CAZyme Information: MGYG000001548_00686

Basic Information

• Species: Paenibacillus_A tuaregi
• Lineage: Bacteria; Firmicutes; Bacilli; Paenibacillales; Paenibacillaceae; Paenibacillus_A; Paenibacillus_A tuaregi
• CAZyme ID: MGYG000001548_00686
• CAZy Family: SLH
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
917	MGYG000001548_4|CGC11	97700.55	6.3766

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001548	5663842	Isolate	not provided	not provided

• Gene Location: Start: 680235; End: 682988 Strand: +

Full Sequence      

MALYKNDRLGCNMKALQKTRAWQLIVYSLCSALIFSSFALTGKASAQSSDIKGHWAETQL
AEWQSHGLLKGYADGSLKPDNSITRAELIALINRYFNFTEEKAISFSDTKGDKWYHSEIA
KAVQAGYVNGYSDGTIRPDQKVSRQETAVMLARALKLDPAASTGNLNSFKDAAAIASWSK
DAVSTLAGKGVIEGYEDGTYRPNANLTRAEGVVLLSRMSNAQTVTYDKAGTYGPAAGTVT
VLGNVTINAAGTTLQNTVIRGNLLLGKGIENGDVTLKNVKVDGTTTVNGGGESSIHLVNT
VLTKLIVNKLGGVVRIVAEGTSSIQETYVVSSAKLEEAGTGAGFIKVIFAKELPTGSVVT
LTGAFSTLAMEASNIKVEFLKGLVESMTVNGSGNTIHLGKDATIAKLILNATVKVLGFGQ
VQHATVNEGGKGSSFETAPGKVDGPQSGSISSGTSGSNNGGTGGSTGNNGGSAGGGSNNG
GGTDPSGPAAPVVLNVVEGKTYTSGVLPNWTDAAGTTSTATLNGKTYVKGTGITDAGEYA
LVVTASKNGKSASTTVKFKIDPALRIIGYVPGWVDWSDANTVDVAKMTHLNYAFNHIDKD
HKLIPFQGNYHDDQNYAYLSSLKSKNPNLKILNSVGGWGADGFSDAAATPAARETFVNSV
IEHIKKYNLDGVDLDWEYPTQTAGDLIKASPEDKENFTLLLQMVRERLNKLGLENNKYYE
LTICAATASDYPKWVELDKIIPLLDSLNIMTYDLAGGWVQKTAHHTNLYAGRSVDSTVQM
FLDNHVPASKIAIGAAFYAHKWTDVEADGENILDQKAKGSEETPTYNDILTKYNEEHGFI
RHWDEAAKAPYLYNPTTKEFLSYDDPQSLTEKGKYVLDKKLGGVLFWEYSQDKTGALLGA
LYDALQGKAPEPGTNTN

Enzyme Prediction     

No EC number prediction in MGYG000001548_00686.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH18	565	896	3e-76	0.9459459459459459
CBM54	223	334	2.7e-29	0.9385964912280702
SLH	106	146	5.8e-18	0.9523809523809523

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06548	GH18_chitinase	7.26e-116	566	892	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	1.32e-96	565	892	1	334	Glyco_18 domain.
COG3325	ChiA	1.68e-91	541	908	21	439	Chitinase, GH18 family [Carbohydrate transport and metabolism].
pfam00704	Glyco_hydro_18	2.75e-86	565	892	1	307	Glycosyl hydrolases family 18.
cd02872	GH18_chitolectin_chitotriosidase	1.26e-71	588	887	29	336	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QAV16301.1	0.0	13	916	1	817
BAM67143.1	8.77e-229	13	912	1	931
BBH23221.1	1.95e-116	27	458	9	448
QGQ95647.1	1.12e-114	24	442	12	430
ANY66681.1	7.51e-114	23	439	8	431

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5GZT_B	1.02e-123	294	912	1	649	CrystalStructure of Chitinase ChiW from Paenibacillus sp. str. FPU-7 Reveals a Novel Type of Bacterial Cell-Surface-Expressed Multi-Modular Enzyme Machinery [Paenibacillus sp. FPU-7]
5GZU_A	1.08e-98	552	911	503	885	CrystalStructure of Chitinase ChiW from Paenibacillus sp. str. FPU-7 Reveals a Novel Type of Bacterial Cell-Surface-Expressed Multi-Modular Enzyme Machinery [Paenibacillus sp. FPU-7],5GZU_B Crystal Structure of Chitinase ChiW from Paenibacillus sp. str. FPU-7 Reveals a Novel Type of Bacterial Cell-Surface-Expressed Multi-Modular Enzyme Machinery [Paenibacillus sp. FPU-7],5GZV_A Crystal Structure of Chitinase ChiW from Paenibacillus sp. str. FPU-7 Reveals a Novel Type of Bacterial Cell-Surface-Expressed Multi-Modular Enzyme Machinery [Paenibacillus sp. FPU-7],5GZV_B Crystal Structure of Chitinase ChiW from Paenibacillus sp. str. FPU-7 Reveals a Novel Type of Bacterial Cell-Surface-Expressed Multi-Modular Enzyme Machinery [Paenibacillus sp. FPU-7]
6INX_A	3.65e-81	583	906	23	343	Structuralinsights into a novel glycoside hydrolase family 18 N-acetylglucosaminidase from Paenibacillus barengoltzii [Paenibacillus barengoltzii]
6KST_A	9.55e-68	565	905	8	370	Crystalstructure of the catalytic domain of chitinase ChiL from Chitiniphilus shinanonensis (CsChiL) [Chitiniphilus shinanonensis],6KST_B Crystal structure of the catalytic domain of chitinase ChiL from Chitiniphilus shinanonensis (CsChiL) [Chitiniphilus shinanonensis],6KXL_A Crystal structure of the catalytic domain of Chitiniphilus shinanonensis chitinase ChiL (CsChiL) complexed with N,N'-diacetylchitobiose [Chitiniphilus shinanonensis],6KXL_B Crystal structure of the catalytic domain of Chitiniphilus shinanonensis chitinase ChiL (CsChiL) complexed with N,N'-diacetylchitobiose [Chitiniphilus shinanonensis]
1ITX_A	2.55e-67	565	897	13	411	ChainA, Glycosyl Hydrolase [Niallia circulans]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P20533	5.00e-64	565	914	45	456	Chitinase A1 OS=Niallia circulans OX=1397 GN=chiA1 PE=1 SV=1
P32470	5.57e-41	585	896	62	387	Chitinase 1 OS=Aphanocladium album OX=12942 GN=CHI1 PE=1 SV=2
A6N6J0	1.18e-40	585	907	63	407	Endochitinase 46 OS=Trichoderma harzianum OX=5544 GN=chit46 PE=1 SV=1
Q13231	3.50e-39	563	892	21	363	Chitotriosidase-1 OS=Homo sapiens OX=9606 GN=CHIT1 PE=1 SV=1
Q9D7Q1	1.52e-38	563	892	21	361	Chitotriosidase-1 OS=Mus musculus OX=10090 GN=Chit1 PE=1 SV=2

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
0.123499	0.870841	0.003995	0.000813	0.000408	0.000423

TMHMM  Annotations     

start	end
21	40