CAZyme Information: MGYG000001640_00045

Basic Information

• Species: Duncaniella sp900549445
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae; Duncaniella; Duncaniella sp900549445
• CAZyme ID: MGYG000001640_00045
• CAZy Family: GH38
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
867		96672.27	7.0541

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001640	2860567	MAG	United States	North America

• Gene Location: Start: 59426; End: 62029 Strand: -

Full Sequence      

MNRTLSIVIALSLSATMTGRGDNYFVDGYHGGIYGHYPLEWKTGFIVDEMHRHPSWRLGL
EIEPETWDSVRSRTPEAYEAFRTLMKEGRMEYTNPTYAQPYCYNILGESLIRQFSYGIRK
LHSHFPGMTFTTYSSEEPCFTSCLPAILKGFGFRYASLKCPNTCWGGYVAPYGGQLVNWE
GPDGTVILTVPRYACENLEPRSVWQTTAWGNSPAYLEACRKAGIKNPAGMCYQDAGWRKG
PWLGADGHGSEYVLWSDYISLHTPGATADTHRFTQDDIRVNLMWGSQVLQRIARQVRRAE
NAMLMAEKIGAIAWGINPGVTPDSAKIDEAWRQLMLAQHHDSWIVPYNRLWNFGTWADAI
EKWTSYAETVARGEILRTAKAVNPGDKLMVKVFNTTALDREEVVEVELPTGFPSEGRGVC
VTDHLGREIHSCVIEHKKNSKTNKKGKDQGIKDCFKIQKLQFKATVPPMGYATYNIARIS
ENKNDVDLGFVPDTPGGGENVRIENDRIMLEINLRNGGTVKSLKLKGKEGYEYAPADTSR
FSLCELRGFFYEEGRFRSSTETPARIIAYEQTPLAQSVTVAGEIGGHPFLQTYRLTKGSA
RVDCSLHIDWQGNPGIGEYRETNWKSDRRGFCDDRYKLCLLLPASFKGERLLKDAPFDSY
ETTYSSNVFNRWSGIKNNIILNWIDVTDREGRVGLGLMTDHTGSYVHDPAYPTALTLQYS
GPGLWGMDYGIKGPLDVDFSIIPHGAGHGADVMADEADRFNEPLQAILCGGSGNAETKSL
LGVDGKGYKVSAAIVNPDGKSMTLRMLNTHADEPCSIGININDALVAETDLRGNVTATPS
SKSKHGVVSMEVRMPRNGFTTYSISRK

Enzyme Prediction     

No EC number prediction in MGYG000001640_00045.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH38	46	190	2.3e-28	0.5241635687732342

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam01074	Glyco_hydro_38	4.29e-13	46	189	32	172	Glycosyl hydrolases family 38 N-terminal domain. Glycosyl hydrolases are key enzymes of carbohydrate metabolism.
cd10789	GH38N_AMII_ER_cytosolic	2.59e-11	50	206	36	191	N-terminal catalytic domain of endoplasmic reticulum(ER)/cytosolic class II alpha-mannosidases; glycoside hydrolase family 38 (GH38). The subfamily is represented by Saccharomyces cerevisiae vacuolar alpha-mannosidase Ams1, rat ER/cytosolic alpha-mannosidase Man2C1, and similar proteins. Members in this family share high sequence similarity. None of them have any classical signal sequence or membrane spanning domains, which are typical of sorting or targeting signals. Ams1 functions as a second resident vacuolar hydrolase in S. cerevisiae. It aids in recycling macromolecular components of the cell through hydrolysis of terminal, non-reducing alpha-d-mannose residues. Ams1 utilizes both the cytoplasm to vacuole targeting (Cvt, nutrient-rich conditions) and autophagic (starvation conditions) pathways for biosynthetic delivery to the vacuole. Man2C1is involved in oligosaccharide catabolism in both the ER and cytosol. It can catalyze the cobalt-dependent cleavage of alpha 1,2-, alpha 1,3-, and alpha 1,6-linked mannose residues. Members in this family are retaining glycosyl hydrolases of family GH38 that employs a two-step mechanism involving the formation of a covalent glycosyl-enzyme complex. Two carboxylic acids positioned within the active site act in concert: one as a catalytic nucleophile and the other as a general acid/base catalyst.
cd10791	GH38N_AMII_like_1	1.99e-09	71	189	63	177	N-terminal catalytic domain of mainly uncharacterized eukaryotic proteins similar to alpha-mannosidases; glycoside hydrolase family 38 (GH38). The subfamily of mainly uncharacterized eukaryotic proteins shows sequence homology with class II alpha-mannosidases (AlphaAMIIs). AlphaAMIIs possess a-1,3, a-1,6, and a-1,2 hydrolytic activity, and catalyze the degradation of N-linked oligosaccharides. The N-terminal catalytic domain of alphaMII adopts a structure consisting of parallel 7-stranded beta/alpha barrel. This subfamily belongs to the GH38 family of retaining glycosyl hydrolases, which employ a two-step mechanism involving the formation of a covalent glycosyl enzyme complex; two carboxylic acids positioned within the active site act in concert: one as a catalytic nucleophile and the other as a general acid/base catalyst.
pfam09261	Alpha-mann_mid	5.36e-09	294	346	15	65	Alpha mannosidase middle domain. Members of this family adopt a structure consisting of three alpha helices, in an immunoglobulin/albumin-binding domain-like fold. They are predominantly found in the enzyme alpha-mannosidase.
smart00872	Alpha-mann_mid	2.49e-08	294	342	14	62	Alpha mannosidase, middle domain. Members of this entry belong to the glycosyl hydrolase family 38, This domain, which is found in the central region adopts a structure consisting of three alpha helices, in an immunoglobulin/albumin-binding domain-like fold. The domain is predominantly found in the enzyme alpha-mannosidase.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QGT73473.1	6.25e-290	24	865	23	852
QDH54455.1	6.25e-290	1	865	1	852
QUT27309.1	1.78e-289	1	865	1	852
QRM98564.1	3.56e-289	1	865	1	852
QUR41760.1	1.44e-288	1	865	1	852

PDB Hits     

has no PDB hit.

Swiss-Prot Hits     

has no Swissprot hit.

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000847	0.997774	0.000645	0.000241	0.000239	0.000226

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001640_00045.