CAZyme Information: P168DRAFT_308712-t37_1-p1

Basic Information

• Species: Aspergillus campestris
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus campestris
• CAZyme ID: P168DRAFT_308712-t37_1-p1
• CAZy Family: GH75
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
575		64925.30	4.7200

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AcampestrisIBT28561	9929	1392248	173	9756

• Gene Location: location=MSFM01000001:3660858-3662873(+)

Full Sequence      

MGPARTNWFWQRLLVFSCYCAQAIANGPCKNSPTSRRCWGEYNITTDYSVVTPDTGVTRE
YWLAAQNLTLAPDGYERQVLVFNGSLPGPTIEADWGDTVVVHVTNQLTDNGTTVHWHGIR
QQNSNPSDGVPGVTQCPIAPGDSMTYRFRAQQYGTAWYHGHFSMQMADGLYGPIVIHGPA
SADYDVDLGPVFVSDWYHQSAFITWRQKTMYGGFPARTNANAENGLFNSTNNYPCDDSDD
PACLGTGKRSETTVTKGKRYRMRLIDSSLDGWMRVSIDNHKLIVIAADLVPIVPYVTDNV
VITSGQRYDIIFEADQDVGNYWMRTEYQSVCNMLDIDRNDIRGILHYEGAEPDEEPTSEK
WPILPACGDEPYDKLVPYVAKDVDVADTQEDLGIGWFYEKDLVFHWAINTKPLTIDWSHP
TDLLAAQHAVEYPEETNVYNISGNQWTYWVIQDVGFVDAFHPFHLHGHDFHILAQGRGLY
NPTTVKLNRKNPPRRDTATMAGSGYLVIGFETDNPGSWLMHCHIAWHTSQSLALQFVERE
SEIPALMDMEKFQDTCDKWDKYAKGAAHEQDDSGI

Enzyme Prediction     

EC	1.10.3.2:4	1.10.3.-:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	46	367	4.9e-132	0.9935897435897436

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
274555	ascorbase	9.08e-87	58	544	1	532	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	5.34e-80	57	544	30	555	L-ascorbate oxidase
274556	laccase	3.55e-73	77	544	22	525	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.
259923	CuRO_1_MaLCC_like	3.10e-71	56	177	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.
215324	PLN02604	9.35e-71	71	545	37	556	oxidoreductase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BCS23441.1|AA1_3	4.79e-287	21	575	19	565
EAA61461.1|AA1_3	1.30e-271	29	575	31	570
AWI47682.1|AA1_3	4.49e-236	29	515	15	492
CAM12502.1|AA1_3	9.76e-201	29	575	37	581
ABM21605.1|AA1_3	2.11e-190	29	575	43	584

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3SQR_A	6.22e-187	29	575	39	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	1.25e-186	29	575	39	580	Structure of the L499M mutant of the laccase from B.aclada [Botrytis aclada]
5LWX_A	3.47e-156	39	564	32	558	Crystal structure of the H253D mutant of McoG from Aspergillus niger [Aspergillus niger]
5LM8_A	1.59e-155	39	564	4	530	Crystal structure of a laccase-like multicopper oxidase McoG from from Aspergillus niger [Aspergillus niger]
5LWW_A	1.65e-155	39	564	5	531	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	1.79e-188	29	575	39	581	Laccase-2 OS=Botryotinia fuckeliana OX=40559 GN=lcc2 PE=2 SV=1
sp|J5JH35|OPS5_BEAB2	4.35e-181	23	575	38	590	Oxidoreductase OpS5 OS=Beauveria bassiana (strain ARSEF 2860) OX=655819 GN=OpS5 PE=1 SV=1
sp|Q12570|LAC1_BOTFU	9.08e-160	29	575	37	561	Laccase-1 OS=Botryotinia fuckeliana OX=40559 GN=lcc1 PE=2 SV=3
sp|Q0CCX6|GEDJ_ASPTN	1.86e-139	3	575	2	605	Dihydrogeodin oxidase OS=Aspergillus terreus (strain NIH 2624 / FGSC A1156) OX=341663 GN=gedJ PE=1 SV=1
sp|A0A067XMP0|PTAE_PESFW	1.71e-135	29	575	26	610	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 SP

Other	SP_Sec_SPI	CS Position
0.000243	0.999730	CS pos: 25-26. Pr: 0.9718

TMHMM  Annotations     

There is no transmembrane helices in P168DRAFT_308712-t37_1-p1.