CAZyme Information: GBF66802.1

Basic Information

• Species: Trichophyton mentagrophytes
• Lineage: Ascomycota; Eurotiomycetes; ; Arthrodermataceae; Trichophyton; Trichophyton mentagrophytes
• CAZyme ID: GBF66802.1
• CAZy Family: GT62
• CAZyme Description: laccase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
652	BFBS01016519|CGC1	73706.44	6.9439

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_TmentagrophytesTIMM2789	7958	N/A	98	7860

• Gene Location: location=BFBS01016519:106893-109274(-)

Full Sequence      

MKSLNLIPRSSLKRLGLAALYIGSALAWPEPHGAPSRNVPRDDFPLFNPLPSTDLNTRLI
RCEYPSMKGWTYSNKKNGDWLKYVGSKPGDITEYNIDTDNDKYVPQGITRKYHLEVTDES
VNMDGTMFDQAKVFNKQYPGPWIQACWGDDLEITVTNKLKHNGTAIHWHGIRMMENMFND
GVPGVTQCPIPPGSSMTYRFKASQYGSSWYHSHYSLQYADGLFGPMTIHGPTSAGYDKAV
DPLLMTDHLHSSAFEEYHKELEGKPPLMDSIILNGKGDYDQTGDLKKKYRTVLRPGKKYL
LRLINTSVATTFVFSIDGHKFQVVGSDFVPIEPYVTDHIAVGTGQRYHIILEGLSEEEAR
KNGRYWVRTTPAKGCSKFAPGRGTDDRTGVIYYNKDDGVSPTTEIGAFSLDCRDEPLEKL
VPKVKWTVPDPGLNMVGAFEKPADVQLGKWHRPGYPDTGNLVSNWEFGPSPMWINYSEPI
IKNLDKESFPSTWVVYPADNYVNDKWVYLVITGKKLKQLSSQVAVAHPIHLHGHDFVLLQ
QSMEPWDSTKVNLKLDNPPRRDVTLLPAGGFIVIAFKPDNPGSWLLHCHIAWHVSAGLAL
QVLERKEDLKALTVNNPDFDFMQENCRRWDAWHSDKTNYWNPSGHFQDDSGV

Enzyme Prediction     

EC	1.10.3.2:4	1.10.3.-:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	100	412	2e-122	0.9871794871794872

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
259923	CuRO_1_MaLCC_like	1.40e-69	107	229	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.
259968	CuRO_3_MaLCC_like	6.86e-62	454	603	17	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.
259947	CuRO_2_MaLCC_like	2.60e-59	242	404	3	160	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.
225043	SufI	1.31e-54	131	602	54	446	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].
177843	PLN02191	1.27e-50	135	604	48	546	L-ascorbate oxidase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
UPK95500.1|AA1_3	5.25e-210	37	652	37	651
QKD58662.1|AA1_3	1.66e-205	32	652	39	659
AHZ65141.1|AA1_3	2.05e-204	37	652	37	651
QKX62792.1|AA1_3	8.14e-204	34	652	37	661
CCT71494.1|AA1_3	1.83e-199	36	652	43	659

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3SQR_A	1.63e-128	93	652	51	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]
3V9E_A	3.24e-128	93	652	51	580	Structure of the L499M mutant of the laccase from B.aclada [Botrytis aclada]
5LM8_A	2.88e-113	94	645	7	536	Crystal structure of a laccase-like multicopper oxidase McoG from from Aspergillus niger [Aspergillus niger]
5LWW_A	2.97e-113	94	645	8	537	Crystal structure of a laccase-like multicopper oxidase McoG from Aspergillus niger bound to zinc [Aspergillus niger]
5LWX_A	6.50e-113	94	645	35	564	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|D4APX3|LAC1_ARTBC	0.0	12	652	1	633	Laccase ARB_05828 OS=Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) OX=663331 GN=ARB_05828 PE=1 SV=1
sp|Q96WM9|LAC2_BOTFU	5.65e-132	93	652	51	581	Laccase-2 OS=Botryotinia fuckeliana OX=40559 GN=lcc2 PE=2 SV=1
sp|J5JH35|OPS5_BEAB2	1.44e-128	93	652	56	590	Oxidoreductase OpS5 OS=Beauveria bassiana (strain ARSEF 2860) OX=655819 GN=OpS5 PE=1 SV=1
sp|Q0CCX6|GEDJ_ASPTN	2.76e-126	97	652	47	605	Dihydrogeodin oxidase OS=Aspergillus terreus (strain NIH 2624 / FGSC A1156) OX=341663 GN=gedJ PE=1 SV=1
sp|Q12570|LAC1_BOTFU	3.98e-123	93	652	49	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
0.016562	0.983405	CS pos: 27-28. Pr: 0.9469

TMHMM  Annotations     

There is no transmembrane helices in GBF66802.1.