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CAZyme Information: EPrPIT00000023222-p1

You are here: Home > Sequence: EPrPIT00000023222-p1

Basic Information | Genomic context | Full Sequence | Enzyme annotations |  CAZy signature domains |  CDD domains | CAZyme hits | PDB hits | Swiss-Prot hits | SignalP and Lipop annotations | TMHMM annotations

Basic Information help

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 Start: 2879; End:7424  Strand: +

Full Sequence      Download help

MHRQKIVRTP  PHAVSSAPLL  PTAKRPAVAV  QKRKQMHSAL  LLLLTTATLA  CCGXXXXXLV60
AGVSTQLTND  GDLMPVLSKP  LLEILHPTND  LVIGSTDLHI  EVAIRAELHG  GFRDAKLCIS120
MDPVFIPADM  ELEDGTSQLQ  ETCFDQAINY  TTFHVDGLVP  GLTVAVALDT  GATYHNAGER180
MLAASIYRQV  LDMFPEHPYA  LHLLGLVFYQ  DGNPYEGYAY  IQRALQRNAS  ENAFHNSLGL240
CLKSMGRVQE  AVQSYRRALE  IHPFGFQTAL  NLGDALQELG  KWEDAMHEYR  KVVASAQSAQ300
AERFLKDAWR  RVCELTRLTE  GWLACEKCIA  ELLARWPSEP  EFHNDRGSLL  LSAGQFEVAL360
TEFKSAQDLA  SVNGMVNVAD  VLESLGETEE  SLQQYQLVTC  LVNDLISSWS  SILRSLAPMK420
GNLETRIRVM  KATVLPRILP  ETQELIDIYR  QRFESEIDSL  REDLEKLRRT  DMDPARISFS480
TAITMSAHNR  NNRVLKEKLG  SLYADLLYKY  RIAEPRRLRV  GFVSRHLYNP  MAGLYVSDLI540
RQFDSRKYET  IAFAVGQSHS  MTKQERLEQI  AETVHALPKD  LTVARDEIRA  AEIDVLIFPE600
LGMDKTTYFL  SLSRLAPVQA  VWWGNADTSG  VKNVDYRLVS  EYEHEDYRAH  YSERTYQFKG660
MGFYHRFAEP  HDYNVSREQV  RGAVMGRFGL  PPDFRMYLSI  ESILNMHPDF  DYAVGQILRQ720
DEKARIFLLG  SSNRNRWRDQ  LVARIYANTG  FEVAAGRIYF  LNDVDAKQEL  LLLGAADAVL780
ASIHLTRPRA  TIQAFTAGVP  VVTLPGELWG  TRIAYGFYRQ  MDMYDLVAGS  LDEYVALVLR840
LAQDTEFRLE  MSERIKERRV  CLHEDAQALL  RFDPQLLGFQ  LLQLRLLPRD  ELVSNSTIAF900
FGVHVLACEV  LVLCFKGPAL  SVQVSQLTGE  KVFGTHALGL  FLCEFALEVQ  LSHALNLALL960
ILDRVFFAHA  LEFFCLLLAL  VHPEQPLLLF  IELELAGFAL  CSQSPLMQYL  GLDVVQLSVV1020
AIAVIISKLM  HLIDDSKHTT  ILSILLLLLL  1050

Enzyme Prediction      help

No EC number prediction in EPrPIT00000023222-p1.

CAZyme Signature Domains help

Created with Snap5210515721026231536742047252557763068273578784089294599786495GT41
Family Start End Evalue family coverage
GT41 268 862 1.2e-64 0.5801418439716312

CDD Domains      download full data without filtering help

Created with Snap52105157210262315367420472525577630682735787840892945997514859Spy198294TPR171260TPR519859GT4_PimA-like165298TPR
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      help

Created with Snap5210515721026231536742047252557763068273578784089294599772868UIZ20641.1|GT41335869BAZ61948.1|GT41335869BAZ15802.1|GT41427877QQP88841.1|GT41427880UEM04252.1|GT41
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      download full data without filtering help

Created with Snap521051572102623153674204725255776306827357878408929459976878605A01_A
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      help

EPrPIT00000023222-p1 has no Swissprot hit.

SignalP and Lipop Annotations help

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      download full data without filtering help

Start End
39 61