CAZyme Information: RQM15542.1

Basic Information

• Species: Peronospora effusa
• Lineage: Oomycota; NA; ; Peronosporaceae; Peronospora; Peronospora effusa
• CAZyme ID: RQM15542.1
• CAZy Family: GH81
• CAZyme Description: unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
629	QKXF01000153|CGC1	70766.73	4.6543

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_PeffusaR13	8603	N/A	0	8603

• Gene Location: location=QKXF01000153:47432-49321(-)

Full Sequence      

MQLSVCLNVLLLFVAIVVTSAVYDYKPLRQPKTYESDCVKQWSKLSTSSSDGLDDRSIVK
SSTSELRINLTVMLKRFTSDYVDFNTRSFDGLIPAPTIKLCPGDRLVVTLTNSLEAGRNN
NTNLHLHGMHVPPVGEADNVIPIVEPGGQRRYTYDIRADHPAGTLWYHPHAHGNVNSQLN
GMMAGTLIIVDQPADFPIELAAMDDLVMILQAICVKDCFNMFDNLKDSIENKYSSSMKDM
EATNEEDEQKVWPTDLEIVEDDADIPLNDTSLPTVFVNGQYLPSLDLVVKEYKRLRFVNA
IPNNVAELVTTRDSSCKLTVLAMDGIYFDKPKAKEVIVIPPGGRADVAIMCAETGEFYLE
TDCASSRNKLLGLVNQHRVPSQRIVKLKVMKEDDKSEESESSIVATRLPPVLPKRPAYME
DTFGSAPVIADSNKYNFEFSVWMDKEITYGVNYQTFDMANINHSMPVNELQQWELSVKDY
RMSAGQMCDHNDGSSMERRLTMSSHCHTMSHPFHIHATHFQVTDIHDDTDPDGILFSVGD
WRDTLPLYRGGVQIRFMPRDYMVGNIFAHCHIASHVDAGMAQLVTVYDPRTRPQGDKKDG
KEDDSSNPESEPDDDDDESESDETEKEKR

Enzyme Prediction     

EC	1.10.3.2:4	1.10.3.-:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	86	581	1.4e-31	0.9692737430167597

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
259922	CuRO_1_Tth-MCO_like	1.22e-54	65	189	1	138	The first cupredoxin domain of the bacterial laccases similar to Tth-MCO from Thermus Thermophilus. The subfamily of bacterial laccases includes Tth-MCO and similar proteins. Tth-MCO is a hyperthermophilic multicopper oxidase (MCO) from thermus thermophilus HB27. 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 in fungi and plants. 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.
225043	SufI	1.96e-37	91	586	59	448	Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and spore coat protein CotA) [Cell cycle control, cell division, chromosome partitioning, Inorganic ion transport and metabolism, Cell wall/membrane/envelope biogenesis].
259869	CuRO_1_LCC_like	7.39e-26	89	189	24	119	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.
400195	Cu-oxidase_3	5.66e-24	89	193	20	118	Multicopper oxidase. This entry contains many divergent copper oxidase-like domains that are not recognized by the pfam00394 model.
236810	PRK10965	2.33e-22	86	586	67	523	multicopper oxidase; Provisional

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
UIZ21019.1|AA1	6.32e-40	120	580	5	462
CCO14930.1|AA1	7.40e-27	85	586	9	475
CAK44017.1|AA1	2.81e-10	90	584	107	584
QOU18517.1|AA1_2	1.59e-09	90	589	48	501
QPG75623.1|AA1_2	1.63e-09	90	591	48	503

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3ZX1_A	7.64e-23	88	580	74	473	Multicopper oxidase from Campylobacter jejuni: a metallo-oxidase [Campylobacter jejuni subsp. jejuni]
6IM8_A	6.45e-18	67	591	19	493	CueO-PM2 multicopper oxidase [Escherichia coli K-12],6IM9_A MDM2 bound CueO-PM2 sensor [Escherichia coli K-12]
6IM7_A	1.52e-17	67	591	19	493	CueO-12.1 multicopper oxidase [Escherichia coli K-12]
4HAL_A	4.18e-16	67	586	19	488	Multicopper Oxidase CueO mutant E506I [Escherichia coli K-12]
2YXV_A	6.04e-16	67	586	19	440	Chain A, Blue copper oxidase cueO [Escherichia coli],2YXV_B Chain B, Blue copper oxidase cueO [Escherichia coli],2YXW_A Chain A, Blue copper oxidase cueO [Escherichia coli],2YXW_B Chain B, Blue copper oxidase cueO [Escherichia coli]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|P36649|CUEO_ECOLI	9.73e-15	67	586	47	516	Multicopper oxidase CueO OS=Escherichia coli (strain K12) OX=83333 GN=cueO PE=1 SV=2
sp|Q8X947|CUEO_ECO57	2.26e-14	67	586	47	516	Multicopper oxidase CueO OS=Escherichia coli O157:H7 OX=83334 GN=cueO PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.017883	0.982089	CS pos: 21-22. Pr: 0.7896

TMHMM  Annotations     

Start	End
5	23