CAZyme Information: EFQ36405.1

Basic Information

• Species: Colletotrichum graminicola
• Lineage: Ascomycota; Sordariomycetes; ; Glomerellaceae; Colletotrichum; Colletotrichum graminicola
• CAZyme ID: EFQ36405.1
• CAZy Family: GT71
• CAZyme Description: Multicopper oxidase [Source:UniProtKB/TrEMBL;Acc:E3QZW7]

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
625		70348.83	7.1109

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_CgraminicolaM1-001	12400	645133	380	12020

• Gene Location: location=GG697422:60252-62454(-)

Full Sequence      

MARARLMDGGRDTDDAKQLHGAKALINFTGQMPCRSRWSIPGVFFIMFVLSWWLHWPITN
SVKTLLRKGNKCDRETADQVVRRYNLTIGARWMNLVFTDGGYWRGIFVCNGESPCPTLFA
EEGDIVELNVHNDLFAQVSIHWSGMNHRRFGFYNDGTGGLNQYGILQRGNFTHRYDTTGH
WGLNWYADHTGTGIMDGAHGVAYIAPSPSRPRPYRQIATSPTELVLIQEAERNAQHLLVW
NYYRRDAGWRVLEMRSEGTNLNCYDSILVNSKGRRHCRHLEYSHLGGKRLDESGCAIEAG
NEGVQCSPTEADYEIIETHGKPWIMLNILNIGFEHAVQFAIDDHQMWIVANDGGFVDPKL
VDVLYLTNGARYTVVVKLDREGADYAMRLVSTSTHQNLHGYAILRYPALRYPQHGAPMSI
QNPQSGSPPCVNPDGSIHASCNTTAPSTLAPHPPSPPPPANKTLHFRIGHQPSRYEEHVT
EYYLNQKPYQLFHAQMSPLLFLNNLTAIEPPIVGDLPWGTTVDVIVHNSIDDTMPLYKHG
DPMFLLGSKANASWEWDTVQDAIAAGMEELDLKKPSLQLVHDVPPLGWAVLRWKIQVKGA
TMLHSNKFKYYAVSVSILVPNCNGI

Enzyme Prediction     

No EC number prediction in EFQ36405.1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	102	605	1.4e-46	0.9497206703910615

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
259944	CuRO_2_Abr2_like	2.35e-50	235	407	1	138	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.
259919	CuRO_1_Abr2_like	5.69e-21	84	204	1	116	The first 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 1 of 3-domain MCOs contains part the trinuclear copper binding site, which is located at the interface of domains 1 and 3.
259868	CuRO_2_LCC_like	6.94e-20	236	406	1	152	Cupredoxin domain 2 of laccase-like multicopper oxidases; including laccase, CueO, spore coat protein A, ascorbate oxidase and similar proteins. Laccase-like multicopper oxidases (MCOs) are able to couple oxidation of substrates with reduction of dioxygen to water. MCOs are capable of oxidizing a vast range of substrates, varying from aromatic compounds to inorganic compounds such as metals. Although the members of this family have diverse functions, majority of them have three cupredoxin domain repeats. 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.
215324	PLN02604	4.05e-19	102	604	41	529	oxidoreductase
259926	CuRO_1_Diphenol_Ox	6.30e-19	82	200	1	114	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
SMQ47095.1|AA1	1.20e-222	35	625	22	614
SMR45620.1|AA1	1.20e-222	35	625	22	614
QKD61049.1|AA1	8.03e-194	49	625	45	610
CEI62062.1|AA1	6.35e-191	80	625	62	612
QPC59569.1|AA1	3.31e-188	80	625	62	612

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1HFU_A	6.20e-18	94	584	13	445	Chain A, LACCASE 1 [Coprinopsis cinerea]
1A65_A	6.23e-18	94	584	13	445	Chain A, Laccase [Coprinopsis cinerea]
1AOZ_A	9.40e-17	110	604	28	506	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]
3SQR_A	1.34e-16	76	604	62	525	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]
3V9E_A	1.34e-16	76	604	62	525	Structure of the L499M mutant of the laccase from B.aclada [Botrytis aclada]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|W3X732|PFMAY_PESFW	7.43e-74	81	619	22	560	Laccase PFICI_06862 OS=Pestalotiopsis fici (strain W106-1 / CGMCC3.15140) OX=1229662 GN=PFICI_06862 PE=3 SV=1
sp|P17489|LAC1_EMENI	1.79e-46	99	604	37	585	Laccase-1 OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=yA PE=2 SV=3
sp|I1RF62|GIP1_GIBZE	4.98e-43	101	619	40	586	Multicopper oxidase GIP1 OS=Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1) OX=229533 GN=GIP1 PE=1 SV=1
sp|A0A4Y6F0M8|USTL_USTVR	6.24e-42	101	613	38	584	Laccase ustL OS=Ustilaginoidea virens OX=1159556 GN=ustL PE=1 SV=1
sp|E9RBR0|ABR2_ASPFU	1.65e-40	98	604	32	554	Laccase abr2 OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=abr2 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
0.999955	0.000066

TMHMM  Annotations     

Start	End
38	56