CAZyme Information: EKG16565.1

Basic Information

• Species: Macrophomina phaseolina
• Lineage: Ascomycota; Dothideomycetes; ; Botryosphaeriaceae; Macrophomina; Macrophomina phaseolina
• CAZyme ID: EKG16565.1
• CAZy Family: GH3
• CAZyme Description: Multicopper oxidase type 1

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1105	AHHD01000267|CGC3	123500.02	5.0280

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=AHHD01000267:377182-382072(-)

Full Sequence      

MDGIPSVSSCPIAPNNTFVYTFKADLYGTGWYHSHYSGQSTGGLLGPIVVHGPSALDYDI
DLGPVFLNDWYHKDYLQLIDGVVGTDPSLWHPKADNNMINGKMDYDCSLVTDGTPCVSNA
GLATFSFTKGATHRLRLINGGSASLQHFSIDGHEMTVISNDFVAVEPYQTKTVTLAVGQR
TDVLVTANGDATGAYWMRSTVADDESCNWSNQPAALAAVYYDAANPTVKPNSTGWPPVAN
QQGSCDNDPLTQTIPLFPIPADPSPSTTLELDFGWTQNATGHQVWTVNDRGFRGNYNRPV
LQLAAGSDTASSAYAWEPEWNVYDTGRNRTVRIVMHNNSSMYHPMHLHGHNAQILAAGAN
GPWDGRTVARPANPARRDVYQLPPNGHLVIQKPSSGDSFVDVASTTTDSNADAIPQSTDD
APPKKIKGGVAEIRTLYEGPHDEEDNWEYQAEYPADLIRKGPALSKVPPNALYSLVVREE
RTGLRSKPLRPASVTVQSPHVKRVLATLFADYHNVGEMRRLRNPVFAPPFRELYDVWPAF
EEAVDAAERKREERGDGEEDAAAAAEHLRLFHSLVARDVRRLRAKQLPLDRQQKATFDTL
FTYFRPGQVVYHKEEAGYDRFFKVIRTEYSASQRPQTFTVDYVELEWDGVRLGWNRHSKS
FWRFPGAKKVAELSMFPAELHPEYERIRAHLLARGRRWAAMRKPTTVEYEGPTPETIEAD
RWGRGGGTRMVKGRVVIDPAAYEAYGSRSIYLRSMDECSEYFKPELQLDSGEDDDEDDEE
ITKPEPGDDSSSESDDEEFQDEGKDGENEEVKPEDKPLDDDLVVLASHVIHGCYLKTKAW
VDLYIDLANPVPWNHDAFDRLVLPGRYKEMILAFVESQATNRDVFDDVIEGKGQGIIMLL
HGAPGLGKTLTAEAVSDRLKKPLYSVQAGELGSDASDVETKLEQILEIAAKWDAVLLLDE
ADVFLEQRSHSNLKRSKIVSVFLRLLEYYRGILFLTTNRVETFDKAFRSRIHMRINYPGL
TTEAKTGIWNNFIEASKKKNESSISAEDIAELAKLPFNGREIKNMVKTGQLLASREQQPL
AMRHFRVCMDVMEDLVGDNAEESTA

Enzyme Prediction     

EC	1.10.3.2:2	-

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	1	236	1e-77	0.717948717948718

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
259947	CuRO_2_MaLCC_like	1.24e-57	62	237	1	165	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.
259968	CuRO_3_MaLCC_like	1.07e-52	258	394	1	132	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.
225043	SufI	5.14e-44	1	390	99	418	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].
274555	ascorbase	1.75e-41	2	359	71	460	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.
215324	PLN02604	8.35e-40	2	358	94	482	oxidoreductase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QFF92556.1|AA1_3	8.95e-133	1	391	146	527
ATZ46043.1|AA1_3	5.11e-131	1	391	146	527
QFF92555.1|AA1_3	1.40e-130	1	391	146	527
QSZ30962.1|AA1_3	1.12e-129	1	391	146	528
UKZ56777.1|AA1_3	4.88e-129	2	391	145	521

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3SQR_A	5.22e-60	2	390	137	512	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]
3V9E_A	5.22e-60	2	390	137	512	Structure of the L499M mutant of the laccase from B.aclada [Botrytis aclada]
5LM8_A	3.79e-50	1	394	92	478	Crystal structure of a laccase-like multicopper oxidase McoG from from Aspergillus niger [Aspergillus niger]
5LWW_A	3.86e-50	1	394	93	479	Crystal structure of a laccase-like multicopper oxidase McoG from Aspergillus niger bound to zinc [Aspergillus niger]
5LWX_A	6.23e-50	1	394	120	506	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	6.68e-105	2	390	133	518	Oxydoreductase ptaK OS=Pestalotiopsis fici (strain W106-1 / CGMCC3.15140) OX=1229662 GN=ptaK PE=2 SV=2
sp|Q96WM9|LAC2_BOTFU	6.93e-63	2	390	138	513	Laccase-2 OS=Botryotinia fuckeliana OX=40559 GN=lcc2 PE=2 SV=1
sp|J5JH35|OPS5_BEAB2	8.37e-63	2	389	143	520	Oxidoreductase OpS5 OS=Beauveria bassiana (strain ARSEF 2860) OX=655819 GN=OpS5 PE=1 SV=1
sp|Q12570|LAC1_BOTFU	5.05e-56	2	390	132	491	Laccase-1 OS=Botryotinia fuckeliana OX=40559 GN=lcc1 PE=2 SV=3
sp|Q96UM2|LAC3_BOTFU	3.36e-51	2	390	42	424	Laccase-3 (Fragment) OS=Botryotinia fuckeliana OX=40559 GN=lcc3 PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000008	0.000016

TMHMM  Annotations     

There is no transmembrane helices in EKG16565.1.