CAZyme Information: PV06_03048-t43_1-p1

Basic Information

• Species: Exophiala oligosperma
• Lineage: Ascomycota; Eurotiomycetes; ; Herpotrichiellaceae; Exophiala; Exophiala oligosperma
• CAZyme ID: PV06_03048-t43_1-p1
• CAZy Family: CE16
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
635	KN847334.1|CGC6	68990.61	6.4498

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_EoligospermaCBS72588	11938	N/A	45	11893

• Gene Location: location=KN847334.1:574369-576344(-)

Full Sequence      

MAFSRLIVLLSLLSFAIFAYAAPSSSSVSSLEKRAKKVKFEVDLTWEDYSPIGGKPKKMI
LVNGTFPGPALEATVGDEVEFLVHNNMPDATAVHFHGIVQQGTPWSDGVPGLSQKPISPG
SSYLYKWTADASGVYFYHAHYRSQMMDGLYGAIIIKAAENAPKPFSLISNDTAAVAAMVA
AEKSQEVIFVSDYVKYTSAEFHKQEEAANVDISCADAIIINGKGSQYCLSRGEITAYTSP
KVLPMLATVSPSEMTNKGCLPPNLIPTQGNFSFKIDTLPPDAYFECTPSTGEMATFDVDP
AKGWAAFTFINPGGFELLKFTIDGHKMWVYAVDGGYVVPQLVDQVMINNGDRYSVLVQLN
QAPAQYAIRVANNGLNQIISGFGVLNYKGSYGPATEDPNALSTMNFAGANLTLLRPFNDV
KAAPYPPNPPAKKADITYQFNIKKLGQPFGAYQWTLSGVDGFNASMEDATPLIDQDPAKL
PTDDLVLTTKMGQWVDLIIKTQGPLAQPHPMHKHSNKAYVLGKGVGPFNWTTVDEAATVL
PANTFNFVNPPLRDGYTTTPSESNNTWMALRYEVVNPGAFLFHCHVQTHMAGGMAVALLD
GVDKWPKVPEEYVNGNGIGNSHKLKMKGRLHPKSS

Enzyme Prediction     

No EC number prediction in PV06_03048-t43_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	57	595	1e-80	0.9748603351955307

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
259965	CuRO_3_Abr2_like	1.82e-79	435	601	1	164	The third cupredoxin domain of a group of fungal Laccases similar to Abr2 from Aspergillus fumigatus. Abr2 is involved in conidial pigment biosynthesis in Aspergillus fumigatus. 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. Laccase 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. Like other related multicopper oxidases (MCOs), laccase is composed of three cupredoxin domains 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.
259919	CuRO_1_Abr2_like	6.07e-60	43	156	2	117	The first cupredoxin domain of a group of fungal Laccases similar to Abr2 from Aspergillus fumigatus. Abr2 is involved in conidial pigment biosynthesis in Aspergillus fumigatus. 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. Laccase 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. Like other related multicopper oxidases (MCOs), laccase is composed of three cupredoxin domains 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.
177843	PLN02191	7.94e-60	42	629	24	573	L-ascorbate oxidase
274555	ascorbase	4.69e-59	39	611	5	534	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.
259944	CuRO_2_Abr2_like	1.51e-57	186	388	1	138	The second cupredoxin domain of a group of fungal Laccases similar to Abr2 from Aspergillus fumigatus. Abr2 is involved in conidial pigment biosynthesis in Aspergillus fumigatus. 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. Laccase 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. Like other related multicopper oxidases (MCOs), laccase is composed of three cupredoxin domains 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 2 of 3-domain MCOs has lost the ability to bind copper.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AIW00656.1|AA1	7.82e-226	33	618	33	618
QRC97610.1|AA1	1.55e-218	38	618	40	620
UJO20936.1|AA1	1.08e-196	34	618	20	610
UQC89926.1|AA1	9.32e-185	36	618	37	621
QBZ54343.1|AA1	7.60e-183	38	618	28	610

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1AOZ_A	9.10e-48	62	621	27	544	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]
5LM8_A	1.62e-41	52	600	37	504	Crystal structure of a laccase-like multicopper oxidase McoG from from Aspergillus niger [Aspergillus niger]
5LWW_A	1.64e-41	52	600	38	505	Crystal structure of a laccase-like multicopper oxidase McoG from Aspergillus niger bound to zinc [Aspergillus niger]
5LWX_A	4.34e-41	52	600	65	532	Crystal structure of the H253D mutant of McoG from Aspergillus niger [Aspergillus niger]
1HFU_A	3.03e-39	44	600	11	468	Chain A, LACCASE 1 [Coprinopsis cinerea]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q0UHZ8|ELCG_PHANO	2.76e-219	38	618	40	620	Multicopper oxidase elcG OS=Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) OX=321614 GN=elcG PE=1 SV=1
sp|A0A2G5I8N8|CTB12_CERBT	5.20e-194	32	618	42	630	Multicopper oxidase CTB12 OS=Cercospora beticola OX=122368 GN=CTB12 PE=3 SV=1
sp|E9RBR0|ABR2_ASPFU	2.04e-153	34	608	16	579	Laccase abr2 OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=abr2 PE=1 SV=1
sp|I1RF62|GIP1_GIBZE	3.28e-146	38	612	25	600	Multicopper oxidase GIP1 OS=Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1) OX=229533 GN=GIP1 PE=1 SV=1
sp|A0A443HK79|VDTB1_BYSSP	5.47e-137	38	624	20	609	Multicopper oxidase VdtB OS=Byssochlamys spectabilis OX=264951 GN=VdtB PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000215	0.999759	CS pos: 21-22. Pr: 0.9822

TMHMM  Annotations     

Start	End
7	29