CAZyme Information: MGYG000002002_00975

Basic Information

• Species: CAG-460 sp900551525
• Lineage: Bacteria; Firmicutes; Bacilli; RF39; UBA660; CAG-460; CAG-460 sp900551525
• CAZyme ID: MGYG000002002_00975
• CAZy Family: GT2
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
361		43158.33	5.7662

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002002	1156266	MAG	Spain	Europe

• Gene Location: Start: 71406; End: 72491 Strand: -

Full Sequence      

MVCIKICVYAICKNEEKFVDRWYESIKDADGIFVLDTGSSDDSAKKLKKHGISVKEMEIK
PWRFDVARNEALKMIPEDFDICISLDLDEIMLDGWKENILKAWKSDTDRLRYVYNWYIED
GIPKVTYYADKIHKRSGCKWVNPVHEVLEFDHSEKQVFTDDVIVNHYPDREKSRSNYLPL
LELAVKEKPDNDRNMHYLGREYMYYGKWNDAIDTLIKHLKMKNATWKDERCASMRFIARC
YKNMERYDEALMWLYKAINEAPYLRDPYTETAILYYILEDFENVCKYGNKALEIKYNPKT
YMNEVFSYDETLNDLLSISYFYLGDYENAIKNAKEALKINPNNERIKKNLKVFKDEKKFE
D

Enzyme Prediction     

No EC number prediction in MGYG000002002_00975.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd02511	Beta4Glucosyltransferase	1.93e-15	5	191	1	193	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	1.45e-08	237	338	7	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	1.88e-06	268	361	4	87	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	2.20e-06	195	293	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.
TIGR04195	S_glycosyl_SunS	6.61e-05	11	276	64	341	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	9.20e-125	1	354	1	357
ACV63878.1	7.70e-118	4	354	4	356
AQS58818.1	5.22e-116	4	354	4	357
QAT50106.1	1.02e-113	5	350	5	353
QOX65321.1	1.23e-111	5	355	5	358

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
1.000070	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002002_00975.