CAZyme Information: PUG3_T001265-RA-p1

Basic Information

• Species: Globisporangium ultimum
• Lineage: Oomycota; NA; ; Pythiaceae; Globisporangium; Globisporangium ultimum
• CAZyme ID: PUG3_T001265-RA-p1
• CAZy Family: AA17
• CAZyme Description: Methyltransferase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
838	PultBR650_SC0048|CGC1	96044.79	4.7234

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_GultimumBR650	14086	1223559	0	14086

• Gene Location: location=PultBR650_SC0048:16155-19669(-)

Full Sequence      

MFPTATKTLLEIVHPPNDLVLVGSDLRIEILIRNELTAELVDSKVCISMDPVFIPDDLGN
RQEAASIYSLVLDLFPDHPRAMHLLGFMLCQEDTPHRGYAYIYRAVQANTSEWSFAISLG
MCLMNMRNFTEAIQYYRKALELHPTSYDAALNMGDAFQAMGNWDDALHEYRKVAASASGA
YQEPTSRIEDPDKYVTDALGRVCETMRVMEGGFACEKCLVEAITRFPDDAQLRNDHGNLL
LSAGRFESALQEYHSASDLGSLFGMISVADTLEILGETYESLEQYELILRTLNSEQSYPD
TRIRIMKATVLPRILPGSQQEIDMYRQRFESEIDALRDDIETLQPTDMEPNRIPFSTAVT
MNSHNRNNRLLKTKIGTLYFDLLYTHRLLREKYMLGYAAIPSPDRFIRSSGMLTQRRLRV
GFVSRFLFSPTVGLYMSNLIPALDPLKYQTIAFAIGLSSSMKKREYAGQIAEEVWALPKD
LPTARNEIRTANLDVLIYPELGMDKTTYFLSLLRLAPIQAVWWGNADTSGVQAIDYRLIS
EYEHENAREHYTEKELYQFKGMGFYHSFPEPRDYNVSRAHVRDAIIKRFNLPADFHMYFS
LESILNMHPDYDEAVVEILRRDDKARMFFLGSSTRNRWRDQLVARIVARAGDSVRAFERI
YFMNDVDPKQELLLAGAADTVMASVHLTRPRAAIQAFTAGVPIITLPGEFWGTRVAYGFY
QIMEMNNLIASNMDEYITLAVRMADDADFRNEMMEKIKERRSRLHEDSRAVEEWEKFLDF
AGAKLYPSGEDNDYEVSDLKGDEESDTQDQTEENELNCSKSDEDENAQTCLREEERAK

Enzyme Prediction     

No EC number prediction in PUG3_T001265-RA-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT41	215	778	2.1e-61	0.5191489361702127

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
226428	Spy	8.64e-26	399	762	239	593	Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones].
276809	TPR	1.40e-13	79	173	1	95	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	2.87e-10	57	141	13	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	3.45e-10	119	256	7	95	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.
404688	Glyco_transf_41	5.45e-08	658	762	425	529	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
UIZ20641.1|GT41	2.69e-160	57	789	168	911
BAZ61948.1|GT41	4.18e-52	225	781	366	884
BAZ15802.1|GT41	4.18e-52	225	781	366	884
BAI76932.1|GT41	6.05e-51	59	771	47	640
BBO88349.1|GT41	1.28e-50	300	786	425	877

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2JLB_A	1.22e-06	399	746	187	522	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]
2VSN_A	1.22e-06	399	746	187	522	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]
5A01_A	1.78e-06	587	757	504	668	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|O82039|SPY_PETHY	6.59e-07	415	746	485	808	Probable UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase SPINDLY OS=Petunia hybrida OX=4102 GN=SPY PE=2 SV=1
sp|Q8RVB2|SPY_SOLLC	1.14e-06	381	746	455	808	Probable UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase SPINDLY OS=Solanum lycopersicum OX=4081 GN=SPY PE=2 SV=1
sp|Q9M8Y0|SEC_ARATH	5.92e-06	416	744	590	912	Probable UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase SEC OS=Arabidopsis thaliana OX=3702 GN=SEC PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000062	0.000000

TMHMM  Annotations     

There is no transmembrane helices in PUG3_T001265-RA-p1.