CAZyme Information: MGYG000002607_00961

Basic Information

• Species: CAG-878 sp000432255
• Lineage: Bacteria; Firmicutes; Bacilli; RF39; UBA660; CAG-878; CAG-878 sp000432255
• CAZyme ID: MGYG000002607_00961
• CAZy Family: GT2
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
356		42555.76	6.0776

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002607	1265326	MAG	China	Asia

• Gene Location: Start: 15561; End: 16631 Strand: +

Full Sequence      

MKVAVYAICKNESKFVDRFMDSVSEADNVFILDTGSTDDTIDKLKKRGAFVKQEIIEPFR
FDIARNKSLEMVPDYYDICVCVDLDEVISPGFRDELIKLFSDKTTRIRYIYNWKLIDNKP
VVSFYADKIHKRKGYTWKHPVHEVLVGEEEVIKTTDNIIINHYPDETKSRSNYLELLELS
IREEPEDDRNMHYLGREYMYHKKYNESIDTLIKHLNLKTSTWKDERCASMQYIARCYQNL
NRFEEARMWLEKAIKEAPYLREPYVEMMFLNYNLEEWELLIKYSYDALKIKKHNKTYINE
PFCYDHTIYDLLSIAYFNLSNYAKALDCVNKAIEISPNIERLKENKKTIEDKINLL

Enzyme Prediction     

No EC number prediction in MGYG000002607_00961.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd02511	Beta4Glucosyltransferase	3.93e-17	2	184	1	190	UDP-glucose LOS-beta-1,4 glucosyltransferase is required for biosynthesis of lipooligosaccharide. UDP-glucose: lipooligosaccharide (LOS) beta-1-4-glucosyltransferase catalyzes the addition of the first residue, glucose, of the lacto-N-neotetrase structure to HepI of the LOS inner core. LOS is the major constituent of the outer leaflet of the outer membrane of gram-positive bacteria. It consists of a short oligosaccharide chain of variable composition (alpha chain) attached to a branched inner core which is lined in turn to lipid A. Beta 1,4 glucosyltransferase is required to attach the alpha chain to the inner core.
sd00006	TPR	1.23e-07	232	334	6	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.
sd00006	TPR	1.68e-06	191	289	4	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.
sd00006	TPR	3.70e-06	174	255	21	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.
TIGR04195	S_glycosyl_SunS	4.30e-06	8	223	64	291	peptide S-glycosyltransferase, SunS family. Members of this family include SunS, the S-glycosyltransferase that transfers a sugar (substrate is variable in reconstitution assays) onto the precursor of the glycopeptide sublancin, which once was thought to be a lantibiotic.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AQS58819.1	1.16e-121	1	353	4	360
AQS58818.1	3.10e-121	1	352	4	359
QOX65321.1	2.43e-120	2	354	5	361
BBB90152.1	9.27e-114	1	354	4	361
ACV63878.1	4.48e-113	1	351	4	357

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
1.000061	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002607_00961.