CAZyme Information: PHYSODRAFT_292877-t26_1-p1

Basic Information

• Species: Phytophthora sojae
• Lineage: Oomycota; NA; ; Peronosporaceae; Phytophthora; Phytophthora sojae
• CAZyme ID: PHYSODRAFT_292877-t26_1-p1
• CAZy Family: AA7
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
573		62346.18	6.2401

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_PsojaeP6497	28142	1094619	1653	26489

• Gene Location: location=JH159151:196937-198687(+)

Full Sequence      

MLPLSSFCSMAPACWAVQPLVAAPNASPRSQEPTRVRETFTTIFSFCNLHPTVDSNCSTS
THFDGDSRHAACSLLCLCSSLAGHPPRLQRCRCCHLRLACTASYDGVSIQSLGINGKPSD
QSVIDVELGQEVEVRVTNELNEPTCLHWHGLKQLGTQEMDGTSGLTQCHIDPTERRCIAS
HPTRLAHSGGTATTSRIVHAPASEQQEWEKDVDGEFIIQMADLYHRPPQPVRMWDNILIN
NRGRYNCTAAAHHNFTECTDNQPLSHFRFKAGNKYLLRLINMAALSPIQFSIDDHMLQVV
AADGEPLQPSKPINSVTLNAAQRYDILVQAKGSPSVGKQQGGKQEDVGSFWMRATGLHGL
PWTRGTAAVAGEGYNYEGLAIVSYEAESDKEPTSQQQMNTTTVSEYDFTPLVPVVLPSTP
SDRAVLQLKMQNGSGYFAIDDGDFNHFTLPSDPPLYSIAAGLKTEQLPASTNARKINYGG
HIEVVLVNAKDEQHPFHMHSHTPWVVDSGVASMDAIRNNTLPALRLVSPMKGDVYTIPPC
TSDGNGGCLDAGYVVMPTTPACGSCTVTSTGIY

Enzyme Prediction     

No EC number prediction in PHYSODRAFT_292877-t26_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	112	518	2.3e-51	0.8603351955307262

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
259868	CuRO_2_LCC_like	4.94e-31	217	384	2	152	Cupredoxin domain 2 of laccase-like multicopper oxidases; including laccase, CueO, spore coat protein A, ascorbate oxidase and similar proteins. Laccase-like multicopper oxidases (MCOs) 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 compounds 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 2 of 3-domain MCOs has lost the ability to bind copper.
274555	ascorbase	2.65e-30	111	509	22	459	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.
215324	PLN02604	1.06e-29	114	540	48	511	oxidoreductase
259947	CuRO_2_MaLCC_like	6.25e-28	226	404	26	165	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.
259953	CuRO_2_MCO_like_1	7.99e-27	216	385	1	163	The second cupredoxin domain of uncharacterized multicopper oxidase. Multicopper Oxidases (MCOs) are multi-domain enzymes that are able to couple oxidation of substrates with reduction of dioxygen to water. MCOs oxidise their substrate by accepting electrons at a mononuclear copper centre and transferring them to a trinuclear copper centre which binds a dioxygen. The dioxygen, following the transfer of four electrons, is reduced to two molecules of water. These MCOs are capable of oxidizing a vast range of substrates, varying from aromatic to inorganic compounds such as metals. This family of MCOs 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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AFY09916.1|AA1	2.70e-239	101	559	36	496
UIZ26488.1|AA1	4.92e-206	104	556	30	485
AFY09915.1|AA1	6.08e-140	101	556	33	513
UIZ26495.1|AA1	8.07e-140	101	556	35	509
AIG56347.1|AA1_2	8.75e-48	105	556	56	506

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1HFU_A	3.71e-29	133	537	45	429	Chain A, LACCASE 1 [Coprinopsis cinerea]
1A65_A	3.75e-29	133	537	45	429	Chain A, Laccase [Coprinopsis cinerea]
2HRG_A	5.88e-26	103	512	16	412	Crystal Structure of Blue Laccase from Trametes trogii complexed with p-methylbenzoate [Coriolopsis trogii],2HRH_A Crystal Structure of Blue Laccase from Trametes trogii [Coriolopsis trogii]
5NQ8_A	1.25e-25	103	512	37	434	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]
3SQR_A	1.33e-25	101	546	78	508	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|A0A067XMP2|PTAK_PESFW	1.29e-30	123	514	96	493	Oxydoreductase ptaK OS=Pestalotiopsis fici (strain W106-1 / CGMCC3.15140) OX=1229662 GN=ptaK PE=2 SV=2
sp|Q12570|LAC1_BOTFU	2.86e-29	101	538	73	484	Laccase-1 OS=Botryotinia fuckeliana OX=40559 GN=lcc1 PE=2 SV=3
sp|Q02081|LAC4_THACU	2.78e-26	105	508	37	441	Laccase-4 OS=Thanatephorus cucumeris OX=107832 GN=LCC4 PE=1 SV=1
sp|Q09920|FIO1_SCHPO	1.44e-25	112	539	49	461	Iron transport multicopper oxidase fio1 OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=fio1 PE=3 SV=1
sp|O59896|LAC1_PYCCI	3.58e-25	103	512	37	434	Laccase OS=Pycnoporus cinnabarinus OX=5643 GN=LCC3-1 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
0.987148	0.012876

TMHMM  Annotations     

There is no transmembrane helices in PHYSODRAFT_292877-t26_1-p1.