dbCAN-seq: a database of CAZyme sequence and annotation

Basic Information help

Species

Phytophthora capsici

Lineage

Oomycota; NA; ; Peronosporaceae; Phytophthora; Phytophthora capsici

CAZyme ID

KAG1691586.1

CAZy Family

CBM48

CAZyme Description

unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1335		151504.54	6.0021

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_PcapsiciLT1534	28579	763924	5206	23373

Gene Location

Enzyme Prediction help

EC	-	-

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
GT41	109	699	2.9e-108	0.5716312056737589

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
226428	Spy	7.77e-91	119	698	64	614	Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones].
404688	Glyco_transf_41	4.12e-64	242	688	2	540	Glycosyl transferase family 41. This family of glycosyltransferases includes O-linked beta-N-acetylglucosamine (O-GlcNAc) transferase, an enzyme which catalyzes the addition of O-GlcNAc to serine and threonine residues. In addition to its function as an O-GlcNAc transferase, human OGT also appears to proteolytically cleave the epigenetic cell-cycle regulator HCF-1.
276809	TPR	1.29e-18	84	185	1	97	Tetratricopeptide repeat. The Tetratricopeptide repeat (TPR) typically contains 34 amino acids and is found in a variety of organisms including bacteria, cyanobacteria, yeast, fungi, plants, and humans. It is present in a variety of proteins including those involved in chaperone, cell-cycle, transcription, and protein transport complexes. The number of TPR motifs varies among proteins. Those containing 5-6 tandem repeats generate a right-handed helical structure with an amphipathic channel that is thought to accommodate an alpha-helix of a target protein. It has been proposed that TPR proteins preferentially interact with WD-40 repeat proteins, but in many instances several TPR-proteins seem to aggregate to multi-protein complexes.
340831	GT4_PimA-like	2.40e-16	986	1329	7	365	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.
276809	TPR	2.17e-15	744	836	5	97	Tetratricopeptide repeat. The Tetratricopeptide repeat (TPR) typically contains 34 amino acids and is found in a variety of organisms including bacteria, cyanobacteria, yeast, fungi, plants, and humans. It is present in a variety of proteins including those involved in chaperone, cell-cycle, transcription, and protein transport complexes. The number of TPR motifs varies among proteins. Those containing 5-6 tandem repeats generate a right-handed helical structure with an amphipathic channel that is thought to accommodate an alpha-helix of a target protein. It has been proposed that TPR proteins preferentially interact with WD-40 repeat proteins, but in many instances several TPR-proteins seem to aggregate to multi-protein complexes.

CAZyme Hits help

Hit ID	E-Value	Query Start	Query End	Hit Start
5.84e-92	3	537	30	559
1.52e-84	327	698	16	370
2.96e-84	327	701	23	380
9.60e-84	234	701	176	617
4.29e-81	234	701	583	1024

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
3.53e-55	174	698	85	559	Structure and topological arrangement of an O-GlcNAc transferase homolog: insight into molecular control of intracellular glycosylation [Xanthomonas campestris pv. campestris str. 8004],2VSN_B Structure and topological arrangement of an O-GlcNAc transferase homolog: insight into molecular control of intracellular glycosylation [Xanthomonas campestris pv. campestris str. 8004]
3.53e-55	174	698	85	559	Xanthomonas campestris putative OGT (XCC0866), complex with UDP- GlcNAc phosphonate analogue [Xanthomonas campestris pv. campestris],2JLB_B Xanthomonas campestris putative OGT (XCC0866), complex with UDP- GlcNAc phosphonate analogue [Xanthomonas campestris pv. campestris],2VSY_A Xanthomonas campestris putative OGT (XCC0866), apostructure [Xanthomonas campestris pv. campestris str. ATCC 33913],2VSY_B Xanthomonas campestris putative OGT (XCC0866), apostructure [Xanthomonas campestris pv. campestris str. ATCC 33913],2XGM_A Substrate and product analogues as human O-GlcNAc transferase inhibitors. [Xanthomonas campestris],2XGM_B Substrate and product analogues as human O-GlcNAc transferase inhibitors. [Xanthomonas campestris],2XGO_A XcOGT in complex with UDP-S-GlcNAc [Xanthomonas campestris],2XGO_B XcOGT in complex with UDP-S-GlcNAc [Xanthomonas campestris],2XGS_A XcOGT in complex with C-UDP [Xanthomonas campestris],2XGS_B XcOGT in complex with C-UDP [Xanthomonas campestris]
9.41e-51	239	698	156	705	Crystal structure of the O-GlcNAc transferase Asn648Tyr mutation [Homo sapiens]
1.56e-50	239	698	150	699	The human O-GlcNAc transferase in complex with a thiol-linked bisubstrate inhibitor [Homo sapiens]
1.58e-50	239	698	151	700	The human O-GlcNAc transferase in complex with a bisubstrate inhibitor [Homo sapiens]

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
2.54e-60	234	698	501	951	Probable UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase SEC OS=Arabidopsis thaliana OX=3702 GN=SEC PE=1 SV=1
1.91e-49	239	698	474	1023	UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit OS=Mus musculus OX=10090 GN=Ogt PE=1 SV=2
7.70e-49	239	698	474	1023	UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit OS=Oryctolagus cuniculus OX=9986 GN=OGT PE=1 SV=2
1.02e-48	239	698	474	1023	UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit OS=Homo sapiens OX=9606 GN=OGT PE=1 SV=3
2.35e-48	239	698	474	1023	UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit OS=Sus scrofa OX=9823 GN=OGT PE=2 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000073	0.000000

TMHMM Annotations help

There is no transmembrane helices in KAG1691586.1.

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