CAZyme Information: TRIREDRAFT_124079-t26_1-p1

Basic Information

• Species: Trichoderma reesei
• Lineage: Ascomycota; Sordariomycetes; ; Hypocreaceae; Trichoderma; Trichoderma reesei
• CAZyme ID: TRIREDRAFT_124079-t26_1-p1
• CAZy Family: GH105
• CAZyme Description: multicopper oxidase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
623	GL985088|CGC2	69959.63	4.7375

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_TreeseiQM6a	9138	431241	7	9131

• Gene Location: location=GL985088:18673-20865(+)

Full Sequence      

MSRFAWVLLVASLLHTDAWAKTVRETLRITWEEGAPNGQARELIRTNGQFPSPTLVWDEG
DDVEVTVINDMAKNVTVHWHGLDQKDTPWADGTPGLTQRPIQPGTDFVYKFKASPPGNHW
YHSHDKMSLVDGLYGAVHIRPKQDRSGLWSQISDNQKDIEAMEKAARDPEYLVVSDWSQY
TSEEYWKISTDSGLLVFCLDSILVNGVGELYCPGQKFLQKELAPGLAQNGFPPGTEVSDK
GCFPADIDQIQGGPWNITKRPDLIPPRVQEGCVASRNENATIFVDPSKNNGWVSMHIVAA
ATIAQIAFSVDQHPFWIYEVDGNYVQPKRFVSTVMSAGETFSIMMKLDQEPGKYTMRIPN
SGASQVLGGYAEMVYAGHAQSPRSEKAYLSYGGNPITPDVELHSYFPWQLETDHMPPWPP
NKPRPGNADQEVLLALGRVGAPYNYTMNTKYLLPVDFQNDDPLLFYPNATLGTEDENLVI
RTKNGTWVDLILQVSTLPGDKSAFEHFIHKHGSKTWRIGFGTGVWNYTSVEEAIQERPED
FNLETPGLRDTWITAFSFNEEASWSVFRYFVDNPGPWLFHCHIELHLMGGMGIVILDGVD
AWPEDIPVEYQLDKPHVTPNACS

Enzyme Prediction     

No EC number prediction in TRIREDRAFT_124079-t26_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	39	591	2.9e-73	0.9776536312849162

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
259965	CuRO_3_Abr2_like	5.83e-81	429	598	1	164	The third cupredoxin domain of a group of fungal Laccases similar to Abr2 from Aspergillus fumigatus. Abr2 is involved in conidial pigment biosynthesis in Aspergillus fumigatus. 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. Laccase 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. Like other related multicopper oxidases (MCOs), 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 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.
177843	PLN02191	3.13e-64	6	600	7	549	L-ascorbate oxidase
274555	ascorbase	2.05e-57	29	600	8	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.
215324	PLN02604	1.02e-51	1	600	2	549	oxidoreductase
259944	CuRO_2_Abr2_like	4.07e-50	170	375	1	137	The second cupredoxin domain of a group of fungal Laccases similar to Abr2 from Aspergillus fumigatus. Abr2 is involved in conidial pigment biosynthesis in Aspergillus fumigatus. 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. Laccase 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. Like other related multicopper oxidases (MCOs), 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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
UKZ69556.1|AA1	0.0	1	613	2	614
UKZ95950.1|AA1	0.0	1	613	2	614
QLI74771.1|AA1	0.0	1	612	1	612
UKZ57040.1|AA1	0.0	1	614	1	615
UKZ82773.1|AA1	0.0	1	614	1	615

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1AOZ_A	7.59e-53	35	600	16	526	Refined Crystal Structure Of Ascorbate Oxidase At 1.9 Angstroms Resolution [Cucurbita pepo var. melopepo],1AOZ_B Refined Crystal Structure Of Ascorbate Oxidase At 1.9 Angstroms Resolution [Cucurbita pepo var. melopepo],1ASO_A X-Ray Structures And Mechanistic Implications Of Three Functional Derivatives Of Ascorbate Oxidase From Zucchini: Reduced-, Peroxide-, And Azide-Forms [Cucurbita pepo var. melopepo],1ASO_B X-Ray Structures And Mechanistic Implications Of Three Functional Derivatives Of Ascorbate Oxidase From Zucchini: Reduced-, Peroxide-, And Azide-Forms [Cucurbita pepo var. melopepo],1ASP_A X-ray Structures And Mechanistic Implications Of Three Functional Derivatives Of Ascorbate Oxidase From Zucchini: Reduced-, Peroxide-, And Azide-forms [Cucurbita pepo var. melopepo],1ASP_B X-ray Structures And Mechanistic Implications Of Three Functional Derivatives Of Ascorbate Oxidase From Zucchini: Reduced-, Peroxide-, And Azide-forms [Cucurbita pepo var. melopepo],1ASQ_A X-Ray Structures And Mechanistic Implications Of Three Functional Derivatives Of Ascorbate Oxidase From Zucchini: Reduced-, Peroxide-, And Azide-Forms [Cucurbita pepo var. melopepo],1ASQ_B X-Ray Structures And Mechanistic Implications Of Three Functional Derivatives Of Ascorbate Oxidase From Zucchini: Reduced-, Peroxide-, And Azide-Forms [Cucurbita pepo var. melopepo]
5Z1X_A	6.03e-39	27	600	8	468	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]
2HRG_A	1.60e-36	29	599	8	468	Crystal Structure of Blue Laccase from Trametes trogii complexed with p-methylbenzoate [Coriolopsis trogii],2HRH_A Crystal Structure of Blue Laccase from Trametes trogii [Coriolopsis trogii]
1HFU_A	1.76e-36	25	610	7	483	Chain A, LACCASE 1 [Coprinopsis cinerea]
1A65_A	1.78e-36	25	610	7	483	Chain A, Laccase [Coprinopsis cinerea]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|E9F648|MLAC1_METRA	0.0	1	612	1	612	Laccase 1 OS=Metarhizium robertsii (strain ARSEF 23 / ATCC MYA-3075) OX=655844 GN=Mlac1 PE=2 SV=2
sp|C3SAH7|MLAC1_METAN	0.0	1	612	1	602	Laccase 1 OS=Metarhizium anisopliae OX=5530 GN=Mlac1 PE=2 SV=1
sp|E9E686|MLAC1_METAQ	0.0	1	613	1	613	Laccase 1 OS=Metarhizium acridum (strain CQMa 102) OX=655827 GN=Mlac1 PE=3 SV=2
sp|A0A0B4F1I0|MLAC1_METAF	0.0	1	611	1	611	Laccase 1 OS=Metarhizium anisopliae (strain ARSEF 549) OX=1276135 GN=Mlac1 PE=2 SV=1
sp|A0A0B2WJN5|MLAC1_METAS	0.0	1	614	1	600	Laccase 1 OS=Metarhizium album (strain ARSEF 1941) OX=1081103 GN=Mlac1 PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000248	0.999724	CS pos: 20-21. Pr: 0.9782

TMHMM  Annotations     

There is no transmembrane helices in TRIREDRAFT_124079-t26_1-p1.