CAZyme Information: MELLADRAFT_124658-t26_1-p1

Basic Information

• Species: Melampsora larici-populina
• Lineage: Basidiomycota; Pucciniomycetes; ; Melampsoraceae; Melampsora; Melampsora larici-populina
• CAZyme ID: MELLADRAFT_124658-t26_1-p1
• CAZy Family: CE5
• CAZyme Description: multi-copper oxidase laccase-like protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
642	GL883115|CGC2	71091.86	7.4611

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=GL883115:903563-906925(+)

Full Sequence      

MINHFGLLLLLMYGVIQDIQCHDTKEAVAPRKEYKLDCEFEVSSKKRLRKYEWIVTNTTG
APDGFWRSVLAINNQMPGPLIEANEGDDVEVTVINKLDSPLTIHWHGLYQNGTNWEDGIS
GITQCPIPAGVTYTYKFTLANQYGTFWYHAHYQSLKTDGLVGPLVVHSPRDPLKRGIDFD
EEIVLLLQDWYHTPSNVIDPQMRSTQGYMGFPSPPSANSALINGIGQWDCRFALTDDRCR
KNSPPEFHLVAGTKTRFRLIQAGSHAMFFFSADEHTLNVTEADATPVHGPPAIHRVKFHN
GQRYSVILSVAANETGTSFFLRASMDPDCWVWVTSDLQKTAFAIIRVVDATTRTFSTKRP
TSRDWADRINGDCRDLDPNTLVPIIPVRVPQTVDGAGALAVGLGFRVFSTGAQLPTSAGV
PSSNNSRPTHPVLQIKDIKSGIVSIPPPGTNTTLPSITVNAQVTSAPAGAGGAYFVNNVT
WQANQLNPVLHDFAAGGPGRTDNSKIASVVYPTLGWYDLYLVNLEQATNHPFHLHGPEMH
IVAIGTGTPTPENLRNLTYSTQNPLRRDTIFLQGGTYAVIRLRTDLPGIWAVHCHIQFHL
ADGFLGMIVIQPDKIKNFKIPPKTRDLCKTPIPSLRMYADRI

Enzyme Prediction     

No EC number prediction in MELLADRAFT_124658-t26_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	59	603	4.7e-98	0.9776536312849162

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
259950	CuRO_2_Diphenol_Ox	1.32e-80	183	348	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	1.22e-74	472	610	20	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	3.40e-71	49	167	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	6.07e-60	49	623	2	534	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	7.60e-60	43	621	18	555	L-ascorbate oxidase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QRV98945.1|AA1	8.10e-165	36	628	55	591
QRW13493.1|AA1	4.57e-164	36	628	55	591
QRV91744.1|AA1	1.09e-156	39	628	38	559
QRV76916.1|AA1	1.09e-156	39	628	38	559
QRV82887.1|AA1	2.87e-155	24	629	24	565

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3KW7_A	3.26e-65	55	630	10	493	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]
5LM8_A	9.42e-65	48	618	23	512	Crystal structure of a laccase-like multicopper oxidase McoG from from Aspergillus niger [Aspergillus niger]
5LWW_A	9.62e-65	48	618	24	513	Crystal structure of a laccase-like multicopper oxidase McoG from Aspergillus niger bound to zinc [Aspergillus niger]
5LWX_A	8.79e-64	17	618	18	540	Crystal structure of the H253D mutant of McoG from Aspergillus niger [Aspergillus niger]
2QT6_A	1.58e-62	55	630	10	489	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	4.54e-127	34	634	47	584	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	7.40e-127	36	634	49	584	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	2.66e-122	34	634	47	584	Laccase-1 OS=Cryptococcus neoformans var. neoformans serotype D (strain B-3501A) OX=283643 GN=LAC1 PE=1 SV=1
sp|A0A067XMP2|PTAK_PESFW	3.24e-76	48	629	64	567	Oxydoreductase ptaK OS=Pestalotiopsis fici (strain W106-1 / CGMCC3.15140) OX=1229662 GN=ptaK PE=2 SV=2
sp|Q02081|LAC4_THACU	1.18e-66	48	597	22	483	Laccase-4 OS=Thanatephorus cucumeris OX=107832 GN=LCC4 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000333	0.999618	CS pos: 21-22. Pr: 0.9705

TMHMM  Annotations     

There is no transmembrane helices in MELLADRAFT_124658-t26_1-p1.