CAZyme Information: PHYSODRAFT_320491-t26_1-p1

Basic Information

• Species: Phytophthora sojae
• Lineage: Oomycota; NA; ; Peronosporaceae; Phytophthora; Phytophthora sojae
• CAZyme ID: PHYSODRAFT_320491-t26_1-p1
• CAZy Family: GH1
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
523	JH159151|CGC13	56560.79	4.1810

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=JH159151:225860-227533(-)

Full Sequence      

MDIARYFIAALLGLSLLTAISSADTSIVAYDWHVTYISSACDGVHMTSYGINGNSSNYAL
IEVELGQTVQVTVTNELDEPTCLHWHGLQQLGTQEMDGTSDITQCGIAAGGTAVYTTVVH
APADQQQSWEQEVAAEYTLQLADLYHASPGVVPMWDSIVINDLGRYNCTAAASHGYSECN
SDQPLSRFKFEAGNKYRLRLINMAALAPIEFSIDGHELSVVAADSEYIEPSEQITTLRIN
AGQRYDIIVEAKAASGSAIGSFWVRATGLYGLPWTAGTATVAGDGFNYQGHGDIYNEDDD
VDDPTSSDWTETTTINEFEFTPLEVSVLPTVPSDRPVLEFDFRRGLGYFSIDGADYLHFA
APEEPPLFTIAAGLKTEELPATTLARKIEYGKHIEVHPFHMHTHSPWVVGSGTASLSDIQ
AGNLNLKLSGAMKRDVYTIPPCDTDDSGACTNHGYVMLRFTADNPGVWIIHCHIDWHLDA
GLAMVLVEGEDELQAAGVGAFANSILSVCGTEFTNSTSSNSTA

Enzyme Prediction     

No EC number prediction in PHYSODRAFT_320491-t26_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	118	483	2.6e-47	0.6983240223463687

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
274555	ascorbase	9.88e-48	27	510	1	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	1.63e-43	14	499	10	562	L-ascorbate oxidase
215324	PLN02604	2.49e-42	7	510	4	562	oxidoreductase
225043	SufI	8.86e-39	5	490	2	450	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].
259868	CuRO_2_LCC_like	7.19e-34	137	278	1	143	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AFY09916.1|AA1	1.04e-218	20	510	20	545
UIZ26488.1|AA1	2.26e-196	14	510	5	537
AFY09915.1|AA1	2.54e-153	16	514	10	570
UIZ26495.1|AA1	1.08e-151	17	509	13	561
AIG55536.1|AA1	9.05e-62	21	498	34	545

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1V10_A	7.39e-41	17	488	15	489	Chain A, Laccase [Rigidoporus microporus]
5Z1X_A	1.30e-40	31	496	7	473	Crystal Structure of Laccase from Cerrena sp. RSD1 [Cerrena],5Z1X_B Crystal Structure of Laccase from Cerrena sp. RSD1 [Cerrena],5Z22_A Crystal Structure of Laccase from Cerrena sp. RSD1 [Cerrena]
5MHW_A	6.92e-40	14	496	11	496	The study of the X-ray induced enzymatic reduction of molecular oxygen to water for laccase from Steccherinum murashkinskyi.The fifth structure of the series with total exposition time 123 min. [Steccherinum murashkinskyi],5MHX_A The study of the X-ray induced enzymatic reduction of molecular oxygen to water for laccase from Steccherinum murashkinskyi.The sixth structure of the series with total exposition time 153 min. [Steccherinum murashkinskyi],5MHY_A The study of the X-ray induced enzymatic reduction of molecular oxygen to water for laccase from Steccherinum murashkinskyi.The seventh structure of the series with total exposition time 183 min. [Steccherinum murashkinskyi],5MHZ_A The study of the X-ray induced enzymatic reduction of molecular oxygen to water for laccase from Steccherinum murashkinskyi.The 8-th structure of the series with total exposition time 213 min. [Steccherinum murashkinskyi],5MI1_A The study of the X-ray induced enzymatic reduction of molecular oxygen to water for laccase from Steccherinum murashkinskyi.The 9-th structure of the series with total exposition time 243 min. [Steccherinum murashkinskyi],5MI2_A The study of the X-ray induced enzymatic reduction of molecular oxygen to water for laccase from Steccherinum murashkinskyi.The 10-th structure of the series with total exposition time 273 min. [Steccherinum murashkinskyi],5MIA_A The study of the X-ray induced enzymatic reduction of molecular oxygen to water for laccase from Steccherinum murashkinskyi.The 11-th structure of the series with total exposition time 303 min. [Steccherinum murashkinskyi],5MIB_A The study of the X-ray induced enzymatic reduction of molecular oxygen to water for laccase from Steccherinum murashkinskyi.The 12-th structure of the series with total exposition time 333 min. [Steccherinum murashkinskyi],5MIC_A The study of the X-ray induced enzymatic reduction of molecular oxygen to water for laccase from Steccherinum murashkinskyi.The 13-th structure of the series with total exposition time 363 min. [Steccherinum murashkinskyi],5MID_A The study of the X-ray induced enzymatic reduction of molecular oxygen to water for laccase from Steccherinum murashkinskyi.The 14-th structure of the series with total exposition time 393 min. [Steccherinum murashkinskyi],5MIE_A The study of the X-ray induced enzymatic reduction of molecular oxygen to water for laccase from Steccherinum murashkinskyi.The 15-th structure of the series with total exposition time 423 min. [Steccherinum murashkinskyi],5MIG_A The study of the X-ray induced enzymatic reduction of molecular oxygen to water for laccase from Steccherinum murashkinskyi.The 16-th structure of the series with total exposition time 453 min. The crystal was quick refreezing before this data collection. [Steccherinum murashkinskyi]
5NQ8_A	8.94e-40	17	496	15	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]
6RHH_A	9.19e-40	31	496	8	477	Single crystal serial study of the X-ray induced enzymatic reduction of molecular oxygen to water for laccase from Steccherinum murashkinskyi at sub-atomic resolution. Third structure of the series with 315 KGy dose. [Steccherinum murashkinskyi],6RHI_A Single crystal serial study of the X-ray induced enzymatic reduction of molecular oxygen to water for laccase from Steccherinum murashkinskyi at sub-atomic resolution. Ninth structure of the series with 1215 KGy dose. [Steccherinum murashkinskyi],6RHO_A Single crystal serial study of the X-ray induced enzymatic reduction of molecular oxygen to water for laccase from Steccherinum murashkinskyi at sub-atomic resolution. Twentieth structure of the series with 4065 KGy dose. [Steccherinum murashkinskyi],6RHP_A Single crystal serial study of the X-ray induced enzymatic reduction of molecular oxygen to water for laccase from Steccherinum murashkinskyi at sub-atomic resolution. Twenty first structure of the series with 4415 KGy dose (collected after refreezing). [Steccherinum murashkinskyi],6RHR_A Single crystal serial study of the inhibition of laccases from Steccherinum murashkinskyi by chloride anions at sub-atomic resolution. First structure of the series with 15 KGy dose. [Steccherinum murashkinskyi],6RHU_A Single crystal serial study of the inhibition of laccases from Steccherinum murashkinskyi by chloride anions at sub-atomic resolution. Second structure of the series with 165 KGy dose. [Steccherinum murashkinskyi],6RHX_A Single crystal serial study of the inhibition of laccases from Steccherinum murashkinskyi by chloride anions at sub-atomic resolution. Third structure of the series with 315 KGy dose. [Steccherinum murashkinskyi],6RI0_A Single crystal serial study of the inhibition of laccases from Steccherinum murashkinskyi by chloride anions at sub-atomic resolution. Ninth structure of the series with 1215 KGy dose. [Steccherinum murashkinskyi],6RI2_A Single crystal serial study of the inhibition of laccases from Steccherinum murashkinskyi by chloride anions at sub-atomic resolution. Twentieth structure of the series with 4065 KGy dose. [Steccherinum murashkinskyi],6RI4_A Single crystal serial study of the inhibition of laccases from Steccherinum murashkinskyi by fluoride anions at sub-atomic resolution. First structure of the series with 13 KGy dose. [Steccherinum murashkinskyi],6RI6_A Single crystal serial study of the inhibition of laccases from Steccherinum murashkinskyi by fluoride anions at sub-atomic resolution. Second structure of the series with 400 KGy dose. [Steccherinum murashkinskyi],6RI8_A Single crystal serial study of the inhibition of laccases from Steccherinum murashkinskyi by fluoride anions at sub-atomic resolution. Third structure of the series with 800 KGy dose. [Steccherinum murashkinskyi],6RII_A Single crystal serial study of the inhibition of laccases from Steccherinum murashkinskyi by fluoride anions at sub-atomic resolution. Fourth structure of the series with 1200 KGy dose. [Steccherinum murashkinskyi],6RIK_A Single crystal serial study of the inhibition of laccases from Steccherinum murashkinskyi by fluoride anions at sub-atomic resolution. Thirteenth structure of the series with 5200 KGy dose. [Steccherinum murashkinskyi],6RIL_A Single crystal serial study of the inhibition of laccases from Steccherinum murashkinskyi by fluoride anions at sub-atomic resolution. Fourteenth structure of the series with 5600 KGy dose (data was collected after refreezing). [Steccherinum murashkinskyi]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q12739|LAC2_PLEOS	3.56e-41	60	495	69	507	Laccase-2 OS=Pleurotus ostreatus OX=5322 GN=POX2 PE=1 SV=1
sp|A0A067XMP2|PTAK_PESFW	1.32e-40	29	493	66	553	Oxydoreductase ptaK OS=Pestalotiopsis fici (strain W106-1 / CGMCC3.15140) OX=1229662 GN=ptaK PE=2 SV=2
sp|Q12570|LAC1_BOTFU	6.51e-40	40	503	75	540	Laccase-1 OS=Botryotinia fuckeliana OX=40559 GN=lcc1 PE=2 SV=3
sp|O59896|LAC1_PYCCI	3.35e-39	17	495	15	495	Laccase OS=Pycnoporus cinnabarinus OX=5643 GN=LCC3-1 PE=1 SV=1
sp|Q12729|LAC1_PLEOS	1.89e-38	52	495	57	505	Laccase-1 OS=Pleurotus ostreatus OX=5322 GN=POX1 PE=2 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000198	0.999772	CS pos: 23-24. Pr: 0.8650

TMHMM  Annotations     

Start	End
7	29