CAZyme Information: GBF62523.1

Basic Information

• Species: Trichophyton mentagrophytes
• Lineage: Ascomycota; Eurotiomycetes; ; Arthrodermataceae; Trichophyton; Trichophyton mentagrophytes
• CAZyme ID: GBF62523.1
• CAZy Family: GH16
• CAZyme Description: laccase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
638	BFBS01016101|CGC1	72211.57	6.2781

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=BFBS01016101:347-2699(-)

Full Sequence      

MRLNYLLNIGFFAPCALSLSVPRWKDTLSGPSFSPPPNVDSNSRVIECKYPSMNGWVADN
SSKTGWLKWVGNGPTPSPGAFNITTDYENIFPEGVTRKYNLVVDEGTVNLDGVTANHAML
FNGQYPGPWIQACWGDIVEITVTNKLKYNGTALHCHGLRMFDNLLMDGVPGVTQCPIAPE
DTFTYRFRATQYGSTWYHSHYSLQYSDGLVGPLTIHGPSSAEYDASIDPLLLGDHLHRSA
FQDYYKVQTRIPPEMDSQILNGIGNYNNDTSRRPYTTLVKAGKKYLMRLINTSTDTTFVF
SIDKHNFTVIGADLVPLEPYDTSHILIGIGQRYHVILNTLPDVKDGDSFWIRMVPAGDGC
SRFRKDHVPDERMGALYYEKKTNVLPKSEGGGYDISCRDEPYERLKPIQKWTVPDPLLAP
DLMTKTQKIGIDIWNPPGRPADAPKIANWGVGPQPMWLNYSKPIVKNMDIEDWPETWTVY
PANDYTHEQWVYLVVTGQEKQAELARTQAPNAHPLHFHGHDFALLQQSYEPFNNKNLNLK
LDNPPRRDVVLLPSNGFVVIAFKADNPGSWLMHCHIAWHASAGLALQILEDKNDVVKYLK
SHPEDVKEMRRVCDNWDKWYGNAENHYPAEFFQEDSGI

Enzyme Prediction     

EC	1.10.3.2:4	1.10.3.-:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	85	397	2.5e-118	0.9935897435897436

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
259923	CuRO_1_MaLCC_like	2.26e-70	94	216	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	6.59e-57	440	589	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.
225043	SufI	1.18e-55	107	588	46	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	5.45e-53	119	597	45	553	L-ascorbate oxidase
259947	CuRO_2_MaLCC_like	5.32e-52	229	389	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QKX62792.1|AA1_3	1.20e-212	27	638	41	661
UPK95500.1|AA1_3	6.94e-212	31	638	43	651
AHZ65141.1|AA1_3	1.39e-211	31	638	43	651
QKD58662.1|AA1_3	8.40e-210	31	638	47	659
QGI68425.1|AA1_3	1.96e-205	31	638	47	658

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3SQR_A	2.52e-123	79	638	50	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	5.01e-123	79	638	50	580	Structure of the L499M mutant of the laccase from B.aclada [Botrytis aclada]
5LWX_A	9.45e-112	60	638	23	577	Crystal structure of the H253D mutant of McoG from Aspergillus niger [Aspergillus niger]
5LM8_A	9.16e-111	75	638	2	549	Crystal structure of a laccase-like multicopper oxidase McoG from from Aspergillus niger [Aspergillus niger]
5LWW_A	9.43e-111	75	638	3	550	Crystal structure of a laccase-like multicopper oxidase McoG from Aspergillus niger bound to zinc [Aspergillus niger]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|D4APX3|LAC1_ARTBC	1.96e-247	31	638	34	633	Laccase ARB_05828 OS=Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) OX=663331 GN=ARB_05828 PE=1 SV=1
sp|A0A067XMP0|PTAE_PESFW	2.66e-127	81	638	40	610	Oxidoreductase ptaE OS=Pestalotiopsis fici (strain W106-1 / CGMCC3.15140) OX=1229662 GN=ptaE PE=2 SV=2
sp|Q0CCX6|GEDJ_ASPTN	1.57e-124	51	638	2	605	Dihydrogeodin oxidase OS=Aspergillus terreus (strain NIH 2624 / FGSC A1156) OX=341663 GN=gedJ PE=1 SV=1
sp|Q96WM9|LAC2_BOTFU	2.40e-123	79	638	50	581	Laccase-2 OS=Botryotinia fuckeliana OX=40559 GN=lcc2 PE=2 SV=1
sp|J5JH35|OPS5_BEAB2	1.93e-121	79	638	55	590	Oxidoreductase OpS5 OS=Beauveria bassiana (strain ARSEF 2860) OX=655819 GN=OpS5 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000235	0.999724	CS pos: 18-19. Pr: 0.9781

TMHMM  Annotations     

There is no transmembrane helices in GBF62523.1.