CAZyme Information: EEQ28605.1

Basic Information

• Species: Microsporum canis
• Lineage: Ascomycota; Eurotiomycetes; ; Arthrodermataceae; Microsporum; Microsporum canis
• CAZyme ID: EEQ28605.1
• CAZy Family: AA7
• CAZyme Description: FG-GAP repeat domain-containing protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
999	DS995710|CGC1	109101.75	6.0350

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_McanisCBS113480	8847	554155	82	8765

• Gene Location: location=DS995710:146396-150035(-)

Full Sequence      

MHVPWSLNVVLALSGLIVCQTLPKDPSGPDDPPAFPGHGELGTEGNWLGIRLFKYSGCDS
GQQKKINDAYWDMYKILDTPGVGREVDFNSAAALEFFGPPALNRNEQKGILHVLDRLSTN
WPSFANPFAHWIHVRCDDPSKLCTHPEDPCQPNNRRILDLATAETVAYSANRDSESGYPR
INFCPIFFNNAEYPYLQNAVAKGVLLREPFKYDLNSYHKNKATIFLHEMCHLDLAVGSPD
KVPHIRDISIVYEVLGSEGEKYETGIAYGPRLTKILARMDLETGKWVQRNADNFALFATA
KHVQKALGNIYPHYPVVAERAEIPPDLPPPQLTTFTRTSNGAVFDYSPGVNGTYCGPGDV
DLTKRRLISDSTYPAAYRKEKALKIEALWPSSELKGKNLKILPLGGTIAPSSSPKKYSIT
FGYGSSHGNGYRGELLGKLSGNFVDMIGSVKSGNMADNDNEGHSGAVIDGIASHTGAYSQ
KPNIVLLHAGTNDMNNPTSPNTAPARLGSLIDQILRACPDAVVLVALIIPATNADTNGRI
NLYNDEVASIVKSRFRSGKHVLLVDMNSMLTDSHLGDGLHPNDEGYSVMADAWFRHIKIA
EGLGWIKTASNTKPREECPRLPTWIEQGQIANGAGLGGDTPNIVACGVSSVHSSNCVCFD
RVTNTTYNFDQGSPPDCPNFFRTHAVRFADLNGDGRDEYLYVDSRGAVTAFQNLGWKYVN
GTTGTVTWWPKGKIAAGVGTLNWQIHFADINGDGRADYLSVEPDGSVKMWLNVLDDPSDI
SKITWVQQGTIATGIGKPGVGVRFADINGDGRAEYLYVDPVGAVTAYLNAGFTYGNNKDG
TVVWIPQGLIATGVGPGRREDIIFTDINGDGRADYLWTGERGSVKLWQNLGGPDNGPNAA
KVTWWERGLIASGSTTYSNEIVFGDVTGDGRADYLWPDLKTSAVKARQKDGITSVDIYRE
NTMLIVLYYIVVYMQMVQLTGSLQQVKQSDTSLEDNSIV

Enzyme Prediction     

No EC number prediction in EEQ28605.1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
CE3	418	597	4.4e-50	0.9536082474226805

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
238871	XynB_like	3.47e-53	457	597	14	157	SGNH_hydrolase subfamily, similar to Ruminococcus flavefaciens XynB. Most likely a secreted hydrolase with xylanase activity. SGNH hydrolases are a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the Ser-His-Asp(Glu) triad found in other serine hydrolases.
404371	Lipase_GDSL_2	2.02e-20	418	586	5	174	GDSL-like Lipase/Acylhydrolase family. This family of presumed lipases and related enzymes are similar to pfam00657.
238141	SGNH_hydrolase	3.34e-17	418	596	7	187	SGNH_hydrolase, or GDSL_hydrolase, is a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the typical Ser-His-Asp(Glu) triad from other serine hydrolases, but may lack the carboxlic acid.
199914	M35_deuterolysin_like	8.58e-15	57	299	1	167	Peptidase M35 domain of deuterolysins and related proteins. This family M35 Zn2+-metallopeptidase extracellular domain is found in fungal deutrolysins (acid metalloproteinase, neutral proteinase II), including some well-characterized metallopeptidase domains in Aspergillus oryzae (NpII), Aspergillus fumigatus (MEP20), Penicillium roqueforti (protease II) and Emericella nidulans (PepJ peptidase). The neutral proteinase II from Aspergillus oryzae (NpII) unfolds reversibly upon incubation at higher temperatures, and loss in activity is mainly due to autoproteolysis. MEP20 is encoded by the mepB gene, which appears to be associated with the cytoplasmic degradation of small peptides. PepJ peptidase is a thermostable enzyme released under carbon starvation. Most members of this family contain a unique zinc-binding motif (the aspzincin motif), defined by the HExxH + D motif where an aspartic acid is the third zinc ligand and is found in a GTXDXXYG or similar motif C-terminal to the His zinc ligands. The aspzincin motif is poorly conserved in one subgroup, that includes Asp f2, a major allergen from Aspergillus fumigatus. This subgroup in addition lacks the key conserved Tyr residue which acts as a proton donor during catalysis, and no protease activity has been detected to date for Asp f2.
239945	SGNH_hydrolase_like_4	2.09e-09	418	592	9	178	Members of the SGNH-hydrolase superfamily, a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the Ser-His-Asp(Glu) triad from other serine hydrolases, but may lack the carboxlic acid.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QKX54758.1|CE3	8.61e-113	399	935	21	498
UQC87654.1|CE0	3.32e-93	398	946	312	824
AQZ64416.1|CE3	1.87e-91	397	946	263	769
UQI47280.1|CE3	5.96e-91	399	935	57	501
QSY50603.1|CE3	1.58e-89	399	935	144	588

PDB Hits     

EEQ28605.1 has no PDB hit.

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|P15329|GUNX_ACETH	5.90e-07	479	614	23	150	Putative endoglucanase X (Fragment) OS=Acetivibrio thermocellus OX=1515 GN=celX PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000248	0.999738	CS pos: 21-22. Pr: 0.7160

TMHMM  Annotations     

There is no transmembrane helices in EEQ28605.1.