CAZyme Information: Bcin06g07580.1:RNA-p1

Basic Information

• Species: Botrytis cinerea
• Lineage: Ascomycota; Leotiomycetes; ; Sclerotiniaceae; Botrytis; Botrytis cinerea
• CAZyme ID: Bcin06g07580.1:RNA-p1
• CAZy Family: GH17
• CAZyme Description: unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
460		50733.80	5.1597

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_BcinereaB05-10	12073	332648	366	11707

• Gene Location: location=bcin_chr_6:2670293-2671837(+)

Full Sequence      

MPSFVQLSQLKEILTPTCKILTDPNDLNFAEYLKRWTDIDLKTPGAIVLPTSEIDCQNIV
TWASKYSIPFVTKSGGHSAWSTIGSDGIIIDLSLYKAIEVYAESGTAIIKGSILSKEVAV
TLADAGFFTALGNGNTVGAIPYFLGGGCSITSSITGFGSDQIISARVITADGKLLNVTDD
TYPDLLYAIRGAGQHFGLVTQLVIKIHPLKNLGNDDGVIWVGSFVFPLDRASEVTSVMKN
LMNNDRYATAGLMMIMAPPPARNPCLVIAARYTGNPDDAALAYKNIYDLEPLIANGAPVP
IQHASDRGEALAAKGGFKQFGIVGLDQFDEEAFLQTIAVWTEMIFQCPDAINTAFNFQWD
SRPVKRPDIESAMCLHDIRYWQNNFIWHTESKNRSKVDEFNDRSIAIMRGNDDSNFVDFQ
NGTRIGPIERRFRGNERITRLKALKREWDPRGVFTSELLN

Enzyme Prediction     

EC	1.1.3.-:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA7	35	262	1.3e-44	0.4890829694323144

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
396238	FAD_binding_4	3.19e-22	44	178	1	139	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	1.96e-18	19	454	10	450	FAD/FMN-containing dehydrogenase [Energy production and conversion].
178402	PLN02805	5.98e-07	44	209	134	307	D-lactate dehydrogenase [cytochrome]
171497	PRK12436	1.86e-04	31	182	23	171	UDP-N-acetylmuramate dehydrogenase.
273751	FAD_lactone_ox	0.004	34	212	5	184	sugar 1,4-lactone oxidases. This model represents a family of at least two different sugar 1,4 lactone oxidases, both involved in synthesizing ascorbic acid or a derivative. These include L-gulonolactone oxidase (EC 1.1.3.8) from rat and D-arabinono-1,4-lactone oxidase (EC 1.1.3.37) from Saccharomyces cerevisiae. Members are proposed to have the cofactor FAD covalently bound at a site specified by Prosite motif PS00862; OX2_COVAL_FAD; 1.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CBX96933.1|AA7|CBM18	1.94e-16	44	208	213	381
QRW22693.1|AA7	3.19e-16	41	208	58	228
VBB80456.1|AA7	5.29e-16	60	248	27	214
CCD53507.1|AA7|CBM18	1.00e-14	8	205	41	242
ATZ50223.1|AA7|CBM18	1.00e-14	8	205	41	242

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2BVF_A	6.83e-20	24	325	19	313	Crystal structure of 6-hydoxy-D-nicotine oxidase from Arthrobacter nicotinovorans. Crystal Form 3 (P1) [Paenarthrobacter nicotinovorans],2BVF_B Crystal structure of 6-hydoxy-D-nicotine oxidase from Arthrobacter nicotinovorans. Crystal Form 3 (P1) [Paenarthrobacter nicotinovorans],2BVG_A Crystal structure of 6-hydoxy-D-nicotine oxidase from Arthrobacter nicotinovorans. Crystal Form 1 (P21) [Paenarthrobacter nicotinovorans],2BVG_B Crystal structure of 6-hydoxy-D-nicotine oxidase from Arthrobacter nicotinovorans. Crystal Form 1 (P21) [Paenarthrobacter nicotinovorans],2BVG_C Crystal structure of 6-hydoxy-D-nicotine oxidase from Arthrobacter nicotinovorans. Crystal Form 1 (P21) [Paenarthrobacter nicotinovorans],2BVG_D Crystal structure of 6-hydoxy-D-nicotine oxidase from Arthrobacter nicotinovorans. Crystal Form 1 (P21) [Paenarthrobacter nicotinovorans],2BVH_A Crystal structure of 6-hydoxy-D-nicotine oxidase from Arthrobacter nicotinovorans. Crystal Form 2 (P21) [Paenarthrobacter nicotinovorans],2BVH_B Crystal structure of 6-hydoxy-D-nicotine oxidase from Arthrobacter nicotinovorans. Crystal Form 2 (P21) [Paenarthrobacter nicotinovorans],2BVH_C Crystal structure of 6-hydoxy-D-nicotine oxidase from Arthrobacter nicotinovorans. Crystal Form 2 (P21) [Paenarthrobacter nicotinovorans],2BVH_D Crystal structure of 6-hydoxy-D-nicotine oxidase from Arthrobacter nicotinovorans. Crystal Form 2 (P21) [Paenarthrobacter nicotinovorans]
6FYE_A	1.26e-19	24	313	25	310	The crystal structure of EncM H138T mutant [Streptomyces maritimus],6FYE_B The crystal structure of EncM H138T mutant [Streptomyces maritimus]
6FYD_A	3.04e-19	24	313	25	310	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	4.08e-19	24	313	25	310	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	4.08e-19	24	313	25	310	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|Q0CF74|AZPB3_ASPTN	8.94e-35	14	454	35	474	FAD-linked oxidoreductase ATEG_07660 OS=Aspergillus terreus (strain NIH 2624 / FGSC A1156) OX=341663 GN=ATEG_07660 PE=1 SV=1
sp|G4N285|OXR1_MAGO7	3.53e-32	29	454	63	496	FAD-linked oxidoreductase OXR1 OS=Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) OX=242507 GN=OXR1 PE=1 SV=1
sp|A0A2V5HCN7|PYVE_ASPV1	5.17e-30	7	454	1	443	FAD-linked oxidoreductase pyvE OS=Aspergillus violaceofuscus (strain CBS 115571) OX=1450538 GN=pyvE PE=3 SV=1
sp|G9N4A7|VIRF_HYPVG	2.93e-28	24	454	9	444	FAD-linked oxidoreductase virF (Fragment) OS=Hypocrea virens (strain Gv29-8 / FGSC 10586) OX=413071 GN=virF PE=3 SV=1
sp|G3XMD0|AZAL_ASPNA	1.99e-26	14	237	31	249	FAD-linked oxidoreductase azaL OS=Aspergillus niger (strain ATCC 1015 / CBS 113.46 / FGSC A1144 / LSHB Ac4 / NCTC 3858a / NRRL 328 / USDA 3528.7) OX=380704 GN=azaL PE=2 SV=2

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000064	0.000000

TMHMM  Annotations     

There is no transmembrane helices in Bcin06g07580.1:RNA-p1.