CAZyme Information: P174DRAFT_418746-t37_1-p1

Basic Information

• Species: Aspergillus novofumigatus
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus novofumigatus
• CAZyme ID: P174DRAFT_418746-t37_1-p1
• CAZy Family: GH13|GH13
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
417	MSZS01000002|CGC28	46748.10	4.4451

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AnovofumigatusIBT16806	11729	1392255	197	11532

• Gene Location: location=MSZS01000002:4229909-4232157(+)

Full Sequence      

MPDQPCPEGTVLLGAAPETPECLLHSVFDHDTKRLDQEAAQSTAIREPDACSSVDRESPY
DQDKNGQFRSPTLILDEGDDVEIVINNHMHQNTTIHWHGILMQNTPWSDGVPGLSQTPLE
PGERYVYRCTASPPGQYWYHSYLRANLLDGLYGKPGTPGPWATISQGPVEIQVMERAAND
PQIIALSDWGYYNSSQYKEADANSHLQILYENDDSSASFHTLTWLIDKQIPFMHKSWPND
NIPDKGYDLVLLFKIETRNIDTHSCFPFAAYAEGPWLKDGNVSAIPPGLQGGCRPSTGPT
EVIEVDASDLWVSINCIAGSMQPTIDEHEMWIYEVDGHYIEPRRAETFLIWAGERYLALV
RLDNKQMDYSIRMPDGGYSQMIAALGVLRYKNGDPDAHQPSDRFGFTAISQPHIPSI

Enzyme Prediction     

No EC number prediction in P174DRAFT_418746-t37_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	65	198	3.4e-32	0.35195530726256985

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
259919	CuRO_1_Abr2_like	1.45e-41	65	153	23	112	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.
259927	CuRO_1_tcLCC2_insect_like	2.35e-32	65	153	11	100	The first cupredoxin domain of insect laccases similar to laccase 2 in Tribolium castaneum. This multicopper oxidase (MCO) family includes the majority of insect laccases. One member of the family is laccase 2 from Tribolium castaneum. Laccase 2 is required for beetle cuticle tanning. Laccase (polyphenol oxidase EC 1.10.3.2) is a blue multi-copper enzyme that catalyzes the oxidation of a variety of organic substrates coupled to the reduction of molecular oxygen to water. It displays broad substrate specificity, catalyzing the oxidation of a wide variety of aromatic - notably phenolic and inorganic substances. 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, plants and insects. 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.
259944	CuRO_2_Abr2_like	1.28e-30	302	391	45	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.
400195	Cu-oxidase_3	2.63e-30	65	153	21	110	Multicopper oxidase. This entry contains many divergent copper oxidase-like domains that are not recognized by the pfam00394 model.
259869	CuRO_1_LCC_like	7.53e-30	65	153	25	115	Cupredoxin domain 1 of laccase-like multicopper oxidases; including laccase, CueO, spore coat protein A, ascorbate oxidase and similar proteins. Laccase-like multicopper oxidases (MCOs) in this family contain three cupredoxin domains. They 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 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 1 of 3-domain MCOs contains part the trinuclear copper binding site, which is located at the interface of domains 1 and 3. Also included in this family are cupredoxin domains 1, 3, and 5 of the 6-domain MCO ceruloplasmin and similar proteins.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ATY66872.1|AA1	2.91e-133	65	412	54	398
CEI66207.1|AA1	1.01e-92	65	415	49	407
CEF74605.1|AA1	1.44e-89	65	393	49	380
CZS77880.1|AA1	1.44e-89	65	393	49	380
QKX57114.1|AA1	3.93e-87	65	400	48	381

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1AOZ_A	2.47e-22	65	368	28	274	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]
4E9V_A	8.68e-19	65	199	29	157	Multicopper Oxidase mgLAC (data1) [uncultured bacterium],4E9V_B Multicopper Oxidase mgLAC (data1) [uncultured bacterium],4E9V_C Multicopper Oxidase mgLAC (data1) [uncultured bacterium],4E9W_A Multicopper Oxidase mgLAC (data2) [uncultured bacterium],4E9W_B Multicopper Oxidase mgLAC (data2) [uncultured bacterium],4E9W_C Multicopper Oxidase mgLAC (data2) [uncultured bacterium],4E9X_A Multicopper Oxidase mgLAC (data3) [uncultured bacterium],4E9X_B Multicopper Oxidase mgLAC (data3) [uncultured bacterium],4E9X_C Multicopper Oxidase mgLAC (data3) [uncultured bacterium],4E9Y_A Multicopper Oxidase mgLAC (data4) [uncultured bacterium],4E9Y_B Multicopper Oxidase mgLAC (data4) [uncultured bacterium],4E9Y_C Multicopper Oxidase mgLAC (data4) [uncultured bacterium]
3G5W_A	1.68e-18	65	189	28	146	Crystal structure of Blue Copper Oxidase from Nitrosomonas europaea [Nitrosomonas europaea],3G5W_B Crystal structure of Blue Copper Oxidase from Nitrosomonas europaea [Nitrosomonas europaea],3G5W_C Crystal structure of Blue Copper Oxidase from Nitrosomonas europaea [Nitrosomonas europaea],3G5W_D Crystal structure of Blue Copper Oxidase from Nitrosomonas europaea [Nitrosomonas europaea],3G5W_E Crystal structure of Blue Copper Oxidase from Nitrosomonas europaea [Nitrosomonas europaea],3G5W_F Crystal structure of Blue Copper Oxidase from Nitrosomonas europaea [Nitrosomonas europaea]
3V9E_A	1.32e-16	65	191	92	207	Structure of the L499M mutant of the laccase from B.aclada [Botrytis aclada]
3SQR_A	1.32e-16	65	191	92	207	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|A0A443HK79|VDTB1_BYSSP	6.25e-179	65	414	44	390	Multicopper oxidase VdtB OS=Byssochlamys spectabilis OX=264951 GN=VdtB PE=1 SV=1
sp|I1RF62|GIP1_GIBZE	2.55e-90	65	393	49	380	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	1.43e-84	65	393	48	372	Multicopper oxidase MCE OS=Talaromyces pinophilus OX=128442 GN=MCE PE=1 SV=1
sp|A0A4Y6F0M8|USTL_USTVR	5.21e-82	65	394	47	375	Laccase ustL OS=Ustilaginoidea virens OX=1159556 GN=ustL PE=1 SV=1
sp|A0A0B4HQH6|MLAC1_METMF	4.17e-72	65	391	48	377	Laccase 1 OS=Metarhizium majus (strain ARSEF 297) OX=1276143 GN=Mlac1 PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000043	0.000000

TMHMM  Annotations     

There is no transmembrane helices in P174DRAFT_418746-t37_1-p1.