CAZyme Information: I314_04686-t35_1-p1

Basic Information

• Species: Cryptococcus gattii VGIII
• Lineage: Arthropoda; Insecta; ; Eriococcidae; Cryptococcus; Cryptococcus gattii VGIII
• CAZyme ID: I314_04686-t35_1-p1
• CAZy Family: GT90
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
167	KN848900|CGC1	19477.97	4.5600

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_CgattiiCA1873	6782	1296111	148	6634

• Gene Location: location=KN848900:651562-652233(-)

Full Sequence      

MVQTNPRWKDVYTKLWIFNLTSYDRLVYYDADHLVLRSVDSIWEAENSWPESGLAALGSG
DGGHVEDSDYFLAGFFIAIPKKEIMEGPLAEKDYDPVFPEQNLMNKYSSRDGPRPWAPLD
PIIHEKCWQGWVERRLAELFYERLGRMERYWLAKELNGTIPTPDPYG

Enzyme Prediction     

No EC number prediction in I314_04686-t35_1-p1.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
133018	GT8_Glycogenin	9.99e-32	3	156	70	240	Glycogenin belongs the GT 8 family and initiates the biosynthesis of glycogen. Glycogenin initiates the biosynthesis of glycogen by incorporating glucose residues through a self-glucosylation reaction at a Tyr residue, and then acts as substrate for chain elongation by glycogen synthase and branching enzyme. It contains a conserved DxD motif and an N-terminal beta-alpha-beta Rossmann-like fold that are common to the nucleotide-binding domains of most glycosyltransferases. The DxD motif is essential for coordination of the catalytic divalent cation, most commonly Mn2+. Glycogenin can be classified as a retaining glycosyltransferase, based on the relative anomeric stereochemistry of the substrate and product in the reaction catalyzed. It is placed in glycosyltransferase family 8 which includes lipopolysaccharide glucose and galactose transferases and galactinol synthases.
133064	GT8_GNT1	1.43e-06	2	40	71	109	GNT1 is a fungal enzyme that belongs to the GT 8 family. N-acetylglucosaminyltransferase is a fungal enzyme that catalyzes the addition of N-acetyl-D-glucosamine to mannotetraose side chains by an alpha 1-2 linkage during the synthesis of mannan. The N-acetyl-D-glucosamine moiety in mannan plays a role in the attachment of mannan to asparagine residues in proteins. The mannotetraose and its N-acetyl-D-glucosamine derivative side chains of mannan are the principle immunochemical determinants on the cell surface. N-acetylglucosaminyltransferase is a member of glycosyltransferase family 8, which are, based on the relative anomeric stereochemistry of the substrate and product in the reaction catalyzed, retaining glycosyltransferases.
227884	Gnt1	2.76e-06	7	49	152	194	Alpha-N-acetylglucosamine transferase [Cell wall/membrane/envelope biogenesis].
224359	RfaJ	8.25e-06	6	105	79	196	Lipopolysaccharide biosynthesis protein, LPS:glycosyltransferase [Cell wall/membrane/envelope biogenesis].
132996	Glyco_transf_8	8.31e-06	3	94	75	179	Members of glycosyltransferase family 8 (GT-8) are involved in lipopolysaccharide biosynthesis and glycogen synthesis. Members of this family are involved in lipopolysaccharide biosynthesis and glycogen synthesis. GT-8 comprises enzymes with a number of known activities: lipopolysaccharide galactosyltransferase, lipopolysaccharide glucosyltransferase 1, glycogenin glucosyltransferase, and N-acetylglucosaminyltransferase. GT-8 enzymes contains a conserved DXD motif which is essential in the coordination of a catalytic divalent cation, most commonly Mn2+.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ADV21652.1|GT8	2.48e-120	1	167	133	299
KGB78671.1|GT8	3.09e-113	1	167	133	316
AUB24113.1|GT8	1.38e-111	2	167	91	273
AGV14250.1|GT8	1.38e-111	2	167	91	273
AUB24114.1|GT8	5.90e-111	2	167	134	316

PDB Hits     

I314_04686-t35_1-p1 has no PDB hit.

Swiss-Prot Hits     

I314_04686-t35_1-p1 has no Swissprot hit.

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000036	0.000000

TMHMM  Annotations     

There is no transmembrane helices in I314_04686-t35_1-p1.