CAZyme Information: MGYG000004105_01557

Basic Information

• Species: Alistipes_A sp900546005
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Rikenellaceae; Alistipes_A; Alistipes_A sp900546005
• CAZyme ID: MGYG000004105_01557
• CAZy Family: GH78
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
821	MGYG000004105_8|CGC1	91872.03	5.0336

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004105	2464466	MAG	United Kingdom	Europe

• Gene Location: Start: 30101; End: 32566 Strand: +

Full Sequence      

MKPYLPLLGAAFFLLLTASGNPSKKISTELKIQEPYPPISGSFSGKTIDESPDPLVAYRW
ENPQADDDLQTYILYPETVTHEATGKVSKNAQGAIKITEPVSLRFDFGQVNAGWLEFDSK
DLAGKVTMSISEYTEPAILNAGAQHPVKTAEPVRYGDTYRLELNKELYEGVRYGWIHIAS
VEHPFTIDEVRLVCQIKPTNYEGSFSCNDPELTRIWYTGAYTVKMNLLKDYFGAILMERS
DRHSWTGDAHPSQAASMVAFGNFDFVKKNLFYTSTQFNGIASYSLYWVLSLIDYYNYTGD
QKTFDELFDNACQKLDVAYAHYGKNPDLQFHGWDERLGAGFENPNCTEAQNTYKMLSIRA
WNEFSQAAHHAGRLDAAEKYAGYVSEKSDELRASTAPFDGFGIFAASDAVNAGFTSVSEN
DRLWKSAFSDRMQRLSYSPFNQYFIIQAMARMGRYSEALQTIDDCWGGQLRYGGTTFFEV
FRPSWIPELAPNGAPVNNQCGYTSMTHPWSGGVTKWLSEEVLGIKPTEPGFTRFQVVPHL
DANIYSVDGSVPTPLGTIRFAFDLKSGKGSLVVLEGSYATIGIPKAGRTLKEVLINGQAA
SRFAAKSSEDEGFIYYRDLRPGTYTIQVDYTGNIPAVQEEAFEYANMQVVEQDTTTQGDW
KGHYGSDGYVLFNYDSAGGHRIELPDYIDSIHLAKTGNLHIVSGTTDSRAPISADGTTKR
NMGSVITLDPIPCNQTFTIDLPNSRNAPYRIALYFVDWEKVGRRSAIEVFDLESKQLLMP
VEIVRDYQEGKYVVFSVDRPVRLRINQVRGTNAALCALFFD

Enzyme Prediction     

No EC number prediction in MGYG000004105_01557.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH78	98	571	2.8e-72	0.9642857142857143

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam17390	Bac_rhamnosid_C	2.97e-06	523	584	1	64	Bacterial alpha-L-rhamnosidase C-terminal domain. This family consists of bacterial rhamnosidase A and B enzymes. L-Rhamnose is abundant in biomass as a common constituent of glycolipids and glycosides, such as plant pigments, pectic polysaccharides, gums or biosurfactants. Some rhamnosides are important bioactive compounds. For example, terpenyl glycosides, the glycosidic precursor of aromatic terpenoids, act as important flavouring substances in grapes. Other rhamnosides act as cytotoxic rhamnosylated terpenoids, as signal substances in plants or play a role in the antigenicity of pathogenic bacteria.
pfam17389	Bac_rhamnosid6H	0.002	203	517	4	336	Bacterial alpha-L-rhamnosidase 6 hairpin glycosidase domain. This family consists of bacterial rhamnosidase A and B enzymes. L-Rhamnose is abundant in biomass as a common constituent of glycolipids and glycosides, such as plant pigments, pectic polysaccharides, gums or biosurfactants. Some rhamnosides are important bioactive compounds. For example, terpenyl glycosides, the glycosidic precursor of aromatic terpenoids, act as important flavouring substances in grapes. Other rhamnosides act as cytotoxic rhamnosylated terpenoids, as signal substances in plants or play a role in the antigenicity of pathogenic bacteria.
cd04103	Centaurin_gamma	0.006	563	599	8	46	Centaurin gamma (CENTG) GTPase. The centaurins (alpha, beta, gamma, and delta) are large, multi-domain proteins that all contain an ArfGAP domain and ankyrin repeats, and in some cases, numerous additional domains. Centaurin gamma contains an additional GTPase domain near its N-terminus. The specific function of this GTPase domain has not been well characterized, but centaurin gamma 2 (CENTG2) may play a role in the development of autism. Centaurin gamma 1 is also called PIKE (phosphatidyl inositol (PI) 3-kinase enhancer) and centaurin gamma 2 is also known as AGAP (ArfGAP protein with a GTPase-like domain, ankyrin repeats and a Pleckstrin homology domain) or GGAP. Three isoforms of PIKE have been identified. PIKE-S (short) and PIKE-L (long) are brain-specific isoforms, with PIKE-S restricted to the nucleus and PIKE-L found in multiple cellular compartments. A third isoform, PIKE-A was identified in human glioblastoma brain cancers and has been found in various tissues. GGAP has been shown to have high GTPase activity due to a direct intramolecular interaction between the N-terminal GTPase domain and the C-terminal ArfGAP domain. In human tissue, AGAP mRNA was detected in skeletal muscle, kidney, placenta, brain, heart, colon, and lung. Reduced expression levels were also observed in the spleen, liver, and small intestine.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QGA24541.1	0.0	11	821	11	820
ATP56756.1	1.54e-286	36	821	31	818
QMW04815.1	1.29e-285	31	821	32	816
ACT93515.1	1.32e-281	33	821	51	831
QEC76313.1	2.93e-277	36	821	45	844

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3CIH_A	7.73e-36	22	573	100	694	Crystalstructure of a putative alpha-rhamnosidase from Bacteroides thetaiotaomicron [Bacteroides thetaiotaomicron VPI-5482]
2OKX_A	6.45e-17	103	556	439	910	Crystalstructure of GH78 family rhamnosidase of Bacillus SP. GL1 AT 1.9 A [Bacillus sp. GL1],2OKX_B Crystal structure of GH78 family rhamnosidase of Bacillus SP. GL1 AT 1.9 A [Bacillus sp. GL1]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P9WF03	2.14e-07	466	628	766	910	Alpha-L-rhamnosidase OS=Alteromonas sp. (strain LOR) OX=1537994 GN=LOR_34 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as LIPO

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.001675	0.286097	0.711804	0.000155	0.000145	0.000125

TMHMM  Annotations     

There is no transmembrane helices in MGYG000004105_01557.