CAZyme Information: PHPALM_21023-t46_1-p1

Basic Information

• Species: Phytophthora palmivora
• Lineage: Oomycota; NA; ; Peronosporaceae; Phytophthora; Phytophthora palmivora
• CAZyme ID: PHPALM_21023-t46_1-p1
• CAZy Family: GH3
• CAZyme Description: Hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
566		62075.30	4.4664

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_Ppalmivorasbr112.9	28185	N/A	3511	24674

• Gene Location: location=NCKW01011410:761-2536(-)

Full Sequence      

MSRTFHPHLGTPNLFHSTIMRSSYLPVTAVLLLLLQLWPSATNAVSFDWRITAINAAFDG
VSVPTIGINDESSDHAVIDVEIGQEVEVRVTNELDVPTCLHWHGLKQLGTQEMDGTSGIT
QCHIDPNGTAVYRFTPDKVGTFWWHSHHSTQYAYGLRGPLIVRSSANKTLSWENDIAGEF
IVQLADHYHDAPVGAPIWDSMLINNRGRYNCTAAASHGFLDCTEDQPLSKFHFQSGNKYL
LRLINMAALSPIVFSIDDHEFQVVAADGDPLQPSSFINSVMITAGQRYDIVVQAKEPNTS
SQQHNGSFWMRATGLHGIPWTGGNAQMAGDGFNYEGLAIVHYEVDDETEPTSEQSTNATT
VSEFEFTPLVSTVLPTIPSDRVILEFGLSFGLGYFSIDGGEFNNFVVPDEPPLFTIAGGL
TTEELPNSANARKIEYGKHIEVVLVNDMNEQHGTASIDEIRNNTLSGLKLEGAMTRDVYT
VPPCTYDASGACTDVGYLVLRFTADNPGVWILHCHIDWHMDAGLSMIFVEGETELQDKGV
NAFSNSMLSVCGNMEFTNSSSNSTAA

Enzyme Prediction     

EC	1.10.3.2:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	67	524	5.3e-87	0.9608938547486033

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
274555	ascorbase	9.83e-49	47	531	4	524	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	1.42e-45	38	531	36	547	L-ascorbate oxidase
225043	SufI	5.43e-45	77	532	65	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].
215324	PLN02604	6.68e-41	66	531	46	547	oxidoreductase
259869	CuRO_1_LCC_like	6.98e-41	45	163	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AFY09916.1|AA1	3.30e-267	40	561	21	555
UIZ26488.1|AA1	1.76e-236	32	552	4	537
AFY09915.1|AA1	7.22e-183	32	557	9	570
UIZ26495.1|AA1	3.11e-181	28	551	7	561
AIG56347.1|AA1_2	1.56e-69	39	540	36	546

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5Z1X_A	8.90e-60	48	531	7	466	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]
1HFU_A	2.91e-57	87	530	45	468	Chain A, LACCASE 1 [Coprinopsis cinerea]
1A65_A	2.97e-57	87	530	45	468	Chain A, Laccase [Coprinopsis cinerea]
1V10_A	3.03e-56	40	530	19	489	Chain A, Laccase [Rigidoporus microporus]
6RHH_A	3.64e-55	48	530	8	469	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|Q12717|LAC5_TRAVE	1.22e-52	83	530	64	497	Laccase-5 OS=Trametes versicolor OX=5325 GN=LCC5 PE=2 SV=1
sp|Q12729|LAC1_PLEOS	2.43e-52	62	535	52	503	Laccase-1 OS=Pleurotus ostreatus OX=5322 GN=POX1 PE=2 SV=1
sp|Q99056|LAC5_TRAVI	8.61e-52	83	530	64	497	Laccase-5 OS=Trametes villosa OX=47662 GN=LCC5 PE=3 SV=2
sp|Q01679|LAC1_PHLRA	2.00e-51	83	530	62	490	Laccase OS=Phlebia radiata OX=5308 GN=LAC PE=1 SV=2
sp|A0A067XMP2|PTAK_PESFW	4.55e-51	39	537	58	555	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
0.001291	0.998675	CS pos: 44-45. Pr: 0.9648

TMHMM  Annotations     

There is no transmembrane helices in PHPALM_21023-t46_1-p1.