CAZyme Information: EHY60611.1

Basic Information

• Species: Exophiala dermatitidis
• Lineage: Ascomycota; Eurotiomycetes; ; Herpotrichiellaceae; Exophiala; Exophiala dermatitidis
• CAZyme ID: EHY60611.1
• CAZy Family: GT69
• CAZyme Description: unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
747		80104.02	5.5938

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=JH226136:2135580-2138016(+)

Full Sequence      

MGVTSVLIWVTLLFAASIHAVPDFRGPGDFDFGIRARPTGRRHAGFHPTGHSRPHLFLTT
PAHPHPVGPSHRPPGPGHGSNTVSSQNPVYYSGPPIIGTASLPASLSTIVFPSNLPTSGF
PKPTSGSSLGNNALPQSETNGQSLLGTFDAPKYPLWIGHSSSGDHNHGGSPSGSPPWGNR
TASNTNPYKGAPSTGVVRSYDFVISRGTIAPDGVERSVLLVNGAFPGPTIEANWGDTIQV
TVTNSITGPEEGTALHWHGMLQKGTPYEDGVPGITQCPIAPGQTFTYSFNAALYGTTWYH
SHYSAQYAGGILGPMIIHGPLNAEYDEDLGPILLTDYYHEDYYTIVEEVMGTDLTLVAPT
SVNNLINGKGVYDCSLVSNDTTCTPNAGLSKFGFTSGQSYRLRLINAGAEGIQRFSIDNH
ALTVMAYDLVPIEPYTTNVVTLGIGQRADVIVQANGSSSDLVWMRSTISSLCSATTQPDG
LAIIYYQDANTTAEPTSSAWPIDDTSCGNDALDTTVPFYPITPPASSNDNSTTSAAAAAA
VPTVNVALNFEINSTGHFLWTMDGSSFRVDYNDPVLMLAAAGNDSHPYDPEWNMYDFGSN
QSFVIVVNNESPIAHPMHIHGHNMFVLSEGLGTWDGSVVNPSNPTRRDVQMLQPDGYMAI
QVDADNPGVWPFHCHIAWHVSGGLYINILEHPELIPSAFHIPSNVNNLCTSWDAFTNRGP
IDQIDSGLRKRNHLGNRAFSNPIRRTL

Enzyme Prediction     

EC	1.10.3.2:2	-

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	185	505	7.4e-122	0.9903846153846154

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
259923	CuRO_1_MaLCC_like	3.15e-71	195	318	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.
274555	ascorbase	5.69e-71	197	684	1	517	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	1.47e-68	197	684	24	540	oxidoreductase
259968	CuRO_3_MaLCC_like	1.22e-67	548	689	14	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	1.40e-65	193	690	19	546	L-ascorbate oxidase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
APA07098.1|AA1_3	3.25e-242	132	728	19	596
ATZ46043.1|AA1_3	2.04e-237	134	728	21	593
QFF92556.1|AA1_3	4.10e-237	132	728	19	593
QFF92555.1|AA1_3	7.65e-235	132	728	19	593
QSZ30962.1|AA1_3	1.65e-234	132	728	19	595

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3SQR_A	7.48e-119	185	728	56	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	1.48e-118	185	728	56	580	Structure of the L499M mutant of the laccase from B.aclada [Botrytis aclada]
5LM8_A	1.28e-113	184	720	10	533	Crystal structure of a laccase-like multicopper oxidase McoG from from Aspergillus niger [Aspergillus niger]
5LWW_A	1.31e-113	184	720	11	534	Crystal structure of a laccase-like multicopper oxidase McoG from Aspergillus niger bound to zinc [Aspergillus niger]
5LWX_A	1.46e-113	184	720	38	561	Crystal structure of the H253D mutant of McoG from Aspergillus niger [Aspergillus niger]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|A0A067XMP2|PTAK_PESFW	9.55e-192	176	728	44	585	Oxydoreductase ptaK OS=Pestalotiopsis fici (strain W106-1 / CGMCC3.15140) OX=1229662 GN=ptaK PE=2 SV=2
sp|Q96WM9|LAC2_BOTFU	9.98e-123	185	728	56	581	Laccase-2 OS=Botryotinia fuckeliana OX=40559 GN=lcc2 PE=2 SV=1
sp|J5JH35|OPS5_BEAB2	7.25e-118	177	715	54	576	Oxidoreductase OpS5 OS=Beauveria bassiana (strain ARSEF 2860) OX=655819 GN=OpS5 PE=1 SV=1
sp|Q12570|LAC1_BOTFU	3.36e-113	177	728	47	561	Laccase-1 OS=Botryotinia fuckeliana OX=40559 GN=lcc1 PE=2 SV=3
sp|P78722|LAC2_PODAS	1.79e-108	184	735	65	612	Laccase-2 OS=Podospora anserina OX=2587412 GN=LAC2 PE=2 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000216	0.999768	CS pos: 20-21. Pr: 0.9800

TMHMM  Annotations     

Start	End
5	22