CAZyme Information: KIW14452.1

Basic Information

• Species: Exophiala spinifera
• Lineage: Ascomycota; Eurotiomycetes; ; Herpotrichiellaceae; Exophiala; Exophiala spinifera
• CAZyme ID: KIW14452.1
• CAZy Family: GH16
• CAZyme Description: unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
663		70472.86	4.6887

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_EspiniferaCBS89968	12110	N/A	61	12049

• Gene Location: location=KN847496:1883763-1885754(-)

Full Sequence      

MRLSTAAALLTAATSISASSNSPTSTNASICSTASTCKPFLIELTWGPTNASNVFSREAI
LTNGSFPGPPLRLNVGECVDFTVVNNMPNVTGVHFHGIRQLGTPWADGVPGVSQYSIRPG
SSYNYQWTAEESGIYFYHSHYKGQMMDGLYGAIIISPAENATRPFSLISNDSADIEKMKA
AEAKVEAILTSDWNRFTFNEFFEIEKSANIDYSCTDSFVLNGMGSVYCLPISTLSLDEAP
QAAVVLNGSSLTAKGCIPPNNIAVQGAYSRNLAALPAGAYSQCTPYTGTNFTYSVDNKDE
WAALSFISPSGTALFKITIDSHKMYVYEINGHYVEPQLVDQIGLDNGDRISVLIKLDQAP
ADYTIRVANSGLNQVISGYGILSYQGSSGPAPSTGAVMNYGGQNTTTITVLDRATAYPYP
AETVSGTADATFVLDIMKDPQESLAWAWSLNGVDAYNQSRDDETPPLLYQSPANIPPSDL
ILRTNYNDWVDLIIKVAGPLAEPHPIHKHANKYFVIGAGIGDFNYTTVAQAQSAGVKFNL
DNPPFVDGYTTTEAEGPAWMVLRYQANTPGAWLLHCHVQSHLTGGMAVAILDAVDQFPSV
PSDAGAVCSNAGSSFSSSSAAASSTSSVTVKSYTNVAAAPLSKQRTTALGLVLALAGAAG
HIL

Enzyme Prediction     

No EC number prediction in KIW14452.1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	55	587	6.9e-74	0.9804469273743017

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
259965	CuRO_3_Abr2_like	4.19e-72	429	592	1	163	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.
274555	ascorbase	1.02e-59	46	604	13	535	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.
215324	PLN02604	4.80e-57	55	602	41	556	oxidoreductase
177843	PLN02191	6.56e-54	63	604	48	558	L-ascorbate oxidase
259919	CuRO_1_Abr2_like	5.94e-53	40	155	1	116	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AIW00656.1|AA1	9.63e-185	40	601	40	609
QRC97610.1|AA1	5.51e-179	40	601	42	611
UJO20936.1|AA1	3.15e-168	39	603	25	603
UQC89926.1|AA1	1.80e-167	40	602	41	613
QBZ62892.1|AA1	5.95e-162	40	592	43	606

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1AOZ_A	9.71e-48	46	604	15	535	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	2.86e-43	49	597	34	509	Crystal structure of a laccase-like multicopper oxidase McoG from from Aspergillus niger [Aspergillus niger]
5LWW_A	2.91e-43	49	597	35	510	Crystal structure of a laccase-like multicopper oxidase McoG from Aspergillus niger bound to zinc [Aspergillus niger]
5LWX_A	3.12e-43	49	597	62	537	Crystal structure of the H253D mutant of McoG from Aspergillus niger [Aspergillus niger]
3V9E_A	3.35e-36	55	593	84	543	Structure of the L499M mutant of the laccase from B.aclada [Botrytis aclada]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q0UHZ8|ELCG_PHANO	9.78e-180	40	601	42	611	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	7.30e-163	40	601	50	621	Multicopper oxidase CTB12 OS=Cercospora beticola OX=122368 GN=CTB12 PE=3 SV=1
sp|E9RBR0|ABR2_ASPFU	2.54e-144	40	603	22	582	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	1.27e-134	44	605	31	601	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|A0A1S7IUL2|MCE_TALPI	2.09e-128	51	601	36	589	Multicopper oxidase MCE OS=Talaromyces pinophilus OX=128442 GN=MCE PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.499798	0.500205	CS pos: 20-21. Pr: 0.2783

TMHMM  Annotations     

There is no transmembrane helices in KIW14452.1.