CAZyme Information: ETI28473.1

Basic Information

• Species: Cladophialophora carrionii
• Lineage: Ascomycota; Eurotiomycetes; ; Herpotrichiellaceae; Cladophialophora; Cladophialophora carrionii
• CAZyme ID: ETI28473.1
• CAZy Family: GT25
• CAZyme Description: unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
708		75868.03	5.7388

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_CcarrioniiCBS160.54	10428	1279043	55	10373

• Gene Location: location=KB822697:2631220-2633561(+)

Full Sequence      

MRTAFAAALTGAALVGSSLADHPGPLGRWMGGGDCPWGDKTASGSHPATDMPDTGVTRYY
DFTVSRNTLAPDGVQQAVIVVNGQYPGPLIEANWGDWIEVNVHNQIYGPEEPTSIHWHGL
NQPGTPYYDGVVTVSQCPIVPGGNLTYRFRADEYGTTWYHAHYSAQYSSGVLGPIVVHGP
NDAEYDIDLGPILVTDWFHDSYEDIVSLVMSPSESGQPFRPFSDSNLVGGAGQYPCANVT
NGAPCSVVPYASWEFQPGKTHRLRFVNTGASAFESISIDGHTMTVIANDMVPVQPYETQS
ITIGVGQRTDVLVTANQAPGTYWLRAFNTPCGDSNGPDGRGIIYYSGADASLTPTSTASA
PGAVNSNCQNDPLTTTIPQYAIPVAEADTTITITVAGAPDETGVFHWTMNGVSYDGDLAN
PLLTQAVAGQTNFDARYNVINTGAVANVRIIIINLTPAPHPMHMHGHDFQVLAEGFGTWD
GTITNPQNPQRRDVQMLWAGASPDNPSYIVLQYTQDNPGLWPLHCHLAWHLSAGMVVMLL
EHPEQLSSIQIPENIAQTCPTYSAWYAANPGVAVEDGLRKRTLGEKMVDYVKGADHADHA
AAHLDKHAKRGVRGYRGYGHDATFEDFPAHGKFKGSATQGAGAFGTGKPSGSEGEGWSTK
THSGSGSEKAAKSATSKWQTHSRPSSVQSNLAKSSTTGKKTERKRDEV

Enzyme Prediction     

EC	1.10.3.2:4	1.10.3.-:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	49	359	5.3e-115	0.9615384615384616

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
274555	ascorbase	2.73e-74	57	549	1	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.
259923	CuRO_1_MaLCC_like	6.07e-67	55	178	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.
215324	PLN02604	8.62e-66	57	555	24	558	oxidoreductase
177843	PLN02191	9.81e-62	54	549	20	554	L-ascorbate oxidase
274556	laccase	3.10e-61	57	552	3	532	laccase, plant. Members of this protein family include the copper-containing enzyme laccase (EC 1.10.3.2), often several from a single plant species, and additional, uncharacterized, closely related plant proteins termed laccase-like multicopper oxidases. This protein family shows considerable sequence similarity to the L-ascorbate oxidase (EC 1.10.3.3) family. Laccases are enzymes of rather broad specificity, and classification of all proteins scoring about the trusted cutoff of this model as laccases may be appropriate.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QIW99529.1|AA1_3	1.16e-186	7	578	83	663
UJO18649.1|AA1_3	3.03e-184	17	578	119	685
APA07098.1|AA1_3	1.53e-180	36	565	54	583
QFF92555.1|AA1_3	2.21e-179	36	578	54	593
QSZ30962.1|AA1_3	4.74e-179	36	578	54	595

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5LWX_A	1.42e-109	22	570	12	561	Crystal structure of the H253D mutant of McoG from Aspergillus niger [Aspergillus niger]
5LM8_A	4.90e-109	51	570	17	533	Crystal structure of a laccase-like multicopper oxidase McoG from from Aspergillus niger [Aspergillus niger]
5LWW_A	5.05e-109	51	570	18	534	Crystal structure of a laccase-like multicopper oxidase McoG from Aspergillus niger bound to zinc [Aspergillus niger]
1GW0_A	1.40e-107	37	578	13	559	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]
2Q9O_A	2.77e-107	37	578	13	559	Near-atomic resolution structure of a Melanocarpus albomyces laccase [Melanocarpus albomyces],2Q9O_B Near-atomic resolution structure of a Melanocarpus albomyces laccase [Melanocarpus albomyces],3FU7_A Melanocarpus albomyces laccase crystal soaked (4 sec) with 2,6-dimethoxyphenol [Melanocarpus albomyces],3FU8_A Melanocarpus albomyces laccase crystal soaked (10 sec) with 2,6-dimethoxyphenol [Melanocarpus albomyces],3FU8_B Melanocarpus albomyces laccase crystal soaked (10 sec) with 2,6-dimethoxyphenol [Melanocarpus albomyces]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|A0A067XMP2|PTAK_PESFW	9.72e-147	36	559	44	566	Oxydoreductase ptaK OS=Pestalotiopsis fici (strain W106-1 / CGMCC3.15140) OX=1229662 GN=ptaK PE=2 SV=2
sp|P78722|LAC2_PODAS	1.08e-110	52	592	73	620	Laccase-2 OS=Podospora anserina OX=2587412 GN=LAC2 PE=2 SV=1
sp|J5JH35|OPS5_BEAB2	1.37e-109	37	576	54	587	Oxidoreductase OpS5 OS=Beauveria bassiana (strain ARSEF 2860) OX=655819 GN=OpS5 PE=1 SV=1
sp|Q70KY3|LAC1_MELAO	1.44e-107	37	586	63	617	Laccase-1 OS=Melanocarpus albomyces OX=204285 GN=LAC1 PE=1 SV=1
sp|Q12570|LAC1_BOTFU	7.64e-107	37	578	47	561	Laccase-1 OS=Botryotinia fuckeliana OX=40559 GN=lcc1 PE=2 SV=3

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000257	0.999688	CS pos: 20-21. Pr: 0.9797

TMHMM  Annotations     

There is no transmembrane helices in ETI28473.1.