CAZyme Information: TPX50090.1

Basic Information

• Species: Synchytrium endobioticum
• Lineage: Chytridiomycota; Chytridiomycetes; ; Synchytriaceae; Synchytrium; Synchytrium endobioticum
• CAZyme ID: TPX50090.1
• CAZy Family: GT2
• CAZyme Description: unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
639		68908.93	6.3987

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_SendobioticumMB42	8031	N/A	0	8031

• Gene Location: location=QEAN01000072:10550-13244(+)

Full Sequence      

MSLRLALALALALLVAISCLPLPAAASGPSAASSSQPQAVKDPFSTNEYLGYVNPATVSN
NVRALSLTLTRGALNPDGRTVDFAILVNGMFQPAIVAQLGEVLSVTVVNKLEAATSMHWH
GMFQTGSTDQDGSVSVNQCPIPPGATYTYTFKLTQNGTFWYHAHANAQYGEGARGPLIIK
AADEPADVQDVVIATTDWFHTPATTILSKFLDGKNNPDGVEPKIDSVLINGLGQYNCSTN
STAPTPCPNAKYYTLRLNSQNKYRIRLLNMAAAASFTIDIPGIIPQVTELDGVATQVALA
DEIQLDVAQRVSFYLSPKEQGLPSATYTIKAGIGGDEGASLLAIGYIVIDGNTTQALNME
AGERPRVLYGDGFIRAFGPGTISRAWPVPKSDPLPPAKPTVRYMHEFWFDNDVATNLNLA
FVWMYQATNNNNMWTKRFAGSSWAPDNSTGVTYAINGAQQNNLLSATNPKTFPPQWNAFD
VKGGDIVEITFINHEPEVHPFHLHGHNFHIMGSGMLRSRNETNGTVTQFLPTIAEVDASN
DLMTASGTTSRPIRDVISVPANGYSTVRFVANNPGVWALHCHIEWHLMSGLAVTLIEDQA
ALKNYQHSPGWNDLCAASAAQGVLPRANPPLRRPKTIPL

Enzyme Prediction     

No EC number prediction in TPX50090.1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	84	592	1.3e-84	0.9692737430167597

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
177843	PLN02191	9.51e-53	87	597	47	546	L-ascorbate oxidase
274555	ascorbase	5.35e-50	84	597	22	523	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.
225043	SufI	3.12e-48	87	592	57	443	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].
259923	CuRO_1_MaLCC_like	1.23e-41	60	179	1	121	The first 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. 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.
274556	laccase	2.70e-39	84	614	24	536	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CDS09935.1|AA1_2	8.13e-64	65	618	30	512
BAE61606.1|AA1_2	1.08e-63	52	628	20	531
UDD60384.1|AA1_2	4.55e-63	75	628	35	521
UDD60385.1|AA1_2	5.24e-63	75	628	35	521
QMW43510.1|AA1_2	6.25e-63	75	628	35	521

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6RHH_A	3.93e-58	67	617	9	490	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	4.02e-58	67	617	9	490	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	4.02e-58	67	617	9	490	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	7.28e-58	67	617	9	490	Steccherinum murashkinskyi laccase at 0.95 resolution [Steccherinum murashkinskyi]
5MHW_A	1.07e-57	67	617	28	509	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|A0A067XMP2|PTAK_PESFW	6.63e-60	57	606	59	557	Oxydoreductase ptaK OS=Pestalotiopsis fici (strain W106-1 / CGMCC3.15140) OX=1229662 GN=ptaK PE=2 SV=2
sp|I1RMG9|FET3_GIBZE	8.48e-57	75	618	37	518	Iron transport multicopper oxidase FET3 OS=Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1) OX=229533 GN=FET3 PE=2 SV=1
sp|K7NCS2|FETC_EPIFE	2.23e-56	75	597	35	495	Iron transport multicopper oxidase fetC OS=Epichloe festucae (strain E2368) OX=696363 GN=fetC PE=2 SV=1
sp|Q99055|LAC4_TRAVI	2.29e-56	67	615	30	509	Laccase-4 OS=Trametes villosa OX=47662 GN=LCC4 PE=3 SV=1
sp|Q12719|LAC4_TRAVE	3.09e-55	67	615	30	509	Laccase-4 OS=Trametes versicolor OX=5325 GN=LCC4 PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.001580	0.998413	CS pos: 26-27. Pr: 0.9394

TMHMM  Annotations     

Start	End
5	27