CAZyme Information: SMAC_03856-t26_1-p1

Basic Information

• Species: Sordaria macrospora
• Lineage: Ascomycota; Sordariomycetes; ; Sordariaceae; Sordaria; Sordaria macrospora
• CAZyme ID: SMAC_03856-t26_1-p1
• CAZy Family: GH13
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1200		132028.59	5.2483

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_Smacrosporak-hell	11311	771870	484	10827

• Gene Location: location=NW_003546203:550378-554100(+)

Full Sequence      

MAWHAKLALVLALVYPANAAWCSGKSDACSSNPIPLRQFNELNFHADTCNLKWNLGCTKL
NDHGELQQKPPPYPLCNSGHQPAGLVPVDAYTLSLQNNNFAPGSAKWTLHGLWPGSADGS
GAINQPYGCLHGEEFDETILTTFGGLLNYYWPTNAKFNNTMQCFILSEWMKHGTCAEDYF
RTAFVIANEFNENPALRNQLLGKVKLDDVEPLISTRCVQCAYLATEGWTGTEVASVPRMS
ADCLDQCFECGDFWDTCLPAQLESTVMLNTSNAPRKESGSSSSSNGTASFPLLEFAMPAL
ISSENTSPWEGTWRSFGAEQGGSGKFEFAQTFTDNVLTVTTDSPYPNRCTYARRGPKELV
LRCEGDHLEDCLVQRLPDVGGLEVAFLACNHTGEPAPASFYAAMDTTWCGNFLMFRCKAS
EAGCSFSPDAISASEPKTETKTEPESESKPSPVSHFQPGIAGAPPSLLGSWRSLQVSSDY
EKGLARWDFTADGQASLQWPNYSDRTVQRYSVSHSDEDPSLVLLASTSGTITTCRFEFQY
QPVYSYAVLDCGATKWAMGRCNPCSAHCRYSCGPENDFCGAGSCDPDESVEAVSVDTLPS
LSDNTRTTLKPDWCTPEDPDCWPTQTAIRKLEQELDPTVPRLGVRWHSYPDPQPAPVPSG
SFNDQSFYGLGDTPQGLKALYYYEDIAEMQRPCFNATKNPAEWNTASDICKAAVHQNEYR
NWNPFIVVFPLNERHVVAALNFAVRHRLCISTSGTGHEYNSRNSCPTGGILIRTILLKDK
TFMPTWSEDLTLAPAGAFRFGAGTTFAEMHAFSGNHSRVIASGWCSTVGMVGFHLGGGHG
PFAPSMGLGVDNVLEIEVLQIGRNSHGQSVVHKKIASRTRNPQLFWAMRGGGGSVWGVIL
SMTIRAHAVPDGGLSRVYIYQNGTFCPDSRKYGYQWLPGMWDRFTKWQLGLNQKFKFEYI
YAGGQSEPDYIRFRDELKAVLQNDTVQEDNYASAYDYLLSMPPNKFTLIPTNPLPAPLHP
PSDLATGSQNSVFVSRQALETQFTSTMMDVLGICIDTLQNPDTSSPDTSGPGYRCGFHYL
YTSLTGNLGSTQPGDTAISPGFRSAVMLWNARTLTTQQAQDTVYKLGPHSYFSESSYVMH
NWTARYWGGKGYEQLLAVKRAHDPGNHFWCHHCVGDNPGDATGDLVGDGAKAQDEFVEQN

Enzyme Prediction     

EC	1.1.3.-:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA7	714	967	1.9e-41	0.5109170305676856

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
238220	RNase_T2	1.75e-14	89	199	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	1.28e-13	89	199	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	3.73e-13	724	859	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.
223354	GlcD	1.29e-12	724	911	32	208	FAD/FMN-containing dehydrogenase [Energy production and conversion].
395357	Ribonuclease_T2	4.41e-12	102	183	26	109	Ribonuclease T2 family.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QKD57322.1|GH43_11	1.95e-16	724	910	598	775
QKD57322.1|CBM91|GH43_11	1.95e-16	724	910	598	775
UQC87672.1|AA7	5.33e-12	693	910	39	238
UNI23960.1|AA7	1.85e-10	724	924	48	232
UPK90596.1|AA7	5.18e-10	724	924	20	204

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6F72_A	4.37e-22	724	1185	124	571	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	4.98e-13	703	909	24	211	The crystal structure of EncM H138T mutant [Streptomyces maritimus],6FYE_B The crystal structure of EncM H138T mutant [Streptomyces maritimus]
6FYD_A	1.16e-12	703	909	24	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	2.02e-12	703	909	24	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	2.68e-12	703	909	24	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|A0A7L8UYL4|FFSJ_ASPFV	1.73e-23	736	919	135	309	FAD-linked oxidoreductase ffsJ OS=Aspergillus flavipes OX=41900 GN=ffsJ PE=3 SV=1
sp|D4B1Z7|A2478_ARTBC	6.92e-22	724	1175	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|G2QDQ9|VAO15_MYCTT	2.25e-21	724	1185	124	571	VAO-type flavoprotein oxidase VAO615 OS=Myceliophthora thermophila (strain ATCC 42464 / BCRC 31852 / DSM 1799) OX=573729 GN=MYCTH_2305637 PE=1 SV=1
sp|G4MWA7|OXR2B_MAGO7	3.13e-21	736	1175	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|P0CU32|CHEF_CHAGB	1.10e-20	736	1175	177	594	FAD-linked oxidoreductase cheF OS=Chaetomium globosum (strain ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 / NRRL 1970) OX=306901 GN=cheF PE=2 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000230	0.999747	CS pos: 19-20. Pr: 0.9781

TMHMM  Annotations     

There is no transmembrane helices in SMAC_03856-t26_1-p1.