CAZyme Information: PV10_05279-t45_4-p1

Basic Information

• Species: Exophiala mesophila
• Lineage: Ascomycota; Eurotiomycetes; ; Herpotrichiellaceae; Exophiala; Exophiala mesophila
• CAZyme ID: PV10_05279-t45_4-p1
• CAZy Family: GH47
• CAZyme Description: hypothetical protein, variant 3

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
631		69365.28	4.9892

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_EmesophilaCBS40295	9237	N/A	56	9181

• Gene Location: location=KN847522:5081096-5083255(+)

Full Sequence      

MLSYPHLIVLLACSAVQNALAASRSYELTLSTGIRSPDGFAREVYLINNQQPGPLIEAEE
GDDLEIFVQNDLPVETTIHWHGLLQRGTPDMDGVPGVTQFPIPPGGNFTYRFSTADEYGF
YWYHSHFRAYYNDALRGPLLIHPSPSRPRPFKTLAQSSSEFDMMLQVERSGTILLLSDWY
HRLSDRIYDEYFTTGAFPQCVDSLLANGRGRVQCLPQNILEAGPGLGLESNIANDPHDPD
AMSMAMESSTTSGMGMASMSMDTASMPALTTDAMSMSMRKRSDHTASPSTGTAMSDMSAM
SSTLTSMATMGSSTASVGTEDQTMSTTVDMPQMTLGPRGCSPPMMFRPGFNASSLPLETC
TNTTSELFTFTADASRGWTALHLVNAGAVSRLSVSLDGHSMFVYEADGLYVTLQEVQVLH
ISIGQRYSVMIRLDQNPGDYSFRFAAYPYGDMQQVIEGQAILSYQNMTNNTNMTMMSRMV
SPWMLVNGSATSGTVELDDQTLAPFMGNTAPSGAANVTRHFAINQTDIVTWVANREPFVE
PARPIIYGSVSDGWNATTTLLTPANATVDIIMKVANDSMDTVSSPIRSTQRHSNFWLTRY
HFIDGPSDAPTRPQILVPRVRRRRLSIRICY

Enzyme Prediction     

No EC number prediction in PV10_05279-t45_4-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	40	222	3.4e-53	0.44692737430167595

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
259919	CuRO_1_Abr2_like	3.08e-65	26	142	1	117	The first cupredoxin domain of a group of fungal Laccases similar to Abr2 from Aspergillus fumigatus. Abr2 is involved in conidial pigment biosynthesis in Aspergillus fumigatus. 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. Laccase 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. Like other related multicopper oxidases (MCOs), laccase 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 1 of 3-domain MCOs contains part the trinuclear copper binding site, which is located at the interface of domains 1 and 3.
259926	CuRO_1_Diphenol_Ox	4.87e-58	24	142	1	119	The first cupredoxin domain of fungal laccase, diphenol oxidase. Diphenol oxidase belongs to the laccase family. It catalyzes the initial steps in melanin biosynthesis from diphenols. Melanin is one of the virulence factors of infectious fungi. In the pathogenesis of C. neoformans, melanin pigments have been shown to protect the fungal cells from oxidative and microbicidal activities of host defense systems. Laccase is a blue multicopper oxidase (MCO) which 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. 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.
259923	CuRO_1_MaLCC_like	9.42e-52	24	142	4	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.
259869	CuRO_1_LCC_like	1.61e-47	24	142	1	120	Cupredoxin domain 1 of laccase-like multicopper oxidases; including laccase, CueO, spore coat protein A, ascorbate oxidase and similar proteins. Laccase-like multicopper oxidases (MCOs) in this family contain three cupredoxin domains. They are able to couple oxidation of substrates with reduction of dioxygen to water. MCOs are capable of oxidizing a vast range of substrates, varying from aromatic to inorganic compounds such as metals. Although the members of this family have diverse functions, majority of them have three cupredoxin domain repeats. 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. Also included in this family are cupredoxin domains 1, 3, and 5 of the 6-domain MCO ceruloplasmin and similar proteins.
400195	Cu-oxidase_3	2.20e-47	29	146	1	119	Multicopper oxidase. This entry contains many divergent copper oxidase-like domains that are not recognized by the pfam00394 model.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
UPL00042.1|AA1	3.44e-213	21	617	17	579
QOD95012.1|AA1	4.91e-204	1	597	1	562
QPG98040.1|AA1	1.06e-198	3	586	5	552
ATY66532.1|AA1	2.02e-196	16	611	12	583
QLI72976.1|AA1	6.23e-191	19	586	27	565

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3KW7_A	8.41e-31	27	211	7	176	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]
5NQ7_A	1.43e-29	9	211	11	197	Crystal structure of laccases from Pycnoporus sanguineus, izoform I [Trametes sanguinea]
4JHU_A	5.10e-29	27	211	7	175	T2-depleted laccase from Coriolopsis caperata soaked with CuCl [Coriolopsis caperata],4JHV_A T2-depleted laccase from Coriolopsis caperata [Coriolopsis caperata]
5NQ8_A	6.29e-29	9	211	11	197	Crystal structure of laccases from Pycnoporus sanguineus, izoform II [Trametes coccinea],5NQ9_A Crystal structure of laccases from Pycnoporus sanguineus, izoform II, monoclinic [Trametes sanguinea],5NQ9_C Crystal structure of laccases from Pycnoporus sanguineus, izoform II, monoclinic [Trametes sanguinea]
3PXL_A	9.50e-29	27	211	7	176	Type-2 Cu-depleted fungus laccase from Trametes hirsuta [Trametes hirsuta]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|W3X732|PFMAY_PESFW	1.82e-62	24	553	23	439	Laccase PFICI_06862 OS=Pestalotiopsis fici (strain W106-1 / CGMCC3.15140) OX=1229662 GN=PFICI_06862 PE=3 SV=1
sp|E9RBR0|ABR2_ASPFU	6.64e-54	10	465	8	364	Laccase abr2 OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=abr2 PE=1 SV=1
sp|P17489|LAC1_EMENI	2.05e-50	16	594	17	515	Laccase-1 OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=yA PE=2 SV=3
sp|A0A1S7IUL2|MCE_TALPI	5.11e-47	27	505	27	406	Multicopper oxidase MCE OS=Talaromyces pinophilus OX=128442 GN=MCE PE=1 SV=1
sp|A0A0B4HQH6|MLAC1_METMF	2.27e-44	4	583	4	504	Laccase 1 OS=Metarhizium majus (strain ARSEF 297) OX=1276143 GN=Mlac1 PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000243	0.999720	CS pos: 21-22. Pr: 0.9718

TMHMM  Annotations     

There is no transmembrane helices in PV10_05279-t45_4-p1.