CAZyme Information: EJT72445.1

Basic Information

• Species: Gaeumannomyces tritici
• Lineage: Ascomycota; Sordariomycetes; ; Magnaporthaceae; Gaeumannomyces; Gaeumannomyces tritici
• CAZyme ID: EJT72445.1
• CAZy Family: CE5
• CAZyme Description: diphenol oxidase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
696		75985.49	6.6021

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_GtriticiR3-111a-1	14749	644352	291	14458

• Gene Location: location=GL385399:948007-950185(+)

Full Sequence      

MDPESQNREEREELLAGHGGEHEPTRTRRAAPPAPVKRLSAPVMMAVCAVSILALVGFAM
PFWATTQSNPPTSSSGGSSAVGISTRPAGTGTAVAVTTTAAPSTTTAAKVSSPTDMIPKD
EFFNLDVSKSGFVVENKPRAREYEFNITRALGAPDGVVKPMILVNGQSPGPTVEANVGDA
IRVIMYNSLENETATIHWHGIDQRNTVWMDGVPGVTQCGIPPGKSFVYEFTVPNQRGTFW
YHAHVSVQYTDGLYGAIVIHDPDEKVAEHHDDRLVFMGDLHHQYSGDLLTQYLSKSPSYA
PGSAGTEPYPDNIIINGQHLSNCTKPSSDEATAFTGEGCSGGSRHVARVEAGKTVRLRLI
SHSSNTPFLFTVDGHVLEMVEMDGVEIQPVQTTVVFLNPGQRYSVLVKADRAPGNYLMRA
VATCAMLDNSPGSNLGTVGSQGTAVFSYGEGVDPKGPLVVLNDSTKASVAQEPWAKRCRD
LPFDLTKPVREIDAYNVGDGNKHSFLFKFVEDEQGVQRTVINDTIYSDLPSGATLWQVPQ
QDMKQQNMNSSEPKWAWKPEQHVFVSRDEAMGAQVAISAGNMMGHPWHLHGQQFQVVGWG
KGIYGKRETTWNFKNPVRRDTVTVPGHSHVVIRYVADNPGVWALHCHIQWHAEGGMFVQT
AQRLTKLQDMLRDLPGFGDIKYRYCGPTPPRSIDGR

Enzyme Prediction     

No EC number prediction in EJT72445.1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	157	656	1.7e-110	0.9776536312849162

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
274555	ascorbase	9.14e-82	140	669	1	533	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.
215324	PLN02604	1.09e-71	139	667	23	554	oxidoreductase
177843	PLN02191	3.62e-68	141	669	24	556	L-ascorbate oxidase
274556	laccase	8.14e-66	139	656	2	513	laccase, plant. Members of this protein family include the copper-containing enzyme laccase (EC 1.10.3.2), often several from a single plant species, and additional, uncharacterized, closely related plant proteins termed laccase-like multicopper oxidases. This protein family shows considerable sequence similarity to the L-ascorbate oxidase (EC 1.10.3.3) family. Laccases are enzymes of rather broad specificity, and classification of all proteins scoring about the trusted cutoff of this model as laccases may be appropriate.
259926	CuRO_1_Diphenol_Ox	5.79e-64	141	260	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QBZ59810.1|AA1	5.01e-243	111	685	98	688
AUS45860.1|AA1	3.91e-163	113	671	92	665
CAP71374.1|AA1	9.22e-153	111	685	111	691
CDP30774.1|AA1	9.22e-153	111	685	111	691
VBB83984.1|AA1	7.13e-149	111	685	111	691

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5LM8_A	3.54e-73	141	666	24	508	Crystal structure of a laccase-like multicopper oxidase McoG from from Aspergillus niger [Aspergillus niger]
5LWW_A	3.63e-73	141	666	25	509	Crystal structure of a laccase-like multicopper oxidase McoG from Aspergillus niger bound to zinc [Aspergillus niger]
5LWX_A	6.80e-73	141	666	52	536	Crystal structure of the H253D mutant of McoG from Aspergillus niger [Aspergillus niger]
5Z1X_A	1.46e-67	153	666	16	469	Crystal Structure of Laccase from Cerrena sp. RSD1 [Cerrena],5Z1X_B Crystal Structure of Laccase from Cerrena sp. RSD1 [Cerrena],5Z22_A Crystal Structure of Laccase from Cerrena sp. RSD1 [Cerrena]
6RHH_A	5.87e-67	144	662	8	469	Single crystal serial study of the X-ray induced enzymatic reduction of molecular oxygen to water for laccase from Steccherinum murashkinskyi at sub-atomic resolution. Third structure of the series with 315 KGy dose. [Steccherinum murashkinskyi],6RHI_A Single crystal serial study of the X-ray induced enzymatic reduction of molecular oxygen to water for laccase from Steccherinum murashkinskyi at sub-atomic resolution. Ninth structure of the series with 1215 KGy dose. [Steccherinum murashkinskyi],6RHO_A Single crystal serial study of the X-ray induced enzymatic reduction of molecular oxygen to water for laccase from Steccherinum murashkinskyi at sub-atomic resolution. Twentieth structure of the series with 4065 KGy dose. [Steccherinum murashkinskyi],6RHP_A Single crystal serial study of the X-ray induced enzymatic reduction of molecular oxygen to water for laccase from Steccherinum murashkinskyi at sub-atomic resolution. Twenty first structure of the series with 4415 KGy dose (collected after refreezing). [Steccherinum murashkinskyi],6RHR_A Single crystal serial study of the inhibition of laccases from Steccherinum murashkinskyi by chloride anions at sub-atomic resolution. First structure of the series with 15 KGy dose. [Steccherinum murashkinskyi],6RHU_A Single crystal serial study of the inhibition of laccases from Steccherinum murashkinskyi by chloride anions at sub-atomic resolution. Second structure of the series with 165 KGy dose. [Steccherinum murashkinskyi],6RHX_A Single crystal serial study of the inhibition of laccases from Steccherinum murashkinskyi by chloride anions at sub-atomic resolution. Third structure of the series with 315 KGy dose. [Steccherinum murashkinskyi],6RI0_A Single crystal serial study of the inhibition of laccases from Steccherinum murashkinskyi by chloride anions at sub-atomic resolution. Ninth structure of the series with 1215 KGy dose. [Steccherinum murashkinskyi],6RI2_A Single crystal serial study of the inhibition of laccases from Steccherinum murashkinskyi by chloride anions at sub-atomic resolution. Twentieth structure of the series with 4065 KGy dose. [Steccherinum murashkinskyi],6RI4_A Single crystal serial study of the inhibition of laccases from Steccherinum murashkinskyi by fluoride anions at sub-atomic resolution. First structure of the series with 13 KGy dose. [Steccherinum murashkinskyi],6RI6_A Single crystal serial study of the inhibition of laccases from Steccherinum murashkinskyi by fluoride anions at sub-atomic resolution. Second structure of the series with 400 KGy dose. [Steccherinum murashkinskyi],6RI8_A Single crystal serial study of the inhibition of laccases from Steccherinum murashkinskyi by fluoride anions at sub-atomic resolution. Third structure of the series with 800 KGy dose. [Steccherinum murashkinskyi],6RII_A Single crystal serial study of the inhibition of laccases from Steccherinum murashkinskyi by fluoride anions at sub-atomic resolution. Fourth structure of the series with 1200 KGy dose. [Steccherinum murashkinskyi],6RIK_A Single crystal serial study of the inhibition of laccases from Steccherinum murashkinskyi by fluoride anions at sub-atomic resolution. Thirteenth structure of the series with 5200 KGy dose. [Steccherinum murashkinskyi],6RIL_A Single crystal serial study of the inhibition of laccases from Steccherinum murashkinskyi by fluoride anions at sub-atomic resolution. Fourteenth structure of the series with 5600 KGy dose (data was collected after refreezing). [Steccherinum murashkinskyi]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|J9VY90|LAC1_CRYNH	1.64e-81	132	662	53	561	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	2.50e-77	132	662	53	561	Laccase-1 OS=Cryptococcus neoformans var. neoformans serotype D (strain B-3501A) OX=283643 GN=LAC1 PE=1 SV=1
sp|J9VQZ4|LAC2_CRYNH	9.43e-76	127	662	48	561	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|J5JH35|OPS5_BEAB2	1.27e-69	141	663	74	552	Oxidoreductase OpS5 OS=Beauveria bassiana (strain ARSEF 2860) OX=655819 GN=OpS5 PE=1 SV=1
sp|Q99056|LAC5_TRAVI	1.57e-69	144	658	30	493	Laccase-5 OS=Trametes villosa OX=47662 GN=LCC5 PE=3 SV=2

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
0.999883	0.000145

TMHMM  Annotations     

Start	End
43	65