CAZyme Information: EKG20709.1

Basic Information

• Species: Macrophomina phaseolina
• Lineage: Ascomycota; Dothideomycetes; ; Botryosphaeriaceae; Macrophomina; Macrophomina phaseolina
• CAZyme ID: EKG20709.1
• CAZy Family: GT2
• CAZyme Description: Cupredoxin

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
347	AHHD01000080|CGC1	38735.44	6.6604

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=AHHD01000080:44904-46125(+)

Full Sequence      

MDSKYEIIPSAPDITPDTPKKRNLLKALSSFSAVLLCVGGVAKYYLHRPVFEFDRAPNSA
GHAQLKGLPERVPATVNYNLTISQAWRNPDGGHWRPLFVGNSESPFPTINAHEGDMVNIH
IHNDLGLPISAHWVGVHHKMGGTWNDGSSGVTSYPILPRANRTSTFNTSGDWGLKWFLEH
TSTPSVDGMYGAIWIRPSAERERPYHLISDDPLDIQDMMEAEENPAHVTAYNYQHREMPG
LLAQLQTEGYDPYCFQSILINGRNFFFLARRECGSSHLTGKGRVHCKPDDLKDIDGKPVD
SYGCVEQPSGAVAYDECKPSDGDYEVFAKQDGYAKASGLIYRRLSRR

Enzyme Prediction     

No EC number prediction in EKG20709.1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	94	267	4.5e-28	0.43575418994413406

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
259919	CuRO_1_Abr2_like	4.64e-26	78	196	1	117	The first cupredoxin domain of a group of fungal Laccases similar to Abr2 from Aspergillus fumigatus. Abr2 is involved in conidial pigment biosynthesis in Aspergillus fumigatus. 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. Laccase 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. Like other related multicopper oxidases (MCOs), 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 1 of 3-domain MCOs contains part the trinuclear copper binding site, which is located at the interface of domains 1 and 3.
259926	CuRO_1_Diphenol_Ox	1.37e-24	78	195	3	118	The first cupredoxin domain of fungal laccase, diphenol oxidase. Diphenol oxidase belongs to the laccase family. It catalyzes the initial steps in melanin biosynthesis from diphenols. Melanin is one of the virulence factors of infectious fungi. In the pathogenesis of C. neoformans, melanin pigments have been shown to protect the fungal cells from oxidative and microbicidal activities of host defense systems. Laccase is a blue multicopper oxidase (MCO) which 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. 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.
400195	Cu-oxidase_3	8.64e-22	81	200	1	119	Multicopper oxidase. This entry contains many divergent copper oxidase-like domains that are not recognized by the pfam00394 model.
259923	CuRO_1_MaLCC_like	3.26e-19	75	195	3	121	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.
259869	CuRO_1_LCC_like	8.88e-18	76	196	1	120	Cupredoxin domain 1 of laccase-like multicopper oxidases; including laccase, CueO, spore coat protein A, ascorbate oxidase and similar proteins. Laccase-like multicopper oxidases (MCOs) in this family contain three cupredoxin domains. They are able to couple oxidation of substrates with reduction of dioxygen to water. MCOs are capable of oxidizing a vast range of substrates, varying from aromatic to inorganic compounds such as metals. Although the members of this family have diverse functions, majority of them have three cupredoxin domain repeats. 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. Also included in this family are cupredoxin domains 1, 3, and 5 of the 6-domain MCO ceruloplasmin and similar proteins.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
SMR53096.1|AA1	5.84e-120	4	331	9	307
SMR54715.1|AA1	6.71e-120	4	331	14	312
SMY24838.1|AA1	6.71e-120	4	331	14	312
SMQ51193.1|AA1	6.71e-120	4	331	14	312
QBZ57870.1|AA1	3.77e-69	78	326	75	303

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3PPS_A	9.54e-13	75	262	74	243	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]
4E9V_A	5.75e-10	74	197	2	126	Multicopper Oxidase mgLAC (data1) [uncultured bacterium],4E9V_B Multicopper Oxidase mgLAC (data1) [uncultured bacterium],4E9V_C Multicopper Oxidase mgLAC (data1) [uncultured bacterium],4E9W_A Multicopper Oxidase mgLAC (data2) [uncultured bacterium],4E9W_B Multicopper Oxidase mgLAC (data2) [uncultured bacterium],4E9W_C Multicopper Oxidase mgLAC (data2) [uncultured bacterium],4E9X_A Multicopper Oxidase mgLAC (data3) [uncultured bacterium],4E9X_B Multicopper Oxidase mgLAC (data3) [uncultured bacterium],4E9X_C Multicopper Oxidase mgLAC (data3) [uncultured bacterium],4E9Y_A Multicopper Oxidase mgLAC (data4) [uncultured bacterium],4E9Y_B Multicopper Oxidase mgLAC (data4) [uncultured bacterium],4E9Y_C Multicopper Oxidase mgLAC (data4) [uncultured bacterium]
5LM8_A	5.07e-09	95	272	42	199	Crystal structure of a laccase-like multicopper oxidase McoG from from Aspergillus niger [Aspergillus niger]
5LWW_A	5.08e-09	95	272	43	200	Crystal structure of a laccase-like multicopper oxidase McoG from Aspergillus niger bound to zinc [Aspergillus niger]
5LWX_A	5.21e-09	95	272	70	227	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|W3X732|PFMAY_PESFW	1.80e-43	78	333	25	263	Laccase PFICI_06862 OS=Pestalotiopsis fici (strain W106-1 / CGMCC3.15140) OX=1229662 GN=PFICI_06862 PE=3 SV=1
sp|E9RBR0|ABR2_ASPFU	2.70e-27	74	267	18	208	Laccase abr2 OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=abr2 PE=1 SV=1
sp|A0A1S7IUL2|MCE_TALPI	1.26e-21	65	279	12	224	Multicopper oxidase MCE OS=Talaromyces pinophilus OX=128442 GN=MCE PE=1 SV=1
sp|E9E686|MLAC1_METAQ	1.39e-20	75	298	22	254	Laccase 1 OS=Metarhizium acridum (strain CQMa 102) OX=655827 GN=Mlac1 PE=3 SV=2
sp|A0A0B4HQH6|MLAC1_METMF	8.31e-20	75	323	23	249	Laccase 1 OS=Metarhizium majus (strain ARSEF 297) OX=1276143 GN=Mlac1 PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
0.993857	0.006156

TMHMM  Annotations     

There is no transmembrane helices in EKG20709.1.