CAZyme Information: CCE33344.1

Basic Information

• Species: Claviceps purpurea
• Lineage: Ascomycota; Sordariomycetes; ; Clavicipitaceae; Claviceps; Claviceps purpurea
• CAZyme ID: CCE33344.1
• CAZy Family: GT2
• CAZyme Description: Related to laccase [Source:UniProtKB/TrEMBL;Acc:M1WHU6]

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
713	CAGA01000056|CGC2	80062.62	5.9550

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_Cpurpurea20.1	8979	1111077	156	8823

• Gene Location: location=CAGA01000056:65693-67834(-)

Full Sequence      

MSQEEALEEADAEAGQHGEDEPFLSLHDETDRGTPIARAPKKSSPSRPSRPYGSCKFVLF
SLFLVVTILGLAGALLRLTSKDSQGLGVLRPEPQPSDKDDASNLDNDGPSSSLRPDEHMP
LTPRLRDGSEYVLSPSWDATAAPVTRKYHWTIMDARLNPDGVYRPMMLINNQFPGPLVEC
NEGDTLVVQVVNKAVNATSIHFHGLFQNGTNFMDGTVGVTQCPIAPNSSFTYNFTVRGQS
GTYWYHAHHTAQAADGLLGPVIVHSRSERTTQQELGYATDRIIMVQDYYHNTTAELLMDY
LRPDNENNEPVPDNPLINGRGVRSCHDFTGWDCNDSHVSKPVFDLTAGQRHRIRFINVGI
FAEFQIQVDQHPFYITEVDGTDVHPEPFHRLNILPAQRYSIILETNITAHNAYWLRTRMV
SRCFTTKNPRLEAELHGIVRYISPTTKPLTDEVHSTDWPDTVEVICRDLNTSALVPVQAL
TPPPADDFVRLRANFQIGNWALSRGFFNESTWRANVTHPSLYRFLDSDSTTALAHASSSG
GESSAAATINDKVFNKEREFVLQTRGIRTVDMAINNFDDGAHPFHLHGHEFFVMAQAQSG
YPPSSAGAFAEYLKQQQQQQQHRDMPLNPLRRDTVTVEGYSWVVIRVVLDNPGLWSLHCH
NMWHAMAGMAMQVLVRAEEVHTWRVEPWQRDMCRLEGVGLGSRPDDSIWFGSL

Enzyme Prediction     

No EC number prediction in CCE33344.1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	162	670	1.9e-107	0.9804469273743017

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
259926	CuRO_1_Diphenol_Ox	5.68e-68	146	264	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	1.29e-62	145	681	1	526	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.
259953	CuRO_2_MCO_like_1	9.91e-59	281	441	1	162	The second cupredoxin domain of uncharacterized multicopper oxidase. Multicopper Oxidases (MCOs) are multi-domain enzymes that are able to couple oxidation of substrates with reduction of dioxygen to water. MCOs oxidise their substrate by accepting electrons at a mononuclear copper centre and transferring them to a trinuclear copper centre which binds a dioxygen. The dioxygen, following the transfer of four electrons, is reduced to two molecules of water. These MCOs are capable of oxidizing a vast range of substrates, varying from aromatic to inorganic compounds such as metals. This family of MCOs 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.
259977	CuRO_3_MCO_like_4	4.51e-58	491	675	3	166	The third cupredoxin domain of uncharacterized multicopper oxidase. Multicopper Oxidases (MCOs) are multi-domain enzymes that are able to couple oxidation of substrates with reduction of dioxygen to water. MCOs oxidize their substrate by accepting electrons at a mononuclear copper centre and transferring them to a trinuclear copper centre which binds a dioxygen. The dioxygen, following the transfer of four electrons, is reduced to two molecules of water. These MCOs are capable of oxidizing a vast range of substrates, varying from aromatic to inorganic compounds such as metals. This subfamily of MCOs is composed of three cupredoxin domains. 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.
215324	PLN02604	5.64e-58	145	669	24	540	oxidoreductase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QLI73216.1|AA1	0.0	11	713	6	687
UNI14665.1|AA1	0.0	1	713	45	758
QUC17819.1|AA1	0.0	56	713	71	713
UKZ88109.1|AA1	6.29e-306	27	713	60	743
ATY60613.1|AA1	3.57e-302	47	713	24	683

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3V9E_A	5.32e-71	130	672	51	539	Structure of the L499M mutant of the laccase from B.aclada [Botrytis aclada]
3SQR_A	1.43e-70	130	672	51	539	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	4.84e-64	144	693	22	522	Crystal structure of a laccase-like multicopper oxidase McoG from from Aspergillus niger [Aspergillus niger]
5LWW_A	4.95e-64	144	693	23	523	Crystal structure of a laccase-like multicopper oxidase McoG from Aspergillus niger bound to zinc [Aspergillus niger]
5LWX_A	1.68e-63	144	693	50	550	Crystal structure of the H253D mutant of McoG from Aspergillus niger [Aspergillus niger]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|J9VY90|LAC1_CRYNH	1.23e-90	108	688	24	574	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|Q55P57|LAC1_CRYNB	3.38e-90	116	688	32	574	Laccase-1 OS=Cryptococcus neoformans var. neoformans serotype D (strain B-3501A) OX=283643 GN=LAC1 PE=1 SV=1
sp|J9VQZ4|LAC2_CRYNH	1.02e-85	103	693	19	578	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	2.20e-70	138	694	57	567	Oxydoreductase ptaK OS=Pestalotiopsis fici (strain W106-1 / CGMCC3.15140) OX=1229662 GN=ptaK PE=2 SV=2
sp|E9R598|FETC_ASPFU	1.33e-69	140	670	17	487	Iron transport multicopper oxidase fetC OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=fetC PE=2 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
0.999882	0.000129

TMHMM  Annotations     

Start	End
57	79