CAZyme Information: QRD91851.1

Basic Information

• Species: Aspergillus flavus
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus flavus
• CAZyme ID: QRD91851.1
• CAZy Family: GH78
• CAZyme Description: multicopper oxidase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
657		72626.08	5.1046

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AflavusNRRL3357_2020	13958	N/A	249	13709

• Gene Location: location=CP044617:1995927-1998112(-)

Full Sequence      

MSVLRAVTAFFIWLGLVQAKLVRETLEFTWGVGSPDGVPRQMILTNGKYPGPDLVFDEDD
DVEVFLNRANLHTVVIDKLDLDTCHQSHAVQYDSPLARSIVRYCRYSPSETRLIRILCRM
ESAPWSDGVPGLSQAPIQPNSSFVYKFKASPAGTFWYHSHFKNVMQDGQVGALYIRHKPD
TPRPYSMIAQDATEVAQMQHAEANSNLVLITDWTHFTAKEYFQAEIDSGLNLFCVDSILV
NGKGSVYCPGAEYMQSLIGPQIALVLEGTNLTDRGCLVPSLHNVQGSWPNQKPDAVPSSM
HNNCTPSDGGVPIIEVDAKDGWASLNFIGAQAQKGTTFSVDNHPMWIYEVDGQFVEPRQY
EMVGMYNGARYSALVKLNQTPGDYAIRITDNGGDQVISGYAILSYRAANTTENGTRPQAQ
IGPTTKGYIDYAGQNTSASVRHLNYTTNLPAFNVPLPPAFADLTLKTNMTRVNSSYQWSI
GNGVLYEPEVTADTPLMFEKQPLDVIPSNFTLQTLNNTWVDIIIQIISDPEMDPIHPPHP
IHKHGNRAYIIGDGMGVFNWSTVYEGMLERPDLFYLNKPALRDTFVTNTLTAALDGGVWI
AIRYHVSGPFPSLLHCHITTHQEGGMALALLDGIDVWSELPTAAEVVRLQNADGPVG

Enzyme Prediction     

No EC number prediction in QRD91851.1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	119	627	1.8e-57	0.8547486033519553

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
259965	CuRO_3_Abr2_like	2.62e-70	462	633	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.
259944	CuRO_2_Abr2_like	1.56e-57	208	406	3	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	8.28e-37	25	176	2	117	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.
274555	ascorbase	1.01e-35	27	644	3	535	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.
177843	PLN02191	8.47e-32	13	644	7	558	L-ascorbate oxidase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QRD91851.1|AA1	0.0	1	657	1	657
QMW47494.1|AA1	0.0	1	657	1	620
QMW35432.1|AA1	0.0	1	657	1	620
UDD64542.1|AA1	0.0	1	657	1	620
BCS17789.1|AA1	3.24e-244	16	637	17	606

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3DIV_A	3.88e-31	34	634	16	471	Crystal structure of laccase from Cerrena maxima at 1.76A resolution [Cerrena]
3PXL_A	7.04e-31	26	632	8	469	Type-2 Cu-depleted fungus laccase from Trametes hirsuta [Trametes hirsuta]
3FPX_A	7.04e-31	26	632	8	469	Native fungus laccase from Trametes hirsuta [Trametes hirsuta],3V9C_A Type-2 Cu-depleted fungus laccase from Trametes hirsuta at low dose of ionization radiation [Trametes hirsuta]
5LDU_A	1.28e-30	26	632	8	469	Recombinant high-redox potential laccase from Basidiomycete Trametes hirsuta [Trametes hirsuta]
2H5U_A	1.72e-30	34	634	16	471	Crystal structure of laccase from Cerrena maxima at 1.9A resolution [Trametes maxima]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|P17489|LAC1_EMENI	1.64e-257	14	637	15	607	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	8.66e-159	16	641	19	597	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|E9RBR0|ABR2_ASPFU	2.06e-156	16	640	14	579	Laccase abr2 OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=abr2 PE=1 SV=1
sp|A0A1S7IUL2|MCE_TALPI	3.86e-155	13	643	14	591	Multicopper oxidase MCE OS=Talaromyces pinophilus OX=128442 GN=MCE PE=1 SV=1
sp|A0A4Y6F0M8|USTL_USTVR	2.93e-153	19	641	20	602	Laccase ustL OS=Ustilaginoidea virens OX=1159556 GN=ustL PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000208	0.999807	CS pos: 19-20. Pr: 0.9797

TMHMM  Annotations     

There is no transmembrane helices in QRD91851.1.