CAZyme Information: SAPIO_CDS6544-t41_1-p1

Basic Information

• Species: Scedosporium apiospermum
• Lineage: Ascomycota; Sordariomycetes; ; Microascaceae; Scedosporium; Scedosporium apiospermum
• CAZyme ID: SAPIO_CDS6544-t41_1-p1
• CAZy Family: GH45
• CAZyme Description: Laccase-2

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
568		61805.24	4.2274

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_SapiospermumIHEM14462	10920	N/A	2544	8376

• Gene Location: location=JOWA01000104:188979-190883(-)

Full Sequence      

MIASLFSASLLGLAAAIPSPPEPLLFSRAACSGNTANTRSEWCDFSVDTDYTSIAPDTGV
TREYWFDITETTASPDGVERYVQAINGSIPGPTIIADWGDTVIVHVTNSIAESTNGTSLH
FHGIRQNFTNQNDGVPSITQCPTAPGSSMTYTWKALQYGSGWYHSHFALQAYQGVFGGIV
INGPATSNYDEDLGHLFLNDWSHQTVDQLFHAAQTTGPPTLNNGLINGTNVFGEDGEAGQ
VGSRFAVSLTEGNSYRLRIVNAAVDSHFKFMVDNHTLTVIATDFVPIEPFTTDILSIGMG
QRYDVIITANQANVADSFWMRAIPQSACSENESQDNIRGIVRYGSSTATPSTSRPDSYSE
GCEDMDVSNLVPHVAKTASSISSKGVEQATVGFNEKNLFRWYLNSTTMLVEWGDPTLLAI
QRGQTTWDTSDAVIELPNADEWVYIVIETALAIPHPIHLHGHDFLVLAQGSGTFSDSVTL
NTNNPARRDTAMLPASGYLALAFETDNPGAWLMHCHIGWHTSEGFSLQFIERYDEIAGLI
DSDILNSTCSAWATYEEQFSVEQEDSGL

Enzyme Prediction     

EC	1.10.3.2:4	1.10.3.-:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	49	362	4.7e-132	0.9935897435897436

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
259968	CuRO_3_MaLCC_like	1.26e-77	390	530	15	157	The third 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 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.
274555	ascorbase	1.59e-71	61	542	1	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	6.03e-67	58	541	20	556	L-ascorbate oxidase
259947	CuRO_2_MaLCC_like	8.27e-66	193	359	1	165	The second 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. Laccase is 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.
259923	CuRO_1_MaLCC_like	6.17e-64	59	182	1	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
QOU09627.1|AA1_3	1.26e-298	1	568	1	571
AFG30950.1|AA1_3	1.20e-296	19	568	29	571
AFG30951.1|AA1_3	1.20e-296	19	568	29	571
UQC89044.1|AA1_3	2.96e-293	1	568	1	574
UKZ68800.1|AA1_3	6.95e-290	1	568	7	566

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5LWX_A	2.86e-185	33	555	22	556	Crystal structure of the H253D mutant of McoG from Aspergillus niger [Aspergillus niger]
5LM8_A	3.62e-184	42	555	4	528	Crystal structure of a laccase-like multicopper oxidase McoG from from Aspergillus niger [Aspergillus niger]
5LWW_A	3.74e-184	42	555	5	529	Crystal structure of a laccase-like multicopper oxidase McoG from Aspergillus niger bound to zinc [Aspergillus niger]
3V9E_A	1.41e-178	2	568	10	580	Structure of the L499M mutant of the laccase from B.aclada [Botrytis aclada]
3SQR_A	1.41e-178	2	568	10	580	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|Q96WM9|LAC2_BOTFU	4.79e-184	16	568	24	581	Laccase-2 OS=Botryotinia fuckeliana OX=40559 GN=lcc2 PE=2 SV=1
sp|Q12570|LAC1_BOTFU	3.75e-165	3	568	13	561	Laccase-1 OS=Botryotinia fuckeliana OX=40559 GN=lcc1 PE=2 SV=3
sp|J5JH35|OPS5_BEAB2	9.67e-165	37	568	49	590	Oxidoreductase OpS5 OS=Beauveria bassiana (strain ARSEF 2860) OX=655819 GN=OpS5 PE=1 SV=1
sp|Q96UM2|LAC3_BOTFU	2.23e-136	90	529	1	452	Laccase-3 (Fragment) OS=Botryotinia fuckeliana OX=40559 GN=lcc3 PE=3 SV=1
sp|Q70KY3|LAC1_MELAO	5.61e-132	34	568	55	609	Laccase-1 OS=Melanocarpus albomyces OX=204285 GN=LAC1 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000631	0.999348	CS pos: 28-29. Pr: 0.6483

TMHMM  Annotations     

There is no transmembrane helices in SAPIO_CDS6544-t41_1-p1.