CAZyme Information: ASPSYDRAFT_152224-t33_1-p1

Basic Information

• Species: Aspergillus sydowii
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus sydowii
• CAZyme ID: ASPSYDRAFT_152224-t33_1-p1
• CAZy Family: AA9
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
575		64236.87	4.4908

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AsydowiiCBS593.65	13717	1036612	138	13579

• Gene Location: location=KV878586:2141886-2143928(-)

Full Sequence      

MAALARAADVYFKLDLTWGPGSPNGLGRDMIFVNGQFPGPPMILDEGDDVTVHVRNHMPF
NTSVHFHGIEQLHTPWADGVPGLTQWAIQPGESYTYRWHANDYGTYWYHAHDRATLQDGL
YGAIQIRPSADRENPFSLISDDTEDIEAMQHAERHTIPVVMSDWDHLTSVEYMEAMEATG
YDIFCTDSILVGGMGSIYCKDPEELTALQPAGVQQVVNATLTDRGCVPFVTKLQGDWEHH
PENLPPGLNDGCVPSEGYEAEYPVDASQKWASFSFISAASLKALVASIDEHPMYVYEVDG
RYIEPRLAESIEIYNGERYSAMVKLDKEPARYTMRIANTGANQVISGYATVSYLGGEDNE
RQSTPYIDYGGQNVTESVVKLNTSDLPPFPAVYPADTADDFHLLTLGRINSSWEWTLDGT
KFFPSDMDTMQPALCNPDSPDLESALKITTRNGTWIDLVYQLRIDPPTVVQPPHPMHKHS
NKAFLIGRGKGQFQWRSVDEARKQAPGNFFVDKPLYRDTFVTAPSGEAWMAVRYEVVNPG
PFFLHCHMETHLHGGMGMLLLDGIDAWPEVPEGYC

Enzyme Prediction     

No EC number prediction in ASPSYDRAFT_152224-t33_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	27	556	4.5e-80	0.9748603351955307

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
259965	CuRO_3_Abr2_like	1.07e-70	399	563	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.
274555	ascorbase	1.47e-61	12	571	4	532	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.
259919	CuRO_1_Abr2_like	5.65e-61	14	127	1	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.
259944	CuRO_2_Abr2_like	2.27e-60	158	353	2	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.
215324	PLN02604	1.01e-59	4	571	19	555	oxidoreductase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BCS26730.1|AA1	0.0	1	575	10	584
QBK15064.1|AA1	1.36e-303	2	574	15	585
QGA16583.1|AA1	1.90e-262	39	570	3	536
QKX61286.1|AA1	1.99e-223	21	500	499	980
QRD90476.1|AA1	1.39e-213	10	574	24	591

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1AOZ_A	1.03e-44	11	571	5	532	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]
5LM8_A	5.31e-39	24	562	38	504	Crystal structure of a laccase-like multicopper oxidase McoG from from Aspergillus niger [Aspergillus niger]
5LWW_A	5.37e-39	24	562	39	505	Crystal structure of a laccase-like multicopper oxidase McoG from Aspergillus niger bound to zinc [Aspergillus niger]
5Z1X_A	8.85e-39	22	565	16	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]
5LWX_A	1.00e-38	24	562	66	532	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|E9RBR0|ABR2_ASPFU	2.36e-295	1	570	11	579	Laccase abr2 OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=abr2 PE=1 SV=1
sp|A0A443HK79|VDTB1_BYSSP	1.63e-183	4	574	14	597	Multicopper oxidase VdtB OS=Byssochlamys spectabilis OX=264951 GN=VdtB PE=1 SV=1
sp|I1RF62|GIP1_GIBZE	7.15e-183	2	574	17	600	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|A0A1S7IUL2|MCE_TALPI	5.18e-175	13	574	27	592	Multicopper oxidase MCE OS=Talaromyces pinophilus OX=128442 GN=MCE PE=1 SV=1
sp|A0A4Y6F0M8|USTL_USTVR	2.97e-173	1	574	14	605	Laccase ustL OS=Ustilaginoidea virens OX=1159556 GN=ustL PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000057	0.000000

TMHMM  Annotations     

There is no transmembrane helices in ASPSYDRAFT_152224-t33_1-p1.