CAZyme Information: PSURA_78827T0-p1

Basic Information

• Species: Phytophthora ramorum
• Lineage: Oomycota; NA; ; Peronosporaceae; Phytophthora; Phytophthora ramorum
• CAZyme ID: PSURA_78827T0-p1
• CAZy Family: GH35
• CAZyme Description: unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
655		71978.73	5.8488

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_PramorumPr-102	15743	N/A	251	15492

• Gene Location: location=PramPr-102_SC0035:63404-65368(+)

Full Sequence      

MAPTATEGSRKRAAAPRPITSSGYGTGVFCESKRDEADPEADDAKDSDEFLRRGARQLQT
QTIRLRRNIVCSVVVGVGLVALLLVSFAHQERPQNLRGEAATRQATLLQVLEQLPTLPTL
ETRTSTNGELNTTLTVAEKLVDNGPIAFYTRAYEDSVPGPLFVLQPGDVLNIHLVNNLGP
NVPGDWTPNTMHEPNNTNLHFHGMHVDPTGTEDNVFRVVAPGESAETHLHVPLNHPRGLF
HYHPHFHGSVFLQMGGGMVGPIVVDDDPATVPAEYAAIQQKHVVVLQEFKFSGGMMTSLP
DAAKASRSTLDMKLTYTGKVMLDEQVRKLYPDVQEVERPVRNAKMSKELLDEMDSSEDKP
KLPPIAQYFSVNGQYLPKIQVRPHENVLLRMLHAGGTASLEVQVPGCSVMLASSDGLYLP
KPRPMETVVLLPGARVDLVLNCEPTADGGPEVLRPIQSVKDPKLHGFMGNHSDLYSGVLA
FVHVQGESLDQPLVTAVPPPSELYAPSKSLLDLSAEDRAGMDPLPFEFEFTMGDPEMKDG
FYYKPYFINHALFDGTSIRTMTLGRVQEWVIINRRDESGAVTLKNHPFHLHTNAFQIVDM
SHGHGVDYEIGDWRDVISVPTPGNVTIRFRPEDYTGIVAAHCHILGHSDAGMIAA

Enzyme Prediction     

No EC number prediction in PSURA_78827T0-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	154	652	4.3e-24	0.9553072625698324

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
259922	CuRO_1_Tth-MCO_like	5.56e-60	129	265	1	139	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.
259967	CuRO_3_Tth-MCO_like	1.11e-32	527	654	5	119	The third 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 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.
225043	SufI	1.79e-29	150	654	54	444	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].
259870	CuRO_3_LCC_like	6.58e-29	527	654	3	129	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.
400194	Cu-oxidase_2	2.27e-20	522	652	4	128	Multicopper oxidase. This entry contains many divergent copper oxidase-like domains that are not recognized by the pfam00394 model.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
UIZ21019.1|AA1	2.15e-299	191	654	1	464
CCO14930.1|AA1	3.64e-26	150	654	10	471
AHZ65140.1|AA1_2	3.34e-11	245	654	67	474
ACO53431.1|AA1_1	6.60e-11	136	651	26	481
VBB83984.1|AA1	1.14e-10	158	653	167	662

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3ZX1_A	3.56e-20	112	653	33	474	Multicopper oxidase from Campylobacter jejuni: a metallo-oxidase [Campylobacter jejuni subsp. jejuni]
4HAK_A	2.12e-12	115	653	4	483	Multicopper Oxidase CueO mutant E506A [Escherichia coli K-12]
1KV7_A	2.79e-12	115	653	4	483	Crystal Structure of CueO, a multi-copper oxidase from E. coli involved in copper homeostasis [Escherichia coli],1N68_A Copper bound to the Multicopper Oxidase CueO [Escherichia coli],2FQD_A Crystal Structures of E. coli Laccase CueO under different copper binding situations [Escherichia coli],2FQE_A Crystal Structures of E. coli Laccase CueO under different copper binding situations [Escherichia coli],2FQF_A Crystal Structures of E. coli Laccase CueO under different copper binding situations [Escherichia coli],2FQG_A Crystal Structures of E. coli Laccase CueO under different copper binding situations [Escherichia coli],3NSD_A Silver bound to the multicopper oxidase CueO (untagged) [Escherichia coli],3OD3_A CueO at 1.1 A resolution including residues in previously disordered region [Escherichia coli],3PAU_A CueO in the resting oxidized state [Escherichia coli str. K-12 substr. W3110],3PAV_A The reduced form of CueO [Escherichia coli]
4E9Q_A	2.80e-12	115	653	4	483	Multicopper Oxidase CueO (data2) [Escherichia coli K-12],4E9R_A Multicopper Oxidase CueO (data4) [Escherichia coli K-12],4E9S_A Multicopper Oxidase CueO (data5) [Escherichia coli K-12],4E9T_A Multicopper Oxidase CueO (data6) [Escherichia coli K-12],4EF3_A Multicopper Oxidase CueO (Citrate buffer) [Escherichia coli K-12],4NER_A Multicopper Oxidase CueO (data1) [Escherichia coli K-12]
5B7F_A	2.82e-12	115	653	8	487	Structure of CueO - the signal peptide was truncated by HRV3C protease [Escherichia coli K-12],5B7M_A Structure of perdeuterated CueO - the signal peptide was truncated by HRV3C protease [Escherichia coli K-12],5B7M_B Structure of perdeuterated CueO - the signal peptide was truncated by HRV3C protease [Escherichia coli K-12],5B7M_C Structure of perdeuterated CueO - the signal peptide was truncated by HRV3C protease [Escherichia coli K-12]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|P36649|CUEO_ECOLI	1.54e-11	115	653	32	511	Multicopper oxidase CueO OS=Escherichia coli (strain K12) OX=83333 GN=cueO PE=1 SV=2
sp|Q69HT9|MCO_STAAU	2.79e-10	150	653	72	440	Multicopper oxidase mco OS=Staphylococcus aureus OX=1280 GN=mco PE=1 SV=2
sp|Q6GIX3|MCO_STAAR	3.70e-10	150	653	72	440	Multicopper oxidase mco OS=Staphylococcus aureus (strain MRSA252) OX=282458 GN=mco PE=3 SV=2
sp|Q8X947|CUEO_ECO57	4.39e-10	115	653	32	511	Multicopper oxidase CueO OS=Escherichia coli O157:H7 OX=83334 GN=cueO PE=3 SV=1
sp|Q4LAB0|MCO_STAHJ	2.49e-08	121	653	42	440	Multicopper oxidase mco OS=Staphylococcus haemolyticus (strain JCSC1435) OX=279808 GN=mco PE=3 SV=2

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000052	0.000004

TMHMM  Annotations     

Start	End
69	88