dbCAN-seq: a database of CAZyme sequence and annotation

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CAZyme Information: QRC95219.1

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Basic Information help

Species

Parastagonospora nodorum

Lineage

Ascomycota; Dothideomycetes; ; Phaeosphaeriaceae; Parastagonospora; Parastagonospora nodorum

CAZyme ID

QRC95219.1

CAZy Family

CBM508

CAZyme Description

Integral membrane protein [Source:UniProtKB/TrEMBL;Acc:Q0UZ92]

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
424		48736.04	7.7871

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_PnodorumSN15	17580	321614	132	17448

Gene Location

Full Sequence Download help

Enzyme Prediction help

No EC number prediction in QRC95219.1.

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
GT109	3	411	2.1e-130	0.9708029197080292

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
409190	PGAP4-like_fungal	0.0	4	384	2	374	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	1.40e-45	10	382	3	361	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.
409191	PGAP4	7.17e-24	30	375	25	372	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.
398374	Glyco_transf_54	4.00e-13	68	228	24	186	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.

CAZyme Hits help

Hit ID	E-Value	Query Start	Query End	Hit Start
2.49e-312	1	424	1	424
1.29e-182	4	416	6	417
3.08e-167	1	415	1	419
2.18e-101	14	409	36	433
1.22e-99	26	411	41	436

PDB Hits help

QRC95219.1 has no PDB hit.

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
5.28e-07	69	202	133	276	Alpha-1,3-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase B OS=Danio rerio OX=7955 GN=mgat4bQ9UQ53 PE=2 SV=1
6.90e-07	81	202	139	270	Alpha-1,3-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase A OS=Xenopus laevis OX=8355 GN=mgat4a PE=2 SV=1
1.23e-06	81	197	146	272	Alpha-1,3-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase B OS=Mus musculus OX=10090 GN=Mgat4b PE=2 SV=1
2.12e-06	79	203	137	271	Alpha-1,3-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase A OS=Bos taurus OX=9913 GN=MGAT4A PE=1 SV=1
3.72e-06	81	202	139	270	Alpha-1,3-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase A OS=Xenopus tropicalis OX=8364 GN=mgat4a PE=2 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000338	0.999623	CS pos: 27-28. Pr: 0.9730

TMHMM Annotations download full data without filtering help

Start	End
6	28
246	268
283	302