CAZyme Information: KIW05305.1

Basic Information

• Species: Verruconis gallopava
• Lineage: Ascomycota; Dothideomycetes; ; Sympoventuriaceae; Verruconis; Verruconis gallopava
• CAZyme ID: KIW05305.1
• CAZy Family: GH5
• CAZyme Description: unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
600		67411.86	4.7781

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=KN847538:506821-508983(-)

Full Sequence      

MLGRKRIGHNLVLSSLIFCTFGSPTSSAHVSDSSGYGPNNRGVWVDGFDIFSDYTNNSVI
PPGKLVEYEFTLSQEWIFPDGYPKLGQVVNGQYPGPTVEANWGDTIRVTVHNNFTEDYNG
TAIHWHGIRQYQTNWLDGVPGVTQCPSKPLDTQIYEFRAMQYGTSWYHGHLSLQYSNGLY
GPIVIHGPSSANWDEDLGPWLLSDWYHADVFGLEWIGETTFLAALPDSIVLNGKGTFQDK
GELYEVVVSKNKKYKIGLINTSTLLTYNFWIDGHNLTIIQTDFVPIEPYTVPVLNIGIGQ
RYEFIIETNADLSKGNNFWVNAQYCAEPELIPLSNKIGVIRYDAADTSAPYTPPNPYLHF
GCADPDPKNLVPVVKQNVGTRVNGIGPEDYLKLGHQAYPNASDFPGKVRKWIIQETPQFV
DWQKPSLWQYATSDNVTLPPEAVPFILDFETEEWVYFVITSNYTLLPTDIPRNLTPSVHP
MHLHGHDFNILAQGEGMIPDEPELNFVNPARRDVIDIDIGGWAVIAFQINNPGAWLFHCH
IAFHSSAGLSLQFIEQPSKIKPLLKSAGILPEFEDRCKAWSEWYNTVNIPKNAVIEDSGI

Enzyme Prediction     

EC	1.10.3.2:4	1.10.3.-:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	54	356	2e-112	0.9711538461538461

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
177843	PLN02191	2.69e-73	65	560	23	551	L-ascorbate oxidase
274555	ascorbase	1.28e-72	66	567	8	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	8.72e-66	63	566	22	557	oxidoreductase
259923	CuRO_1_MaLCC_like	5.15e-63	63	186	1	122	The first cupredoxin domain of the fungal laccases similar to Ma-LCC from Melanocarpus albomyces. The subfamily of fungal laccases includes Ma-LCC and similar proteins. Ma-LCC is a multicopper oxidase (MCO) from Melanocarpus albomyces. Its crystal structure contains all four coppers at the mono- and trinuclear copper centers. 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. It 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. Although MCOs have diverse functions, majority of them have three cupredoxin domain repeats 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.
225043	SufI	8.68e-59	61	557	29	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].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BAA08486.1|AA1_3|1.10.3.-	1.64e-263	12	600	8	605
QLI68968.1|AA1_3	2.12e-253	13	600	7	601
QIW99253.1|AA1_3	5.47e-244	5	600	22	621
QED41496.1|AA1_3	1.69e-238	36	600	38	613
AEO66253.1|AA1_3	2.39e-211	10	600	5	625

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3SQR_A	2.41e-112	59	600	61	580	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]
3V9E_A	4.78e-112	59	600	61	580	Structure of the L499M mutant of the laccase from B.aclada [Botrytis aclada]
3PPS_A	1.24e-108	38	591	48	599	Crystal structure of an ascomycete fungal laccase from Thielavia arenaria [Canariomyces arenarius],3PPS_B Crystal structure of an ascomycete fungal laccase from Thielavia arenaria [Canariomyces arenarius],3PPS_C Crystal structure of an ascomycete fungal laccase from Thielavia arenaria [Canariomyces arenarius],3PPS_D Crystal structure of an ascomycete fungal laccase from Thielavia arenaria [Canariomyces arenarius]
1GW0_A	1.55e-99	38	591	7	554	Crystal Structure of Laccase from Melanocarpus albomyces in Four Copper Form [Melanocarpus albomyces],1GW0_B Crystal Structure of Laccase from Melanocarpus albomyces in Four Copper Form [Melanocarpus albomyces],2IH8_A A low-dose crystal structure of a recombinant Melanocarpus albomyces laccase [Melanocarpus albomyces],2IH8_B A low-dose crystal structure of a recombinant Melanocarpus albomyces laccase [Melanocarpus albomyces],2IH9_A A high-dose crystal structure of a recombinant Melanocarbus albomyces laccase [Melanocarpus albomyces],2IH9_B A high-dose crystal structure of a recombinant Melanocarbus albomyces laccase [Melanocarpus albomyces],3FU7_B Melanocarpus albomyces laccase crystal soaked (4 sec) with 2,6-dimethoxyphenol [Melanocarpus albomyces],3FU9_A Melanocarpus albomyces laccase crystal soaked (20 min) with 2,6-dimethoxyphenol [Melanocarpus albomyces],3FU9_B Melanocarpus albomyces laccase crystal soaked (20 min) with 2,6-dimethoxyphenol [Melanocarpus albomyces],3QPK_A Probing oxygen channels in Melanocarpus albomyces laccase [Melanocarpus albomyces],3QPK_B Probing oxygen channels in Melanocarpus albomyces laccase [Melanocarpus albomyces]
3DKH_A	1.55e-99	38	591	7	554	L559A mutant of Melanocarpus albomyces laccase [Melanocarpus albomyces],3DKH_B L559A mutant of Melanocarpus albomyces laccase [Melanocarpus albomyces]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q4WQY8|TPCJ_ASPFU	2.67e-268	19	600	13	609	Oxidoreductase tpcJ OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=tpcJ PE=2 SV=1
sp|Q0CCX6|GEDJ_ASPTN	8.33e-264	12	600	8	605	Dihydrogeodin oxidase OS=Aspergillus terreus (strain NIH 2624 / FGSC A1156) OX=341663 GN=gedJ PE=1 SV=1
sp|A0A067XMP0|PTAE_PESFW	4.57e-250	41	600	33	610	Oxidoreductase ptaE OS=Pestalotiopsis fici (strain W106-1 / CGMCC3.15140) OX=1229662 GN=ptaE PE=2 SV=2
sp|J5JH35|OPS5_BEAB2	4.62e-131	32	600	42	590	Oxidoreductase OpS5 OS=Beauveria bassiana (strain ARSEF 2860) OX=655819 GN=OpS5 PE=1 SV=1
sp|D4APX3|LAC1_ARTBC	1.18e-109	53	600	86	633	Laccase ARB_05828 OS=Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) OX=663331 GN=ARB_05828 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000741	0.999228	CS pos: 28-29. Pr: 0.9579

TMHMM  Annotations     

There is no transmembrane helices in KIW05305.1.