dbCAN-seq: a database of CAZyme sequence and annotation

Basic Information help

Species

Aspergillus cristatus

Lineage

Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus cristatus

CAZyme ID

ODM19665.1

CAZy Family

GT90

CAZyme Description

Plastocyanin-like domain-containing protein [Source:UniProtKB/TrEMBL;Acc:A0A1E3BFA4]

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
324	JXNT01000004\|CGC5	36324.16	5.5617

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AcristatusGZAAS20.1005	10344	N/A	0	10344

Gene Location

Enzyme Prediction help

EC	1.10.3.2:1

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
259966	CuRO_3_Fet3p	1.70e-86	75	233	1	160	The third Cupredoxin domain of multicopper oxidase Fet3p. Fet3p catalyzes the ferroxidase reaction, which couples the oxidation of Fe(II) to Fe(III) with the four-electron reduction of molecular oxygen to water. Fet3p is a type I membrane protein with the amino-terminal oxidase domain in the extracellular space and the carboxyl terminus in the cytoplasm. The periplasmic produced Fe(III) is transferred to the permease Ftr1p for import into the cytosol. The four copper ions are inserted post-translationally and are essential for catalytic activity, thus linking copper and iron homeostasis. Like other related multicopper oxidases (MCOs), Fet3p 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.
400194	Cu-oxidase_2	1.76e-43	101	233	1	136	Multicopper oxidase. This entry contains many divergent copper oxidase-like domains that are not recognized by the pfam00394 model.
259970	CuRO_3_Tv-LCC_like	1.06e-41	75	233	1	147	The third cupredoxin domain of the fungal laccases similar to Tv-LCC from Trametes Versicolor. This subfamily of fungal laccases includes Tv-LCC from Trametes versicolor and Rs-LCC2 from plant pathogenic fungus Rhizoctonia solani. 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. 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 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.
259977	CuRO_3_MCO_like_4	1.18e-40	92	226	16	161	The third cupredoxin domain of uncharacterized multicopper oxidase. Multicopper Oxidases (MCOs) are multi-domain enzymes that are able to couple oxidation of substrates with reduction of dioxygen to water. MCOs oxidize their substrate by accepting electrons at a mononuclear copper centre and transferring them to a trinuclear copper centre which binds a dioxygen. The dioxygen, following the transfer of four electrons, is reduced to two molecules of water. These MCOs are capable of oxidizing a vast range of substrates, varying from aromatic to inorganic compounds such as metals. This subfamily of MCOs is composed of three cupredoxin domains. 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.
259870	CuRO_3_LCC_like	6.09e-36	75	230	1	132	Cupredoxin domain 3 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 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. Also included in this family are cupredoxin domains 2, 4, and 6 of the 6-domain MCO ceruloplasmin and similar proteins.

CAZyme Hits help

Hit ID	E-Value	Query Start	Query End	Hit Start
1.82e-155	11	242	1	232
2.17e-135	1	242	261	500
3.23e-135	1	242	261	500
8.99e-135	1	242	261	500
1.11e-134	1	242	261	500

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
4.54e-68	2	238	243	486	Crystal Structure of Fet3p, a Multicopper Oxidase that Functions in Iron Import [Saccharomyces cerevisiae],1ZPU_B Crystal Structure of Fet3p, a Multicopper Oxidase that Functions in Iron Import [Saccharomyces cerevisiae],1ZPU_C Crystal Structure of Fet3p, a Multicopper Oxidase that Functions in Iron Import [Saccharomyces cerevisiae],1ZPU_D Crystal Structure of Fet3p, a Multicopper Oxidase that Functions in Iron Import [Saccharomyces cerevisiae],1ZPU_E Crystal Structure of Fet3p, a Multicopper Oxidase that Functions in Iron Import [Saccharomyces cerevisiae],1ZPU_F Crystal Structure of Fet3p, a Multicopper Oxidase that Functions in Iron Import [Saccharomyces cerevisiae]
2.27e-22	61	231	304	472	Crystal structure of LacB from Trametes sp. AH28-2 [Trametes sp. AH28-2],3KW7_B Crystal structure of LacB from Trametes sp. AH28-2 [Trametes sp. AH28-2]
8.21e-22	48	231	316	489	Chain A, Laccase [Rigidoporus microporus]
4.63e-21	67	231	319	469	Crystal Structure of Laccase from Steccherinum ochraceum [Steccherinum ochraceum],3T6V_B Crystal Structure of Laccase from Steccherinum ochraceum [Steccherinum ochraceum],3T6V_C Crystal Structure of Laccase from Steccherinum ochraceum [Steccherinum ochraceum],3T6W_A Crystal Structure of Steccherinum ochraceum Laccase obtained by multi-crystals composite data collection technique (10% dose) [Steccherinum ochraceum],3T6W_B Crystal Structure of Steccherinum ochraceum Laccase obtained by multi-crystals composite data collection technique (10% dose) [Steccherinum ochraceum],3T6W_C Crystal Structure of Steccherinum ochraceum Laccase obtained by multi-crystals composite data collection technique (10% dose) [Steccherinum ochraceum],3T6X_A Crystal Structure of Steccherinum ochraceum Laccase obtained by multi-crystals composite data collection technique (20% dose) [Steccherinum ochraceum],3T6X_B Crystal Structure of Steccherinum ochraceum Laccase obtained by multi-crystals composite data collection technique (20% dose) [Steccherinum ochraceum],3T6X_C Crystal Structure of Steccherinum ochraceum Laccase obtained by multi-crystals composite data collection technique (20% dose) [Steccherinum ochraceum],3T6Z_A Crystal Structure of Steccherinum ochraceum Laccase obtained by multi-crystals composite data collection technique (60% dose) [Steccherinum ochraceum],3T6Z_B Crystal Structure of Steccherinum ochraceum Laccase obtained by multi-crystals composite data collection technique (60% dose) [Steccherinum ochraceum],3T6Z_C Crystal Structure of Steccherinum ochraceum Laccase obtained by multi-crystals composite data collection technique (60% dose) [Steccherinum ochraceum],3T71_A Crystal Structure of Steccherinum ochraceum Laccase obtained by multi-crystals composite data collection technique (90% dose) [Steccherinum ochraceum],3T71_B Crystal Structure of Steccherinum ochraceum Laccase obtained by multi-crystals composite data collection technique (90% dose) [Steccherinum ochraceum],3T71_C Crystal Structure of Steccherinum ochraceum Laccase obtained by multi-crystals composite data collection technique (90% dose) [Steccherinum ochraceum]
2.93e-20	65	231	316	468	Chain A, LACCASE 1 [Coprinopsis cinerea]

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
1.25e-112	1	242	263	503	Iron transport multicopper oxidase fetC OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=fetC PE=2 SV=1
1.14e-75	2	242	264	506	Iron transport multicopper oxidase fetC OS=Epichloe festucae (strain E2368) OX=696363 GN=fetC PE=2 SV=1
4.43e-75	2	244	266	509	Iron transport multicopper oxidase FET3 OS=Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1) OX=229533 GN=FET3 PE=2 SV=1
1.93e-71	2	241	264	514	Iron transport multicopper oxidase FET3 OS=Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65) OX=284593 GN=FET3 PE=3 SV=1
1.43e-69	2	237	269	511	Iron transport multicopper oxidase FET3 OS=Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) OX=284590 GN=FET3 PE=3 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
0.998832	0.001217

TMHMM Annotations help

There is no transmembrane helices in ODM19665.1.

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