CAZyme Information: KIW07385.1

Basic Information

• Species: Verruconis gallopava
• Lineage: Ascomycota; Dothideomycetes; ; Sympoventuriaceae; Verruconis; Verruconis gallopava
• CAZyme ID: KIW07385.1
• CAZy Family: GT2
• CAZyme Description: unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
566	KN847533|CGC5	62671.44	4.8318

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_VgallopavaCBS43764	9871	N/A	53	9818

• Gene Location: location=KN847533:886570-888386(+)

Full Sequence      

MRSLLIALFSAPLIVLAKTIEREWNITWVSAAPDGYTRPVIGINGQWPCPELRAAKGDKI
IVTINNMLGNQSTGLHWHGIHQRGTPQMDGASGIHQCPVPPGSSFTYEWTAEQAGTYWYH
SHNDAQYPDGLWGPLIIEDDCYPFEYDEEIVMTLTDWYHEQAPDLVALYQSKQGEAADGT
PVPSGGALINTGKNVTISVKPDTTYLIRIICPGSYPGHAWVFDGHNQTTVAIDGVYTKPA
QVNLGGNLTRIAPGQRQDVLIRTKSETDKNYAIWDTMDVNMLFINKGIIPPPANYNPNVT
AWLVYNESAPLPDPPVFHEISNSNFWDDCDYEPLDGTPLLEPVDHQIIMDINAANISGIS
RFVINNETYLMQNVPSLYSALTTGDDASNPEVYGQVNPFVLKYGEVVEIVINNLNTNLHP
WHMHGRQFQLLDRPDPGWGKFNGTYRPGYPHASPAIRDTIMVQDNSWAVIRFRADNPGVW
PFHCHIELHVSSGFTATMIEAPDHLRAMNITIPEDHIAACKAFPMKYQGNAAGNTVNALD
LSGSNTQVPAVDYGAMYPPGTPPSSR

Enzyme Prediction     

No EC number prediction in KIW07385.1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	38	385	4.9e-113	0.9910979228486647

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
274555	ascorbase	1.94e-84	24	493	6	516	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	3.59e-73	17	505	21	551	L-ascorbate oxidase
215324	PLN02604	2.48e-72	3	493	9	539	oxidoreductase
225043	SufI	4.07e-69	4	502	10	450	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].
259966	CuRO_3_Fet3p	9.39e-65	344	502	1	160	The third Cupredoxin domain of multicopper oxidase Fet3p. Fet3p catalyzes the ferroxidase reaction, which couples the oxidation of Fe(II) to Fe(III) with the four-electron reduction of molecular oxygen to water. Fet3p is a type I membrane protein with the amino-terminal oxidase domain in the extracellular space and the carboxyl terminus in the cytoplasm. The periplasmic produced Fe(III) is transferred to the permease Ftr1p for import into the cytosol. The four copper ions are inserted post-translationally and are essential for catalytic activity, thus linking copper and iron homeostasis. Like other related multicopper oxidases (MCOs), Fet3p 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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QGA16578.1|AA1_2	2.85e-216	15	559	17	551
QKX61289.1|AA1_2	1.43e-211	17	563	19	555
QQK43508.1|AA1_2	1.33e-209	17	557	18	548
BCS26736.1|AA1_2	3.53e-181	2	477	3	475
BCS11789.1|AA1_2	2.99e-180	16	520	18	518

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1ZPU_A	5.44e-127	23	547	6	527	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]
1AOZ_A	1.04e-64	23	500	7	523	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]
3KW7_A	3.78e-61	23	503	7	476	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]
1HFU_A	1.07e-58	25	500	10	468	Chain A, LACCASE 1 [Coprinopsis cinerea]
1A65_A	1.10e-58	25	500	10	468	Chain A, Laccase [Coprinopsis cinerea]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q4WZB4|ABR1_ASPFU	2.02e-179	17	523	18	521	Multicopper oxidase abr1 OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=abr1 PE=2 SV=2
sp|K7NCS2|FETC_EPIFE	2.60e-161	17	546	20	540	Iron transport multicopper oxidase fetC OS=Epichloe festucae (strain E2368) OX=696363 GN=fetC PE=2 SV=1
sp|E9R598|FETC_ASPFU	4.93e-151	17	545	20	536	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|W3X7K0|PFMAD_PESFW	9.79e-149	17	558	20	545	Multicopper oxidase PfmaD OS=Pestalotiopsis fici (strain W106-1 / CGMCC3.15140) OX=1229662 GN=PfmaD PE=2 SV=1
sp|I1RMG9|FET3_GIBZE	1.02e-146	7	545	11	540	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

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000207	0.999775	CS pos: 17-18. Pr: 0.9796

TMHMM  Annotations     

There is no transmembrane helices in KIW07385.1.