CAZyme Information: PPTG_09998-t26_1-p1

Basic Information

• Species: Phytophthora parasitica
• Lineage: Oomycota; NA; ; Peronosporaceae; Phytophthora; Phytophthora parasitica
• CAZyme ID: PPTG_09998-t26_1-p1
• CAZy Family: GH3
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
644		72130.46	4.3683

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_PparasiticaINRA-310	23240	761204	119	23121

• Gene Location: location=KI669580:186575-188509(+)

Full Sequence      

MDRGLMRLSVCLQSVILAVAIGVTTAVYDYEPLRQPTLYQSDCAKQWSKATDSSSSSVDD
RSTVKSRTGELRVNLAVKLARFTSEYVDFNTRAYNGHVPAPTIKICPGDRLVVTLTNSLE
AGKSNNTNLHLHGMHVPPVGDADNVMPNVEPGGQRRYTYEIRPDHPAGTFWYHPHTHGNV
NSQLNGMMAGALIVVDRPADFPAELAAMDDLIMILQAVCVENCFNMYDDLEEAIENKYSH
SRRLSDTPDEDEEEHIWPTDLEIVEDDADIPLNDTSLPTVFVNGQYLPTLDLAVGEYKRL
RFINAIANNVAELVTSRGSGCMLEVLAMDGIYFTKPKAKEVIVIPPGGRADVAIMCAEIG
EFYLETDSASSRNKLLGLVNQHRVPSQPIVKLKVTKVEDPDDEDESEISAEFMRLPSSLP
KRPAYMEDTLGTPQSRPIIEESNKYDFEFSVWMDKGITYGVNHEKLDIASINYSMPVNEM
QQWEISVKDYRKAAIWDCDLEDDSTSVERRLAKKSSNCRTMSHPFHMHSTHFQISDMDDI
TDPDGIMFDVGEWRDTLPIFRGGVQIRFTPREYMVGNIFAHCHIASHVDAGMAQLVNVYD
SDTRSNGDEASEEEDSASDEDGDEDESDSSDTEDTKEVQNVEKR

Enzyme Prediction     

EC	1.10.3.2:4	1.10.3.-:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	91	593	6.6e-32	0.9692737430167597

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
259922	CuRO_1_Tth-MCO_like	9.08e-60	70	194	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	3.65e-40	91	593	54	443	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].
400195	Cu-oxidase_3	1.62e-27	93	198	19	118	Multicopper oxidase. This entry contains many divergent copper oxidase-like domains that are not recognized by the pfam00394 model.
259869	CuRO_1_LCC_like	2.73e-27	93	194	23	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.
259894	CuRO_1_CueO_FtsP	2.57e-22	90	196	21	120	The first Cupredoxin domain of the multicopper oxidase CueO, the cell division protein FtsP, and similar proteins. CueO is a multicopper oxidase (MCO) that is part of the copper-regulatory cue operon, which employs a cytosolic metalloregulatory protein CueR that induces expression of CopA and CueO under copper stress conditions. CueO is a periplasmic multicopper oxidase that is stimulated by exogenous copper(II). FtsP (also named SufI) is a component of the cell division apparatus. It is involved in protecting or stabilizing the assembly of divisomes under stress conditions. FtsP belongs to the multicopper oxidase superfamily but lacks metal cofactors. The protein is localized at septal rings and may serve as a scaffolding function. Members of this subfamily contain three cupredoxin domains and this model represents the first domain. 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. FtsP does not contain any copper binding sites.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
UIZ21019.1|AA1	7.26e-43	125	602	5	472
CCO14930.1|AA1	1.97e-25	101	591	20	468
QKX63685.1|AA1	9.07e-13	95	602	99	613
AGO11897.1|AA1_2	3.10e-10	95	596	48	501
UNI19384.1|AA1	5.95e-10	95	200	210	313

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3ZX1_A	5.76e-25	94	592	75	473	Multicopper oxidase from Campylobacter jejuni: a metallo-oxidase [Campylobacter jejuni subsp. jejuni]
2XU9_A	2.23e-24	94	598	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	2.26e-24	94	598	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	2.80e-24	94	598	63	461	Chain A, Laccase [Thermus thermophilus HB27],6WCP_A Chain A, Laccase [Thermus thermophilus HB27]
2YXV_A	8.19e-15	72	592	19	434	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	3.70e-12	72	592	47	510	Multicopper oxidase CueO OS=Escherichia coli (strain K12) OX=83333 GN=cueO PE=1 SV=2
sp|Q8X947|CUEO_ECO57	3.70e-12	72	592	47	510	Multicopper oxidase CueO OS=Escherichia coli O157:H7 OX=83334 GN=cueO PE=3 SV=1
sp|Q8RYM9|LAC2_ORYSJ	1.41e-09	95	600	53	544	Laccase-2 OS=Oryza sativa subsp. japonica OX=39947 GN=LAC2 PE=2 SV=1
sp|P38993|FET3_YEAST	8.10e-09	95	206	49	157	Iron transport multicopper oxidase FET3 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=FET3 PE=1 SV=2
sp|Q96WT3|FET3_CANGA	1.07e-08	95	187	45	136	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

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.424697	0.575295	CS pos: 26-27. Pr: 0.4064

TMHMM  Annotations     

There is no transmembrane helices in PPTG_09998-t26_1-p1.