CAZyme Information: mRNA_M_BR32_EuGene_00099571-p1

Basic Information

• Species: Pyricularia oryzae
• Lineage: Ascomycota; Sordariomycetes; ; Pyriculariaceae; Pyricularia; Pyricularia oryzae
• CAZyme ID: mRNA_M_BR32_EuGene_00099571-p1
• CAZy Family: GH3
• CAZyme Description: unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
687		75595.88	5.5398

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_PoryzaeBR32	14781	N/A	432	14349

• Gene Location: location=BR32_scaffold00013:261555-263765(-)

Full Sequence      

RDEREELLAADDPDHDVPSKEDEEGLLPRRPAPPGRRLGSSIAMLLLVAFSLVLLGGAAL
SGMVVMQTEPAAPPSPPAADDPAKAKTPEESGKSGILPAADAFDLRKTNFFVTDQDAQMR
EYEFNITRVEVEGPDGVKKSMVLVNGQSPGPLIEANSGDLVKVVVHNSMPGDERTTIHWH
GIDQRDSVQMDGVWGVTQCGIPPGESYTYVFGVPQQRGTFWYHAHVSVQYTDGLYGPMII
HDPTEKVPQVEEDRIIMIGDMHHMDGRQAVKEYLSPSSSWSPGMSGMEPYPDNIIINGRN
VFNCSQPEEGEEIVGKRHEGEEMKCSSGTRFNSRIKSNTAARLRIISHSSNTPMWFTVDN
HTLEIVEMDGVEVEPVATTKIFINPGQRYSAILRANQTAGNYLMRAIATCAMLDPNPHSN
FASVNSQGTAILSYDDVDAAAAPIGKPWDLGAFVASKDVGTEPWHNRCSDLPFDLTKPMR
PIDAYEVGDKNRHYFMFRFVDDGKGVQRTSINDTIFTRLDNEATIWQVPDFDETSAAASS
ANSTIPLGGVFQPSQHVLYSADETKGAEIAISAGNMMSHPWHLHGQQFQIVGWGRGEFGR
SKTTWNLANPTRRDTVTVPGHSHVVIRYKADNPGVWALHCHIQWHAEGGMFMQTAQRVSA
LKKLIDGMGAQGTDDVRHKFCKQPGKS

Enzyme Prediction     

No EC number prediction in mRNA_M_BR32_EuGene_00099571-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	137	650	3e-110	0.9776536312849162

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
274556	laccase	5.61e-70	117	652	1	515	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.
274555	ascorbase	2.15e-68	120	671	2	541	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	7.86e-64	116	669	21	562	oxidoreductase
177843	PLN02191	5.67e-61	117	666	21	556	L-ascorbate oxidase
259926	CuRO_1_Diphenol_Ox	1.61e-57	120	241	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	0.0	1	687	8	694
AUS45860.1|AA1	3.24e-159	104	684	101	684
CAP71374.1|AA1	1.22e-150	107	681	126	691
CDP30774.1|AA1	1.22e-150	107	681	126	691
VBB83984.1|AA1	2.13e-148	107	681	126	691

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3V9E_A	2.24e-73	108	661	56	547	Structure of the L499M mutant of the laccase from B.aclada [Botrytis aclada]
3SQR_A	6.05e-73	108	661	56	547	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	1.11e-72	108	682	11	530	Crystal structure of a laccase-like multicopper oxidase McoG from from Aspergillus niger [Aspergillus niger]
5LWW_A	1.14e-72	108	682	12	531	Crystal structure of a laccase-like multicopper oxidase McoG from Aspergillus niger bound to zinc [Aspergillus niger]
5LWX_A	2.12e-72	108	682	39	558	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	2.74e-79	89	649	21	553	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	1.08e-76	109	661	52	565	Laccase-1 OS=Cryptococcus neoformans var. neoformans serotype D (strain B-3501A) OX=283643 GN=LAC1 PE=1 SV=1
sp|J5JH35|OPS5_BEAB2	1.92e-75	108	682	61	571	Oxidoreductase OpS5 OS=Beauveria bassiana (strain ARSEF 2860) OX=655819 GN=OpS5 PE=1 SV=1
sp|J9VQZ4|LAC2_CRYNH	2.11e-75	109	664	52	568	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|Q96WM9|LAC2_BOTFU	2.29e-72	108	661	56	548	Laccase-2 OS=Botryotinia fuckeliana OX=40559 GN=lcc2 PE=2 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
0.999908	0.000096

TMHMM  Annotations     

Start	End
38	60