CAZyme Information: MGYG000001371_01684

Basic Information

• Species: Paenibacillus lautus_A
• Lineage: Bacteria; Firmicutes; Bacilli; Paenibacillales; Paenibacillaceae; Paenibacillus; Paenibacillus lautus_A
• CAZyme ID: MGYG000001371_01684
• CAZy Family: GT4
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
655		75877.19	5.2008

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001371	6950059	Isolate	not provided	not provided

• Gene Location: Start: 49424; End: 51391 Strand: +

Full Sequence      

MNFTSDKDEFNQLSAQLKGKVQQHIVNNELAEAKLILQSIEKYIPLDAEIYSFKGIISLY
EEDKEMAIKEFKAGLAIDSGNSDLLYNLAEVYKGLNDIPNAYRYYQRAKDSTEDMELLNE
LETILTDLEFHPLMDTHEGPDRKKVLIIAHIFPPLGGSGVQRTLKFTKYLTEFQWKPIIV
TTGDSSYPLIDQSLLSEVPENLTIHRINEPTNLTQTDKQELLNVYNTVVNNKEIIDEYIS
EINTKQLSVVAPDPYIYWAVHVIRKIKNDVDMSDIDIIYTTSGPYSDHLIGYMLKKEFNK
PWVADFRDEWTNNPYAEYDPQSSRYKIEYLMEKNITKYADHLVTTTPLTTNNYIQNFHVN
PNKISTITNGYDEDDFNGLIHLQQTSNKFSIFHNGLLYSIRTPITFLKAIHNLVSRGLIN
KEHLHIGFSWTENDELWRKYANDLGLIDQIEFYGYLSHQESLNKALASTALLLIVGPGEK
NKSMYPGKIFEYFRLNKPIISLSPINSGVEALLTETGRGKNADFNDIAEIERIIEDFYKR
WLREELPKFKLDETIVKFERRELTKNLASTFEKVLDSVQQTNTKTRLAFFSIKDGDKFLH
DIIDHLSSLYNIRKFIITDVSQIEPAMEWADICWFEWCDKLIVHASNLSIARSKK

Enzyme Prediction     

No EC number prediction in MGYG000001371_01684.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd03794	GT4_WbuB-like	5.14e-33	144	539	1	361	Escherichia coli WbuB and similar proteins. This family is most closely related to the GT1 family of glycosyltransferases. WbuB in E. coli is involved in the biosynthesis of the O26 O-antigen. It has been proposed to function as an N-acetyl-L-fucosamine (L-FucNAc) transferase.
COG0438	RfaB	1.47e-13	236	575	44	378	Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis].
cd03801	GT4_PimA-like	5.83e-12	144	546	1	340	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.
sd00006	TPR	9.34e-10	24	108	11	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.
sd00006	TPR	1.14e-07	48	129	1	83	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
AOT70024.1	7.20e-161	10	572	783	1351
QHA65011.1	1.85e-147	143	588	2	451
ANR57241.1	1.85e-147	143	588	2	451
QKU27395.1	1.85e-147	143	588	2	451
BBK94534.1	1.85e-147	143	588	2	451

PDB Hits     

has no PDB hit.

Swiss-Prot Hits     

has no Swissprot hit.

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
1.000050	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001371_01684.