CAZyme Information: MELLADRAFT_124650-t26_1-p1

Basic Information

• Species: Melampsora larici-populina
• Lineage: Basidiomycota; Pucciniomycetes; ; Melampsoraceae; Melampsora; Melampsora larici-populina
• CAZyme ID: MELLADRAFT_124650-t26_1-p1
• CAZy Family: CE5
• CAZyme Description: multicopper-oxidase laccase-like protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
663		73188.95	7.3419

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=GL883092:1892235-1895724(-)

Full Sequence      

MHFQNILLFFIGFVYIGTCFPQKKLAQPSTEYILGDFDINSGAVTRKFEFVCTNTTASPD
GFLRGVLAINNQIPGPLIEANEGDHLDITVINNLDSALTIHWHGLYQNGTNSEDGVTGIT
QCPIPSGGRYTYKFQLNGQFGTFWYHAHHQNLLADGLYGPLIIHSPRDPLKRGIDFDEDV
VLMIADWYHNTSSEIVKHMLSEPGYFGTPAAPSPNSVIMNGIGDWDCNRFATIHQRCEKT
NSLPVFNVVGGKRIRFRIINAGSHAMIYFSGDEHSLNVTEADSTPVYGPSNVHRIKFHNG
QRYSVIINTQEKEVGSSFYLRGTMDTDCFAWVAGDIQKTGLAIVRVIKPDEDMKSLKEFT
IPNTKDWSDEKAGSCVDLDPELLNPIIPIDVPETVAGSGTLANAFGFQVISTGVSIPRDQ
ASKLSSEPRSISSSSSSSSSPSSYSSPISRIKQRQLKLDSTRKVLPLGTATSSAPEKNQD
GPPPTPAGARGVFFVNDANWKTYPYHPVLHDMLPGGPGSLDNAEIANVVYPNAEWYDLYL
VNLDPAISHSYHLHAMDMHLVAFGKGKPTPENLSKLKYRTKNPLRRDTIVIDAASYAVVR
VLADIPGVWIMHCHIGWHLAGGFAGVVIVQPNKIKQLKIPNENKSLCKNRKSPLNQYQPG
KRR

Enzyme Prediction     

No EC number prediction in MELLADRAFT_124650-t26_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	62	623	2.5e-96	0.9776536312849162

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
259950	CuRO_2_Diphenol_Ox	4.38e-93	180	347	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	2.37e-76	481	629	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.
259926	CuRO_1_Diphenol_Ox	2.80e-65	46	164	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.
177843	PLN02191	4.17e-51	58	659	36	574	L-ascorbate oxidase
259923	CuRO_1_MaLCC_like	4.61e-50	44	164	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QRV98945.1|AA1	7.37e-160	28	647	50	591
QRW13493.1|AA1	5.87e-159	28	647	50	591
QRV82887.1|AA1	1.42e-155	22	650	24	567
QRW11634.1|AA1	2.84e-155	22	650	24	567
QRV91744.1|AA1	6.85e-155	36	647	38	559

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3SQR_A	5.94e-57	37	624	59	537	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	5.94e-57	37	624	59	537	Structure of the L499M mutant of the laccase from B.aclada [Botrytis aclada]
3KW7_A	8.23e-55	49	647	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]
3X1B_A	1.16e-53	54	626	33	488	Crystal structure of laccase from Lentinus sp. at 1.8 A resolution [Lentinus],3X1B_B Crystal structure of laccase from Lentinus sp. at 1.8 A resolution [Lentinus]
2QT6_A	5.06e-53	43	647	1	487	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|J9VQZ4|LAC2_CRYNH	9.92e-120	27	662	43	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|Q55P57|LAC1_CRYNB	3.63e-118	27	662	43	591	Laccase-1 OS=Cryptococcus neoformans var. neoformans serotype D (strain B-3501A) OX=283643 GN=LAC1 PE=1 SV=1
sp|J9VY90|LAC1_CRYNH	7.20e-118	27	662	43	591	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|A0A067XMP2|PTAK_PESFW	1.55e-63	44	648	63	567	Oxydoreductase ptaK OS=Pestalotiopsis fici (strain W106-1 / CGMCC3.15140) OX=1229662 GN=ptaK PE=2 SV=2
sp|J5JH35|OPS5_BEAB2	1.66e-61	28	634	48	556	Oxidoreductase OpS5 OS=Beauveria bassiana (strain ARSEF 2860) OX=655819 GN=OpS5 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000192	0.999757	CS pos: 21-22. Pr: 0.7302

TMHMM  Annotations     

There is no transmembrane helices in MELLADRAFT_124650-t26_1-p1.