CAZyme Information: EEQ28669.1

Basic Information

• Species: Microsporum canis
• Lineage: Ascomycota; Eurotiomycetes; ; Arthrodermataceae; Microsporum; Microsporum canis
• CAZyme ID: EEQ28669.1
• CAZy Family: GT90
• CAZyme Description: conserved hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
474		52684.66	6.5551

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=DS995702:166061-167485(+)

Full Sequence      

MPLILDSTSSHPKIQSSPMAKDYNKPFLPAIVVLNRRYLITDNGSAAKVGAAAFAASVVQ
AFVERGIFLGMILYHRDEDIVDPYISSEVFSSISTVTISFNFHMDPNKVANALLSCIRIL
NAANPMEGTPMLYYQTDTLMEYHPRHIPLCVTHHGPFFGSFATIFSKEAAALAFGSMEKA
EHLERQQSKGIEIIKSRENAFVLQHSQLQGNYLASRGVTALRELCPPIELLTETEETKDE
LPENITEWFNFDGVVMFTAVARLDYFKNIDLLVDAAILLCVQGIPLRVFIAGGEQPDSKE
HRALMNKVPPQYQHLFLMVPKVSRSALYNLFAVARHTGIFICPSRYETLGITPLEAALNG
VTTVISNSSVVEASRFYPEKFRFNANPEDLSKLIVKLSGPRGTLAHSGDLIRLHIGKSIQ
GSKFRSDLLDAWSDFSVQYLSTLVDEVQPVHPSLCLETPQELGIGIKERIRVVA

Enzyme Prediction     

No EC number prediction in EEQ28669.1.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
340831	GT4_PimA-like	1.15e-15	143	367	102	298	phosphatidyl-myo-inositol mannosyltransferase. This family is most closely related to the GT4 family of glycosyltransferases and named after PimA in Propionibacterium freudenreichii, which is involved in the biosynthesis of phosphatidyl-myo-inositol mannosides (PIM) which are early precursors in the biosynthesis of lipomannans (LM) and lipoarabinomannans (LAM), and catalyzes the addition of a mannosyl residue from GDP-D-mannose (GDP-Man) to the position 2 of the carrier lipid phosphatidyl-myo-inositol (PI) to generate a phosphatidyl-myo-inositol bearing an alpha-1,2-linked mannose residue (PIM1). Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in certain bacteria and archaea.
395425	Glycos_transf_1	2.86e-15	260	397	8	141	Glycosyl transferases group 1. Mutations in this domain of PIGA lead to disease (Paroxysmal Nocturnal haemoglobinuria). Members of this family transfer activated sugars to a variety of substrates, including glycogen, Fructose-6-phosphate and lipopolysaccharides. Members of this family transfer UDP, ADP, GDP or CMP linked sugars. The eukaryotic glycogen synthases may be distant members of this family.
223515	RfaB	9.25e-13	35	397	1	339	Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis].
340830	GT4_sucrose_synthase	1.74e-11	259	367	225	333	sucrose-phosphate synthase and similar proteins. This family is most closely related to the GT4 family of glycosyltransferases. The sucrose-phosphate synthases in this family may be unique to plants and photosynthetic bacteria. This enzyme catalyzes the synthesis of sucrose 6-phosphate from fructose 6-phosphate and uridine 5'-diphosphate-glucose, a key regulatory step of sucrose metabolism. The activity of this enzyme is regulated by phosphorylation and moderated by the concentration of various metabolites and light.
340816	Glycosyltransferase_GTB-type	1.19e-10	260	371	116	222	glycosyltransferase family 1 and related proteins with GTB topology. Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. The structures of the formed glycoconjugates are extremely diverse, reflecting a wide range of biological functions. The members of this family share a common GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QRD94581.1|GT4	5.56e-122	57	438	2	379
QMW33721.1|GT4	5.56e-122	57	438	2	379
QMW45767.1|GT4	5.56e-122	57	438	2	379
UDD62545.1|GT0	5.56e-122	57	438	2	379
APA07210.1|GT4	6.72e-104	28	464	2	434

PDB Hits     

EEQ28669.1 has no PDB hit.

Swiss-Prot Hits     

EEQ28669.1 has no Swissprot hit.

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000048	0.000000

TMHMM  Annotations     

There is no transmembrane helices in EEQ28669.1.