutant of McoG from Aspergillus niger [Aspergillus niger]
3PPS_A	1.36e-148	83	617	51	604	Crystal structure of an ascomycete fungal laccase from Thielavia arenaria [Canariomyces arenarius],3PPS_B Crystal structure of an ascomycete fungal laccase from Thielavia arenaria [Canariomyces arenarius],3PPS_C Crystal structure of an ascomycete fungal laccase from Thielavia arenaria [Canariomyces arenarius],3PPS_D Crystal structure of an ascomycete fungal laccase from Thielavia arenaria [Canariomyces arenarius]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q96UM2|LAC3_BOTFU	3.82e-179	135	576	1	452	Laccase-3 (Fragment) OS=Botryotinia fuckeliana OX=40559 GN=lcc3 PE=3 SV=1
sp|Q96WM9|LAC2_BOTFU	6.61e-154	76	617	39	581	Laccase-2 OS=Botryotinia fuckeliana OX=40559 GN=lcc2 PE=2 SV=1
sp|Q70KY3|LAC1_MELAO	5.65e-146	51	617	23	609	Laccase-1 OS=Melanocarpus albomyces OX=204285 GN=LAC1 PE=1 SV=1
sp|P78722|LAC2_PODAS	1.06e-145	83	617	55	605	Laccase-2 OS=Podospora anserina OX=2587412 GN=LAC2 PE=2 SV=1
sp|Q12570|LAC1_BOTFU	3.65e-145	42	617	11	561	Laccase-1 OS=Botryotinia fuckeliana OX=40559 GN=lcc1 PE=2 SV=3

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000388	0.999600	CS pos: 21-22. Pr: 0.9819

TMHMM  Annotations     

There is no transmembrane helices in EKG09647.1.