CAZyme Information: MELLADRAFT_124633-t26_1-p1

Basic Information

• Species: Melampsora larici-populina
• Lineage: Basidiomycota; Pucciniomycetes; ; Melampsoraceae; Melampsora; Melampsora larici-populina
• CAZyme ID: MELLADRAFT_124633-t26_1-p1
• CAZy Family: CE4
• CAZyme Description: multi-copper oxidase laccase-like protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
639		69779.92	5.2510

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

• Gene Location: location=GL883093:1639245-1642720(+)

Full Sequence      

MTMSGNSLAYQRIILVSSLLFSLFSSCYAAVKVNSSELYLSSDFKITSTAQTRNYRWTLT
NETAAPDGYTRNMLVINSHRDDFELRADRTSKNASVLALQEGDTINIVVTNTLNGSVSIH
WHGLHQNGTGWMDGVTGVTQCPIPAGSTFTYTFTVSGQYGTFWYHAHSQNYAADGVAGPL
IIHSVDDPLVRGVDYDQDVILFMNDWYHNLSALILSEQLSPEGYLGSVAAPLRSFFLDLN
HFKISSLINGIGYFDCTNADPGSTCTTPTKYLTFDLHAGRKTRLRLIEGGSHALFRVSVD
QHTLNVTEADATGVAGPTAVHRVPFHNGERYSVILDLSKDTIGSTFYLRAAMDTDCFAWL
APGMDGQAATARAIIRVVDPAATTYNTTVTTPNSTDWSDSVSGDCLDLDPDTLVPLVPED
ACTNVLGRLYYESSFGFTTTTENSTTVSLGRFFVNDTTWLTYVYQPLLSEMTSGGRGFLN
TSEVAAFTMETNGCYDIVINNLDAAINHPYHLHGVDAKTVATGTGELNDTVAATLTYNTT
NPLRRDASFEGSEHRNPRPRWNVPIRIVADNPGVWILHCHIGWHLGAGFAGVFVMNPAAV
SQFTIPAANQALCDGATAATIDEIEPGRRKRSLQSAYQF

Enzyme Prediction     

No EC number prediction in MELLADRAFT_124633-t26_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	97	589	1.8e-81	0.9329608938547486

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
259950	CuRO_2_Diphenol_Ox	3.19e-78	199	378	1	164	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.
259971	CuRO_3_Diphenol_Ox	1.58e-67	428	595	1	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.
259926	CuRO_1_Diphenol_Ox	2.26e-54	53	183	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.
274555	ascorbase	1.02e-47	52	593	1	521	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.
177843	PLN02191	1.23e-47	47	594	18	545	L-ascorbate oxidase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QRV98945.1|AA1	5.94e-161	36	635	51	612
QRW13493.1|AA1	1.19e-160	36	633	51	610
QRV91744.1|AA1	4.44e-155	43	633	38	578
QRV76916.1|AA1	4.44e-155	43	633	38	578
QRW05810.1|AA1	4.48e-152	41	633	36	578

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3SQR_A	1.80e-54	44	601	59	548	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	1.80e-54	44	601	59	548	Structure of the L499M mutant of the laccase from B.aclada [Botrytis aclada]
3KW7_A	7.49e-54	58	626	9	499	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]
5ANH_A	2.42e-53	58	626	9	493	Crystal Structure Of Laccase From Basidiomycete Pm1 (cect 2971) [basidiomycete PM1],5ANH_B Crystal Structure Of Laccase From Basidiomycete Pm1 (cect 2971) [basidiomycete PM1],5ANH_C Crystal Structure Of Laccase From Basidiomycete Pm1 (cect 2971) [basidiomycete PM1]
2QT6_A	2.52e-53	58	626	9	495	Chain A, Laccase [Lentinus tigrinus],2QT6_B Chain B, Laccase [Lentinus tigrinus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|J9VY90|LAC1_CRYNH	8.66e-112	29	613	38	578	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	9.44e-111	29	638	38	598	Laccase-1 OS=Cryptococcus neoformans var. neoformans serotype D (strain B-3501A) OX=283643 GN=LAC1 PE=1 SV=1
sp|J9VQZ4|LAC2_CRYNH	2.94e-107	29	613	38	578	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|Q12729|LAC1_PLEOS	3.71e-55	59	613	33	514	Laccase-1 OS=Pleurotus ostreatus OX=5322 GN=POX1 PE=2 SV=1
sp|Q12719|LAC4_TRAVE	1.57e-54	58	606	31	501	Laccase-4 OS=Trametes versicolor OX=5325 GN=LCC4 PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.002633	0.997334	CS pos: 29-30. Pr: 0.5046

TMHMM  Annotations     

There is no transmembrane helices in MELLADRAFT_124633-t26_1-p1.