CAZyme Information: RQM13688.1

Basic Information

• Species: Peronospora effusa
• Lineage: Oomycota; NA; ; Peronosporaceae; Peronospora; Peronospora effusa
• CAZyme ID: RQM13688.1
• CAZy Family: GH5
• CAZyme Description: Protein O-GlcNAc transferase [Source:UniProtKB/TrEMBL;Acc:A0A425C9M5]

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
888		100384.53	6.1131

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_PeffusaR13	8603	N/A	0	8603

• Gene Location: location=QKXF01000242:14506-17761(-)

Full Sequence      

MILVQTELLVEVQVDKNLVNTEHSTRVCILIQIVYMPMDVALENEEIEPYESCFEQSLGH
AKFHVAGLVPGTSYSVTGKLENNGNIMALSSRIFSVGSVLLPGVDSRVSIADALKAGTKL
HDAWDRANALKIYRYVLDVFPDYGPAQHLLGVALYQDGKQEEALPYLYRAVQSNQSEENF
HNSLGMCLKSLGRVKEAIEHYRRALEINPVLLQASVNLGDAMQAIGRWEDAMDEYSKVAK
VPMSVLDTQLDIEKAENVVKDATGKRCELIHFTDGWYQADRCLNKALKRWADEPAFHNDR
GNLFANAGQFEMALDEYQRSSDFGLLAGTLNLAETLEALGRTQRSIDLYNQILDSEIVDR
FYPRTRIMVMKATVLPRVLPATQIEIDLYRDRFDREVKTLLQNLNSLGETEVDPTRISLS
TAITLTAHNRNNRELKAAMGLLYWQLLYQRQIMREDFVASYGLVPLPFTQQSESIKKPEI
GPRRLRVGFVSRYMFNSAVGLYMSELVPMFNQDKAKQVKKGGKEVEAINETIVGLPKDVR
IAREAIRAWDVDVLIYPELGMDKTTYFVSLARLAPVQAVWWGNADTSGVPTMDNYLTSEF
EHSSVNSHYSEVVYCFKGTGIYHRLPILPKNTSNRDKIRRGIEERFDIPADFHFYLAIES
IIHIHPDFDVAVAEILDKDKKAHFFLLSTSSRKAWKTQLQARMESAGVIADRLHFLVDVD
QKQEPKLMQAADAVLSSLHLTRPRASLQAFAAGAPVVTFPNELWASRITYGFYQQMGIND
LIATSLDEYVALAIKLATNAAFHEKMVQLIQQNRSKLSEDKQAVKEWEQFFDFAGRQIFS
SGGRPTYISSSSYGWCPLQRLKGIVDGNQVEDWSQVVNAEGKLWSANI

Enzyme Prediction     

No EC number prediction in RQM13688.1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT41	274	831	1.8e-60	0.5645390070921986

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
226428	Spy	1.66e-24	467	827	245	598	Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones].
276809	TPR	1.00e-17	146	240	3	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.
276809	TPR	3.13e-14	111	206	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.
223533	TPR	6.37e-11	100	319	49	261	Tetratricopeptide (TPR) repeat [General function prediction only].
411346	social_mot_Tgl	1.32e-10	150	238	37	126	social motility TPR repeat lipoprotein Tgl. Social motility in delta-proteobacterial species such as Myxococcus xanthus depends on a type VI pilus, which in turn depends on assembly of the PilQ secretin complex. Tgl, a tetratricopeptide repeat (TPR) outer membrane lipoprotein, is required for PilQ assembly.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
UIZ20641.1|GT41	0.0	1	888	47	957
BAZ61948.1|GT41	6.43e-59	288	834	365	884
BAZ15802.1|GT41	6.43e-59	288	834	365	884
QTA91146.1|GT41	8.92e-53	367	837	375	866
BBO66743.1|GT41	1.80e-50	369	832	458	899

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5HGV_A	4.93e-07	645	848	512	714	Structure of an O-GlcNAc transferase point mutant, D554N in complex with peptide [Homo sapiens],5HGV_C Structure of an O-GlcNAc transferase point mutant, D554N in complex with peptide [Homo sapiens]
5NPR_A	4.93e-07	645	848	510	712	The human O-GlcNAc transferase in complex with a thiol-linked bisubstrate inhibitor [Homo sapiens]
5NPS_A	4.93e-07	645	848	511	713	The human O-GlcNAc transferase in complex with a bisubstrate inhibitor [Homo sapiens]
3PE3_A	4.94e-07	645	848	516	718	Chain A, UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit [Homo sapiens],3PE3_B Chain B, UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit [Homo sapiens],3PE3_C Chain C, UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit [Homo sapiens],3PE3_D Chain D, UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit [Homo sapiens],3PE4_A Structure of human O-GlcNAc transferase and its complex with a peptide substrate [Homo sapiens],3PE4_C Structure of human O-GlcNAc transferase and its complex with a peptide substrate [Homo sapiens],3TAX_A A Neutral Diphosphate Mimic Crosslinks the Active Site of Human O-GlcNAc Transferase [Homo sapiens],3TAX_C A Neutral Diphosphate Mimic Crosslinks the Active Site of Human O-GlcNAc Transferase [Homo sapiens],4AY5_A Human O-GlcNAc transferase (OGT) in complex with UDP and glycopeptide [Homo sapiens],4AY5_B Human O-GlcNAc transferase (OGT) in complex with UDP and glycopeptide [Homo sapiens],4AY5_C Human O-GlcNAc transferase (OGT) in complex with UDP and glycopeptide [Homo sapiens],4AY5_D Human O-GlcNAc transferase (OGT) in complex with UDP and glycopeptide [Homo sapiens],4AY6_A Human O-GlcNAc transferase (OGT) in complex with UDP-5SGlcNAc and substrate peptide [Homo sapiens],4AY6_B Human O-GlcNAc transferase (OGT) in complex with UDP-5SGlcNAc and substrate peptide [Homo sapiens],4AY6_C Human O-GlcNAc transferase (OGT) in complex with UDP-5SGlcNAc and substrate peptide [Homo sapiens],4AY6_D Human O-GlcNAc transferase (OGT) in complex with UDP-5SGlcNAc and substrate peptide [Homo sapiens],4CDR_A Human O-GlcNAc transferase in complex with a bisubstrate inhibitor, Goblin1 [Homo sapiens],4CDR_B Human O-GlcNAc transferase in complex with a bisubstrate inhibitor, Goblin1 [Homo sapiens],4CDR_C Human O-GlcNAc transferase in complex with a bisubstrate inhibitor, Goblin1 [Homo sapiens],4CDR_D Human O-GlcNAc transferase in complex with a bisubstrate inhibitor, Goblin1 [Homo sapiens],4GYW_A Crystal structure of human O-GlcNAc Transferase in complex with UDP and a glycopeptide [Homo sapiens],4GYW_C Crystal structure of human O-GlcNAc Transferase in complex with UDP and a glycopeptide [Homo sapiens],4GYY_A Crystal structure of human O-GlcNAc Transferase with UDP-5SGlcNAc and a peptide substrate [Homo sapiens],4GYY_C Crystal structure of human O-GlcNAc Transferase with UDP-5SGlcNAc and a peptide substrate [Homo sapiens],4GZ3_A Crystal structure of human O-GlcNAc Transferase with UDP and a thioglycopeptide [Homo sapiens],4GZ3_C Crystal structure of human O-GlcNAc Transferase with UDP and a thioglycopeptide [Homo sapiens],4GZ5_A Crystal structure of human O-GlcNAc Transferase with UDP-GlcNAc [Homo sapiens],4GZ5_B Crystal structure of human O-GlcNAc Transferase with UDP-GlcNAc [Homo sapiens],4GZ5_C Crystal structure of human O-GlcNAc Transferase with UDP-GlcNAc [Homo sapiens],4GZ5_D Crystal structure of human O-GlcNAc Transferase with UDP-GlcNAc [Homo sapiens],4GZ6_A Crystal structure of human O-GlcNAc Transferase with UDP-5SGlcNAc [Homo sapiens],4GZ6_B Crystal structure of human O-GlcNAc Transferase with UDP-5SGlcNAc [Homo sapiens],4GZ6_C Crystal structure of human O-GlcNAc Transferase with UDP-5SGlcNAc [Homo sapiens],4GZ6_D Crystal structure of human O-GlcNAc Transferase with UDP-5SGlcNAc [Homo sapiens],4N39_A Crystal structure of human O-GlcNAc transferase bound to a peptide from HCF-1 pro-repeat 2 (11-26) [Homo sapiens],4N3A_A Crystal Structure of human O-GlcNAc transferase bound to a peptide from HCF-1 pro-repeat 2 (1-26)E10A [Homo sapiens],4N3B_A Crystal Structure of human O-GlcNAc Transferase bound to a peptide from HCF-1 pro-repeat2(1-26)E10Q and UDP-5SGlcNAc [Homo sapiens],4N3C_A Crystal Structure of human O-GlcNAc Transferase bound to a peptide from HCF-1 pro-repeat2(1-26) and UDP-GlcNAc [Homo sapiens],4XI9_A Human OGT in complex with UDP-5S-GlcNAc and substrate peptide (RBL2) [Homo sapiens],4XI9_B Human OGT in complex with UDP-5S-GlcNAc and substrate peptide (RBL2) [Homo sapiens],4XI9_C Human OGT in complex with UDP-5S-GlcNAc and substrate peptide (RBL2) [Homo sapiens],4XI9_D Human OGT in complex with UDP-5S-GlcNAc and substrate peptide (RBL2) [Homo sapiens],4XIF_A Human OGT in complex with UDP-5S-GlcNAc and substrate peptide (keratin-7) [Homo sapiens],4XIF_B Human OGT in complex with UDP-5S-GlcNAc and substrate peptide (keratin-7) [Homo sapiens],4XIF_C Human OGT in complex with UDP-5S-GlcNAc and substrate peptide (keratin-7) [Homo sapiens],4XIF_D Human OGT in complex with UDP-5S-GlcNAc and substrate peptide (keratin-7) [Homo sapiens],5BNW_A The active site of O-GlcNAc transferase imposes constraints on substrate sequence [Homo sapiens],5C1D_A Human OGT in complex with UDP-5S-GlcNAc and substrate peptide (RB2L) [Homo sapiens],5VIE_A Chain A, UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit [Homo sapiens],5VIE_C Chain C, UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit [Homo sapiens],5VIF_A Electrophilic probes for deciphering substrate recognition by O-GlcNAc transferase [Homo sapiens],6E37_A O-GlcNAc Transferase in complex with covalent inhibitor [Homo sapiens],6MA1_A Crystal structure of human O-GlcNAc transferase bound to a peptide from HCF-1 pro-repeat 2 (11-26) and inhibitor 4a [Homo sapiens],6MA2_A Crystal structure of human O-GlcNAc transferase bound to a peptide from HCF-1 pro-repeat 2 (11-26) and inhibitor ent-1a [Homo sapiens],6MA3_A Crystal structure of human O-GlcNAc transferase bound to a peptide from HCF-1 pro-repeat 2 (11-26) and inhibitor 2a [Homo sapiens],6MA4_A Crystal structure of human O-GlcNAc transferase bound to a peptide from HCF-1 pro-repeat 2 (11-26) and inhibitor 3a [Homo sapiens],6MA5_A Crystal structure of human O-GlcNAc transferase bound to a peptide from HCF-1 pro-repeat 2 (11-26) and inhibitor 1a [Homo sapiens]
6IBO_A	4.94e-07	645	848	516	718	Catalytic deficiency of O-GlcNAc transferase leads to X-linked intellectual disability [Homo sapiens]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q9M8Y0|SEC_ARATH	2.75e-08	467	848	574	964	Probable UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase SEC OS=Arabidopsis thaliana OX=3702 GN=SEC PE=1 SV=1
sp|P56558|OGT1_RAT	1.27e-06	645	848	824	1026	UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit OS=Rattus norvegicus OX=10116 GN=Ogt PE=1 SV=1
sp|Q8CGY8|OGT1_MOUSE	1.27e-06	645	848	834	1036	UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit OS=Mus musculus OX=10090 GN=Ogt PE=1 SV=2
sp|O15294|OGT1_HUMAN	2.88e-06	645	848	834	1036	UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit OS=Homo sapiens OX=9606 GN=OGT PE=1 SV=3
sp|P81436|OGT1_RABIT	2.88e-06	645	848	834	1036	UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit OS=Oryctolagus cuniculus OX=9986 GN=OGT PE=1 SV=2

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
0.999658	0.000358

TMHMM  Annotations     

There is no transmembrane helices in RQM13688.1.