CAZyme Information: ATCC64974_63440-t41_1-p1

Basic Information

• Species: Aspergillus niger
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus niger
• CAZyme ID: ATCC64974_63440-t41_1-p1
• CAZy Family: GT69
• CAZyme Description: unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
245		28218.74	4.8933

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AnigerN402ATCC64974	11187	N/A	0	11187

• Gene Location: location=OGUI01000010.1:105612-106741(+)

Full Sequence      

MCVGIASVARKGVNYLQGAVGSVLEGLTAAEREDLYLIVFIAHSDPAEHPAYMEPWLHNL
ADKVLVYDPDLVDIEHIRSLETPEAKKFAREKGLFDHTYLLKACEALNTSYTVILEDDVV
ALDGWYHRTKQALDVAERKAEEEGVDQWFVFPQTRIGDLVSWYERNKVGYVDMLTERYAD
QNGEVRWALTPSVLQHVGSRSSKTNSLGKHRERLTMSERIWNFRFEENDPGELRLEHRLQ
DEEVR

Enzyme Prediction     

No EC number prediction in ATCC64974_63440-t41_1-p1.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
409190	PGAP4-like_fungal	9.49e-102	1	205	75	375	uncharacterized fungal proteins similar to Post-GPI attachment to proteins factor 4. This subfamily contains uncharacterized fungal proteins with similarity to animal post-GPI attachment to proteins factor 4 (PGAP4), also known as post-GPI attachment to proteins GalNAc transferase 4 or transmembrane protein 246 (TMEM246). PGAP4 has been shown to be a Golgi-resident GPI-GalNAc transferase. Many eukaryotic proteins are anchored to the cell surface through glycolipid glycosylphosphatidylinositol (GPI). GPIs have a conserved core but exhibit diverse N-acetylgalactosamine (GalNAc) modifications. PGAP4 knockout cells lose GPI-GalNAc structures. PGAP4 is most likely involved in the initial steps of GPI-GalNAc biosynthesis. In contrast to other Golgi glycotransferases, it contains three transmembrane domains. Proteins from this subfamily contain the putative catalytic site of PGAP4 and may have similar activities.
409189	PGAP4-like	4.96e-25	1	205	71	364	Post-GPI attachment to proteins factor 4 and similar proteins. This family includes post-GPI attachment to proteins factor 4 (PGAP4), also known as post-GPI attachment to proteins GalNAc transferase 4 or transmembrane protein 246 (TMEM246). PGAP4 has been shown to be a Golgi-resident GPI-GalNAc transferase. Many eukaryotic proteins are anchored to the cell surface through glycolipid glycosylphosphatidylinositol (GPI). GPIs have a conserved core but exhibit diverse N-acetylgalactosamine (GalNAc) modifications. PGAP4 knockout cells lose GPI-GalNAc structures. PGAP4 is most likely involved in the initial steps of GPI-GalNAc biosynthesis. In contrast to other Golgi glycotransferases, it contains three transmembrane domains. This family also includes uncharacterized fungal proteins with similarity to PGAP4.
398374	Glyco_transf_54	7.85e-09	1	207	35	273	N-Acetylglucosaminyltransferase-IV (GnT-IV) conserved region. The complex-type of oligosaccharides are synthesized through elongation by glycosyltransferases after trimming of the precursor oligosaccharides transferred to proteins in the endoplasmic reticulum. N-Acetylglucosaminyltransferases (GnTs) take part in the formation of branches in the biosynthesis of complex-type sugar chains. In vertebrates, six GnTs, designated as GnT-I to -VI, which catalyze the transfer of GlcNAc to the core mannose residues of Asn-linked sugar chains, have been identified. GnT-IV (EC:2.4.1.145) catalyzes the transfer of GlcNAc from UDP-GlcNAc to the GlcNAc1-2Man1-3 arm of core oligosaccharide [Gn2(22)core oligosaccharide] and forms GlcNAc1-4(GlcNAc1-2)Man1-3 structure on the core oligosaccharide (Gn3(2,4,2)core oligosaccharide). In some members the conserved region occupies all but the very for N-terminal, where there is a signal sequence on all members. For other members the conserved region does not occupy the entire protein but is still to the N-terminus of the protein.
409191	PGAP4	0.004	87	127	162	200	Post-GPI attachment to proteins factor 4. Post-GPI attachment to proteins factor 4 (PGAP4), also known as post-GPI attachment to proteins GalNAc transferase 4 or transmembrane protein 246 (TMEM246), has been shown to be a Golgi-resident GPI-GalNAc transferase. Many eukaryotic proteins are anchored to the cell surface through glycolipid glycosylphosphatidylinositol (GPI). GPIs have a conserved core but exhibit diverse N-acetylgalactosamine (GalNAc) modifications. PGAP4 knockout cells lose GPI-GalNAc structures. PGAP4 is most likely involved in the initial steps of GPI-GalNAc biosynthesis. In contrast to other Golgi glycotransferases (GTs), it contains three transmembrane domains. Structural modeling suggests that PGAP4 adopts a GT-A fold split by an insertion of tandem transmembrane domains.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BCS15754.1|GT109	1.03e-141	1	242	95	434
BCS04158.1|GT109	1.03e-141	1	242	95	434
CAK49131.1|GT109	6.81e-108	1	184	152	440
UDD59417.1|GT109	5.85e-95	1	240	1	338
QMW30601.1|GT109	3.70e-93	1	240	91	428

PDB Hits     

ATCC64974_63440-t41_1-p1 has no PDB hit.

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q6GMK0|MGT4B_DANRE	2.88e-07	4	213	146	384	Alpha-1,3-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase B OS=Danio rerio OX=7955 GN=mgat4bQ9UQ53 PE=2 SV=1
sp|Q812F8|MGT4B_MOUSE	1.25e-06	4	213	147	385	Alpha-1,3-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase B OS=Mus musculus OX=10090 GN=Mgat4b PE=2 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000049	0.000000

TMHMM  Annotations     

There is no transmembrane helices in ATCC64974_63440-t41_1-p1.