CAZyme Information: KAG6610992.1

Basic Information

• Species: Phytophthora cinnamomi
• Lineage: Oomycota; NA; ; Peronosporaceae; Phytophthora; Phytophthora cinnamomi
• CAZyme ID: KAG6610992.1
• CAZy Family: GH30
• CAZyme Description: Multicopper oxidase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
395	JAFJYM010000050|CGC4	42923.14	4.5441

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_PcinnamomiGKB4	19981	N/A	0	19981

• Gene Location: location=JAFJYM010000050:1064249-1065510(+)

Full Sequence      

MGPGRLTAATAVVFLALQLSQASADVVTYDWRLTPIMTAFDGVRLQTLGVNGKPSHEAVI
DVQLGQEVQVRVTNELSESTCLHWYGMKQLGTQEMDGMSGFTQCAIEPNNSATYHYTPDK
AGTFWWHSHHGTQYAYDGGHLPRTAAAGPVLWDTISINNLGRYNCTAAASHNLADCDAHQ
PLSTFDFVSGRKYLLRLINMAAMGTFEFSMDDHEFQVIAADAEPVVPTKLLNSIIVNVGQ
RYDIIVQAKKDTAGVRSFWMRAIGLTGYPWTAPTVDTGTAGFNDEGLAIVRYDSSSNSEP
TTQKAKETVTIGEFDFIPEDPVVLPSKPDDRTYMRSGINTTIGTGIVSIDGGEFYTLEVP
DEPPLLSIASGVSTADLPITANARAIEYGDHVEVC

Enzyme Prediction     

No EC number prediction in KAG6610992.1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	146	306	7.6e-29	0.44871794871794873
AA1	24	135	8.9e-28	0.3557692307692308

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
259947	CuRO_2_MaLCC_like	3.95e-35	125	305	9	162	The second 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. Laccase is composed of three cupredoxin domains 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 2 of 3-domain MCOs has lost the ability to bind copper.
259869	CuRO_1_LCC_like	4.56e-34	27	138	1	112	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	3.13e-31	29	138	3	111	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.
259927	CuRO_1_tcLCC2_insect_like	3.17e-30	41	138	1	97	The first cupredoxin domain of insect laccases similar to laccase 2 in Tribolium castaneum. This multicopper oxidase (MCO) family includes the majority of insect laccases. One member of the family is laccase 2 from Tribolium castaneum. Laccase 2 is required for beetle cuticle tanning. Laccase (polyphenol oxidase EC 1.10.3.2) is a blue multi-copper enzyme that catalyzes the oxidation of a variety of organic substrates coupled to the reduction of molecular oxygen to water. It displays broad substrate specificity, catalyzing the oxidation of a wide variety of aromatic - notably phenolic and inorganic substances. Laccase 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, plants and insects. 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.
274555	ascorbase	1.35e-29	26	302	1	308	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AFY09916.1|AA1	1.04e-138	9	394	8	421
UIZ26488.1|AA1	1.16e-130	12	394	2	413
AFY09915.1|AA1	9.83e-117	15	394	10	441
UIZ26495.1|AA1	9.34e-114	10	394	7	437
AIG55536.1|AA1	1.16e-43	25	394	39	437

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3V9E_A	1.64e-33	41	302	82	359	Structure of the L499M mutant of the laccase from B.aclada [Botrytis aclada]
3SQR_A	1.64e-33	41	302	82	359	Crystal structure of laccase from Botrytis aclada at 1.67 A resolution [Botrytis aclada],4X4K_A Structure of laccase from Botrytis aclada with full copper content [Botrytis aclada]
1HFU_A	2.64e-32	33	376	11	366	Chain A, LACCASE 1 [Coprinopsis cinerea]
1A65_A	2.66e-32	33	376	11	366	Chain A, Laccase [Coprinopsis cinerea]
3KW7_A	1.13e-30	65	394	41	382	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|Q96WM9|LAC2_BOTFU	4.56e-33	41	302	83	360	Laccase-2 OS=Botryotinia fuckeliana OX=40559 GN=lcc2 PE=2 SV=1
sp|Q12570|LAC1_BOTFU	2.55e-32	41	340	77	383	Laccase-1 OS=Botryotinia fuckeliana OX=40559 GN=lcc1 PE=2 SV=3
sp|Q99056|LAC5_TRAVI	2.59e-32	65	375	64	387	Laccase-5 OS=Trametes villosa OX=47662 GN=LCC5 PE=3 SV=2
sp|Q12717|LAC5_TRAVE	3.20e-31	65	375	64	387	Laccase-5 OS=Trametes versicolor OX=5325 GN=LCC5 PE=2 SV=1
sp|A0A067XMP2|PTAK_PESFW	1.25e-30	28	298	66	359	Oxydoreductase ptaK OS=Pestalotiopsis fici (strain W106-1 / CGMCC3.15140) OX=1229662 GN=ptaK PE=2 SV=2

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000207	0.999747	CS pos: 24-25. Pr: 0.9592

TMHMM  Annotations     

There is no transmembrane helices in KAG6610992.1.