CAZyme Information: K441DRAFT_706698-t45_1-p1

Basic Information

• Species: Cenococcum geophilum
• Lineage: Ascomycota; Dothideomycetes; ; Gloniaceae; Cenococcum; Cenococcum geophilum
• CAZyme ID: K441DRAFT_706698-t45_1-p1
• CAZy Family: GT48
• CAZyme Description: laccase-like multicopper oxidase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
574		63338.45	4.0489

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_Cgeophilum1.58	14745	794803	38	14707

• Gene Location: location=KV748207:580559-582654(+)

Full Sequence      

MWPILCHRSVSVDFTGCIYVFWNLLSPYHSFLYPRATCSGNSASDRTVWCDYDISTDYTT
EVPDTGVTREYYFELTEVTVAPDGYSRSALTVNGSIPGPTIEADWGDTVVVHVTNSLTSS
QNGTSIHFHGIRQNFTNQQDGVSSITQCPTAPGDSITYTWRAMQYGSTWYHSHFALQAWE
GVFGGIIINGPATANYDEDKGVLFLTDWSHQTVDELYTSAQVSGPPTLDNGLINGTNVYG
EDDSSSQTGSRFNTSFTAGTSYRLRLVNGAIDTHFKFSIDNHTLMVIANDLVPIVSYNTT
VLNIGIGQRYDVIVTADQSSVADNFWMRAIPQVACSDNDSADNIKGIVYYGSTASTPTTT
AYSYTDSCDDEDVSDLVPYVSKTVSTEYWDEDETVTVGKNSNSLFRWYMNGTSMVVEWND
PTLLQVYNGDTDFTNTSGVIELPEADEWAYVIIETQVAVPHPIHLHGHDFFVLAQGTGTY
DSSVSLSLSNPPRRDTAMLPASGYLVLAFETDNPGAWLMHCHIGWHTAEGFAIQFVERYS
EISALIDYDTLNSTCAAWETYTTANSITEDDSGI

Enzyme Prediction     

EC	-	-

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	56	368	5.4e-133	0.9935897435897436

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
259968	CuRO_3_MaLCC_like	3.52e-79	383	536	2	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.
259923	CuRO_1_MaLCC_like	5.90e-65	66	189	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.
274556	laccase	1.28e-63	68	536	3	518	laccase, plant. Members of this protein family include the copper-containing enzyme laccase (EC 1.10.3.2), often several from a single plant species, and additional, uncharacterized, closely related plant proteins termed laccase-like multicopper oxidases. This protein family shows considerable sequence similarity to the L-ascorbate oxidase (EC 1.10.3.3) family. Laccases are enzymes of rather broad specificity, and classification of all proteins scoring about the trusted cutoff of this model as laccases may be appropriate.
259947	CuRO_2_MaLCC_like	7.13e-63	201	350	2	149	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.
274555	ascorbase	1.79e-61	68	542	1	531	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QKX58305.1|AA1_3	0.0	29	574	24	569
UKZ68800.1|AA1_3	9.37e-313	1	574	2	566
UQC89044.1|AA1_3	3.43e-310	32	574	33	574
UKZ91485.1|AA1_3	3.62e-310	1	574	2	566
UKZ78755.1|AA1_3	5.14e-310	32	574	30	566

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5LWX_A	4.84e-193	29	565	12	560	Crystal structure of the H253D mutant of McoG from Aspergillus niger [Aspergillus niger]
5LM8_A	2.27e-189	46	565	1	532	Crystal structure of a laccase-like multicopper oxidase McoG from from Aspergillus niger [Aspergillus niger]
5LWW_A	2.35e-189	46	565	2	533	Crystal structure of a laccase-like multicopper oxidase McoG from Aspergillus niger bound to zinc [Aspergillus niger]
3V9E_A	1.27e-183	30	574	27	580	Structure of the L499M mutant of the laccase from B.aclada [Botrytis aclada]
3SQR_A	1.27e-183	30	574	27	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q96WM9|LAC2_BOTFU	6.41e-186	36	574	37	581	Laccase-2 OS=Botryotinia fuckeliana OX=40559 GN=lcc2 PE=2 SV=1
sp|Q12570|LAC1_BOTFU	1.85e-172	30	574	29	561	Laccase-1 OS=Botryotinia fuckeliana OX=40559 GN=lcc1 PE=2 SV=3
sp|J5JH35|OPS5_BEAB2	7.20e-158	44	574	49	590	Oxidoreductase OpS5 OS=Beauveria bassiana (strain ARSEF 2860) OX=655819 GN=OpS5 PE=1 SV=1
sp|Q96UM2|LAC3_BOTFU	3.07e-135	97	535	1	452	Laccase-3 (Fragment) OS=Botryotinia fuckeliana OX=40559 GN=lcc3 PE=3 SV=1
sp|Q70KY3|LAC1_MELAO	4.26e-130	32	574	47	609	Laccase-1 OS=Melanocarpus albomyces OX=204285 GN=LAC1 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
0.984741	0.015271

TMHMM  Annotations     

There is no transmembrane helices in K441DRAFT_706698-t45_1-p1.