CAZyme Information: MELLADRAFT_124643-t26_1-p1

Basic Information

• Species: Melampsora larici-populina
• Lineage: Basidiomycota; Pucciniomycetes; ; Melampsoraceae; Melampsora; Melampsora larici-populina
• CAZyme ID: MELLADRAFT_124643-t26_1-p1
• CAZy Family: CE5
• CAZyme Description: multi-copper oxidase laccase-like protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
604		67345.58	7.0764

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=GL883132:593264-596685(+)

Full Sequence      

MGLNLRSVLCVLALVAYQARAVTFNSSELYLSDHEFEITSITRTRKYDFVITRTNLTLSC
RNTTGAPDGYTRPLLVINNQLPAPLIRCNEGDTLEIRVDNRLDTDVSIHWHGIWQTGTPW
MDGVTGVTQCPIPPGASFTYKFTVAKQFGTFWYHAHTRNLAIDGIAGPLIIHSPRDPLVK
GRDFDNEYILFMSDWYHNHLKRDSISEWLFWDSSSTIGEFKIFIDRGSKCITPTKPLEIT
VAPNQKTRFRLIQAGSHAMFWFSADQHFLNVTEADSTGVSGPPGLHRLQFHNGERYSVII
DTKLDPDGSSFYLRAAMDTDCFAPGMTGPDATALAIVRVVAPNNGTLDTLPPTTRDWKDT
VGGNCTDLDIDLLSPLMTKVCAQNVLGHLFFNTSLGTVLQANPNNSSKLESLSRFFVDNT
TWTNLLKGGKGFVNQSEAATLTLEKPGAYDIVINNLDSAIDHPLHLHGVDSYLVSHGPGN
VGPQDLKNLKYRLTNPLRKDTYVVGGGSHLIVHVRNVGPFILHCHIGWHLAAGFAGIVVM
QPSKLAQITLPVENQRLCIGKNFSNQNEIEPGRRKRWTDPIFDDTQPMFPRPLKGYYLPN
EMLN

Enzyme Prediction     

No EC number prediction in MELLADRAFT_124643-t26_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	70	534	1.4e-82	0.9776536312849162

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
259926	CuRO_1_Diphenol_Ox	2.22e-64	45	172	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.
259971	CuRO_3_Diphenol_Ox	3.58e-64	390	540	3	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	3.23e-55	189	340	2	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.
225043	SufI	3.00e-52	45	542	29	450	Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and spore coat protein CotA) [Cell cycle control, cell division, chromosome partitioning, Inorganic ion transport and metabolism, Cell wall/membrane/envelope biogenesis].
177843	PLN02191	5.98e-51	67	541	37	546	L-ascorbate oxidase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QRW13493.1|AA1	7.68e-143	27	558	51	591
QRV98945.1|AA1	7.68e-143	27	558	51	591
QRV91744.1|AA1	3.25e-139	35	558	38	559
QRV76916.1|AA1	3.25e-139	35	558	38	559
QRW05810.1|AA1	2.88e-137	35	558	38	559

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5LM8_A	8.49e-61	62	544	32	508	Crystal structure of a laccase-like multicopper oxidase McoG from from Aspergillus niger [Aspergillus niger]
5LWW_A	8.66e-61	62	544	33	509	Crystal structure of a laccase-like multicopper oxidase McoG from Aspergillus niger bound to zinc [Aspergillus niger]
5LWX_A	2.82e-59	62	544	60	536	Crystal structure of the H253D mutant of McoG from Aspergillus niger [Aspergillus niger]
3V9E_A	1.49e-57	58	546	72	548	Structure of the L499M mutant of the laccase from B.aclada [Botrytis aclada]
3SQR_A	1.49e-57	58	546	72	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|J9VY90|LAC1_CRYNH	8.40e-116	17	574	34	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|J9VQZ4|LAC2_CRYNH	1.99e-115	20	574	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|Q55P57|LAC1_CRYNB	1.30e-114	17	574	34	591	Laccase-1 OS=Cryptococcus neoformans var. neoformans serotype D (strain B-3501A) OX=283643 GN=LAC1 PE=1 SV=1
sp|S8FGV1|LAC2_FOMPI	7.85e-59	57	552	31	513	Laccase-2 OS=Fomitopsis pinicola (strain FP-58527) OX=743788 GN=LCC2 PE=1 SV=1
sp|Q96WM9|LAC2_BOTFU	1.02e-54	58	546	73	549	Laccase-2 OS=Botryotinia fuckeliana OX=40559 GN=lcc2 PE=2 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000194	0.999768	CS pos: 21-22. Pr: 0.9756

TMHMM  Annotations     

There is no transmembrane helices in MELLADRAFT_124643-t26_1-p1.