CAZyme Information: SMR51427.1

Basic Information

• Species: Zymoseptoria tritici
• Lineage: Ascomycota; Dothideomycetes; ; Mycosphaerellaceae; Zymoseptoria; Zymoseptoria tritici
• CAZyme ID: SMR51427.1
• CAZy Family: GH18
• CAZyme Description: unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
902		96536.43	4.7379

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_ZtriticiST99CH3D1	11991	1276537	0	11991

• Gene Location: location=LT854276:147949-151371(+)

Full Sequence      

MAPAQEHYDFIIVGGGTAGCLLAHRLSHSAAAPSVLLLEAGTKPSGPYLSAPGHRYTAAF
ARSDLDHGYVSEPEPSLNDRELPYARGKGLGGSSILNFGVYLYGSSEDYDRWADLVDDDD
WAWSSVQESFRTIENYATEGAAAYEHLADPASGRHGTSGQVTVSLPAVLEKSVAPQMASL
LAAGESLCLDPNAGDNIGVSLFPYSYGKSGRCTSAIAHLVDPPKNLEVWIDATVGKLLFD
GTSVIGIRTIDGREALSSKEVILCCGAIDTPRLLLLNGIGPKAELEALDIEVKRDLPGVG
KHLRDHVAGIMCVEVDGSFNDRTTFETDPNSVEEAQALWDRDHTGALSLQHSSLWGGFLK
VPDLANSSEFQDLAPADQEFLTRSKVPHFEFLNNALLWPPGSQLTPENTYLSFTAALMNA
QSEGSVTLRSNNPADKPLLRLNLLSHPYDVLVIREAIRRSWNMIIENPDMRPHVRKTLSG
PVSLSDADIDAYAKAEACPIWHANGTVRMGKEADGGSVDSSGKVYGVQGLRVADLSVCPL
TTNNHTQATAYLVGQKIAEKMAEDIENKAEYLANVKIGTPGQTFTLDFDTGSADLWVWST
ELPASTRNGNHGGNKHSIFDPKKSSTFKESSGSTWQIQYGDGSTASGDVGADVVNLGGLK
VQHQAIELAKTLSTQFASGPGDGLLGLAFGSINAVSPSPAQTVVENMITQSDIPKNTELF
TAYLGSTPPGSSSPSANGAATADATSFYTFGYIDQTALAGQTPAYTPTRKGFGCSPVNLL
RLEIRRSGWVFPTSTDLSSLPAVRLAIGDTLFTINPEELPFQDLGDGTFYGGIQSRGDQT
FDIYGDVFLRSVYAIFDQGNTRFGCTQRASTLSSNGEKYSNGEKYSNGEKYSNGEKYSNG
GK

Enzyme Prediction     

No EC number prediction in SMR51427.1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA3	7	563	1.1e-146	0.9947183098591549

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
225186	BetA	6.34e-88	1	565	1	537	Choline dehydrogenase or related flavoprotein [Lipid transport and metabolism, General function prediction only].
235000	PRK02106	4.12e-87	4	561	2	531	choline dehydrogenase; Validated
133161	Aspergillopepsin_like	1.20e-70	571	864	1	275	Aspergillopepsin_like, aspartic proteases of fungal origin. The members of this family are aspartic proteases of fungal origin, including aspergillopepsin, rhizopuspepsin, endothiapepsin, and rodosporapepsin. The various fungal species in this family may be the most economically important genus of fungi. They may serve as virulence factors or as industrial aids. For example, Aspergillopepsin from A. fumigatus is involved in invasive aspergillosis owing to its elastolytic activity and Aspergillopepsins from the mold A. saitoi are used in fermentation industry. Aspartic proteinases are a group of proteolytic enzymes in which the scissile peptide bond is attacked by a nucleophilic water molecule activated by two aspartic residues in a DT(S)G motif at the active site. They have a similar fold composed of two beta-barrel domains. Between the N-terminal and C-terminal domains, each of which contributes one catalytic aspartic residue, there is an extended active-site cleft capable of interacting with multiple residues of a substrate. Although members of the aspartic protease family of enzymes have very similar three-dimensional structures and catalytic mechanisms, each has unique substrate specificity. The members of this family has an optimal acidic pH (5.5) and cleaves protein substrates with similar specificity to that of porcine pepsin A, preferring hydrophobic residues at P1 and P1' in the cleave site. This family of aspartate proteases is classified by MEROPS as the peptidase family A1 (pepsin A, clan AA).
394983	Asp	3.29e-56	570	864	1	309	Eukaryotic aspartyl protease. Aspartyl (acid) proteases include pepsins, cathepsins, and renins. Two-domain structure, probably arising from ancestral duplication. This family does not include the retroviral nor retrotransposon proteases (pfam00077), which are much smaller and appear to be homologous to a single domain of the eukaryotic asp proteases.
133138	pepsin_like	2.26e-43	571	864	1	280	Pepsin-like aspartic proteases, bilobal enzymes that cleave bonds in peptides at acidic pH. Pepsin-like aspartic proteases are found in mammals, plants, fungi and bacteria. These well known and extensively characterized enzymes include pepsins, chymosin, renin, cathepsins, and fungal aspartic proteases. Several have long been known to be medically (renin, cathepsin D and E, pepsin) or commercially (chymosin) important. Structurally, aspartic proteases are bilobal enzymes, each lobe contributing a catalytic Aspartate residue, with an extended active site cleft localized between the two lobes of the molecule. The N- and C-terminal domains, although structurally related by a 2-fold axis, have only limited sequence homology except the vicinity of the active site. This suggests that the enzymes evolved by an ancient duplication event. Most members of the pepsin family specifically cleave bonds in peptides that are at least six residues in length, with hydrophobic residues in both the P1 and P1' positions. The active site is located at the groove formed by the two lobes, with an extended loop projecting over the cleft to form an 11-residue flap, which encloses substrates and inhibitors in the active site. Specificity is determined by nearest-neighbor hydrophobic residues surrounding the catalytic aspartates, and by three residues in the flap.The enzymes are mostly secreted from cells as inactive proenzymes that activate autocatalytically at acidic pH. This family of aspartate proteases is classified by MEROPS as the peptidase family A1 (pepsin A, clan AA).

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
SMR51427.1|AA3_2	0.0	1	880	1	880
SMQ49497.1|AA3_2	0.0	1	880	1	903
SMY23191.1|AA3_2	0.0	1	850	1	850
SMR50493.1|AA3_2	0.0	1	564	1	564
QRC97674.1|AA3_2	1.44e-264	1	564	1	562

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5OC1_A	1.26e-59	8	564	2	564	Crystal structure of aryl-alcohol oxidase from Pleurotus eryngii in complex with p-anisic acid [Pleurotus eryngii]
3FIM_B	2.41e-59	8	564	3	565	Crystal structure of aryl-alcohol-oxidase from Pleurotus eryingii [Pleurotus eryngii]
4H7U_A	1.86e-54	3	563	36	599	Crystal structure of pyranose dehydrogenase from Agaricus meleagris, wildtype [Leucoagaricus meleagris]
1IZD_A	1.64e-45	567	869	13	323	Crystal structure of Aspergillus oryzae Aspartic Proteinase [Aspergillus oryzae],1IZE_A Crystal structure of Aspergillus oryzae Aspartic proteinase complexed with pepstatin [Aspergillus oryzae]
3C9X_A	1.67e-44	569	868	15	329	Crystal structure of Trichoderma reesei aspartic proteinase [unidentified],3EMY_A Chain A, Trichoderma reesei Aspartic protease [Trichoderma reesei]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q47944|SDH_GLUOY	1.12e-58	8	559	5	525	L-sorbose 1-dehydrogenase OS=Gluconobacter oxydans OX=442 PE=3 SV=1
sp|A4XPI5|BETA_PSEMY	5.20e-57	5	563	2	535	Oxygen-dependent choline dehydrogenase OS=Pseudomonas mendocina (strain ymp) OX=399739 GN=betA PE=3 SV=1
sp|Q6D6D9|BETA_PECAS	6.31e-57	8	561	3	529	Oxygen-dependent choline dehydrogenase OS=Pectobacterium atrosepticum (strain SCRI 1043 / ATCC BAA-672) OX=218491 GN=betA PE=3 SV=1
sp|Q4K4K7|BETA_PSEF5	3.52e-56	4	561	2	533	Oxygen-dependent choline dehydrogenase OS=Pseudomonas fluorescens (strain ATCC BAA-477 / NRRL B-23932 / Pf-5) OX=220664 GN=betA PE=3 SV=1
sp|A5WA97|BETA_PSEP1	6.31e-56	5	561	2	533	Oxygen-dependent choline dehydrogenase OS=Pseudomonas putida (strain ATCC 700007 / DSM 6899 / BCRC 17059 / F1) OX=351746 GN=betA PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000039	0.000007

TMHMM  Annotations     

There is no transmembrane helices in SMR51427.1.