CAZyme Information: K441DRAFT_687046-t45_1-p1

Basic Information

• Species: Cenococcum geophilum
• Lineage: Ascomycota; Dothideomycetes; ; Gloniaceae; Cenococcum; Cenococcum geophilum
• CAZyme ID: K441DRAFT_687046-t45_1-p1
• CAZy Family: GH93
• CAZyme Description: laccase-like multicopper oxidase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
721	KV748195|CGC2	77715.48	5.0412

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=KV748195:1229339-1231710(-)

Full Sequence      

MVAAAPYVTSAVTLTSVVHYASSYLPVAYNTTRTSVITKTVTVCPCTDSLATLASATYNP
NGPYVNPYDYSSLPFSWPGKPTHGETTPAPLPTAPFPYGGKASGKYEAPAWIPKGYHSLV
PGIPQNGTNGNSQWGDLHCPHLPVDGLPPYGPSSSISGSASASVIGSHSGSPSGIPSISI
SGIPSISISESISASASTSPSSPCGEMPDTGVTRTYDFHVAYQTIAPDGVQKNGITINGG
FPGPLIEANWGDWIMVNVTNDLPNEGTTLHWHGFRQQGTPWYDGVPAVTQCPIIPGNTLS
YLFRADLFGTSWYHSHYSAQYAGGAVGPMVIHGPKTADYDIDIGPVMVSDWYHQDYFTLV
NQTMQGNFPPSNNNLINGKMNYPCENTTLPCTPNAGISKFQFTSGKKHLVRIVNTGAEGT
QKFSIDNHTLTVIANDFIPVVPYTTNVVTVGIGQRTDVIVEGLSNSAGVYWMRSQLGTDR
CTLNDGVSPNAVAAVYYEDADTSSVPETTSDVTAVELAKCSNDALNQTVPFCPLKIDSNP
ASVETIDITFGSNGTSFLWFMNNSSFRGDYNDPVLLETKAGNLTFKKEWNVIDVGTNSSI
RVILRNHGRFGAHPMHLHGHNFNVLAEGFGDWDGTVVNADNSQRRDVQILQNAPDPDMPS
FIVLQWDNDNPGSWPLHCHLAWHVSGGLFVQMLERKEDIQAQTFDDDVVQTCRDWAAWTG
T

Enzyme Prediction     

EC	1.10.3.2:2	-

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	206	510	3.9e-122	0.9551282051282052

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
259923	CuRO_1_MaLCC_like	1.54e-72	211	332	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.
274555	ascorbase	1.45e-59	213	690	1	519	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.
259947	CuRO_2_MaLCC_like	4.72e-58	343	514	1	166	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.
215324	PLN02604	1.88e-57	213	690	24	542	oxidoreductase
274556	laccase	1.05e-55	213	688	3	513	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CAE7013418.1|AA1_3	4.30e-279	1	719	1	725
QDS68790.1|AA1_3	1.37e-247	59	721	102	789
QIW99529.1|AA1_3	7.79e-241	99	721	55	653
UJO18649.1|AA1_3	2.27e-230	97	720	77	674
QDS70373.1|AA1_3	5.02e-230	98	720	91	687

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3SQR_A	4.32e-121	206	721	60	570	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	8.56e-121	206	721	60	570	Structure of the L499M mutant of the laccase from B.aclada [Botrytis aclada]
5LM8_A	5.57e-103	207	715	17	525	Crystal structure of a laccase-like multicopper oxidase McoG from from Aspergillus niger [Aspergillus niger]
5LWW_A	5.73e-103	207	715	18	526	Crystal structure of a laccase-like multicopper oxidase McoG from Aspergillus niger bound to zinc [Aspergillus niger]
5LWX_A	6.20e-103	207	715	45	553	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	2.59e-162	210	719	61	573	Oxydoreductase ptaK OS=Pestalotiopsis fici (strain W106-1 / CGMCC3.15140) OX=1229662 GN=ptaK PE=2 SV=2
sp|Q96WM9|LAC2_BOTFU	1.23e-123	208	721	63	571	Laccase-2 OS=Botryotinia fuckeliana OX=40559 GN=lcc2 PE=2 SV=1
sp|J5JH35|OPS5_BEAB2	3.26e-111	206	715	66	573	Oxidoreductase OpS5 OS=Beauveria bassiana (strain ARSEF 2860) OX=655819 GN=OpS5 PE=1 SV=1
sp|Q12570|LAC1_BOTFU	1.54e-110	207	721	60	551	Laccase-1 OS=Botryotinia fuckeliana OX=40559 GN=lcc1 PE=2 SV=3
sp|Q0CCX6|GEDJ_ASPTN	1.26e-102	216	700	62	566	Dihydrogeodin oxidase OS=Aspergillus terreus (strain NIH 2624 / FGSC A1156) OX=341663 GN=gedJ PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
0.991066	0.008968

TMHMM  Annotations     

There is no transmembrane helices in K441DRAFT_687046-t45_1-p1.