CAZyme Information: OON08402.1

Basic Information

• Species: Batrachochytrium salamandrivorans
• Lineage: Chytridiomycota; Chytridiomycetes; ; NA; Batrachochytrium; Batrachochytrium salamandrivorans
• CAZyme ID: OON08402.1
• CAZy Family: GT22
• CAZyme Description: unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
562		61758.65	6.5983

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_BsalamandrivoransBS	10186	N/A	51	10135

• Gene Location: location=LYON01000258:18077-20126(+)

Full Sequence      

MFPVFSLLATLVPIAVQAIVQDVTLNLAMYQAAPDGYQTTVYGANNMMEPPIIINKGDLL
SLKVNNNLGLPTAIHCHGLFQKSTPYYDGAAGVTQCPIADQDSFRYDISVPDQHGTYWWH
AHYKAQYVKGLRGPLIIKDPENEPYTADYDEEYIVMLTDWYHAKTSAEILDPFMVSLTGN
EPIPDSGLINGKGRYNCSMATDKTVPCVSNAPLERFNFVAGKRYRLRIINGASMATFNFS
IDGHTLQVIEADGVDTVKTPVDVIRISVAQRYSVIVEAKATPGNYWMRADIDTALYTVYQ
EGVLTPEIRAIISYTGSDADPTSTGPTPQAVMLNPFKLLPVSQIPLSHAVNQSLLFSFAI
VPGPDNITRAYTNIDGHFTDSPYQMPMDTPTLFKAINGNAIESSANVIPVSVGQIIQMTV
YNDDPMEHTFHLHGHTFQVVGTGIQLNFKKNPDAAKVLYPERDTIAIPACRIKANSTGGE
GGMCGGTKGYVTIRFQAKNPGAWLFHCHIEWHMMQGLGITFLTGGTKELKTMKLPPRVID
GCARSGINIKANRFWAAPRIGL

Enzyme Prediction     

No EC number prediction in OON08402.1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	46	517	5.1e-110	0.9497206703910615

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
274555	ascorbase	8.56e-70	33	542	14	538	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.
259953	CuRO_2_MCO_like_1	9.14e-69	153	315	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.
215324	PLN02604	4.63e-66	33	545	37	564	oxidoreductase
274556	laccase	1.82e-62	50	542	34	539	laccase, plant. Members of this protein family include the copper-containing enzyme laccase (EC 1.10.3.2), often several from a single plant species, and additional, uncharacterized, closely related plant proteins termed laccase-like multicopper oxidases. This protein family shows considerable sequence similarity to the L-ascorbate oxidase (EC 1.10.3.3) family. Laccases are enzymes of rather broad specificity, and classification of all proteins scoring about the trusted cutoff of this model as laccases may be appropriate.
225043	SufI	1.02e-60	4	521	9	446	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].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AIG55536.1|AA1	4.55e-100	24	542	44	553
CDS09935.1|AA1_2	5.41e-92	26	562	33	526
AIG56347.1|AA1_2	5.55e-91	24	543	45	555
QRV98312.1|AA1_1	1.43e-85	6	544	9	508
CCA70550.1|AA1_1	1.25e-84	1	521	33	526

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6RHH_A	3.69e-74	25	521	9	467	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]
5MEW_A	3.78e-74	25	521	9	467	The study of the X-ray induced enzymatic reduction of molecular oxygen to water for laccase from Steccherinum murashkinskyi. Second structure of the series with total exposition time 33 min. [Steccherinum murashkinskyi],6RGH_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. First structure of the series with 15 KGy dose. [Steccherinum murashkinskyi],6RGP_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. Second structure of the series with 165 KGy dose. [Steccherinum murashkinskyi]
5MEJ_A	3.78e-74	25	521	9	467	Structural study of the X-ray induced enzymatic reduction of molecular oxygen to water for laccase from Steccherinum murashkinskyi. First structure of the series with 3 min total X-ray exposition time. [Steccherinum murashkinskyi],5MHU_A The study of the X-ray induced enzymatic reduction of molecular oxygen to water for laccase from Steccherinum murashkinskyi.The third structure of the series with total exposition time 63 min. [Steccherinum murashkinskyi],5MHV_A The study of the X-ray induced enzymatic reduction of molecular oxygen to water for laccase from Steccherinum murashkinskyi.The fourth structure of the series with total exposition time 93 min. [Steccherinum murashkinskyi]
5E9N_A	7.56e-74	25	521	9	467	Steccherinum murashkinskyi laccase at 0.95 resolution [Steccherinum murashkinskyi]
5MHW_A	1.19e-73	25	521	28	486	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q02081|LAC4_THACU	7.88e-80	18	510	20	483	Laccase-4 OS=Thanatephorus cucumeris OX=107832 GN=LCC4 PE=1 SV=1
sp|E9R598|FETC_ASPFU	5.16e-78	26	546	28	515	Iron transport multicopper oxidase fetC OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=fetC PE=2 SV=1
sp|Q4PIF8|FER1_USTMA	6.36e-77	34	552	46	564	Iron multicopper oxidase fer1 OS=Ustilago maydis (strain 521 / FGSC 9021) OX=237631 GN=fer1 PE=2 SV=1
sp|Q12718|LAC2_TRAVE	1.23e-72	5	521	6	487	Laccase-2 OS=Trametes versicolor OX=5325 GN=LCC2 PE=1 SV=1
sp|Q12729|LAC1_PLEOS	2.19e-72	55	540	71	511	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
0.000398	0.999588	CS pos: 18-19. Pr: 0.9742

TMHMM  Annotations     

There is no transmembrane helices in OON08402.1.