CAZyme Information: HMPREF1541_09043-t46_1-p1

Basic Information

• Species: Cyphellophora europaea
• Lineage: Ascomycota; Eurotiomycetes; ; Cyphellophoraceae; Cyphellophora; Cyphellophora europaea
• CAZyme ID: HMPREF1541_09043-t46_1-p1
• CAZy Family: GT2
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
713	KB822725|CGC1	78430.98	4.5143

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_CeuropaeaCBS101466	11153	1220924	59	11094

• Gene Location: location=KB822725:1555989-1558595(-)

Full Sequence      

MRPPQSIVLFLLWLNSQCVLGALRSYNFTIHEGDRAPDGVMRKVYLINDQQPGPLIEADE
GDDLEIFVQNNLRVEQTIHWHGLLQRGTAEMDGVPGVTQFPIPANGNFTYRFSTASEYGF
FWYHSHFRAYYNDAVRGPLIIHPSPSRRRPFESLAADSAELDTMLRVERDATPILLTDWY
HRSSDLIFEEYFTTGAFPQCVDSLLANGQGRVQCLPENVLQAGPGLGIQSYVANDPHDPE
PMEMSTPMPSQSMSSMSSSETSNSKMPIETMSASTMSMSSMSMDPSMSMRKRSEHTAMTM
PMSDSPASDMGSPTASMSGMSDMSTLGPKGCSMPMMFMPGFNASSLPLETCSNTTSDVFM
FDVDASRGWAAFHLVNAAAVSRMSVSLDGHSMIVYAADGLYVEPQEVKVLHISIGQRYSV
MVRLDQQQGMYSLRFASYPYGDMQQIIEGHAMMSYMDKNMTSGATLVEEPSLTWMLVNGS
AKLDASELDDQKLAPFEGVSPPNGPSNVTQLFTINQTGIVTWVVNDQAYSEPTTPIIYGS
VSDGWDSATTLRLPGNATIDLIMHVANDSMDVMGHPIHLHGHKFWFLGAGQGMFPYNSVD
AAPSSMINLENPPYRDTIDLPASGWAVVRYVTDNPGAWLLHCHVQWHLVSGMAVVLVENE
EQMLTMVGSIENAANNPNMPGMQSGGLSLTFATKPIFLFLAILLTTLADLPLF

Enzyme Prediction     

No EC number prediction in HMPREF1541_09043-t46_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	40	216	3.2e-52	0.44692737430167595
AA1	351	653	1.1e-41	0.5363128491620112

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
259919	CuRO_1_Abr2_like	6.57e-56	28	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.
274555	ascorbase	1.42e-54	24	674	2	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.
259926	CuRO_1_Diphenol_Ox	1.77e-54	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	2.07e-50	21	142	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.
177843	PLN02191	2.64e-50	22	674	22	558	L-ascorbate oxidase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QOD95012.1|AA1	4.23e-260	23	680	26	655
QLI72976.1|AA1	1.05e-257	6	698	16	685
QPG98040.1|AA1	2.48e-247	5	683	7	658
UPL00042.1|AA1	2.03e-238	7	629	2	601
ATY66532.1|AA1	1.40e-231	19	686	12	643

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3KW7_A	2.09e-45	27	659	7	473	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]
3V9E_A	2.49e-44	21	663	65	547	Structure of the L499M mutant of the laccase from B.aclada [Botrytis aclada]
5A7E_A	3.13e-44	27	659	7	467	Chain A, CORIOLOPSIS GALLICA LACCASE [Coriolopsis gallica]
2HRG_A	5.83e-44	27	659	7	467	Crystal Structure of Blue Laccase from Trametes trogii complexed with p-methylbenzoate [Coriolopsis trogii],2HRH_A Crystal Structure of Blue Laccase from Trametes trogii [Coriolopsis trogii]
4JHU_A	5.83e-44	27	659	7	467	T2-depleted laccase from Coriolopsis caperata soaked with CuCl [Coriolopsis caperata],4JHV_A T2-depleted laccase from Coriolopsis caperata [Coriolopsis caperata]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|W3X732|PFMAY_PESFW	1.18e-88	11	687	10	591	Laccase PFICI_06862 OS=Pestalotiopsis fici (strain W106-1 / CGMCC3.15140) OX=1229662 GN=PFICI_06862 PE=3 SV=1
sp|E9RBR0|ABR2_ASPFU	5.79e-77	12	658	1	571	Laccase abr2 OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=abr2 PE=1 SV=1
sp|A0A1S7IUL2|MCE_TALPI	1.69e-70	6	666	7	588	Multicopper oxidase MCE OS=Talaromyces pinophilus OX=128442 GN=MCE PE=1 SV=1
sp|I1RF62|GIP1_GIBZE	7.47e-69	4	686	5	619	Multicopper oxidase GIP1 OS=Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1) OX=229533 GN=GIP1 PE=1 SV=1
sp|A0A443HK79|VDTB1_BYSSP	1.13e-66	9	662	5	589	Multicopper oxidase VdtB OS=Byssochlamys spectabilis OX=264951 GN=VdtB PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000249	0.999738	CS pos: 21-22. Pr: 0.9745

TMHMM  Annotations     

There is no transmembrane helices in HMPREF1541_09043-t46_1-p1.