CAZyme Information: CC1G_01315-t26_1-p1

Basic Information

• Species: Coprinopsis cinerea
• Lineage: Basidiomycota; Agaricomycetes; ; Psathyrellaceae; Coprinopsis; Coprinopsis cinerea
• CAZyme ID: CC1G_01315-t26_1-p1
• CAZy Family: AA3
• CAZyme Description: endochitinase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
425		45773.34	7.7486

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_Ccinereaokay7-130	13657	240176	301	13356

• Gene Location: location=AACS02000005:2139308-2140861(+)

Full Sequence      

MVSFRLSLLGPWCLVALLSTLVVASPAAVEGKTRGKVAAAWYAGWHATTGYPLSRVSWKK
YTHLTYAFAETSPDVHKLSFEEATWTNPQLLPQFVSEAHKHGVKALISIGGWTGSRFFST
AVGSASNRTAFVKTVVNFAQKYHLDGVDFDWEYPGNQGIGCNTINPQDTSNFLLFLQELR
RDPVGSKLLVTAAAATVPFYGSNGRPSSDVAAFAKLLDYIAIMNYDLWGPWSPTVGPNAP
LDDACAPANSRYGSATSAVRQWSAAGIPHNQLVLGVAAYGHGFRVRRANAFAAGSNSVLA
SYPPFDGVDRPIGDSWDGPGGGTDVCGSPTLPGGTFNFWGLIENGFLNKDGSPTQGIHYR
YDTCSQTPYVYNRTTEIMVAFDNAQSFAAKGNFIKSNGLRGFATWEAGGDYNDILLDSIR
KAGGY

Enzyme Prediction     

EC	3.2.1.14:2

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH18	38	412	5.3e-70	0.9358108108108109

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
214753	Glyco_18	2.34e-82	42	410	6	334	Glyco_18 domain.
395573	Glyco_hydro_18	1.72e-70	42	410	6	307	Glycosyl hydrolases family 18.
119365	GH18_chitinase	1.11e-68	39	410	2	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.
119351	GH18_chitolectin_chitotriosidase	4.79e-62	62	405	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.
225862	ChiA	8.62e-62	18	425	15	438	Chitinase, GH18 family [Carbohydrate transport and metabolism].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CAQ51152.1|GH18|3.2.1.14	1.69e-201	26	425	41	437
ABB90389.1|GH18	1.34e-166	33	424	35	420
QRV99381.1|GH18	2.58e-157	33	425	40	426
QRW13886.1|GH18	2.58e-157	33	425	40	426
QRV85311.1|GH18	2.58e-157	33	425	40	426

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5XWF_A	1.28e-51	56	423	17	372	Chain A, Fungal chitinase from Rhizomucor miehei (SeMet-substituted proteins) [Rhizomucor miehei]
1ITX_A	1.51e-42	103	420	123	416	Chain A, Glycosyl Hydrolase [Niallia circulans]
6BT9_A	7.69e-38	103	410	158	448	Chitinase ChiA74 from Bacillus thuringiensis [Bacillus thuringiensis],6BT9_B Chitinase ChiA74 from Bacillus thuringiensis [Bacillus thuringiensis]
3FXY_A	6.17e-35	62	405	31	339	Acidic Mammalian Chinase, Catalytic Domain [Homo sapiens],3FXY_B Acidic Mammalian Chinase, Catalytic Domain [Homo sapiens],3FXY_C Acidic Mammalian Chinase, Catalytic Domain [Homo sapiens],3FXY_D Acidic Mammalian Chinase, Catalytic Domain [Homo sapiens],3FY1_A The Acidic Mammalian Chitinase catalytic domain in complex with methylallosamidin [Homo sapiens],3FY1_B The Acidic Mammalian Chitinase catalytic domain in complex with methylallosamidin [Homo sapiens],3RM4_A AMCase in complex with Compound 1 [Homo sapiens],3RM4_B AMCase in complex with Compound 1 [Homo sapiens],3RM8_A AMCase in complex with Compound 2 [Homo sapiens],3RM8_B AMCase in complex with Compound 2 [Homo sapiens],3RM9_A AMCase in complex with Compound 3 [Homo sapiens],3RM9_B AMCase in complex with Compound 3 [Homo sapiens],3RME_A AMCase in complex with Compound 5 [Homo sapiens],3RME_B AMCase in complex with Compound 5 [Homo sapiens]
2YBT_A	6.65e-35	62	405	35	343	Crystal structure of human acidic chitinase in complex with bisdionin C [Homo sapiens],2YBT_B Crystal structure of human acidic chitinase in complex with bisdionin C [Homo sapiens],2YBT_C Crystal structure of human acidic chitinase in complex with bisdionin C [Homo sapiens],2YBT_D Crystal structure of human acidic chitinase in complex with bisdionin C [Homo sapiens],2YBT_E Crystal structure of human acidic chitinase in complex with bisdionin C [Homo sapiens],2YBT_F Crystal structure of human acidic chitinase in complex with bisdionin C [Homo sapiens],2YBU_A Crystal structure of human acidic chitinase in complex with bisdionin F [Homo sapiens],2YBU_B Crystal structure of human acidic chitinase in complex with bisdionin F [Homo sapiens],2YBU_C Crystal structure of human acidic chitinase in complex with bisdionin F [Homo sapiens],2YBU_D Crystal structure of human acidic chitinase in complex with bisdionin F [Homo sapiens],2YBU_E Crystal structure of human acidic chitinase in complex with bisdionin F [Homo sapiens],2YBU_F Crystal structure of human acidic chitinase in complex with bisdionin F [Homo sapiens]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|P20533|CHIA1_NIACI	2.70e-40	103	420	155	448	Chitinase A1 OS=Niallia circulans OX=1397 GN=chiA1 PE=1 SV=1
sp|A6N6J0|CHI46_TRIHA	5.66e-34	14	422	12	404	Endochitinase 46 OS=Trichoderma harzianum OX=5544 GN=chit46 PE=1 SV=1
sp|Q95M17|CHIA_BOVIN	1.03e-33	62	405	52	360	Acidic mammalian chitinase OS=Bos taurus OX=9913 GN=CHIA PE=1 SV=1
sp|Q9BZP6|CHIA_HUMAN	2.06e-33	62	405	52	360	Acidic mammalian chitinase OS=Homo sapiens OX=9606 GN=CHIA PE=1 SV=1
sp|Q91XA9|CHIA_MOUSE	5.13e-33	62	405	52	360	Acidic mammalian chitinase OS=Mus musculus OX=10090 GN=Chia PE=1 SV=2

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000322	0.999645	CS pos: 24-25. Pr: 0.9827

TMHMM  Annotations     

Start	End
7	29