CAZyme Information: EPrPVT00000015880-p1

Basic Information

• Species: Phytopythium vexans
• Lineage: Oomycota; NA; ; Pythiaceae; Phytopythium; Phytopythium vexans
• CAZyme ID: EPrPVT00000015880-p1
• CAZy Family: CBM9
• CAZyme Description: MCO is implicated in celullar iron transport playing also role in the copper resistance

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
571	PvexDAOMBR484_SC0107|CGC1	63131.64	5.2177

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_PvexansDAOMBR484	11991	1223560	34	11957

• Gene Location: location=PvexDAOMBR484_SC0107:33844-35559(-)

Full Sequence      

MWRGLASDTNWESELLAQMALEKLAGQLEPLFEPETRTSVNGELNTTLRVGAKLFEAGPI
SFWTRAYEDSIPGPILRVKPGDVLHLHLVNELGPNVAGEWTMNTMHNPNNTNVHFHGMHV
DPTGVEDNVFRVCAPGESMDTTLHVPASHPRGVFHYHPHYHGSVFLQMGGGMVGAVVVED
DPDTVPAAYAAMKQHVVALQEFRFDGGLMSSLLDAAEAARSTLDMQPTYTRGSFLESRVR
SLFPREQVVQRPSKAVKMPEDWESSDDDLVPPISMYFAVNGQYLPKIEVRPRENRLLRLI
NAGGTAELEIVLPGCSMTLAASDGIYLSKPRLVRTLLLSPGGRVDVVINCEPNAEGEKDL
EALRPLHSVKNKAINEFLGGSTDVFKGVLAFIHVQGDSLEQPEIAAIPPAPAMYGEDTSL
MSLSTEDREQMDLLPFVFEYTMGTPVVKDGFQYKQYFINHKLFDGTSVHTMVLGRVQEWV
IVNHHDEQGELTQKNHPFHLHTNAFQVIDMSHGHGLDYEIGDWRDTILVPTPGNVTIRFR
PLDYTGVVAAHCHILGHSDAGMIAGVDMVSA

Enzyme Prediction     

No EC number prediction in EPrPVT00000015880-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	68	562	1.6e-28	0.9553072625698324

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
259922	CuRO_1_Tth-MCO_like	3.33e-51	43	167	1	127	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	1.54e-36	64	569	54	449	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].
259967	CuRO_3_Tth-MCO_like	4.39e-32	454	567	18	122	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.
259870	CuRO_3_LCC_like	4.89e-27	453	567	17	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.
400194	Cu-oxidase_2	1.72e-22	434	562	6	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	1.28e-229	105	570	1	470
CCO14930.1|AA1	2.73e-33	64	564	10	471
UHU71023.1|AA1_2	8.50e-16	72	564	58	496
CAX40993.1|AA1_2	9.34e-13	67	562	48	491
AOW29994.1|AA1_2	8.76e-12	56	562	34	492

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2XU9_A	8.92e-36	67	568	40	438	Crystal structure of Laccase from Thermus thermophilus HB27 [Thermus thermophilus HB27],2XUW_A Crystal Structure of Apolaccase from Thermus thermophilus HB27 [Thermus thermophilus HB27],2XVB_A Crystal structure of Laccase from Thermus thermophilus HB27 complexed with Hg, crystal of the apoenzyme soaked for 5 min. in 5 mM HgCl2 at 278 K. [Thermus thermophilus HB27],2YAE_A X-ray induced reduction of laccase from Thermus thermophilus HB27(0.0- 12.5 percent dose) [Thermus thermophilus HB27],2YAF_A X-ray induced reduction of laccase from Thermus thermophilus HB27 (12. 5-25.0 percent dose) [Thermus thermophilus HB27],2YAH_A X-ray induced reduction of laccase from Thermus thermophilus HB27 (25. 0-37.5 percent dose) [Thermus thermophilus HB27],2YAM_A X-ray induced reduction of laccase from Thermus thermophilus HB27 (37. 5-50.0 percent dose) [Thermus thermophilus HB27],2YAO_A X-ray induced reduction of laccase from Thermus thermophilus HB27 (50. 0-62.5 percent dose) [Thermus thermophilus HB27],2YAP_A X-ray induced reduction of laccase from Thermus thermophilus HB27 (62. 5-75.0 percent dose) [Thermus thermophilus HB27],2YAQ_A X-ray induced reduction of laccase from Thermus thermophilus HB27 (75. 0-87.5 percent dose) [Thermus thermophilus HB27],2YAR_A X-ray induced reduction of laccase from Thermus thermophilus HB27 (87. 5-100.0 percent dose) [Thermus thermophilus HB27],4AI7_A Crystal structure of Laccase from Thermus thermophilus HB27 complexed with Hg, crystal of the apoenzyme soaked for 2 h in 5 mM HgCl2 at 278 K. [Thermus thermophilus HB27],5AFA_A Crystal structure of Laccase from Thermus thermophilus HB27 complexed with Ag, crystal of the holoenzyme soaked for 30 m in 5 mM AgNO3 at 278 K. [Thermus thermophilus HB27],5G3B_A Preserving metallic sites affected by radiation damage: the CuT2 case in Thermus thermophilus multicopper oxidase [Thermus thermophilus],5G3C_A Preserving Metallic sites affected by radiation damage the CuT2 case in thermus termophilus multicopper oxidase [Thermus thermophilus],5G3D_A preserving Metallic Sites Affected by Radiation Damage the CuT2 cCase in Thermus Thermophilus Multicopper Oxidase [Thermus thermophilus],5G3E_A Preserving Metallic Sites Affected by Radiation DAmage the CuT2 CAse in THermus Thermophilus Multicopper Oxidase [Thermus thermophilus],5G3F_A Preserving Metallic Sites Affected by Radiation Damage the CuT2 CAse in Thermus Thermophilus Multicopper Oxidase [Thermus thermophilus],5G3G_A Preserving MEtallic Sites Affected by Radiation Damage the CuT2 case in Thermus Thermophilus multicopper Oxidase [Thermus thermophilus],5G3H_A Preserving Metallic Sites Affected by Radiation Damage the CuT2 Case in Thermus Thermophilus Multicopper oxidase [Thermus thermophilus],5JRR_A Crystal structure of native laccase from Thermus thermophilus HB27 [Thermus thermophilus HB27],5JX9_A Crystal structure of laccase from Thermus thermophilus HB27 (Cu(II)-cyclophanes, 5 min) [Thermus thermophilus HB27],5K0D_A Crystal structure of laccase from Thermus thermophilus HB27 (Cu(II)-cyclophanes, 3 min) [Thermus thermophilus HB27],5K15_A Crystal structure of laccase from Thermus thermophilus HB27 (Cu2PO, 8 min) [Thermus thermophilus HB27],5K3K_A Crystal structure of laccase from Thermus thermophilus HB27 (CuSO4, 20 min) [Thermus thermophilus HB27],5K5K_A Crystal structure of laccasse from Thermus thermophilus HB27 (ascorbic acid 10 min) [Thermus thermophilus HB27],5K7A_A Crystal structure of laccase fron Thermus thermophilus HB27 (sodium nitrate 1.5 min) [Thermus thermophilus HB27],5K84_A Crystal structure of laccase from Thermus thermophilus HB27 (sodium nitrate 10 min) [Thermus thermophilus HB27],6Q29_A Chain A, Laccase [Thermus thermophilus HB27],6TYR_A Chain A, Laccase [Thermus thermophilus HB27]
6W2K_A	9.07e-36	67	568	41	439	Chain A, Laccase [Thermus thermophilus HB27],6W2K_B Chain B, Laccase [Thermus thermophilus HB27],6W9X_A Chain A, Laccase [Thermus thermophilus HB27],6WCG_A Chain A, Laccase [Thermus thermophilus HB27],6WCH_A Chain A, Laccase [Thermus thermophilus HB27],6WCL_A Chain A, Laccase [Thermus thermophilus HB27],6WCM_A Chain A, Laccase [Thermus thermophilus HB27]
6WCN_A	1.28e-35	67	568	63	461	Chain A, Laccase [Thermus thermophilus HB27],6WCP_A Chain A, Laccase [Thermus thermophilus HB27]
3ZX1_A	1.08e-21	67	568	75	479	Multicopper oxidase from Campylobacter jejuni: a metallo-oxidase [Campylobacter jejuni subsp. jejuni]
7Z5P_A	6.35e-15	243	569	198	509	Chain A, Copper oxidase [Bacillus pumilus SAFR-032],7Z5P_B Chain B, Copper oxidase [Bacillus pumilus SAFR-032]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q8ZBK0|CUEO_YERPE	1.40e-13	24	565	27	528	Multicopper oxidase CueO OS=Yersinia pestis OX=632 GN=cueO PE=3 SV=1
sp|Q6GIX3|MCO_STAAR	1.41e-13	41	568	48	445	Multicopper oxidase mco OS=Staphylococcus aureus (strain MRSA252) OX=282458 GN=mco PE=3 SV=2
sp|Q69HT9|MCO_STAAU	2.49e-13	41	568	48	445	Multicopper oxidase mco OS=Staphylococcus aureus OX=1280 GN=mco PE=1 SV=2
sp|Q6CII3|FET3_KLULA	5.14e-13	68	562	53	499	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
sp|P36649|CUEO_ECOLI	5.49e-13	38	565	42	513	Multicopper oxidase CueO OS=Escherichia coli (strain K12) OX=83333 GN=cueO PE=1 SV=2

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000043	0.000004

TMHMM  Annotations     

There is no transmembrane helices in EPrPVT00000015880-p1.