CAZyme Information: EHY56497.1

Basic Information

• Species: Exophiala dermatitidis
• Lineage: Ascomycota; Eurotiomycetes; ; Herpotrichiellaceae; Exophiala; Exophiala dermatitidis
• CAZyme ID: EHY56497.1
• CAZy Family: GH36
• CAZyme Description: unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
736		79682.94	5.6477

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_EdermatitidisNIHUT8656	9356	858893	71	9285

• Gene Location: location=JH226133:705237-707447(+)

Full Sequence      

MCRSICFLKVVFCLCAIIVAVGAFNSSTTTSTARSYNYTSGYSNSSSRTTTTTSSQIDTF
TYPPSPQDTVTHILPESISDIIFPTAIPLRPIRPQNIRSGRWGLPQARTNGRSLLGTLPQ
GGKGGAPRFPRFLGVPGYGGGVYAGNNNCNSDDCNGASNGSGETTTPGPQFAGGGQGGGP
RTFPWGSRTATNTDPYSDPPKTGVVRKYNFVIKRSVMAPDGVERDVIVINGQFPGPTIEA
NWGDTIEVTVVNAITGPQEGTSLHWHGLLQKGTPYEDGVPGVTQCPIAPGQTFTYSFNAD
LYGTSWYHAHYSAQYAGGVFGAMIIHGPVNAQYDVDLGPVLLTDYYHGSYYDLVEQVMGT
DLNKVAPPSDNNLINGKGTFDCSVIGNSTNCTSGAGYSKFQFTKGQSYRLRLINAGAEAI
QKFSIDNHQLKVIAYDFVPIVPYTTQIVTLGAGQRADVVVEASGASTDAVWMRTVISNCS
LTNQPYGYAMVYYEKADVYSKPNTTAWPDTTPTGVDHCANDALSLTTPYFPISPPSTPAN
EISVDLNFGLNATGHLVWTMNNSTFRTCYNDPVLVRTQENASNTNNGTLQFPTEWNVFDF
GNASSIRIILRNLSPIPHPMHMHGHNMYLLAEGMGEWDGTIVRPENPMRRDTQLLRPADA
SGNPGYMVLQIDADNPGVWPFHCHIAWHVSGGLYLNILEHPDDIANIQTPSEVTDLCQTW
GDYTRLGPIDQIDSGL

Enzyme Prediction     

EC	1.10.3.2:2	-

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	193	509	4.2e-121	0.9807692307692307

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
274555	ascorbase	2.32e-76	205	713	1	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	1.09e-72	205	693	24	540	oxidoreductase
259923	CuRO_1_MaLCC_like	1.26e-71	203	326	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.
259968	CuRO_3_MaLCC_like	9.96e-69	533	698	1	157	The third 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 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.
177843	PLN02191	1.22e-66	202	712	20	557	L-ascorbate oxidase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
APA07098.1|AA1_3	3.21e-224	180	736	50	596
QIW99529.1|AA1_3	5.72e-224	180	736	109	663
ATZ52184.1|AA1_3	5.77e-223	180	736	40	589
ATZ46043.1|AA1_3	3.50e-220	180	736	50	593
QFF92556.1|AA1_3	1.14e-218	180	736	50	593

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5LM8_A	8.02e-112	192	728	10	533	Crystal structure of a laccase-like multicopper oxidase McoG from from Aspergillus niger [Aspergillus niger]
5LWW_A	8.26e-112	192	728	11	534	Crystal structure of a laccase-like multicopper oxidase McoG from Aspergillus niger bound to zinc [Aspergillus niger]
5LWX_A	9.15e-112	192	728	38	561	Crystal structure of the H253D mutant of McoG from Aspergillus niger [Aspergillus niger]
3SQR_A	4.90e-108	185	736	49	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	9.66e-108	185	736	49	580	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|A0A067XMP2|PTAK_PESFW	4.03e-185	180	736	40	585	Oxydoreductase ptaK OS=Pestalotiopsis fici (strain W106-1 / CGMCC3.15140) OX=1229662 GN=ptaK PE=2 SV=2
sp|Q96WM9|LAC2_BOTFU	1.13e-109	185	736	49	581	Laccase-2 OS=Botryotinia fuckeliana OX=40559 GN=lcc2 PE=2 SV=1
sp|J5JH35|OPS5_BEAB2	5.04e-106	185	736	54	590	Oxidoreductase OpS5 OS=Beauveria bassiana (strain ARSEF 2860) OX=655819 GN=OpS5 PE=1 SV=1
sp|Q12570|LAC1_BOTFU	6.72e-100	185	736	47	561	Laccase-1 OS=Botryotinia fuckeliana OX=40559 GN=lcc1 PE=2 SV=3
sp|Q96UM2|LAC3_BOTFU	4.04e-97	234	693	1	448	Laccase-3 (Fragment) OS=Botryotinia fuckeliana OX=40559 GN=lcc3 PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.001229	0.998760	CS pos: 23-24. Pr: 0.9304

TMHMM  Annotations     

Start	End
5	24