CAZyme Information: RhiirA1_405355-t46_1-p1

Basic Information

• Species: Rhizophagus irregularis
• Lineage: Mucoromycota; Glomeromycetes; ; Glomeraceae; Rhizophagus; Rhizophagus irregularis
• CAZyme ID: RhiirA1_405355-t46_1-p1
• CAZy Family: CE9
• CAZyme Description: Cupredoxin

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
187		21567.34	4.9690

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_RirregularisA1DAOM664342	26582	N/A	106	26476

• Gene Location: location=LLXH01007086:26-876(-)

Full Sequence      

IHDPDDPYLNEYDEEIIVMLTDYHHTESEILLKKFLTPSSEGDEINGKNNFDCSQAPHVS
KCVDNSGLAKFEFVSNKRYRLCIINTSAFSAFFFSIDKHEMEVIEVEGSYTKRNKIHRLP
INVAQRYSVIVTVNQPVDNYIMRSEFQKKCMPDDAKKLSIVKAIVHYDGAPEDSAPKDVP
WKDFLEE

Enzyme Prediction     

No EC number prediction in RhiirA1_405355-t46_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	1	174	7e-36	0.45251396648044695

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
259953	CuRO_2_MCO_like_1	1.95e-47	16	168	1	163	The second 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 oxidise 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 family of MCOs 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.
259868	CuRO_2_LCC_like	2.37e-38	16	167	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.
395317	Cu-oxidase	1.71e-31	14	170	1	146	Multicopper oxidase. Many of the proteins in this family contain multiple similar copies of this plastocyanin-like domain.
259949	CuRO_2_Tv-LCC_like	2.71e-31	17	172	2	148	The second 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. Laccase is a multicopper oxidase (MCO) 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.
259945	CuRO_2_Fet3p_like	8.64e-31	14	142	1	120	The second 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 2 of 3-domain MCOs has lost the ability to bind copper.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QBZ62742.1|AA1	2.94e-28	1	185	305	505
AUS45844.1|AA1	2.13e-26	1	183	241	437
QKX53525.1|AA1	9.71e-25	1	167	224	402
AEO70365.1|AA1	3.03e-24	12	185	241	427
CDS12866.1|AA1_2	4.26e-23	1	178	142	311

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5LM8_A	3.08e-18	7	181	144	315	Crystal structure of a laccase-like multicopper oxidase McoG from from Aspergillus niger [Aspergillus niger]
5LWW_A	3.08e-18	7	181	145	316	Crystal structure of a laccase-like multicopper oxidase McoG from Aspergillus niger bound to zinc [Aspergillus niger]
5LWX_A	5.80e-18	7	181	172	343	Crystal structure of the H253D mutant of McoG from Aspergillus niger [Aspergillus niger]
5EHF_A	6.39e-17	1	171	126	287	Laccase from Antrodiella faginea [Antrodiella faginea]
3KW7_A	1.19e-16	1	144	126	261	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q02081|LAC4_THACU	1.12e-19	1	171	145	318	Laccase-4 OS=Thanatephorus cucumeris OX=107832 GN=LCC4 PE=1 SV=1
sp|J5JH35|OPS5_BEAB2	8.79e-18	7	168	194	357	Oxidoreductase OpS5 OS=Beauveria bassiana (strain ARSEF 2860) OX=655819 GN=OpS5 PE=1 SV=1
sp|Q12729|LAC1_PLEOS	9.89e-17	1	173	158	318	Laccase-1 OS=Pleurotus ostreatus OX=5322 GN=POX1 PE=2 SV=1
sp|Q01679|LAC1_PHLRA	1.33e-16	1	170	147	307	Laccase OS=Phlebia radiata OX=5308 GN=LAC PE=1 SV=2
sp|D0VWU3|LAC1_TRAMX	1.78e-16	1	171	126	285	Laccase OS=Trametes maxima OX=259368 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000078	0.000000

TMHMM  Annotations     

There is no transmembrane helices in RhiirA1_405355-t46_1-p1.