CAZyme Information: PPTG_11320-t26_1-p1

Basic Information

• Species: Phytophthora parasitica
• Lineage: Oomycota; NA; ; Peronosporaceae; Phytophthora; Phytophthora parasitica
• CAZyme ID: PPTG_11320-t26_1-p1
• CAZy Family: GH43
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
550		60312.26	4.3286

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=KI669584:270633-272698(+)

Full Sequence      

MDYARFFVALLSIFIADTAADNSTVTYDWRVTYVSTACDGVSLTEYGINGDVATLALIEL
ELGQTVQVTVTNELNEPTCLHWHGLQQLGTQEMDGTSDITQCEIPAGGSAVYTFTPERAG
TFWWHSHHATQYAFGLRGPLIVHAPADKQQSWEQEVAAEYTLQIADLYHTSPGIVPMWDS
VIINSLGRYNCSAAASHGYSECNTDQPLSRFKFEGRFFLGSYTERIRSLNRPTHSDCDQV
PEQGITEPSEEITTLRINAGQRYDIIVEAKPASSFKMGSFWIRATALYGLPWTAGTASIA
GDGFNYEGLAVVDYEDDDTADPTSLAWTETTTIEEFDFTPLEISVLPTVPSDRPILEFDF
RRGLGYFSNDGADYLHFAAPEEPPLFSIASGLKTEELPATALARKIEYGKHVEVVLVNDM
NEQHPFHMHTHAPWVVGSGAASLSDIQAGNIPLKLQGAMKRDVYTVPPCDTDATGACTNH
GYVVLRFTADNPGVWIMHCHIDWHLDAGLAMILVEGEIELQKAGVGAFANSILSICGTEF
TNSTSSNSTA

Enzyme Prediction     

No EC number prediction in PPTG_11320-t26_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	38	347	1.5e-44	0.9834983498349835
AA1	251	510	3.6e-25	0.39385474860335196

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
274555	ascorbase	5.98e-47	27	537	4	539	L-ascorbate oxidase, plant type. Members of this protein family are the copper-containing enzyme L-ascorbate oxidase (EC 1.10.3.3), also called ascorbase. This family is found in flowering plants, and shows greater sequence similarity to a family of laccases (EC 1.10.3.2) from plants than to other known ascorbate oxidases.
177843	PLN02191	4.54e-43	10	516	9	547	L-ascorbate oxidase
259869	CuRO_1_LCC_like	3.04e-41	25	143	1	120	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.
259926	CuRO_1_Diphenol_Ox	6.17e-41	27	143	3	119	The first cupredoxin domain of fungal laccase, diphenol oxidase. Diphenol oxidase belongs to the laccase family. It catalyzes the initial steps in melanin biosynthesis from diphenols. Melanin is one of the virulence factors of infectious fungi. In the pathogenesis of C. neoformans, melanin pigments have been shown to protect the fungal cells from oxidative and microbicidal activities of host defense systems. Laccase is a blue multicopper oxidase (MCO) which 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. 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	6.23e-41	3	518	7	451	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].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AFY09916.1|AA1	9.11e-227	1	537	1	545
UIZ26488.1|AA1	9.88e-205	8	537	2	537
AFY09915.1|AA1	1.50e-167	8	541	7	570
UIZ26495.1|AA1	6.73e-163	13	536	12	561
AIG55536.1|AA1	8.99e-78	18	525	34	545

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3KW7_A	1.06e-53	57	515	35	472	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]
2XYB_A	1.85e-53	28	523	7	475	CRYSTAL STRUCTURE OF A FULLY FUNCTIONAL LACCASE FROM THE LIGNINOLYTIC FUNGUS PYCNOPORUS CINNABARINUS [Trametes cinnabarina]
5NQ8_A	7.48e-53	4	523	2	496	Crystal structure of laccases from Pycnoporus sanguineus, izoform II [Trametes coccinea],5NQ9_A Crystal structure of laccases from Pycnoporus sanguineus, izoform II, monoclinic [Trametes sanguinea],5NQ9_C Crystal structure of laccases from Pycnoporus sanguineus, izoform II, monoclinic [Trametes sanguinea]
2QT6_A	4.99e-52	28	515	7	468	Chain A, Laccase [Lentinus tigrinus],2QT6_B Chain B, Laccase [Lentinus tigrinus]
1GYC_A	1.88e-51	39	523	18	477	Chain A, LACCASE 2 [Trametes versicolor]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q12717|LAC5_TRAVE	3.38e-54	28	523	30	505	Laccase-5 OS=Trametes versicolor OX=5325 GN=LCC5 PE=2 SV=1
sp|Q99056|LAC5_TRAVI	2.41e-53	28	523	30	505	Laccase-5 OS=Trametes villosa OX=47662 GN=LCC5 PE=3 SV=2
sp|O59896|LAC1_PYCCI	1.42e-51	7	515	4	488	Laccase OS=Pycnoporus cinnabarinus OX=5643 GN=LCC3-1 PE=1 SV=1
sp|Q12718|LAC2_TRAVE	5.34e-51	39	523	38	497	Laccase-2 OS=Trametes versicolor OX=5325 GN=LCC2 PE=1 SV=1
sp|Q02497|LAC1_TRAHI	2.00e-50	7	523	4	498	Laccase OS=Trametes hirsuta OX=5327 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000254	0.999709	CS pos: 20-21. Pr: 0.9786

TMHMM  Annotations     

There is no transmembrane helices in PPTG_11320-t26_1-p1.