CAZyme Information: PIW_T003567-RA-p1

Basic Information

• Species: Globisporangium iwayamae
• Lineage: Oomycota; NA; ; Pythiaceae; Globisporangium; Globisporangium iwayamae
• CAZyme ID: PIW_T003567-RA-p1
• CAZy Family: GH1
• CAZyme Description: Di-N-acetylchitobiase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
401		45445.44	6.2330

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_GiwayamaeDAOMBR242034	14874	1223558	0	14874

• Gene Location: location=PiwaDAOMBR242034_SC00394:16924-18560(+)

Full Sequence      

MTRPRRRSRGLLLLLSLWALYADARAVVFSYQSFPAQQQQPLSVFERTALRSCPCEKPEL
CLPIADIGANARKEVFAFSVTTSDQWKLYDWNQLTTVAWNEDKELLCHAHSKDVKIVIKH
NFDDVEKLCDAQFRNQWVQETYKRIVNSFADGVNIDTEKAMHGATAKCMTTLVQELRREL
QQHAFTQHAQITFDVSWAPRGVDGRYYQWKELADAVDFLFVMSYDMRSQIYYQCIAAANS
PLALVKQGLEEFIFGFSIAPEKLVLGVPWYGYKYACVESDGSSAGSRFCSMNPTPFFGAP
CSDAAGQQVDYGDIEKLIEREKSPVQWDAVTQSPFVTSANGSYQIWFDNPQSLRLKYQLV
RELGLRGAGMWNADTLDYASSGSGAHAHETQAMWQALHAIT

Enzyme Prediction     

EC	3.2.1.-:18

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH18	84	374	2.9e-38	0.777027027027027

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
119354	GH18_chitobiase	1.20e-121	41	397	7	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	7.84e-33	130	375	88	333	Glyco_18 domain.
395573	Glyco_hydro_18	8.61e-28	75	374	27	305	Glycosyl hydrolases family 18.
119353	GH18_CFLE_spore_hydrolase	8.74e-23	151	371	105	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	1.96e-18	151	371	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	2.28e-151	42	397	456	833
CCA16750.1|GH18	1.48e-131	43	400	25	384
CCA27450.1|GH18	2.07e-129	49	400	2	355
AIG55971.1|GH18	6.08e-115	45	397	19	381
BAE00476.1|GH18	2.43e-86	53	397	38	375

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6JM7_A	1.32e-11	130	378	98	352	Crystal structure of Ostrinia furnacalis Group IV chitinase [Ostrinia furnacalis],6JMB_A Chain A, ofchtiv-allosamidin [Ostrinia furnacalis]
3CZ8_A	1.59e-11	134	371	96	306	Chain A, Putative sporulation-specific glycosylase ydhD [Bacillus subtilis subsp. subtilis str. 168],3CZ8_B Chain B, Putative sporulation-specific glycosylase ydhD [Bacillus subtilis subsp. subtilis str. 168]
6JM8_A	4.18e-11	130	378	98	352	Crystal structure of Ostrinia furnacalis Group IV chitinase [Ostrinia furnacalis]
4P8U_A	3.85e-10	170	378	137	348	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]
1E9L_A	9.32e-10	132	381	93	349	The crystal structure of novel mammalian lectin Ym1 suggests a saccharide binding site [Mus musculus],1VF8_A The Crystal Structure of Ym1 at 1.31 A Resolution [Mus musculus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q01459|DIAC_HUMAN	7.48e-86	53	397	41	378	Di-N-acetylchitobiase OS=Homo sapiens OX=9606 GN=CTBS PE=1 SV=1
sp|Q8R242|DIAC_MOUSE	8.40e-86	42	397	14	362	Di-N-acetylchitobiase OS=Mus musculus OX=10090 GN=Ctbs PE=1 SV=2
sp|Q01460|DIAC_RAT	5.47e-84	42	397	15	363	Di-N-acetylchitobiase OS=Rattus norvegicus OX=10116 GN=Ctbs PE=1 SV=1
sp|Q8T293|DIAC2_DICDI	8.85e-68	53	397	26	370	Probable di-N-acetylchitobiase 2 OS=Dictyostelium discoideum OX=44689 GN=ctbs2 PE=3 SV=1
sp|Q7KWW8|DIAC1_DICDI	3.58e-59	51	400	21	369	Probable di-N-acetylchitobiase 1 OS=Dictyostelium discoideum OX=44689 GN=ctbs1 PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000345	0.999628	CS pos: 26-27. Pr: 0.6291

TMHMM  Annotations     

There is no transmembrane helices in PIW_T003567-RA-p1.