CAZyme Information: ASPZODRAFT_57033-t33_1-p1

Basic Information

• Species: Penicilliopsis zonata
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Penicilliopsis; Penicilliopsis zonata
• CAZyme ID: ASPZODRAFT_57033-t33_1-p1
• CAZy Family: GH72|CBM43
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
563		62809.71	4.3011

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_PzonataCBS506.65	10027	1073090	158	9869

• Gene Location: location=KV878336:3265496-3267506(+)

Full Sequence      

MLLLALLSFLSSAIAAAVGRRECANGPTTRHCWGQYDINTNFYDVVPDTGVTREFWLSAQ
NLTLAPDGYEREVLAFNGQIPGPLIEADWGDTIVVHVTNELENNGTSIHWHGIRQLNNNE
NDGVPGVTQCPIPPGETYTYTWRATQYGHSWYHSHFSLQYGNGLFGPILIHGPSSANWDV
DLGVLPLQDWAHESVFTLWAGITQYGAPPPLPNGLINGTNTFDCRGSSDPACLGTGKRYE
NSFVQGKKYLIRLVNTAVDGYFRFSIDNHKLTVAATDLVPIQPYETDNVLLGSGQRYDII
VEADQPIGNYWLRATYQTACRNNSNANNILGIIRYEGSDPVAVPTTHMKDFPEECQDEPL
DKLVPYMALNAGQGVEKSLDLSNNKIDNIFHWTMNGSAFYIDWSEPALLMLESNDTVYPA
DYGVYELDAANEWIYWIIRDESTFATSHPIHLHGHDFNILAQGEGELDLTTITLNTDNPP
RRDVATLPGGGYLVIAFQTDNPGFWLMHCHIAWHSSQGFAVQFAERRSEILATVSDQSAI
QEQCDLWDGYFDTEPYEQDDAGV

Enzyme Prediction     

EC	1.10.3.2:4	1.10.3.-:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	40	355	1.2e-136	0.9935897435897436

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
274555	ascorbase	6.68e-82	52	525	1	523	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.
259923	CuRO_1_MaLCC_like	5.31e-79	50	171	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	5.03e-75	387	523	21	156	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.
177843	PLN02191	8.47e-75	66	525	37	546	L-ascorbate oxidase
215324	PLN02604	2.71e-71	65	525	37	546	oxidoreductase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CAM12502.1|AA1_3	4.39e-226	9	563	23	581
BCS23441.1|AA1_3	5.44e-223	15	563	19	565
AFC76164.1|AA1_3|1.10.3.2	6.49e-223	22	563	38	580
ATZ57071.1|AA1_3	7.74e-222	22	563	38	581
AAK77953.1|AA1_3	7.74e-222	22	563	38	581

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3V9E_A	2.24e-224	22	563	38	580	Structure of the L499M mutant of the laccase from B.aclada [Botrytis aclada]
3SQR_A	2.24e-224	22	563	38	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]
5LWX_A	8.91e-183	33	556	32	562	Crystal structure of the H253D mutant of McoG from Aspergillus niger [Aspergillus niger]
5LM8_A	3.97e-182	33	556	4	534	Crystal structure of a laccase-like multicopper oxidase McoG from from Aspergillus niger [Aspergillus niger]
5LWW_A	4.11e-182	33	556	5	535	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|Q96WM9|LAC2_BOTFU	1.38e-222	22	563	38	581	Laccase-2 OS=Botryotinia fuckeliana OX=40559 GN=lcc2 PE=2 SV=1
sp|J5JH35|OPS5_BEAB2	1.43e-219	12	563	33	590	Oxidoreductase OpS5 OS=Beauveria bassiana (strain ARSEF 2860) OX=655819 GN=OpS5 PE=1 SV=1
sp|Q12570|LAC1_BOTFU	1.06e-199	20	563	34	561	Laccase-1 OS=Botryotinia fuckeliana OX=40559 GN=lcc1 PE=2 SV=3
sp|Q0CCX6|GEDJ_ASPTN	1.05e-152	14	563	17	605	Dihydrogeodin oxidase OS=Aspergillus terreus (strain NIH 2624 / FGSC A1156) OX=341663 GN=gedJ PE=1 SV=1
sp|P06811|LAC1_NEUCR	3.25e-152	25	563	56	606	Laccase OS=Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) OX=367110 GN=lacc PE=1 SV=3

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000230	0.999747	CS pos: 15-16. Pr: 0.9751

TMHMM  Annotations     

There is no transmembrane helices in ASPZODRAFT_57033-t33_1-p1.