CAZyme Information: MELLADRAFT_124640-t26_1-p1

Basic Information

• Species: Melampsora larici-populina
• Lineage: Basidiomycota; Pucciniomycetes; ; Melampsoraceae; Melampsora; Melampsora larici-populina
• CAZyme ID: MELLADRAFT_124640-t26_1-p1
• CAZy Family: CE5
• CAZyme Description: multi-copper oxidase laccase-like protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
595		65769.40	6.8817

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=GL883101:1227520-1230565(-)

Full Sequence      

MALGSLYTVNSSSSQDGPTAKKHARRQNNHVQVNSQELNLSPDFVITSTPQTRNYVFEIT
EETAAMDGFERAEGFSEWIRRVLVINKQFPGPLIEANDGDTLNILVKNHITLPVAIHWHG
IWQKGTPWMDGVSGVTQCPIPAGASFTYSFKLDGQFGTFWYHAHSQNLVADGLMGPLIVH
SVDDPLKRGRDYDNDIVLFYTDWYHDRMSTVMLNALMSPQRYRGSWAAPSPNSALVNGIG
YFHCAYAEEGSVCEQSNIKLELKVAPNEKTRLRLIDGAAHAMFRFSADGHPLTIIEADAT
GVKGSSNIHRLPIHGGQRYSVILDTTNDTVGSSFLLRSVMDTDCFAWLAPGMEGRARSVI
AVVKVVAKEEKGRCGCSSKNTPTHQIKKPSRSEGQCTEHDAWKESGFGALVYPDPTNRDH
MLRVGRFFVNGVPWKAHIFKPLLARMMKGGNGKLNESEVGFVTLEKPGWYDIVINNLDRG
LDHPYHLHGVDSYLVGKGTGRLTENSTIQPTESLSNPPRRDTYVIPADSHIIIRILADNP
GVFMLHCHLGWHLGDGFAGVIVMQPQILSTLEEPALNRDLCRVTAGSNANDTEAG

Enzyme Prediction     

No EC number prediction in MELLADRAFT_124640-t26_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	78	557	5.9e-95	0.9776536312849162

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
259971	CuRO_3_Diphenol_Ox	1.89e-83	401	563	2	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	2.37e-72	196	356	1	159	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.
177843	PLN02191	5.25e-64	82	562	44	545	L-ascorbate oxidase
274555	ascorbase	3.67e-63	52	561	1	520	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	2.08e-61	53	180	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QRV91744.1|AA1	6.59e-154	43	595	38	574
QRV76916.1|AA1	6.59e-154	43	595	38	574
QRV98945.1|AA1	7.13e-153	37	595	52	606
QRW13493.1|AA1	1.01e-152	37	595	52	606
QRW05810.1|AA1	2.97e-152	43	595	38	574

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3V9E_A	2.56e-62	46	581	61	561	Structure of the L499M mutant of the laccase from B.aclada [Botrytis aclada]
3SQR_A	2.56e-62	46	581	61	561	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]
5LM8_A	7.06e-62	46	581	17	522	Crystal structure of a laccase-like multicopper oxidase McoG from from Aspergillus niger [Aspergillus niger]
5LWW_A	7.21e-62	46	581	18	523	Crystal structure of a laccase-like multicopper oxidase McoG from Aspergillus niger bound to zinc [Aspergillus niger]
6H5Y_A	8.34e-62	67	581	12	485	PM1 mutant, 7D5 [Aspergillus oryzae],6H5Y_B PM1 mutant, 7D5 [Aspergillus oryzae]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q55P57|LAC1_CRYNB	3.40e-129	9	584	18	581	Laccase-1 OS=Cryptococcus neoformans var. neoformans serotype D (strain B-3501A) OX=283643 GN=LAC1 PE=1 SV=1
sp|J9VY90|LAC1_CRYNH	1.35e-128	9	584	18	581	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|J9VQZ4|LAC2_CRYNH	1.52e-125	40	584	49	581	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|A0A067XMP2|PTAK_PESFW	7.41e-66	47	582	59	567	Oxydoreductase ptaK OS=Pestalotiopsis fici (strain W106-1 / CGMCC3.15140) OX=1229662 GN=ptaK PE=2 SV=2
sp|W3X7K0|PFMAD_PESFW	5.32e-63	45	592	15	522	Multicopper oxidase PfmaD OS=Pestalotiopsis fici (strain W106-1 / CGMCC3.15140) OX=1229662 GN=PfmaD PE=2 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000057	0.000002

TMHMM  Annotations     

There is no transmembrane helices in MELLADRAFT_124640-t26_1-p1.