CAZyme Information: MELLADRAFT_90956-t26_1-p1

Basic Information

• Species: Melampsora larici-populina
• Lineage: Basidiomycota; Pucciniomycetes; ; Melampsoraceae; Melampsora; Melampsora larici-populina
• CAZyme ID: MELLADRAFT_90956-t26_1-p1
• CAZy Family: GT4
• CAZyme Description: multi-copper-oxidase laccase-like protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
677		73513.02	6.6076

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_Mlarici-populina98AG31	16380	747676	8	16372

Full Sequence      

MMISNLVNCGTKWSADAPKSQYQLSPDFKICSDKVTRKYEFVITNTTAAPDGFLRTVLAI
NNQIPGPLIEVNEGDSLEVTVVNHSGGPLTIHWHGLYQNGTNWEDGPTGITQCPIAAGIS
YTYKFTVDNQFGTFWYHAHALNTMADGIHGPLIVHSTRDPLVRGIDFDEEAVLVLADWYH
NTSAQIIHDMFYTDKGYFGTPGTPSPNSVVMNGVGEWDCKYATTQQFCKPTTVLPEFSVA
AGNKIRFRLINSGSHSMLFFSADEHALNVTEADATPVHGPSKVHRLKFHNGQRYSVIVTI
DSKEAGNSFYIRASADTDCWAWVSADLQTTARGIVRVAKPGKTLSSKDKQVRPNSKDWSD
PANGPCVDLDPDLLSPIIPQEVPTTVAGSGQFANAFGFVSVLEGEKVANPPPPPSPPSGT
GNPRNTGITRNTTGASKALGSDSEISLGASLSTSDIPIILKRQISTGVDSASIPAGTAAL
PPNFTVIPGLPTIPREARGAFFVNNVTWATYPYQPIMHDLAPGGVGKVNSDRVANVVYPT
EDWYDLYLVNMDPALAHAYHLHGMDMHIVAIGQGQPTPESLAKLDYNTKNPLRRDTIAIA
AGTFVVARLFTDLPGVWAMHCHFGWHLAIGFAGVVVVQPDKIAKFKIPDENLALCSHGQA
NEREPGRRKRSIITEFR

Enzyme Prediction     

No EC number prediction in MELLADRAFT_90956-t26_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	47	631	8e-97	0.9804469273743017

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
259971	CuRO_3_Diphenol_Ox	1.15e-83	472	637	5	158	The third 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 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.
259950	CuRO_2_Diphenol_Ox	2.59e-75	172	337	2	163	The second 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 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. Laccase is a multicopper oxidase (MCO) 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 2 of 3-domain MCOs has lost the ability to bind copper.
259926	CuRO_1_Diphenol_Ox	7.10e-66	37	155	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	5.19e-50	35	155	2	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	1.02e-49	37	652	24	559	L-ascorbate oxidase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QRV98945.1|AA1	QRV98945.1|AA1	3.68e-155	20	656	51	592
QRW13493.1|AA1	QRW13493.1|AA1	7.35e-155	20	656	51	592
QRV91744.1|AA1	QRV91744.1|AA1	1.91e-149	27	656	38	560
QRV76916.1|AA1	QRV76916.1|AA1	1.91e-149	27	656	38	560
QRW05810.1|AA1	QRW05810.1|AA1	6.74e-147	27	656	38	560

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3KW7_A	3KW7_A	8.54e-60	40	655	7	491	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]
2QT6_A	2QT6_A	3.81e-57	40	655	7	487	Chain A, Laccase [Lentinus tigrinus],2QT6_B Chain B, Laccase [Lentinus tigrinus]
4A2D_A	4A2D_A	1.85e-56	40	655	7	485	Coriolopsis gallica Laccase T2 Copper Depleted at pH 4.5 [Coriolopsis gallica],4A2E_A Crystal Structure of a Coriolopsis gallica Laccase at 1.7 A Resolution pH 5.5 [Coriolopsis gallica],4A2G_A Coriolopsis gallica laccase collected at 8.98 keV [Coriolopsis gallica],4A2H_A Crystal Structure of Laccase from Coriolopsis gallica pH 7.0 [Coriolopsis gallica]
5A7E_A	5A7E_A	1.85e-56	40	655	7	485	Chain A, CORIOLOPSIS GALLICA LACCASE [Coriolopsis gallica]
4A2F_A	4A2F_A	1.89e-56	40	655	7	485	Coriolopsis gallica laccase collected at 12.65 keV [Coriolopsis gallica]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|J9VQZ4|LAC2_CRYNH	sp|J9VQZ4|LAC2_CRYNH	2.17e-111	12	668	37	591	Laccase-2 OS=Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 / CBS 10515 / FGSC 9487) OX=235443 GN=LAC2 PE=3 SV=2
sp|J9VY90|LAC1_CRYNH	sp|J9VY90|LAC1_CRYNH	3.58e-111	12	671	37	594	Laccase-1 OS=Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 / CBS 10515 / FGSC 9487) OX=235443 GN=LAC1 PE=1 SV=1
sp|Q55P57|LAC1_CRYNB	sp|Q55P57|LAC1_CRYNB	1.05e-105	12	671	37	594	Laccase-1 OS=Cryptococcus neoformans var. neoformans serotype D (strain B-3501A) OX=283643 GN=LAC1 PE=1 SV=1
sp|Q01679|LAC1_PHLRA	sp|Q01679|LAC1_PHLRA	4.87e-61	40	655	28	509	Laccase OS=Phlebia radiata OX=5308 GN=LAC PE=1 SV=2
sp|A0A067XMP2|PTAK_PESFW	sp|A0A067XMP2|PTAK_PESFW	2.60e-60	35	648	63	559	Oxydoreductase ptaK OS=Pestalotiopsis fici (strain W106-1 / CGMCC3.15140) OX=1229662 GN=ptaK PE=2 SV=2

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000050	0.000004

TMHMM  Annotations     

There is no transmembrane helices in MELLADRAFT_90956-t26_1-p1.