CAZyme Information: EKG15345.1

Basic Information

• Species: Macrophomina phaseolina
• Lineage: Ascomycota; Dothideomycetes; ; Botryosphaeriaceae; Macrophomina; Macrophomina phaseolina
• CAZyme ID: EKG15345.1
• CAZy Family: GH18
• CAZyme Description: Multicopper oxidase type 1

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
355	AHHD01000302|CGC1	38302.36	4.4431

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=AHHD01000302:66814-67979(-)

Full Sequence      

MAMGTKYMETNTKESMRMESMALDTTSMEHHMRRMDSMSAEDMSMNTMTAHSTPAAAPDS
GMPMGSMSMASLPVSGISGTSGLSGMSNMASGPLGPRGCSAPMMFRPGYNISSLPPETCT
DTSAPLLTVDANYTRGWLALNLVNSGSVTKLSVSLDAHSMFVYAADGFFVKPQEVEVLQI
SIGQRYSVMIKLNQRPGNYTLRFASYPYGDMQQVIEGQATVSYKVDAAEDIMPVDLTNDP
TATWMLVNGSAKSNASELKTDMLAPFEAIAPPSQADITYDFTISQTEIVTWVLNGYPYSE
PSTPIIYGNASEAWNANTTIRIPSNSTVDIIMRIANDSMDTASCSPGRRQNACIS

Enzyme Prediction     

No EC number prediction in EKG15345.1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	139	338	3.1e-20	0.4441340782122905

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
259944	CuRO_2_Abr2_like	8.19e-38	127	224	44	138	The second 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 2 of 3-domain MCOs has lost the ability to bind copper.
259868	CuRO_2_LCC_like	4.34e-20	106	223	39	152	Cupredoxin domain 2 of laccase-like multicopper oxidases; including laccase, CueO, spore coat protein A, ascorbate oxidase and similar proteins. Laccase-like multicopper oxidases (MCOs) 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 compounds 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 2 of 3-domain MCOs has lost the ability to bind copper.
395317	Cu-oxidase	6.11e-16	142	202	64	124	Multicopper oxidase. Many of the proteins in this family contain multiple similar copies of this plastocyanin-like domain.
259953	CuRO_2_MCO_like_1	4.04e-15	120	202	57	137	The second cupredoxin domain of uncharacterized multicopper oxidase. Multicopper Oxidases (MCOs) are multi-domain enzymes that are able to couple oxidation of substrates with reduction of dioxygen to water. MCOs oxidise their substrate by accepting electrons at a mononuclear copper centre and transferring them to a trinuclear copper centre which binds a dioxygen. The dioxygen, following the transfer of four electrons, is reduced to two molecules of water. These MCOs are capable of oxidizing a vast range of substrates, varying from aromatic to inorganic compounds such as metals. This family of MCOs 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.
259951	CuRO_2_tcLCC_insect_like	3.66e-12	115	223	43	150	The second cupredoxin domain of the insect laccases similar to laccase 2 in Tribolium castaneum. This multicopper oxidase (MCO) subfamily includes the majority of insect laccases. One member is laccase 2 from Tribolium castaneum, which is required for beetle cuticle tanning. Laccase (polyphenol oxidase EC 1.10.3.2) is a blue multi-copper enzyme that catalyzes the oxidation of a variety of organic substrates coupled to the reduction of molecular oxygen to water. It displays broad substrate specificity, catalyzing the oxidation of a wide variety of aromatic - notably phenolic and inorganic substances. 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, plants and insects. 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
QLI72976.1|AA1	5.74e-99	97	341	315	560
QOD95012.1|AA1	2.36e-98	97	340	300	547
UPL00042.1|AA1	2.67e-92	97	341	301	544
ATY66532.1|AA1	3.77e-91	97	341	305	551
QPG98040.1|AA1	4.00e-90	97	341	304	547

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1V10_A	5.33e-11	110	330	183	409	Chain A, Laccase [Rigidoporus microporus]
2QT6_A	1.59e-08	111	330	171	381	Chain A, Laccase [Lentinus tigrinus],2QT6_B Chain B, Laccase [Lentinus tigrinus]
1A65_A	6.66e-08	140	332	197	387	Chain A, Laccase [Coprinopsis cinerea]
1HFU_A	6.66e-08	140	332	197	387	Chain A, LACCASE 1 [Coprinopsis cinerea]
4JHU_A	1.55e-07	154	347	211	391	T2-depleted laccase from Coriolopsis caperata soaked with CuCl [Coriolopsis caperata],4JHV_A T2-depleted laccase from Coriolopsis caperata [Coriolopsis caperata]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|W3X732|PFMAY_PESFW	7.08e-23	117	298	245	421	Laccase PFICI_06862 OS=Pestalotiopsis fici (strain W106-1 / CGMCC3.15140) OX=1229662 GN=PFICI_06862 PE=3 SV=1
sp|P17489|LAC1_EMENI	2.86e-20	109	340	256	502	Laccase-1 OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=yA PE=2 SV=3
sp|A0A1S7IUL2|MCE_TALPI	1.25e-19	105	336	252	482	Multicopper oxidase MCE OS=Talaromyces pinophilus OX=128442 GN=MCE PE=1 SV=1
sp|Q0UHZ8|ELCG_PHANO	2.32e-19	97	334	259	503	Multicopper oxidase elcG OS=Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) OX=321614 GN=elcG PE=1 SV=1
sp|A0A4Y6F0M8|USTL_USTVR	3.42e-18	119	335	270	490	Laccase ustL OS=Ustilaginoidea virens OX=1159556 GN=ustL PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000062	0.000000

TMHMM  Annotations     

There is no transmembrane helices in EKG15345.1.