dbCAN-seq: a database of CAZyme sequence and annotation

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CAZyme Information: MGYG000004464_00202

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Basic Information help

Species

Barnesiella sp900542255

Lineage

Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Barnesiellaceae; Barnesiella; Barnesiella sp900542255

CAZyme ID

MGYG000004464_00202

CAZy Family

GH36

CAZyme Description

hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
755	MGYG000004464_2\|CGC1	83653.42	4.6016

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004464	2487387	MAG	Israel	Asia

Gene Location

Start: 79233; End: 81500 Strand: +

Full Sequence Download help

Enzyme Prediction help

No EC number prediction in MGYG000004464_00202.

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd14791	GH36	4.62e-15	281	570	1	297	glycosyl hydrolase family 36 (GH36). GH36 enzymes occur in prokaryotes, eukaryotes, and archaea with a wide range of hydrolytic activities, including alpha-galactosidase, alpha-N-acetylgalactosaminidase, stachyose synthase, and raffinose synthase. All GH36 enzymes cleave a terminal carbohydrate moiety from a substrate that varies considerably in size, depending on the enzyme, and may be either a starch or a glycoprotein. GH36 members are retaining enzymes that cleave their substrates via an acid/base-catalyzed, double-displacement mechanism involving a covalent glycosyl-enzyme intermediate. Two aspartic acid residues have been identified as the catalytic nucleophile and the acid/base, respectively.
pfam17801	Melibiase_C	7.34e-07	606	669	14	74	Alpha galactosidase C-terminal beta sandwich domain. This domain is found at the C-terminus of alpha galactosidase enzymes.
cd14792	GH27	3.78e-06	283	524	2	214	glycosyl hydrolase family 27 (GH27). GH27 enzymes occur in eukaryotes, prokaryotes, and archaea with a wide range of hydrolytic activities, including alpha-glucosidase (glucoamylase and sucrase-isomaltase), alpha-N-acetylgalactosaminidase, and 3-alpha-isomalto-dextranase. All GH27 enzymes cleave a terminal carbohydrate moiety from a substrate that varies considerably in size, depending on the enzyme, and may be either a starch or a glycoprotein. GH27 members are retaining enzymes that cleave their substrates via an acid/base-catalyzed, double-displacement mechanism involving a covalent glycosyl-enzyme intermediate. Two aspartic acid residues have been identified as the catalytic nucleophile and the acid/base, respectively.
TIGR04183	Por_Secre_tail	2.64e-04	696	755	12	71	Por secretion system C-terminal sorting domain. Species that include Porphyromonas gingivalis, Fibrobacter succinogenes, Flavobacterium johnsoniae, Cytophaga hutchinsonii, Gramella forsetii, Prevotella intermedia, and Salinibacter ruber average twenty or more copies of a C-terminal domain, represented by this model, associated with sorting to the outer membrane and covalent modification.

CAZyme Hits help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AII66839.1	5.06e-186	22	669	31	673
ALA72670.1	5.06e-186	22	669	31	673
QJR53686.1	5.06e-186	22	669	31	673
QJR61515.1	5.06e-186	22	669	31	673
AND18605.1	1.01e-185	22	669	31	673

PDB Hits help

has no PDB hit.

Swiss-Prot Hits help

has no Swissprot hit.

SignalP and Lipop Annotations help

This protein is predicted as SP

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000497	0.732691	0.266006	0.000285	0.000271	0.000228

TMHMM Annotations help

There is no transmembrane helices in MGYG000004464_00202.