CAZyme Information: KIS70450.1

Basic Information

• Species: Ustilago maydis
• Lineage: Basidiomycota; Ustilaginomycetes; ; Ustilaginaceae; Ustilago; Ustilago maydis
• CAZyme ID: KIS70450.1
• CAZy Family: GT90
• CAZyme Description: unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
2119	CM003142|CGC6	231126.65	6.8439

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_Umaydis521	6910	237631	145	6765

• Gene Location: location=CM003142:568471-574830(+)

Full Sequence      

MPNLPSSSFSSEASSTASYRRGSEQLPSAYLASQAGFPPRRASFGNAPPTGSANMMLRAA
SAMIAQASSGAEGLHAVSSALLNQAKAQASAVSHPSQDVNAHTASATHSQSIPMARNASD
SASYSAAISAHIASALENQMTSPRPPHSASLLPHTTTPNSTAIDPLIALPDSDSIQPEVQ
MGRIAAQAAAREAQTQWRTQLALRRSSLQPHSATAAQASNTAPRPSTSSTAAAASTSSGD
TANVHSQSQPSANPASPNQRSNTQSTLDPDTADMSFTEYLRFLGLSHIPLPSEGIELSFG
PDNSSNSRYWDATNPHMGFSLSGVPSMPLMPNPPLQMLPPPASPSFRRKLPRAHSWFRHR
SSASASSFECTDTSNDFEPNVMSPFPYPFQVVQTPGGTARAGWWVPVSEVPPERRAEAVK
IGEEPASSAVFGVARATKLQSVPEHVSGAERDGGDQEAQLLFQPSYRDFTQDEYSTLATA
AAYATAALTSIASTPGGTSQSSSWRPLTASEQEAIAIQLRAWAGLDGPHAQAQARKALEQ
RQMHLIQQAIRKDPSTPYAADQQQVASQDHLSQLHGPAGAARFFPPDFASHYRTQLRALA
EGYYTRLHNENLTQAHYAQSAAKDPGMDTPVIHHDATPTCDAHKAPTGETVQPPSPDIAV
LSRTQPPVHTPTLRPGACDPVELLSAASNAAGQESSSPEVRDQLLQYAHTLYTQGNPQAD
SSAKGTDKLHPTLLPLLHTLHKLHPTHLPILLLLSCAYYAASNYAGSLWYNNQILRIDPN
YVESMSNIGTTLRALGRYKEAESWWWRAIRLRPGYWDAYENLLGVMCSVNAPTAVANKSD
PEHGPGEAPPSQPRFQEALQLCEFVEAHVVGQQDVSGMSMMPLYLPPNLPLTQTPRLQNL
FYAKGNLKFVLPEFGSVPAAAEYQKAVEVVLSTDASSRYSLRDLVVATCAVGLLSMGAML
PETAAAAAAVEVALALGINPTNPEHAVILASGSFSRFCQGGVLALVQLSGDVVVQTLLRL
GNGQLPMLLLLPEAATQLCKVVFAETAGNLPALSRPSQSQIAKPQNLATLQQVQKQAAQT
TSTILLTLAKLFQDAIASPMAGPHGSLTLGGIPPSISLLLPLYYLSISMHASASTCNNLG
ILLSSIPVVTTVINAAGQPQQLNGQALAMQYYTQGLQLDPRHPHIYTNLGSLLKDLGHLN
EAIKMYQKAVECNPNFDVALANLGNAIKDQGRTQDSVVYYRRAVQVNPHFPEALCGLVNA
LLAVCDWSEVYTDRRDAEEPKQKSDERGETRASASTSGWMDKVSELVSKQLSEGYRYGAG
AFQTAASLADWVRAIIEAIGDTRTDAPQIWTRRLQPFYQPGFDRVANQVCEGGYLIQLVE
RMIRQSQRRWYVDVYGADTLQTSTELPRVTAAAAAAASNSSRYARPKLPSCLVTPAVPTV
LPFHTFTYPLSARQIRLICHRNALRISHTTLTQMWMPDVVYPPPSPPSPKINIGYISSDF
NNHPLAHLMQSVFGLHDRSLFNVFLYATTPSDASPYRQKIEREAQHFLDVSAWSNQQVVE
RIVMDNIHVLVNLNGYTKGARNEIFAARPCAVQVEFMGFAGCMASRWTDWVVADPIVCPP
EMTSVDRWRQQSELAAKSGSVLQQRATDLLADLDPEDGSEDWVYPERFIYMPHSYFVNDH
KQGFRENVAVAGTVDAPGVVSQGAQRSSDSARESTCSSSDEQLWASEEEKRYAMRRELFP
NLPDDYVIFADFNQLYKCDPMLFRLWLRILERVPKSILWLLRFPAAGEEHLMHEARRYAG
DRVACRVIFTDVAPKHIHIHRGRIADLFLDTIECNAHTTAADILWSATPMLTWPRHVHKM
CSRVAASIVHATGFGDEMTVHSEKEYEDRAVELAESISYVYYDDKGREVVGRVDHNRVRF
ASELEADANSAAAQAHSSGASTRPTGEAEANSGETWTKSADEECQGQGEQQARVQVASRV
KRVRSANCEDDSASAQTRSGMSSGAHVDAKQTRVAGACKWRSTIRLAASAEYAGATTRRL
KVSEASLASLRKRLLVTRQHSALFDTAQWTRDLEKGFVEAWTRWVYAIDYEDSPQMHGLQ
HPHSAHRLRRSGHIWVNQL

Enzyme Prediction     

No EC number prediction in KIS70450.1.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
404688	Glyco_transf_41	3.50e-105	1438	1899	28	516	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.
226428	Spy	3.39e-55	1490	1894	259	575	Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones].
276809	TPR	1.51e-17	1168	1245	20	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	7.41e-16	1185	1269	3	87	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	1.98e-11	750	822	3	75	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
CBQ71837.1|GT41	0.0	1	2119	1	2070
SAM80369.1|GT41	0.0	1	2119	1	2101
CDI52495.1|GT41	0.0	1	2119	1	2097
CDS82054.1|GT41	0.0	1	2095	1	2040
SJX61709.1|GT41	0.0	1	2119	1	2071

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5A01_A	1.09e-73	1437	1900	182	661	O-GlcNAc transferase from Drososphila melanogaster [Drosophila melanogaster],5A01_B O-GlcNAc transferase from Drososphila melanogaster [Drosophila melanogaster],5A01_C O-GlcNAc transferase from Drososphila melanogaster [Drosophila melanogaster]
5NPR_A	9.05e-71	1437	1918	178	678	The human O-GlcNAc transferase in complex with a thiol-linked bisubstrate inhibitor [Homo sapiens]
5NPS_A	9.23e-71	1437	1918	179	679	The human O-GlcNAc transferase in complex with a bisubstrate inhibitor [Homo sapiens]
3PE3_A	1.02e-70	1437	1918	184	684	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]
6TKA_AAA	1.10e-70	1437	1918	183	683	Chain AAA, UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit [Homo sapiens]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q9M8Y0|SEC_ARATH	4.30e-81	1437	1894	534	912	Probable UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase SEC OS=Arabidopsis thaliana OX=3702 GN=SEC PE=1 SV=1
sp|O18158|OGT1_CAEEL	3.66e-69	1437	1893	606	1088	UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase OS=Caenorhabditis elegans OX=6239 GN=ogt-1 PE=1 SV=2
sp|O15294|OGT1_HUMAN	5.82e-68	1437	1918	502	1002	UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit OS=Homo sapiens OX=9606 GN=OGT PE=1 SV=3
sp|P81436|OGT1_RABIT	7.76e-68	1437	1918	502	1002	UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit OS=Oryctolagus cuniculus OX=9986 GN=OGT PE=1 SV=2
sp|Q8CGY8|OGT1_MOUSE	1.38e-67	1437	1918	502	1002	UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit OS=Mus musculus OX=10090 GN=Ogt PE=1 SV=2

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000059	0.000000

TMHMM  Annotations     

There is no transmembrane helices in KIS70450.1.