CAZyme Information: VBB73169.1

Basic Information

• Species: Podospora comata
• Lineage: Ascomycota; Sordariomycetes; ; Podosporaceae; Podospora; Podospora comata
• CAZyme ID: VBB73169.1
• CAZy Family: AA7
• CAZyme Description: Putative laccase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
696	LR026964|CGC6	77700.34	6.1184

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_PcomataTmat	13100	N/A	2652	10448

• Gene Location: location=LR026964:5655750-5657897(+)

Full Sequence      

MGSFWVLVARLLGVTTLSTYEGLDRSQSPLQLTDSHSHVESSLVPTAAKDPLHFRPPGHR
QDNGNGSDFKCDYRKMVGWEKCSTPEDRSCWLVNKKTGERFDINSDYENYYPTGKTREYF
ITVDKSNITADGYTFYGATVFNETYPGPWIQACWGDTVKVHVRNLNPDRGTSIHWHGIRQ
LNTMHMDGVNGITQCPIAPGSTFTYEWKVMQYGSSWYHSHYSEQYGDGAVGPITLHGPSS
APYDEAADIPLLMTDWRHGSLFPVGNMLKERWIQSILLNGIGNVTKFGARKVQNTSKIPK
PYTLTFTADKVYEDEPPELEVPNSRPKRYLLRLINTSIGSTFIFSIDNHLLSIVSADFVP
IYPYLNSSILVGIGQRYNVIVEANPRNNTKQPLDSNGNYWIRTWVAPNCGAGVVINKDSK
ETYMQTGILRYNKSSTEDPESKPWTDISMACSDETATSLRPVLPWVVEDPINVMSTESKI
QHMAVISGPPADPIPSFPQASYSFRNVSGGINGPNPLQINFSDPVFLNLDNDEPFKNKLW
EIYPEGRPNQTDWVWLAITVDYSPDGDTSAHPIHLHGHDFAILQQAEKTTYVPENIHLNL
INPPRRDVVLMPKSGFIIIAFKADNPGAWLLHCHIASHASQGLALQILERQADAAAMWPK
ASPAAQTAATLCSSWDSWVAASYTSTPTPLPDDSGI

Enzyme Prediction     

EC	1.10.3.2:4	1.10.3.-:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	106	451	2.5e-117	0.9903846153846154

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
259923	CuRO_1_MaLCC_like	1.47e-60	114	236	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	6.12e-57	142	643	26	517	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	9.03e-53	142	649	48	546	L-ascorbate oxidase
259968	CuRO_3_MaLCC_like	3.46e-52	487	648	7	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	5.99e-50	112	647	28	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].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
VBB73169.1|AA1_3	0.0	1	696	1	696
UPK95743.1|AA1_3	1.87e-226	4	678	7	655
QKD61499.1|AA1_3	3.17e-213	27	679	30	651
QLI67119.1|AA1_3	7.49e-206	38	678	28	650
AVI02162.1|AA1_3	1.69e-197	27	679	26	632

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3SQR_A	5.96e-121	88	696	46	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	1.18e-120	88	696	46	580	Structure of the L499M mutant of the laccase from B.aclada [Botrytis aclada]
5LM8_A	8.79e-92	101	653	7	508	Crystal structure of a laccase-like multicopper oxidase McoG from from Aspergillus niger [Aspergillus niger]
5LWW_A	9.02e-92	101	653	8	509	Crystal structure of a laccase-like multicopper oxidase McoG from Aspergillus niger bound to zinc [Aspergillus niger]
5LWX_A	1.32e-91	101	653	35	536	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|D4APX3|LAC1_ARTBC	1.82e-141	69	696	49	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	2.46e-119	88	696	46	581	Laccase-2 OS=Botryotinia fuckeliana OX=40559 GN=lcc2 PE=2 SV=1
sp|Q12570|LAC1_BOTFU	1.42e-107	83	696	39	561	Laccase-1 OS=Botryotinia fuckeliana OX=40559 GN=lcc1 PE=2 SV=3
sp|A0A067XMP0|PTAE_PESFW	3.31e-105	83	678	28	593	Oxidoreductase ptaE OS=Pestalotiopsis fici (strain W106-1 / CGMCC3.15140) OX=1229662 GN=ptaE PE=2 SV=2
sp|J5JH35|OPS5_BEAB2	5.30e-105	85	696	48	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
0.081335	0.918663	CS pos: 16-17. Pr: 0.8310

TMHMM  Annotations     

There is no transmembrane helices in VBB73169.1.