CAZyme Information: NEUTE1DRAFT_129073-t26_1-p1

Basic Information

• Species: Neurospora tetrasperma
• Lineage: Ascomycota; Sordariomycetes; ; Sordariaceae; Neurospora; Neurospora tetrasperma
• CAZyme ID: NEUTE1DRAFT_129073-t26_1-p1
• CAZy Family: GH125
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1265	GL891303|CGC12	139214.59	5.3345

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_NtetraspermaFGSC2508	10380	510951	0	10380

• Gene Location: location=GL891303:4765315-4769112(-)

Full Sequence      

MTWHAQLALVLALVCPATAWCSGKSDACSSNPIPLRQFNALNYQANTCNLKWNRGCTSLD
KHGALQQKPPPYSLCNSGHQPAGRVPVDAYTLSLQNNNFAPGSARWTLHGLWPGSVDGTG
GKNQPYGCLNGEDFNETILTTFDGLLNYFWPTNAKFNNTMQCFILSEWMKHGTCAVIPGA
DGTAFRLPQEDYFRTAFVIANEFNESPTLRNQLLEKVKLDDVEPLISTRCVQCAYLATVG
WTGTDVASVPRMSGDCIDQCFECGDFWDTCPPAQLESTVMLNSSNAPREKRDSSSNSNAT
ASFPLLEFAMPAFMSSENSSPWEGTWRSFGAEEGGSGKFEFAQTFTDNVLTVTTDSPYPR
TCTYERRGPKELVLRCGGDHLEDCLVQRLPDIGGLEAAFLACNHTGEPAPASFYAAMDTK
GCGNFLMFRCKASAAGCSFSPDSISASEPKTETKTEPESGFESESKPSPVSHFQPGIAGA
PPALLGSWRSLQVDSDYEEGLAQWNFTSDGQASLRWPNYPSRAVQRYSVSHSDEDPSLVL
LASASGTITTCRFQFQYQPVYSYAVLDCGSAGDNEEDTQNTKWAMGRCNPCSAHCRYSCG
AENDFCGAGSCDPAESVEAASVDALPSLFDNTRATLKDDHDWCTPEDSGCWPTKTAIRKL
EQELDPTVPRLGLRWHSYPDPQPAPVPMGSIDNQSFYGLGNAPQGLKALYYYEDIAEMQR
PCFNQADPPAVYNTASDMCKAAVHQNEYRNWNPFIVVFPLNERHVVAALNFAARHRLCIA
TAGTGHEYNSRNSCPTGGILIRTILLKDKTFMPTWHEDSTLAPAGAFRFGAGSTFAEMHA
FSKDYSRVISSGWCSTVGMVGFHLGGGHGPFAPSMGLGVDNVLEIEVLQVGRNTYGQPVV
HKKIASRNRNPQLFWAMRGGGGSVWGVVLSMTIRAHPVPDGGLSRVYMSQTGTFCPDDSS
KFGYQWLRGMWTRFTAWQLSLNQKVSTQPGFFINTTLYNEKRNLCSVTWEFKFEYFYAGG
QAERDYIRFRDGLKDVLQTDTVWEDNYKSAYDYLVSMPADKFTLVPVNPLPAQHPPSDVA
TGSQNSVLVSRQALKTKFTSTMMDVLDICVKSLKNPDKTSPDVSGYRCGFHYLYTSLTGN
LGSTQPGDTAISPGFRSALMLWNARTLTTQQSNDTVYKLGPNSYFSESSYVMHNWTARYW
GEKAYEQLLGVKKAHDPGNHFWCHHCVGDNPDDAFGEPLGAAAQADFGDQPDAAAQAEFV
EQDKL

Enzyme Prediction     

EC	1.1.3.-:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA7	743	942	2.1e-41	0.3951965065502183

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
238220	RNase_T2	2.88e-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	8.40e-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	9.71e-14	753	888	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	3.16e-12	101	196	26	109	Ribonuclease T2 family.
223354	GlcD	9.77e-10	753	887	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	2.77e-16	753	939	598	775
QKD57322.1|CBM91|GH43_11	2.77e-16	753	939	598	775
UQC87672.1|AA7	5.71e-12	722	939	39	238
UNI23960.1|AA7	2.12e-11	753	953	48	232
QUC19098.1|AA7	4.54e-10	753	947	48	226

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6F72_A	7.39e-20	753	1228	124	559	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	4.03e-13	749	949	35	222	The crystal structure of EncM H138T mutant [Streptomyces maritimus],6FYE_B The crystal structure of EncM H138T mutant [Streptomyces maritimus]
6FYD_A	9.34e-13	749	949	35	222	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	1.63e-12	749	949	35	222	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	2.16e-12	749	949	35	222	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|A0A7L8UYL4|FFSJ_ASPFV	3.47e-24	765	949	135	310	FAD-linked oxidoreductase ffsJ OS=Aspergillus flavipes OX=41900 GN=ffsJ PE=3 SV=1
sp|G4MWA7|OXR2B_MAGO7	4.72e-22	765	1228	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|A0A0E0RTV6|ZEB1_GIBZE	1.32e-21	625	1228	9	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|D4B1Z7|A2478_ARTBC	1.74e-21	753	1228	122	558	Uncharacterized FAD-linked oxidoreductase ARB_02478 OS=Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) OX=663331 GN=ARB_02478 PE=1 SV=1
sp|A2TBU3|EASE_EPIFI	1.50e-20	764	1236	139	579	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
0.000194	0.999780	CS pos: 19-20. Pr: 0.9790

TMHMM  Annotations     

There is no transmembrane helices in NEUTE1DRAFT_129073-t26_1-p1.