CAZyme Information: K441DRAFT_742834-t45_1-p1

Basic Information

• Species: Cenococcum geophilum
• Lineage: Ascomycota; Dothideomycetes; ; Gloniaceae; Cenococcum; Cenococcum geophilum
• CAZyme ID: K441DRAFT_742834-t45_1-p1
• CAZy Family: GT71
• CAZyme Description: laccase-like multicopper oxidase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
593		66148.23	6.2472

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=KV748184:103933-106136(+)

Full Sequence      

MKGLINLVACTIGFGVVGATRLDAAKYHLSDLGTLKAKSLPKYLDNNPLPNGYPWGRKTV
ANTNPKDAPNTGITRHYDFTISRGELAPDGYLKKSGILINGQFPGPLIEANWGDWIEVKV
TNNITGPEEGTSLHWHGMLQAGTPWYDGVPSVSQCPIAPGESFTYLFQASVYGTSWYHSH
YSAQAAGGLFGALVVYGPXHVSYDVDVGPIILADWFHKDYFDIVKNIMSTNQTIWANPSD
NTLINGRMPYNCSLVKDGTPCGNASYSQFRFQTGKTYRLRLINGGAAGMEYFSIDGHQLT
ITSIDLVDIVPYNTTLVTLGVGQRTDVLFTPRANGTQAIWMRTLQSGKFCQRAANPEGRA
VILLDNTPETAIPTTTAWPPPVDDGTCGNEPLENSVPYYAEKLPEPSVTYKIVINSIINA
TGHQLYTMNGYPFQADYNDPLLLLANEKNYSYPYNPEWNVINFGQNTSIRLVIWNNNTGP
HPMHIHGHDMFVLYDDNNAWNGTIVNPQNPQRRDTHNLRPHGWMVMQYNADNPGVWPFHC
HIAWHLSMGLYVNLMERPDEISQYQIPMVMKQTCDNWQQYSSTHVVEQIDSGV

Enzyme Prediction     

EC	1.10.3.2:2	-

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	92	550	3.1e-109	0.9776536312849162

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
274555	ascorbase	3.81e-79	74	563	1	530	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.
177843	PLN02191	8.97e-75	94	563	40	553	L-ascorbate oxidase
215324	PLN02604	2.01e-70	74	552	24	542	oxidoreductase
259923	CuRO_1_MaLCC_like	8.42e-67	72	196	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	1.71e-66	403	555	3	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ATZ46043.1|AA1_3	3.81e-218	13	593	14	593
AEO65600.1|AA1_3	4.53e-217	1	592	4	593
APA07098.1|AA1_3	4.53e-215	33	593	33	596
AEO54598.1|AA1_3	2.50e-214	29	592	34	594
UKZ94937.1|AA1_3	3.19e-211	29	593	29	590

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3SQR_A	4.69e-110	55	593	49	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	9.31e-110	55	593	49	580	Structure of the L499M mutant of the laccase from B.aclada [Botrytis aclada]
5LM8_A	1.85e-91	54	584	3	532	Crystal structure of a laccase-like multicopper oxidase McoG from from Aspergillus niger [Aspergillus niger]
5LWW_A	1.90e-91	54	584	4	533	Crystal structure of a laccase-like multicopper oxidase McoG from Aspergillus niger bound to zinc [Aspergillus niger]
5LWX_A	3.85e-91	54	584	31	560	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	3.38e-189	48	593	38	585	Oxydoreductase ptaK OS=Pestalotiopsis fici (strain W106-1 / CGMCC3.15140) OX=1229662 GN=ptaK PE=2 SV=2
sp|Q96WM9|LAC2_BOTFU	1.46e-111	55	593	49	581	Laccase-2 OS=Botryotinia fuckeliana OX=40559 GN=lcc2 PE=2 SV=1
sp|J5JH35|OPS5_BEAB2	7.62e-107	55	593	54	590	Oxidoreductase OpS5 OS=Beauveria bassiana (strain ARSEF 2860) OX=655819 GN=OpS5 PE=1 SV=1
sp|P78722|LAC2_PODAS	7.30e-97	69	593	73	605	Laccase-2 OS=Podospora anserina OX=2587412 GN=LAC2 PE=2 SV=1
sp|Q12570|LAC1_BOTFU	4.38e-92	55	593	47	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
0.003682	0.996294	CS pos: 19-20. Pr: 0.9059

TMHMM  Annotations     

There is no transmembrane helices in K441DRAFT_742834-t45_1-p1.