CAZyme Information: H310_04069-t26_2-p1

Basic Information

• Species: Aphanomyces invadans
• Lineage: Oomycota; NA; ; Saprolegniaceae; Aphanomyces; Aphanomyces invadans
• CAZyme ID: H310_04069-t26_2-p1
• CAZy Family: GH3
• CAZyme Description: hypothetical protein, variant

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1282		142252.20	6.4521

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AinvadansNJM9701	15416	N/A	168	15248

• Gene Location: location=KI913957:1345515-1349737(+)

Full Sequence      

MAACSLTPCTLAIVLLILFTWLNIEAVGYTYPSTAVNHFQVIAALEEYTLGQKATDEGRI
DDAIAHYQQSIQAYAKFGPSYNNMGILLHKRGNNDEAKRSHEIAAEVSLEEGDWETFASA
HNNLGYLVRLGHAKSYEKTLLAVHHFDLALQVTPPNCTVGVYVSALYNKGSALYGIGQLD
QAQQLLRHVLTLDPSHGSAHLDMGNIYFHQGHLDKALYHQHLLVQLGTTIREVVGALNNQ
GQFLKEIGYVKDALVSHTQALHLQPTDGNTLLNVITARRQLCLWDDADDWHGRLLELTSA
SLHASTLDKRLANLPALLPYDATLMAISDEMKRDIAVSNSLQWEQSSPYFPLKASAASAA
PLTKLNIGYFGYDFRNHPMGQLTIGALEHHNHSRIHLHAYAYGPNDLSTWRNRSEAACDV
FRDLFEASDVDIAAQIHADGIHIAVDLMAHTRGARVGISGLKPAPILVNYLGYPGTMGSS
FTDYAIVDRFVVPPMVAASTFTEKLVYLPHTYQVNMYEWSVDTVAKHTFGDRWLFVFCNF
NTINKMEPVAFGVWMAILRRVPHGVLWLLEPSRVDAGVVRTFRTEAAARGVNPDRLIFAS
RLPHDQHLTRLRNAHLFLDSIIYTAHTTASDMIWAHLPIVTLWGSTFASRVAGSLMDTAL
GSTLWTTHSIKEYEDLAVRLATTDRATLNSFRFTLAQRAAVSPLFDSRRTTFHLEHAYAC
MASLGSGRLHIIVDPRDYNALQRPTLQDMVQRTLALHENGDFEAATLGYARILAVEPSHP
DALHLFGLARYQQHNYGDALDYMLASLQVAKNVGFFHGNLGQVYHALHDYASAAHEFATA
LALDPNQPQVFLNYMTLLQATKQQNVLVQVFGEFGEKLAGALPAASQWDLQFEVAYALVG
QGELQKAMDCLAAIDAMTPPVDILVRARYNSAAILSRLGQHDQANYVSMKTVRLEHEAQQ
VHANLLKFHGEDGHRPRLVIYCYEYGQGWWGEWGPYSTETGVGGSEEAVIYMSRELVAVG
YRVEIFGNPPEAMTDSYGVHWFPHTWFDPDEPSDVFIAWRYHISTALASRASAVFVWLHD
MVNEASFTPSYVDTIDGIFCLSQAHAAGFAPHAMVKIISTGNGLVPSAFASHGANSPTHF
VYGSSPNRGLETVLESWGDIRRRIPNATLHVYYGFTQAFVRFAQPSDAWRQRMDILLQQD
GITYYGLVDHDTLAKGYASAGFYLYPTTYFETSCVSIMKAMANGAIPITSKRGALHEVVA
SFDLGPQEALEGAMSTPLLPTT

Enzyme Prediction     

EC	-	-

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT41	173	722	8.2e-102	0.64822695035461

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
226428	Spy	4.97e-92	114	723	57	616	Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones].
404688	Glyco_transf_41	1.17e-64	281	711	1	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	3.86e-12	118	217	1	89	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	1.67e-11	996	1274	7	327	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	5.67e-11	165	261	3	96	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     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AIG56498.1|GT41	1.01e-152	30	560	26	559
ALF56607.1|GT41	5.82e-85	364	734	16	386
QLA82603.1|GT41	1.45e-82	241	721	261	723
VFU09485.1|GT41	3.58e-82	278	764	306	778
QNP61365.1|GT41	4.22e-82	361	721	328	685

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2VSN_A	2.19e-53	175	655	35	495	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]
2JLB_A	2.19e-53	175	655	35	495	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]
6Q4M_A	9.48e-48	281	721	158	705	Crystal structure of the O-GlcNAc transferase Asn648Tyr mutation [Homo sapiens]
5NPR_A	1.58e-47	281	721	152	699	The human O-GlcNAc transferase in complex with a thiol-linked bisubstrate inhibitor [Homo sapiens]
5NPS_A	1.60e-47	281	721	153	700	The human O-GlcNAc transferase in complex with a bisubstrate inhibitor [Homo sapiens]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q9M8Y0|SEC_ARATH	6.93e-63	281	724	508	954	Probable UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase SEC OS=Arabidopsis thaliana OX=3702 GN=SEC PE=1 SV=1
sp|Q8CGY8|OGT1_MOUSE	1.83e-46	281	721	476	1023	UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit OS=Mus musculus OX=10090 GN=Ogt PE=1 SV=2
sp|P81436|OGT1_RABIT	5.58e-46	281	721	476	1023	UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit OS=Oryctolagus cuniculus OX=9986 GN=OGT PE=1 SV=2
sp|O15294|OGT1_HUMAN	7.36e-46	281	721	476	1023	UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit OS=Homo sapiens OX=9606 GN=OGT PE=1 SV=3
sp|Q27HV0|OGT1_PIG	1.70e-45	281	721	476	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

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000253	0.999743	CS pos: 26-27. Pr: 0.9758

TMHMM  Annotations     

Start	End
2	24