CAZyme Information: EPrPIT00000023222-p1

Basic Information

• Species: Globisporangium irregulare
• Lineage: Oomycota; NA; ; Pythiaceae; Globisporangium; Globisporangium irregulare
• CAZyme ID: EPrPIT00000023222-p1
• CAZy Family: GH89
• CAZyme Description: Methyltransferase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1050		118357.26	6.1463

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_GirregulareDAOMBR486	13869	1223557	65	13804

• Gene Location: location=PirrDAOMBR486_SC1180:2879-7424(+)

Full Sequence      

MHRQKIVRTPPHAVSSAPLLPTAKRPAVAVQKRKQMHSALLLLLTTATLACCGXXXXXLV
AGVSTQLTNDGDLMPVLSKPLLEILHPTNDLVIGSTDLHIEVAIRAELHGGFRDAKLCIS
MDPVFIPADMELEDGTSQLQETCFDQAINYTTFHVDGLVPGLTVAVALDTGATYHNAGER
MLAASIYRQVLDMFPEHPYALHLLGLVFYQDGNPYEGYAYIQRALQRNASENAFHNSLGL
CLKSMGRVQEAVQSYRRALEIHPFGFQTALNLGDALQELGKWEDAMHEYRKVVASAQSAQ
AERFLKDAWRRVCELTRLTEGWLACEKCIAELLARWPSEPEFHNDRGSLLLSAGQFEVAL
TEFKSAQDLASVNGMVNVADVLESLGETEESLQQYQLVTCLVNDLISSWSSILRSLAPMK
GNLETRIRVMKATVLPRILPETQELIDIYRQRFESEIDSLREDLEKLRRTDMDPARISFS
TAITMSAHNRNNRVLKEKLGSLYADLLYKYRIAEPRRLRVGFVSRHLYNPMAGLYVSDLI
RQFDSRKYETIAFAVGQSHSMTKQERLEQIAETVHALPKDLTVARDEIRAAEIDVLIFPE
LGMDKTTYFLSLSRLAPVQAVWWGNADTSGVKNVDYRLVSEYEHEDYRAHYSERTYQFKG
MGFYHRFAEPHDYNVSREQVRGAVMGRFGLPPDFRMYLSIESILNMHPDFDYAVGQILRQ
DEKARIFLLGSSNRNRWRDQLVARIYANTGFEVAAGRIYFLNDVDAKQELLLLGAADAVL
ASIHLTRPRATIQAFTAGVPVVTLPGELWGTRIAYGFYRQMDMYDLVAGSLDEYVALVLR
LAQDTEFRLEMSERIKERRVCLHEDAQALLRFDPQLLGFQLLQLRLLPRDELVSNSTIAF
FGVHVLACEVLVLCFKGPALSVQVSQLTGEKVFGTHALGLFLCEFALEVQLSHALNLALL
ILDRVFFAHALEFFCLLLALVHPEQPLLLFIELELAGFALCSQSPLMQYLGLDVVQLSVV
AIAVIISKLMHLIDDSKHTTILSILLLLLL

Enzyme Prediction     

No EC number prediction in EPrPIT00000023222-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT41	268	862	1.2e-64	0.5801418439716312

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
226428	Spy	4.33e-31	514	859	256	592	Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones].
276809	TPR	3.21e-15	198	294	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.
276809	TPR	1.04e-13	171	260	8	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.
340831	GT4_PimA-like	3.81e-10	519	859	1	348	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.
223533	TPR	7.79e-10	165	298	131	268	Tetratricopeptide (TPR) repeat [General function prediction only].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
UIZ20641.1|GT41	1.12e-174	72	868	28	892
BAZ61948.1|GT41	4.78e-57	335	869	366	874
BAZ15802.1|GT41	4.78e-57	335	869	366	874
QQP88841.1|GT41	1.51e-54	427	877	241	682
UEM04252.1|GT41	3.71e-54	427	880	241	685

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5A01_A	7.09e-06	687	860	505	673	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     

EPrPIT00000023222-p1 has no Swissprot hit.

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.055506	0.944485	CS pos: 52-53. Pr: 0.1759

TMHMM  Annotations     

Start	End
39	61