CAZyme Information: PV10_05279-t45_6-p1

Basic Information

• Species: Exophiala mesophila
• Lineage: Ascomycota; Eurotiomycetes; ; Herpotrichiellaceae; Exophiala; Exophiala mesophila
• CAZyme ID: PV10_05279-t45_6-p1
• CAZy Family: GH47
• CAZyme Description: hypothetical protein, variant 2

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
687		75404.40	5.0657

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_EmesophilaCBS40295	9237	N/A	56	9181

• Gene Location: location=KN847522:5081328-5083706(+)

Full Sequence      

MILKYLSRTICQSRQQFIGMVGRSSRKGWRAVYAIQQNIDMIALGLLQRGTPDMDGVPGV
TQFPIPPGGNFTYRFSTADEYGFYWYHSHFRAYYNDALRGPLLIHPSPSRPRPFKTLAQS
SSEFDMMLQVERSGTILLLSDWYHRLSDRIYDEYFTTGAFPQCVDSLLANGRGRVQCLPQ
NILEAGPGLGLESNIANDPHDPDAMSMAMESSTTSGMGMASMSMDTASMPALTTDAMSMS
MRKRSDHTASPSTGTAMSDMSAMSSTLTSMATMGSSTASVGTEDQTMSTTVDMPQMTLGP
RGCSPPMMFRPGFNASSLPLETCTNTTSELFTFTADASRGWTALHLVNAGAVSRLSVSLD
GHSMFVYEADGLYVTLQEVQVLHISIGQRYSVMIRLDQNPGDYSFRFAAYPYGDMQQVIE
GQAILSYQNMTNNTNMTMMSRMVSPWMLVNGSATSGTVELDDQTLAPFMGNTAPSGAANV
TRHFAINQTDIVTWVANREPFVEPARPIIYGSVSDGWNATTTLLTPANATVDIIMKVAND
SMDTMGHPMHLHGHKFWFLGSGEGDFPFESVTDAPSSMINLQNPPYRDTIDLPPSGWAVI
RYITDNPGAWLFHCHVQWHLVSGMAVVLVENEERMMDMVGSIQNAFNNPATNNSQAEGTS
AASTLSGNCPRQYLSFLFSLLLLFVLL

Enzyme Prediction     

No EC number prediction in PV10_05279-t45_6-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	331	625	3.8e-41	0.5223463687150838

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
274555	ascorbase	3.39e-50	45	642	61	531	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	4.44e-44	45	635	83	551	L-ascorbate oxidase
259977	CuRO_3_MCO_like_4	7.05e-40	478	630	13	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.
215324	PLN02604	1.17e-37	45	642	84	558	oxidoreductase
259870	CuRO_3_LCC_like	3.62e-37	481	629	3	132	Cupredoxin domain 3 of laccase-like multicopper oxidases; including laccase, CueO, spore coat protein A, ascorbate oxidase and similar proteins. Laccase-like multicopper oxidases (MCOs) in this family contain three cupredoxin domains. They are able to couple oxidation of substrates with reduction of dioxygen to water. MCOs are capable of oxidizing a vast range of substrates, varying from aromatic to inorganic compounds such as metals. Although the members of this family have diverse functions, majority of them have three cupredoxin domain repeats. 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. Also included in this family are cupredoxin domains 2, 4, and 6 of the 6-domain MCO ceruloplasmin and similar proteins.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QOD95012.1|AA1	1.24e-224	45	659	85	662
QPG98040.1|AA1	1.35e-219	45	652	84	658
QLI72976.1|AA1	4.54e-219	45	641	90	657
UPL00042.1|AA1	2.48e-212	45	601	78	601
ATY66532.1|AA1	5.72e-203	45	640	95	630

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3KW7_A	3.93e-29	45	631	67	473	Crystal structure of LacB from Trametes sp. AH28-2 [Trametes sp. AH28-2],3KW7_B Crystal structure of LacB from Trametes sp. AH28-2 [Trametes sp. AH28-2]
5EHF_A	5.01e-29	45	631	67	468	Laccase from Antrodiella faginea [Antrodiella faginea]
1AOZ_A	8.23e-29	45	649	63	549	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]
6H5Y_A	2.89e-28	45	631	67	467	PM1 mutant, 7D5 [Aspergillus oryzae],6H5Y_B PM1 mutant, 7D5 [Aspergillus oryzae]
4JHU_A	3.88e-28	45	631	67	467	T2-depleted laccase from Coriolopsis caperata soaked with CuCl [Coriolopsis caperata],4JHV_A T2-depleted laccase from Coriolopsis caperata [Coriolopsis caperata]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|W3X732|PFMAY_PESFW	1.19e-57	45	635	81	567	Laccase PFICI_06862 OS=Pestalotiopsis fici (strain W106-1 / CGMCC3.15140) OX=1229662 GN=PFICI_06862 PE=3 SV=1
sp|E9RBR0|ABR2_ASPFU	7.45e-57	45	630	78	571	Laccase abr2 OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=abr2 PE=1 SV=1
sp|A0A0B4HQH6|MLAC1_METMF	2.35e-52	37	630	74	598	Laccase 1 OS=Metarhizium majus (strain ARSEF 297) OX=1276143 GN=Mlac1 PE=3 SV=1
sp|A0A0B4GLB5|MLAC1_METGA	4.37e-52	37	630	73	597	Laccase 1 OS=Metarhizium guizhouense (strain ARSEF 977) OX=1276136 GN=Mlac1 PE=3 SV=1
sp|A0A1S7IUL2|MCE_TALPI	9.62e-52	45	634	82	584	Multicopper oxidase MCE OS=Talaromyces pinophilus OX=128442 GN=MCE PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000059	0.000001

TMHMM  Annotations     

There is no transmembrane helices in PV10_05279-t45_6-p1.