CAZyme Information: K441DRAFT_654471-t45_1-p1

Basic Information

• Species: Cenococcum geophilum
• Lineage: Ascomycota; Dothideomycetes; ; Gloniaceae; Cenococcum; Cenococcum geophilum
• CAZyme ID: K441DRAFT_654471-t45_1-p1
• CAZy Family: GH18
• CAZyme Description: laccase-like multicopper oxidase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
680	KV748182|CGC2	76176.61	7.0763

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=KV748182:2440087-2442580(-)

Full Sequence      

MHLFGRFWTTVTYFANLLTLSPINPPGPQQHPIPGILDVGLNVLPHYPIFKPPGGRPQGP
GSDFKCDYRRMPGWYECSTPENRGCWLRHPNGREYNILTDYENDAPIGVDRNYTLVVNDG
WVNADGVNFTVAKLFNNTFPGPWIQACWGDRLNIKVINNLGHNGTSVHWHGIRQKNTMHM
DGVNGITQCPIAPGDHFIYTWNTTQYGSSWYHSHYSVQYADGLQGPITIHGPSSASFDEP
KLPLLMTDWGHNSAFEAIYNRNLQKPSILLNGRGNVTNFYGNKNTSAIPPIYQLHFEKTN
IRLPGRAKRYLLRLINTSFDSTFIFSVDNHWLKIIGADFVPIVPYYNTSVLIGIGQRYHV
IIEADPVGGVANPLPKDGNFWIRTWVADSCGTPGGSTGYEQTGILRYGNTSTSDPTSKPW
TNISKRCSDETYSSLKPKHPWFVGQAVNGNDGEEFDVTFNGTAKPFLLAKFSLEPPSASG
FTPLQINYSDPIFFHLDNFAGTWPKEWVVVPENYTSTDWVYLVLTGAGRNNTSGAHPIHL
HGHDFAILQQVEGTPYSPEKLDLTLINPPRRDVVLLPRNGFVVIAFKTDNPGNWLMHCHI
AYHASFGLALQILERQADANKIWPHGKSNALKEAGRVCQNWNTWYGDCNNWWPGVNQTTG
VNPSCNGTEPLHIFQDDSGI

Enzyme Prediction     

EC	1.10.3.2:4	1.10.3.-:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	99	427	6.7e-116	0.9935897435897436

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
259923	CuRO_1_MaLCC_like	1.13e-58	108	230	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	6.21e-57	136	610	28	515	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.
225043	SufI	4.21e-53	103	612	26	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].
259968	CuRO_3_MaLCC_like	5.19e-52	482	613	31	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	8.35e-52	243	423	3	165	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
UPK95743.1|AA1_3	9.81e-309	1	645	1	656
QKD61499.1|AA1_3	2.53e-293	1	644	1	650
AVI02162.1|AA1_3	3.17e-277	1	644	1	631
UQC83994.1|AA1_3	7.03e-251	8	680	8	702
QLI67119.1|AA1_3	5.36e-233	1	680	1	683

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3SQR_A	2.43e-122	82	644	45	567	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	4.83e-122	82	644	45	567	Structure of the L499M mutant of the laccase from B.aclada [Botrytis aclada]
5LWX_A	4.62e-97	95	623	35	541	Crystal structure of the H253D mutant of McoG from Aspergillus niger [Aspergillus niger]
5LM8_A	2.31e-96	95	623	7	513	Crystal structure of a laccase-like multicopper oxidase McoG from from Aspergillus niger [Aspergillus niger]
5LWW_A	2.38e-96	95	623	8	514	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	4.14e-157	65	680	50	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	1.82e-121	82	618	45	547	Laccase-2 OS=Botryotinia fuckeliana OX=40559 GN=lcc2 PE=2 SV=1
sp|Q12570|LAC1_BOTFU	1.62e-116	78	644	39	548	Laccase-1 OS=Botryotinia fuckeliana OX=40559 GN=lcc1 PE=2 SV=3
sp|J5JH35|OPS5_BEAB2	2.28e-114	80	645	48	577	Oxidoreductase OpS5 OS=Beauveria bassiana (strain ARSEF 2860) OX=655819 GN=OpS5 PE=1 SV=1
sp|A0A067XMP0|PTAE_PESFW	1.54e-105	75	645	24	594	Oxidoreductase ptaE OS=Pestalotiopsis fici (strain W106-1 / CGMCC3.15140) OX=1229662 GN=ptaE PE=2 SV=2

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
0.711681	0.288306

TMHMM  Annotations     

There is no transmembrane helices in K441DRAFT_654471-t45_1-p1.