CAZyme Information: NEUDI_163849T0-p1

Basic Information

• Species: Neurospora discreta
• Lineage: Ascomycota; Sordariomycetes; ; Sordariaceae; Neurospora; Neurospora discreta
• CAZyme ID: NEUDI_163849T0-p1
• CAZy Family: GH17
• CAZyme Description: unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1266	NdisFGSC8579_SC012|CGC6	139450.89	4.9546

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_NdiscretaFGSC8579	10345	510953	397	9948

• Gene Location: location=NdisFGSC8579_SC012:782875-786675(-)

Full Sequence      

MVWHAQLALVLALVSPATAWCSGKSDACSSNPIPLRQFNELNFHADTCNLKWNLGCTNLD
KHGELQQKPPPYSLCNSGHQPAGLVPVDAYTLALQTNNFAPGSAKWTLHGLWPGSVDGTG
GKNQPYGCLNGQEFDETILTTFGGLLDYFWPTNAKFNNTMQCFILSEWMKHGTCAVISGA
DGTAFRLSQEDYFRTAFVFANEFNENPALRNQLLGEVKLDDVEPLISTRCVQCAYLATVG
WTGTDMASVPRMSGDCIDQCFECGDFWDICPPAQLESTVMLNSSNAPRKESDSSSNNNAT
ASFPLLEFAMPAFMSSENTSPWEGTWRSFGAEQGGSGKFEFAQTFTDNVLTVTTDSPYPQ
TCTYERRGPMELALRCGDDHLEGCLVQRLPDIGGLEAAFLACNHTGEPAPASFYAAMDME
GCGNFLMFRCKVSAADCSFSPDAISVSKPKTQTNTEPETESESESNPKPSLVSHFQPGIA
GAPPALLGSWRSLQVSANYESGLAQWNFTADGQASLRWPNYPSRAVQRYSVSHSDEDPSL
VLLASPSGTITTCRFQFQYQPVYSYAVLDCGAALDNEESTQNTKWAMGRCNPCSGHCRYS
CGPENDFCGAGSCDLAETVEAASVDALPSLSDNTRATLKDHHDWCTPEDSDCWPTKTAIR
KLEQELDPTVPRLGLRWESFKDPQPAPVPLGSINNQSFYGLGDAPQGVRALYYYEDIAEM
QRPCFNQADSYAVWNSASDMCKAAVHQNEYRNWNPFIVVFPLNERHVIAALKFAARHRLC
IATSGTGHEYNSRNSCPTGGILIRTILLKDKAFMPTWPEDSTLAPAGAFRFGAGATFAEM
HAFSKDYSRVIASGWCSTVGMVGFHLGGGHGPFAPSMGLGVDNVLEIEVLQVGSNIYGQP
VVHKKIASRSRNPQLFWAMRGGGGSVWGVVLSMTIRAHAVPDGGLSHVYIYQTGTFCPDS
SKFGYQWLRGMWTRFTAWQLSLNQKVSTQPGFFINTDKYNETRDLCSVTWEFKFEYFYAG
GKEERDYKRFRDGLKDVLQNETVYEANYKSVYDYLVSMPADKFALNPVNPLPARSPPSDA
ATGSQNSVFVSRQALETKFTSTMMDVLDICVKSLENPDDTSPDVKGYRCGFHYLYTSLTG
NLGSTQPSDTAISPGFRSALMLWNARTLTTQQSNDTVYKLGPNSYFSESSYVMHNWTARY
WGEKAYEQLLVVKKAHDPGNHFWCHHCVGDNPDDAFGEPLGAAAQPDFGDQPDAATQAEF
VKHEEL

Enzyme Prediction     

EC	1.1.3.-:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA7	745	946	4.6e-41	0.39956331877729256

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
238220	RNase_T2	1.09e-15	88	212	2	123	Ribonuclease T2 (RNase T2) is a widespread family of secreted RNases found in every organism examined thus far. This family includes RNase Rh, RNase MC1, RNase LE, and self-incompatibility RNases (S-RNases). Plant T2 RNases are expressed during leaf senescence in order to scavenge phosphate from ribonucleotides. They are also expressed in response to wounding or pathogen invasion. S-RNases are thought to prevent self-fertilization by acting as selective cytotoxins of "self" pollen.
238512	RNase_T2_euk	1.42e-14	88	212	12	124	Ribonuclease T2 (RNase T2) is a widespread family of secreted RNases found in every organism examined thus far. This family includes RNase Rh, RNase MC1, RNase LE, and self-incompatibility RNases (S-RNases). Plant T2 RNases are expressed during leaf senescence in order to scavenge phosphate from ribonucleotides. They are also expressed in response to wounding or pathogen invasion. S-RNases are thought to prevent self-fertilization by acting as selective cytotoxins of "self" pollen. Generally, RNases have two distinct binding sites: the primary site (B1 site) and the subsite (B2 site), for nucleotides located at the 5'- and 3'- terminal ends of the sessil bond, respectively. This CD includes the eukaryotic RNase T2 family members.
396238	FAD_binding_4	2.76e-14	755	890	1	129	FAD binding domain. This family consists of various enzymes that use FAD as a co-factor, most of the enzymes are similar to oxygen oxidoreductase. One of the enzymes Vanillyl-alcohol oxidase (VAO) has a solved structure, the alignment includes the FAD binding site, called the PP-loop, between residues 99-110. The FAD molecule is covalently bound in the known structure, however the residue that links to the FAD is not in the alignment. VAO catalyzes the oxidation of a wide variety of substrates, ranging form aromatic amines to 4-alkylphenols. Other members of this family include D-lactate dehydrogenase, this enzyme catalyzes the conversion of D-lactate to pyruvate using FAD as a co-factor; mitomycin radical oxidase, this enzyme oxidizes the reduced form of mitomycins and is involved in mitomycin resistance. This family includes MurB an UDP-N-acetylenolpyruvoylglucosamine reductase enzyme EC:1.1.1.158. This enzyme is involved in the biosynthesis of peptidoglycan.
395357	Ribonuclease_T2	3.58e-12	101	196	26	109	Ribonuclease T2 family.
223354	GlcD	4.63e-10	755	889	32	159	FAD/FMN-containing dehydrogenase [Energy production and conversion].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QKD57322.1|GH43_11	4.13e-17	755	941	598	775
QKD57322.1|CBM91|GH43_11	4.13e-17	755	941	598	775
UQC87672.1|AA7	3.27e-12	724	941	39	238
UNI23960.1|AA7	3.71e-11	755	955	48	232
UPK90596.1|AA7	2.39e-10	755	955	20	204

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6F72_A	1.82e-20	755	938	124	297	Crystal structure of VAO-type flavoprotein MtVAO615 at pH 7.5 from Myceliophthora thermophila C1 [Thermothelomyces thermophilus ATCC 42464],6F73_A Crystal structure of VAO-type flavoprotein MtVAO615 at pH 5.0 from Myceliophthora thermophila C1 [Thermothelomyces thermophilus ATCC 42464],6F73_B Crystal structure of VAO-type flavoprotein MtVAO615 at pH 5.0 from Myceliophthora thermophila C1 [Thermothelomyces thermophilus ATCC 42464]
6FYE_A	5.64e-14	733	940	23	211	The crystal structure of EncM H138T mutant [Streptomyces maritimus],6FYE_B The crystal structure of EncM H138T mutant [Streptomyces maritimus]
6FYD_A	1.31e-13	733	940	23	211	The crystal structure of EncM T139V mutant [Streptomyces maritimus],6FYD_B The crystal structure of EncM T139V mutant [Streptomyces maritimus],6FYD_C The crystal structure of EncM T139V mutant [Streptomyces maritimus],6FYD_D The crystal structure of EncM T139V mutant [Streptomyces maritimus]
6FYF_A	2.30e-13	733	940	23	211	The crystal structure of EncM V135M mutant [Streptomyces maritimus],6FYF_B The crystal structure of EncM V135M mutant [Streptomyces maritimus],6FYF_C The crystal structure of EncM V135M mutant [Streptomyces maritimus],6FYF_D The crystal structure of EncM V135M mutant [Streptomyces maritimus]
6FYG_A	3.04e-13	733	940	23	211	The crystal structure of EncM V135T mutant [Streptomyces maritimus],6FYG_B The crystal structure of EncM V135T mutant [Streptomyces maritimus],6FYG_C The crystal structure of EncM V135T mutant [Streptomyces maritimus],6FYG_D The crystal structure of EncM V135T mutant [Streptomyces maritimus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|G4MWA7|OXR2B_MAGO7	1.20e-23	767	1229	144	562	FAD-linked oxidoreductase OXR2 OS=Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) OX=242507 GN=OXR2 PE=2 SV=1
sp|A0A7L8UYL4|FFSJ_ASPFV	1.42e-23	767	950	135	309	FAD-linked oxidoreductase ffsJ OS=Aspergillus flavipes OX=41900 GN=ffsJ PE=3 SV=1
sp|A0A0E0RTV6|ZEB1_GIBZE	4.25e-22	645	1229	29	548	FAD-linked oxidoreductase ZEB1 OS=Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1) OX=229533 GN=ZEB1 PE=2 SV=2
sp|L0E159|MALF_MALAU	6.45e-22	645	939	27	302	FAD-linked oxidoreductase malF OS=Malbranchea aurantiaca OX=78605 GN=malF PE=1 SV=1
sp|A2TBU3|EASE_EPIFI	2.12e-21	766	1246	139	591	FAD-linked oxidoreductase easE OS=Epichloe festucae var. lolii OX=73839 GN=easE PE=2 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000201	0.999767	CS pos: 19-20. Pr: 0.9786

TMHMM  Annotations     

There is no transmembrane helices in NEUDI_163849T0-p1.