CAZyme Information: KAG1702626.1

Basic Information

• Species: Phytophthora capsici
• Lineage: Oomycota; NA; ; Peronosporaceae; Phytophthora; Phytophthora capsici
• CAZyme ID: KAG1702626.1
• CAZy Family: GH72
• CAZyme Description: unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
403		44477.13	7.2097

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_PcapsiciLT1534	28579	763924	5206	23373

• Gene Location: location=JADEVP010000020:724346-725557(-)

Full Sequence      

MNSGRFFVALLSFAFNIATITADNSTVTYDWRVTYVSTACDGVTMTEYGINNDVSTRALI
ELELGQTVQVSVTNELDEMTCLHWHGLQQLGTQEMDGASDITQCGIAPGGSAVYTFTPER
AGTYWWHSHHSTQYAYGLRGPLIVHASADEKQSWEQEIAAEYTLQLADLYHALPGIVPMW
DSVIINSLGRYNCTAAASHGYLECNSDQPLARFKFEAGKKYRLRLINMGALAPFEFSIDG
HEFSVVAADGEYLQPSEEITTLRINAGQRYDIVVEAKATSSSAIGSFWIRATALYGLPWT
AGTAAVAQVFGDLALVMLKVWPLCTTRMMTRRIRRRPTGRRRRPSRSTTSLPSRSQYFRL
YRPTVRSSSSTSVVVSDTSPSTVGTTSTSQPLKNHLSSLSQGV

Enzyme Prediction     

EC	1.10.3.2:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	52	294	1e-70	0.6508379888268156

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
274555	ascorbase	1.12e-44	29	289	4	277	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.
259926	CuRO_1_Diphenol_Ox	3.07e-43	29	145	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.
177843	PLN02191	6.34e-43	17	289	14	300	L-ascorbate oxidase
259869	CuRO_1_LCC_like	2.70e-42	27	145	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.
259923	CuRO_1_MaLCC_like	1.33e-39	24	145	1	122	The first cupredoxin domain of the fungal laccases similar to Ma-LCC from Melanocarpus albomyces. The subfamily of fungal laccases includes Ma-LCC and similar proteins. Ma-LCC is a multicopper oxidase (MCO) from Melanocarpus albomyces. Its crystal structure contains all four coppers at the mono- and trinuclear copper centers. 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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AFY09916.1|AA1	3.08e-129	8	307	9	307
UIZ26488.1|AA1	4.83e-118	8	307	2	298
UIZ26495.1|AA1	1.16e-98	10	304	4	313
AFY09915.1|AA1	9.60e-98	27	318	22	332
AIG56347.1|AA1_2	2.00e-56	23	292	38	312

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1HFU_A	1.52e-43	41	305	7	274	Chain A, LACCASE 1 [Coprinopsis cinerea]
1A65_A	1.55e-43	41	305	7	274	Chain A, Laccase [Coprinopsis cinerea]
1V10_A	3.75e-42	59	291	56	287	Chain A, Laccase [Rigidoporus microporus]
5NQ8_A	9.18e-41	30	302	28	293	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]
3KW7_A	1.01e-40	50	302	26	272	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|A0A067XMP2|PTAK_PESFW	2.67e-44	29	292	67	333	Oxydoreductase ptaK OS=Pestalotiopsis fici (strain W106-1 / CGMCC3.15140) OX=1229662 GN=ptaK PE=2 SV=2
sp|S8FGV1|LAC2_FOMPI	6.29e-44	52	294	52	288	Laccase-2 OS=Fomitopsis pinicola (strain FP-58527) OX=743788 GN=LCC2 PE=1 SV=1
sp|J5JH35|OPS5_BEAB2	3.37e-41	29	291	76	335	Oxidoreductase OpS5 OS=Beauveria bassiana (strain ARSEF 2860) OX=655819 GN=OpS5 PE=1 SV=1
sp|Q12739|LAC2_PLEOS	1.15e-40	59	291	69	294	Laccase-2 OS=Pleurotus ostreatus OX=5322 GN=POX2 PE=1 SV=1
sp|O59896|LAC1_PYCCI	9.02e-40	30	302	28	293	Laccase OS=Pycnoporus cinnabarinus OX=5643 GN=LCC3-1 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000196	0.999756	CS pos: 22-23. Pr: 0.9790

TMHMM  Annotations     

There is no transmembrane helices in KAG1702626.1.