dbCAN-seq: a database of CAZyme sequence and annotation

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CAZyme Information: MGYG000003948_00668

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Basic Information help

Species

Lineage

Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Rikenellaceae; Alistipes;

CAZyme ID

MGYG000003948_00668

CAZy Family

GH18

CAZyme Description

hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
819	MGYG000003948_12\|CGC1	91890.54	6.297

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003948	2150232	MAG	United Kingdom	Europe

Gene Location

Start: 10752; End: 13211 Strand: +

Full Sequence Download help

Enzyme Prediction help

No EC number prediction in MGYG000003948_00668.

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
GH18	35	333	1.9e-72	0.956081081081081

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06548	GH18_chitinase	2.84e-94	37	327	1	322	The GH18 (glycosyl hydrolases, family 18) type II chitinases hydrolyze chitin, an abundant polymer of N-acetylglucosamine and have been identified in bacteria, fungi, insects, plants, viruses, and protozoan parasites. The structure of this domain is an eight-stranded alpha/beta barrel with a pronounced active-site cleft at the C-terminal end of the beta-barrel.
smart00636	Glyco_18	3.77e-76	36	327	1	334	Glyco_18 domain.
pfam00704	Glyco_hydro_18	4.49e-74	36	327	1	307	Glycosyl hydrolases family 18.
cd02872	GH18_chitolectin_chitotriosidase	5.70e-67	37	326	1	345	This conserved domain family includes a large number of catalytically inactive chitinase-like lectins (chitolectins) including YKL-39, YKL-40 (HCGP39), YM1, oviductin, and AMCase (acidic mammalian chitinase), as well as catalytically active chitotriosidases. The conserved domain is an eight-stranded alpha/beta barrel fold belonging to the family 18 glycosyl hydrolases. The fold has a pronounced active-site cleft at the C-terminal end of the beta-barrel. The chitolectins lack a key active site glutamate (the proton donor required for hydrolytic activity) but retain highly conserved residues involved in oligosaccharide binding. Chitotriosidase is a chitinolytic enzyme expressed in maturing macrophages, which suggests that it plays a part in antimicrobial defense. Chitotriosidase hydrolyzes chitotriose, as well as colloidal chitin to yield chitobiose and is therefore considered an exochitinase. Chitotriosidase occurs in two major forms, the large form being converted to the small form by either RNA or post-translational processing. Although the small form, containing the chitinase domain alone, is sufficient for the chitinolytic activity, the additional C-terminal chitin-binding domain of the large form plays a role in processing colloidal chitin. The chitotriosidase gene is nonessential in humans, as about 35% of the population are heterozygous and 6% homozygous for an inactivated form of the gene. HCGP39 is a 39-kDa human cartilage glycoprotein thought to play a role in connective tissue remodeling and defense against pathogens.
COG3325	ChiA	3.25e-58	25	340	28	435	Chitinase, GH18 family [Carbohydrate transport and metabolism].

CAZyme Hits help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QMI79098.1	1.23e-248	18	583	18	573
QUT64703.1	2.48e-248	8	580	3	570
QUT62465.1	3.87e-248	16	580	9	563
QQA31016.1	4.97e-248	16	580	16	570
QUU00240.1	1.41e-247	8	580	3	570

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4JQS_A	1.23e-90	584	816	8	241	Crystalstructure of a Putative thua-like protein (BACUNI_01602) from Bacteroides uniformis ATCC 8492 at 2.30 A resolution [Bacteroides uniformis ATCC 8492],4JQS_B Crystal structure of a Putative thua-like protein (BACUNI_01602) from Bacteroides uniformis ATCC 8492 at 2.30 A resolution [Bacteroides uniformis ATCC 8492],4JQS_C Crystal structure of a Putative thua-like protein (BACUNI_01602) from Bacteroides uniformis ATCC 8492 at 2.30 A resolution [Bacteroides uniformis ATCC 8492],4PXY_A Crystal structure of a Putative thua-like protein (BACUNI_01602) from Bacteroides uniformis ATCC 8492 at 1.50 A resolution [Bacteroides uniformis ATCC 8492],4PXY_B Crystal structure of a Putative thua-like protein (BACUNI_01602) from Bacteroides uniformis ATCC 8492 at 1.50 A resolution [Bacteroides uniformis ATCC 8492]
6INX_A	1.38e-57	54	341	27	342	Structuralinsights into a novel glycoside hydrolase family 18 N-acetylglucosaminidase from Paenibacillus barengoltzii [Paenibacillus barengoltzii]
4NZC_A	5.42e-52	50	330	30	386	Crystalstructure of Chitinase D from Serratia proteamaculans at 1.45 Angstrom resolution [Serratia proteamaculans 568],4Q22_A Crystal structure of Chitinase D from Serratia proteamaculans in complex with N-acetyl glucosamine at 1.93 Angstrom resolution [Serratia proteamaculans 568]
6HM1_A	5.69e-52	50	330	27	383	Structuraland thermodynamic signatures of ligand binding to an enigmatic chitinase-D from Serratia proteamaculans [Serratia proteamaculans 568]
4PTM_A	6.12e-52	50	330	30	386	CrystalStructure of Chitinase D from Serratia proteamaculans in complex with N-acetyl glucosamine, a hydrolyzed product of hexasaccharide at 1.7 Angstrom resolution [Serratia proteamaculans 568]

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P20533	2.79e-42	31	327	40	438	Chitinase A1 OS=Niallia circulans OX=1397 GN=chiA1 PE=1 SV=1
Q13231	1.77e-34	37	326	24	367	Chitotriosidase-1 OS=Homo sapiens OX=9606 GN=CHIT1 PE=1 SV=1
P32470	5.29e-34	55	332	85	388	Chitinase 1 OS=Aphanocladium album OX=12942 GN=CHI1 PE=1 SV=2
Q5AM60	5.73e-33	55	327	49	355	Chitinase 4 OS=Candida albicans (strain SC5314 / ATCC MYA-2876) OX=237561 GN=CHT4 PE=3 SV=1
P48827	1.44e-32	55	332	85	388	Endochitinase 42 OS=Trichoderma harzianum OX=5544 GN=chit42 PE=1 SV=1

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
0.000791	0.998308	0.000336	0.000194	0.000168	0.000162

TMHMM Annotations download full data without filtering help

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