CAZyme Information: P168DRAFT_301744-t37_1-p1

Basic Information

• Species: Aspergillus campestris
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus campestris
• CAZyme ID: P168DRAFT_301744-t37_1-p1
• CAZy Family: GH51
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
588	MSFM01000001|CGC6	64133.03	5.6111

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=MSFM01000001:4274468-4276831(-)

Full Sequence      

MKKRSYSIFLYPLTVCALILVVFWQQTNTPDPLHFISPKISPAAYPANPANQSHQTNTNP
DALRPSIQLHPEDHIHRAPTTQHLDWTVTAEGIRPDGVLKRVYLINGAFLLFLYLTPPTL
TTTGLFPGPTIEALSGDNLIINVTNALQDVPFTIHWHGLHIANSMDGVAGVTQCAIPPGS
SFIYNVSIPSDQSGTFWYHAHTGLARADGLYGGLVVHAPSGAGVASEGIHDASDGDMLLL
IGDWYHQPAEEVMEWYMQPASFGNEPVPDSLLINGAGIFNCSMAVPARPVDCVDHHSMSL
PYLHPGDDTYRVRIVNTGSLTGLTITFDNMDVTLIAVDSIAVDPLDAAHPSSLGVLYPGQ
RMDVLLRRSTSASTDGVSASALRIDLDEEYLAIRHNAPYGFFNGTSWLPQREPRVPVAAL
DRKLWDENQFGVGVPYSGSGAGDDSPSAEVERDGDSGEQWVDLVVNNLDDGGHPFHLHGH
HFYILSTHESRTGWGSFNPFTPSDSTSPSTPKQQYDLSKAMLRDTVYIPRRGHAVLRFKA
NNPGVWMFHCHILWHLGSGMGMLVDVGYDRRNNTLGDNGGVSGEVCVV

Enzyme Prediction     

No EC number prediction in P168DRAFT_301744-t37_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	120	560	1.3e-86	0.9636871508379888

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
274555	ascorbase	3.77e-63	81	570	1	527	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	6.29e-60	124	570	49	550	L-ascorbate oxidase
259977	CuRO_3_MCO_like_4	1.72e-54	394	566	12	166	The third cupredoxin domain of uncharacterized multicopper oxidase. Multicopper Oxidases (MCOs) are multi-domain enzymes that are able to couple oxidation of substrates with reduction of dioxygen to water. MCOs oxidize their substrate by accepting electrons at a mononuclear copper centre and transferring them to a trinuclear copper centre which binds a dioxygen. The dioxygen, following the transfer of four electrons, is reduced to two molecules of water. These MCOs are capable of oxidizing a vast range of substrates, varying from aromatic to inorganic compounds such as metals. This subfamily of MCOs is composed of three cupredoxin domains. 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	7.95e-54	124	567	59	449	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].
215324	PLN02604	8.65e-53	81	570	24	550	oxidoreductase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QMW37919.1|AA1	1.27e-207	7	567	23	599
QRD88142.1|AA1	2.59e-206	7	567	40	616
QMW25836.1|AA1	2.59e-206	7	567	40	616
CAK44017.1|AA1	1.52e-186	1	566	9	586
UPX44859.1|AA1	3.34e-181	52	577	63	638

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1AOZ_A	4.99e-50	124	570	29	527	Refined Crystal Structure Of Ascorbate Oxidase At 1.9 Angstroms Resolution [Cucurbita pepo var. melopepo],1AOZ_B Refined Crystal Structure Of Ascorbate Oxidase At 1.9 Angstroms Resolution [Cucurbita pepo var. melopepo],1ASO_A X-Ray Structures And Mechanistic Implications Of Three Functional Derivatives Of Ascorbate Oxidase From Zucchini: Reduced-, Peroxide-, And Azide-Forms [Cucurbita pepo var. melopepo],1ASO_B X-Ray Structures And Mechanistic Implications Of Three Functional Derivatives Of Ascorbate Oxidase From Zucchini: Reduced-, Peroxide-, And Azide-Forms [Cucurbita pepo var. melopepo],1ASP_A X-ray Structures And Mechanistic Implications Of Three Functional Derivatives Of Ascorbate Oxidase From Zucchini: Reduced-, Peroxide-, And Azide-forms [Cucurbita pepo var. melopepo],1ASP_B X-ray Structures And Mechanistic Implications Of Three Functional Derivatives Of Ascorbate Oxidase From Zucchini: Reduced-, Peroxide-, And Azide-forms [Cucurbita pepo var. melopepo],1ASQ_A X-Ray Structures And Mechanistic Implications Of Three Functional Derivatives Of Ascorbate Oxidase From Zucchini: Reduced-, Peroxide-, And Azide-Forms [Cucurbita pepo var. melopepo],1ASQ_B X-Ray Structures And Mechanistic Implications Of Three Functional Derivatives Of Ascorbate Oxidase From Zucchini: Reduced-, Peroxide-, And Azide-Forms [Cucurbita pepo var. melopepo]
3V9E_A	2.06e-49	93	562	61	538	Structure of the L499M mutant of the laccase from B.aclada [Botrytis aclada]
3SQR_A	5.37e-49	93	562	61	538	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]
1ZPU_A	8.07e-47	81	564	2	477	Crystal Structure of Fet3p, a Multicopper Oxidase that Functions in Iron Import [Saccharomyces cerevisiae],1ZPU_B Crystal Structure of Fet3p, a Multicopper Oxidase that Functions in Iron Import [Saccharomyces cerevisiae],1ZPU_C Crystal Structure of Fet3p, a Multicopper Oxidase that Functions in Iron Import [Saccharomyces cerevisiae],1ZPU_D Crystal Structure of Fet3p, a Multicopper Oxidase that Functions in Iron Import [Saccharomyces cerevisiae],1ZPU_E Crystal Structure of Fet3p, a Multicopper Oxidase that Functions in Iron Import [Saccharomyces cerevisiae],1ZPU_F Crystal Structure of Fet3p, a Multicopper Oxidase that Functions in Iron Import [Saccharomyces cerevisiae]
5LM8_A	9.99e-43	118	559	43	497	Crystal structure of a laccase-like multicopper oxidase McoG from from Aspergillus niger [Aspergillus niger]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|K7NCS2|FETC_EPIFE	6.65e-60	78	560	20	489	Iron transport multicopper oxidase fetC OS=Epichloe festucae (strain E2368) OX=696363 GN=fetC PE=2 SV=1
sp|J9VY90|LAC1_CRYNH	8.15e-55	50	559	29	553	Laccase-1 OS=Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 / CBS 10515 / FGSC 9487) OX=235443 GN=LAC1 PE=1 SV=1
sp|E9R598|FETC_ASPFU	1.21e-53	81	560	22	486	Iron transport multicopper oxidase fetC OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=fetC PE=2 SV=1
sp|I1RMG9|FET3_GIBZE	1.36e-52	81	560	24	490	Iron transport multicopper oxidase FET3 OS=Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1) OX=229533 GN=FET3 PE=2 SV=1
sp|Q6CII3|FET3_KLULA	7.26e-51	81	574	27	513	Iron transport multicopper oxidase FET3 OS=Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) OX=284590 GN=FET3 PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
0.866031	0.133985

TMHMM  Annotations     

Start	End
7	24