CAZyme Information: PIW_T004773-RA-p1

Basic Information

• Species: Globisporangium iwayamae
• Lineage: Oomycota; NA; ; Pythiaceae; Globisporangium; Globisporangium iwayamae
• CAZyme ID: PIW_T004773-RA-p1
• CAZy Family: GH17
• CAZyme Description: UDP-N-acetylglucosamine-peptide N-acetylglucosaminyltransferase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
2201		247660.53	7.0759

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_GiwayamaeDAOMBR242034	14874	1223558	0	14874

• Gene Location: location=PiwaDAOMBR242034_SC00602:1033-9071(+)

Full Sequence      

MRNLSTISHVVVLLVLLYMTVAAAAATGTASNYASLSSAEVHSLLSGLYRNGELVAVEKI
AAQVIRENPADVNFTTPYEYLGVAQYALGDLDKATKTFQEAVRVNDRDVESWLQLGKCYL
YALKMPQAAVALEKAVMGKGAVKDTHTLFKVRIWMADWHDREPMLEQIQVFVDANLPSLT
SISALDFAEFSPSIILALSRQAAADNTSGGQTLCCDRSDLHLQTSALRVGFVSSDFGVHP
VSTLMRGMLEMLSNGAGHHAMVVYCFSLTAESSWWRRNISRSVDHMVSLVGKNPAEGAAI
IKQHGIHVLIDLNGHTLHSGLTMFNHRPSPVQMSFLGYPMTTGSAHIDYFISDAVSTPAE
YSAEIFTEKLLILPTNYIKIDPAVFSAWMAVLARVPHSVLWFLRYAGHEDAERNLRREAN
GHGVDGEKRLVFSDLAPWIHHTHSKRAADLILDTSMKNGHTTIIDALMAGVPVVTLEGNR
MSNRAGSSALHSLDLHDLTVNSFKEYVEVAVLLATNSKLLSKLRARVEANRLQYPLFDTR
KYTTNFESALQSSWAVIKASRLRDSTPSSFHIFPASRLDQIAPREFPILSGQDDTHRVDE
YIVKVNDAIADDRNILLHIGGHVAKRDWWIVDANDRADVDFHTRMDNLHPFPDSSVTALY
ASHVLEHCHYRLLDEVRATLHEWFRVLRPGGVLFVSVPDLLVLSALFANATTTDAERFFI
MNMMYGGQADAFDVHKVGFFTPLLESYLQDAGFCEIERVEAFGLFADASAMRYKDVAISL
NVKATACKGANERIHVDLLVNTTEMLLIEGEKREENNVKRESMSAPTSGPNSTTTSPRTL
NQESWNQLSAATLEFGDPYGKSSQASPAKMSPKFLRSMFDPTVESKNESECLFRVRISGI
QCRNLQGRKFSGKSDPFVEFFWDDEEEQAPYGTPVIKADLNPNYKGVLISFEYKGTLNLL
PKKYLVAKVFTNRKFQSKTMIGCAKVDLWTVATGPVHHDHHLIGCDNGRIVFNCYMEQCS
EWNISVSDVGVMMPAIANELDRPEGHDFQEDASLPLKKFAVSYKCTVGTSETFYMGNVLK
HAEKRVMSEINDVSFQSLARLAVLSSRVSRPNSQQLPPSDEDAFSDPLVAEDPVGVQWTT
ATDLLPAITRYSTFDELMSATLTLEIRQLCVGRGQMATDPDGGFLTMLDKYNKDKVTISS
EDRRFDEEIRNTLLFGQTWLSLEKSFEDALQERIKKKFDADPSLGLNGLGFSEQFVTSKF
EQSLTLKGHQVAVVYGTILFKKIPDVRQLRCGVISESGISSSSSVIVGGIQSSKKAPRKS
KVVIPIEAQRVLEKMQDLVELMSVRQKDDKEGKVRKATKILKMLQISHKASMLSWVYASA
EALDETKSILLRLWQFLLENIRVRHYTLRNVFYELLFYLVKRAELSDLPLLGFDSTVVTN
SLGFKQTHKVNKSDIEFGLKLRAMLVETKFCVLQTVSVRGVMNNNLMFFVARMLSVLCFR
LPSFGVELYQLWADSYIEDIPNLSEYRPNANADLFAMDGLEAHLDWRRFHKAIYDEYGEK
VLKKQEEEAEDKYEITSEAWKSRFRRLNGEANTLNILLVDQWLWYVLDTLAVLNQKIGWI
HLPGYSQVLKVFFLELKTQKSGWLPPTLYKLSCTMLSNPTLINPMTKFLLISTSVHDVTA
VIGSVELLGVWMYMIRSWRVRLGSYRLSHLENNDRWNFHQDDQYSIPAGDEVSLLPPSFD
FRFLCAALRILLESEHTQVVLTTLEFLYNCWDCFPERHADKLRFELLQSFTRLFLHWHRE
VRHFYHTLIAYRAMKPHGWTQKGASFVNTPPHSRRQIDAVAADFNSSLGREEQTENTKRS
RSYSASNLIESVQKRFGSASPRSVLASPRSSPRSSPAPSPRASSSGLSLTISSPSNRGVN
SNSSTPTSTSGSDRKSVDGFNTSFSDRKTRSISEDFNKVPLQQQPKMDPNIQLQFNRLLE
SIYAAAKKYIDRQAQDGNLLRAAKQPLKATWKKKGVLLKQGFIYKNTWKQKFFSLQNNKL
GYSDTETGPIKREINVIGSVVAEVANQIDQSQGSRVVLFNCFHIDSGYQKFTLCAPTYED
QREWIEVLTQNATAETAVKKPDEQLSQMDVAEVTGKLESLAGKHDAAEAISEMLLPYTAL
AVKEWLQFRVDAMDIESRIAAGLQFQMPVLLSKSSLYADDD

Enzyme Prediction     

No EC number prediction in PIW_T004773-RA-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT41	34	562	1.6e-90	0.6312056737588653

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
226428	Spy	4.33e-67	227	555	260	616	Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones].
404688	Glyco_transf_41	8.05e-59	219	545	73	542	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.
226975	COG4627	5.90e-28	615	784	7	183	Predicted SAM-depedendent methyltransferase [General function prediction only].
400754	DUF1765	9.14e-21	1731	1812	38	124	Protein of unknown function (DUF1765). This region represents a conserved region found in hypothetical proteins from fungi, mycetozoa and entamoebidae.
269977	PH_DAPP1	2.25e-10	2013	2108	5	92	Dual Adaptor for Phosphotyrosine and 3-Phosphoinositides Pleckstrin homology (PH) domain. DAPP1 (also known as PHISH/3' phosphoinositide-interacting SH2 domain-containing protein or Bam32) plays a role in B-cell activation and has potential roles in T-cell and mast cell function. DAPP1 promotes B cell receptor (BCR) induced activation of Rho GTPases Rac1 and Cdc42, which feed into mitogen-activated protein kinases (MAPK) activation pathways and affect cytoskeletal rearrangement. DAPP1can also regulate BCR-induced activation of extracellular signal-regulated kinase (ERK), and c-jun NH2-terminal kinase (JNK). DAPP1 contains an N-terminal SH2 domain and a C-terminal pleckstrin homology (PH) domain with a single tyrosine phosphorylation site located centrally. DAPP1 binds strongly to both PtdIns(3,4,5)P3 and PtdIns(3,4)P2. The PH domain is essential for plasma membrane recruitment of PI3K upon cell activation. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AGA31831.1|GT41	1.12e-63	227	791	189	739
QRJ63612.1|GT41	2.06e-61	223	784	267	824
UIZ23060.1|GT41	1.70e-60	149	554	478	923
ALF56607.1|GT41	2.62e-59	224	562	14	379
CCA22532.1|GT41	1.99e-58	149	554	487	931

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6Q4M_A	7.23e-41	219	554	230	706	Crystal structure of the O-GlcNAc transferase Asn648Tyr mutation [Homo sapiens]
6IBO_A	9.63e-41	219	554	230	706	Catalytic deficiency of O-GlcNAc transferase leads to X-linked intellectual disability [Homo sapiens]
5NPR_A	1.21e-40	219	554	224	700	The human O-GlcNAc transferase in complex with a thiol-linked bisubstrate inhibitor [Homo sapiens]
5NPS_A	1.22e-40	219	554	225	701	The human O-GlcNAc transferase in complex with a bisubstrate inhibitor [Homo sapiens]
3PE3_A	1.28e-40	219	554	230	706	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q9M8Y0|SEC_ARATH	1.04e-53	158	554	511	952	Probable UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase SEC OS=Arabidopsis thaliana OX=3702 GN=SEC PE=1 SV=1
sp|Q8CGY8|OGT1_MOUSE	1.14e-39	219	554	548	1024	UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit OS=Mus musculus OX=10090 GN=Ogt PE=1 SV=2
sp|P81436|OGT1_RABIT	2.60e-39	219	554	548	1024	UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit OS=Oryctolagus cuniculus OX=9986 GN=OGT PE=1 SV=2
sp|O15294|OGT1_HUMAN	3.42e-39	219	554	548	1024	UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit OS=Homo sapiens OX=9606 GN=OGT PE=1 SV=3
sp|Q27HV0|OGT1_PIG	7.78e-39	219	554	548	1024	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
0.000205	0.999793	CS pos: 24-25. Pr: 0.9799

TMHMM  Annotations     

Start	End
7	29