CAZyme Information: EPrPIT00000013775-p1

Basic Information

• Species: Globisporangium irregulare
• Lineage: Oomycota; NA; ; Pythiaceae; Globisporangium; Globisporangium irregulare
• CAZyme ID: EPrPIT00000013775-p1
• CAZy Family: AA17
• CAZyme Description: Di-N-acetylchitobiase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
412		46535.84	5.2547

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_GirregulareDAOMBR486	13869	1223557	65	13804

• Gene Location: location=PirrDAOMBR486_SC0019:60934-62610(-)

Full Sequence      

MELFRWHLPLPLPLLLLCLLLAGHIVHASVYVPHRFPLQLLNAFERSALRACPCEKQEQC
LPVAGTGATAASQREDSRKKEVFAFSVTTTDQWKRYDWEQLTTVAWNEDKELLCHAHSKG
VKVVIKHNFDDVETLCDPQFRKQWIQKTYGRIVNNYADGVNIDTEKAMHGDAAKCMTTLV
QELRQELLQHAFTQHAQITFDVSWAPRGVDGRYYQWKELADAVDFLFVMSYDMRSQIYYQ
CLAAANSPLALVKQGLEEFIFGFGVAPEKLVLGVPWYGYKYTCANVGSQFCLLEPTSFFG
APCSDAAGAQVNFGDIETLIAREKLPMQWDEMTQSPFVVSKNGSFQIWFDNPHSLTLKYQ
LVKELGLRGAGMWNADTLDYASNADDDGADDDGDGARAHETQAMWQALHAIS

Enzyme Prediction     

EC	3.2.1.-:18

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH18	91	377	1.6e-37	0.7804054054054054

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
119354	GH18_chitobiase	2.65e-117	36	408	3	358	Chitobiase (also known as di-N-acetylchitobiase) is a lysosomal glycosidase that hydrolyzes the reducing-end N-acetylglucosamine from the chitobiose core of oligosaccharides during the ordered degradation of asparagine-linked glycoproteins in eukaryotes. Chitobiase can only do so if the asparagine that joins the oligosaccharide to protein is previously removed by a glycosylasparaginase. Chitobiase is therefore the final step in the lysosomal degradation of the protein/carbohydrate linkage component of asparagine-linked glycoproteins. The catalytic domain of chitobiase is an eight-stranded alpha/beta barrel fold similar to that of other family 18 glycosyl hydrolases such as hevamine and chitotriosidase.
214753	Glyco_18	6.50e-32	82	377	30	333	Glyco_18 domain.
395573	Glyco_hydro_18	2.54e-27	82	376	27	305	Glycosyl hydrolases family 18.
119353	GH18_CFLE_spore_hydrolase	2.70e-21	116	373	54	300	Cortical fragment-lytic enzyme (CFLE) is a peptidoglycan hydrolase involved in bacterial endospore germination. CFLE is expressed as an inactive preprotein (called SleB) in the forespore compartment of sporulating cells. SleB translocates across the forespore inner membrane and is deposited as a mature enzyme in the cortex layer of the spore. As part of a sensory mechanism capable of initiating germination, CFLE degrades a spore-specific peptidoglycan constituent called muramic-acid delta-lactam that comprises the outer cortex. CFLE has a C-terminal glycosyl hydrolase family 18 (GH18) catalytic domain as well as two N-terminal LysM peptidoglycan-binding domains. In addition to SleB, this family includes YaaH, YdhD, and YvbX from Bacillus subtilis.
226376	YaaH	1.12e-18	158	373	209	405	Spore germination protein YaaH [Cell cycle control, cell division, chromosome partitioning].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
UIZ27644.1|GH18	2.61e-144	19	408	432	833
CCA16750.1|GH18	1.64e-128	42	411	25	384
CCA27450.1|GH18	4.64e-126	48	411	2	355
AIG55971.1|GH18	5.29e-111	42	408	17	381
XP_422372.2|GH18	1.59e-85	38	408	13	362

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6JM7_A	1.83e-13	137	380	98	352	Crystal structure of Ostrinia furnacalis Group IV chitinase [Ostrinia furnacalis],6JMB_A Chain A, ofchtiv-allosamidin [Ostrinia furnacalis]
6JM8_A	5.85e-13	137	380	98	352	Crystal structure of Ostrinia furnacalis Group IV chitinase [Ostrinia furnacalis]
4P8U_A	3.00e-12	177	384	137	352	The crystal structures of YKL-39 in the absence of chitooligosaccharides was solved to resolutions of 2.4 angstrom [Homo sapiens],4P8V_A The crystal structures of YKL-39 in the presence of chitooligosaccharides (GlcNAc2) were solved to resolutions of 1.5 angstrom [Homo sapiens],4P8W_A The crystal structures of YKL-39 in the presence of chitooligosaccharides (GlcNAc4) were solved to resolutions of 1.9 angstrom [Homo sapiens],4P8X_A The crystal structures of YKL-39 in the presence of chitooligosaccharides (GlcNAc6) were solved to resolutions of 2.48 angstrom [Homo sapiens]
4AY1_A	9.29e-12	177	384	131	346	Human YKL-39 is a pseudo-chitinase with retained chitooligosaccharide binding properties [Homo sapiens],4AY1_B Human YKL-39 is a pseudo-chitinase with retained chitooligosaccharide binding properties [Homo sapiens],4AY1_C Human YKL-39 is a pseudo-chitinase with retained chitooligosaccharide binding properties [Homo sapiens],4AY1_D Human YKL-39 is a pseudo-chitinase with retained chitooligosaccharide binding properties [Homo sapiens],4AY1_E Human YKL-39 is a pseudo-chitinase with retained chitooligosaccharide binding properties [Homo sapiens],4AY1_F Human YKL-39 is a pseudo-chitinase with retained chitooligosaccharide binding properties [Homo sapiens],4AY1_G Human YKL-39 is a pseudo-chitinase with retained chitooligosaccharide binding properties [Homo sapiens],4AY1_H Human YKL-39 is a pseudo-chitinase with retained chitooligosaccharide binding properties [Homo sapiens],4AY1_I Human YKL-39 is a pseudo-chitinase with retained chitooligosaccharide binding properties [Homo sapiens],4AY1_J Human YKL-39 is a pseudo-chitinase with retained chitooligosaccharide binding properties [Homo sapiens],4AY1_K Human YKL-39 is a pseudo-chitinase with retained chitooligosaccharide binding properties [Homo sapiens],4AY1_L Human YKL-39 is a pseudo-chitinase with retained chitooligosaccharide binding properties [Homo sapiens]
3WL1_A	5.92e-10	158	380	123	361	Crystal structure of Ostrinia furnacalis Group I chitinase catalytic domain in complex with reaction products (GlcNAc)2,3 [Ostrinia furnacalis],3WQV_A Crystal structure of Ostrinia furnacalis Group I chitinase catalytic domain in complex with a(GlcN)5 [Ostrinia furnacalis],3WQW_A Crystal structure of Ostrinia furnacalis Group I chitinase catalytic domain in complex with a(GlcN)6 [Ostrinia furnacalis]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q8R242|DIAC_MOUSE	4.74e-85	36	408	9	362	Di-N-acetylchitobiase OS=Mus musculus OX=10090 GN=Ctbs PE=1 SV=2
sp|Q01460|DIAC_RAT	9.76e-85	38	408	12	363	Di-N-acetylchitobiase OS=Rattus norvegicus OX=10116 GN=Ctbs PE=1 SV=1
sp|Q01459|DIAC_HUMAN	1.17e-81	52	408	41	378	Di-N-acetylchitobiase OS=Homo sapiens OX=9606 GN=CTBS PE=1 SV=1
sp|Q7KWW8|DIAC1_DICDI	1.11e-56	46	378	17	352	Probable di-N-acetylchitobiase 1 OS=Dictyostelium discoideum OX=44689 GN=ctbs1 PE=3 SV=1
sp|Q8T293|DIAC2_DICDI	1.23e-54	52	408	26	370	Probable di-N-acetylchitobiase 2 OS=Dictyostelium discoideum OX=44689 GN=ctbs2 PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000310	0.999672	CS pos: 28-29. Pr: 0.9708

TMHMM  Annotations     

Start	End
12	34