CAZyme Information: P175DRAFT_0507138-t39_1-p1

Basic Information

• Species: Aspergillus ochraceoroseus
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus ochraceoroseus
• CAZyme ID: P175DRAFT_0507138-t39_1-p1
• CAZy Family: GH55
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
663	MSFN02000002|CGC30	74328.16	6.3701

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AochraceoroseusIBT24754	9070	1392256	153	8917

• Gene Location: location=MSFN02000002:203401-205821(-)

Full Sequence      

MQRDSSRRRKPRPADKLEEPIDSARSDTPQKHKKEASSRDWPCGLVLYPLALCLVVVLLL
WNQYTTRLVLPSSFFSPTRIHHEPNLEEHDVLMKSPDDSRPQIELHPKHHIYRDPATHYL
DWTVTAGNLRPDGVLKDVHLINGLFPGPTIEARSGDTVIVNVTNALQDESFTVHWHGLHI
QNSMDGVAAVTQRPILPGASFLYHIDIPSDQSGTFWYHGHAGLARADGLYGGFVVHKPAP
KSTVRGLMSREGDVSLNRGADEKDVLLMIGDWYHRPAAEVMAWYMRAGSFGNEPVPDSLV
LNGIGYFNCSMAVPARPLDCIDSPINLSRVLPTDAVCRVRVVNTGSLAGFTLTFDNHDVT
VLEVDSAPVQAQQGTRSMHSVGILYPGQRMDLLIRRSTDDKSSTLKIHLDEECFKYPNPA
LKSTQTFFMSEGQDETEPTHIAAEPPSNEQQISSLIDVQDLPSTEQILSQIPPSAAVQRT
EVVYTKIQKLSIRHNVPYGFFNRTSWVPQMDPAIPLNELERERWDKNQFGITIPSPPSLH
QRDEGEQGIWVDLVVNNLDEGGHPFHLHGHHFYILAVYKAAIGWGSYNPFVDPSPPGLDP
ERFPETKGYDLSRAMLRDTVYIPSRAYAVLRFRADNPGIWLFHCHILWHLANGMSMLVDV
GGV

Enzyme Prediction     

No EC number prediction in P175DRAFT_0507138-t39_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	134	654	3.6e-86	0.9776536312849162

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
274555	ascorbase	1.04e-60	118	654	3	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.
259977	CuRO_3_MCO_like_4	3.09e-59	482	660	2	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.
177843	PLN02191	1.47e-56	122	657	28	543	L-ascorbate oxidase
225043	SufI	1.03e-54	122	661	38	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	1.53e-51	118	661	26	547	oxidoreductase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QRD88142.1|AA1	1.17e-266	27	661	14	616
QMW25836.1|AA1	1.17e-266	27	661	14	616
QMW37919.1|AA1	5.16e-266	26	661	4	599
CAK44017.1|AA1	1.14e-228	42	660	13	586
UPX44859.1|AA1	2.36e-227	72	662	56	629

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1ZPU_A	8.22e-55	117	658	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]
3V9E_A	7.10e-50	123	656	73	538	Structure of the L499M mutant of the laccase from B.aclada [Botrytis aclada]
3SQR_A	1.83e-49	123	656	73	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]
1AOZ_A	4.24e-46	118	661	5	524	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]
5EHF_A	1.53e-45	121	658	7	465	Laccase from Antrodiella faginea [Antrodiella faginea]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q6CII3|FET3_KLULA	2.51e-60	116	658	26	503	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
sp|I1RMG9|FET3_GIBZE	3.74e-58	116	654	23	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|W3X7K0|PFMAD_PESFW	3.44e-57	120	655	25	484	Multicopper oxidase PfmaD OS=Pestalotiopsis fici (strain W106-1 / CGMCC3.15140) OX=1229662 GN=PfmaD PE=2 SV=1
sp|K7NCS2|FETC_EPIFE	1.57e-54	116	654	21	489	Iron transport multicopper oxidase fetC OS=Epichloe festucae (strain E2368) OX=696363 GN=fetC PE=2 SV=1
sp|J9VY90|LAC1_CRYNH	1.62e-54	115	660	59	560	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

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
0.999979	0.000047

TMHMM  Annotations     

Start	End
43	65