CAZyme Information: SAPIO_CDS1773-t41_1-p1

Basic Information

• Species: Scedosporium apiospermum
• Lineage: Ascomycota; Sordariomycetes; ; Microascaceae; Scedosporium; Scedosporium apiospermum
• CAZyme ID: SAPIO_CDS1773-t41_1-p1
• CAZy Family: AA9
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1249		135221.39	5.0313

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_SapiospermumIHEM14462	10920	N/A	2544	8376

• Gene Location: location=JOWA01000077:399819-403999(+)

Full Sequence      

MTPSSLLATLCVAASSVAAHGFVLSSPLKACPVPCSQAKLRDNWSVYNSLDRLKFCPLPI
LFDTSLYTSLDNPGQTFSIRACSVGNLPEKNATMAEDAPGILVLKSGVGTQRIATPAACS
NKASDAKAKAQLIPWSDGGSNSVGIGVAVSAVRDFIKDNHRCEASTAVFSYYEGVVVGAY
AGSKITADSAASSLQIKGPQLLQICGDGRNSEHVLGIAVDTEADFRRMQEAVKSWNEATC
VQSGRDGGSSVSEVTLSVYPEGVSGRESLTRRLMPRWLERRADCRTIQVVSGDGCASLAS
RCGISGNDFTKYNPKAGLCATLAVGQYVCCSAGTLPDMTPKPGADATSHQITVDNLVSFN
NKKSNTGNPPMPAPISNAVCGPTMPGTVQPSDGRNISTLNPCPLKVCCNVWGQCGMDKDF
CVISPSSSGNPGTSAPGKDSCISNCGMDILMNTGPPSEWRAVGYFEAWNGNRPCLHMDVD
QPPSQEYTTIHFSFAVIAPGTWDVVIPPDSQHQFDLFVTREMPGNKKVLAFGGWTFSTDP
STYKIFRDVVLPGNRDVFARKVVDFINQHNLDGVDLDWEYPGAPDLPRFDPGGPNEGFNY
LITLLTIKSMLPAGKTLSIGAPASYWYLKAFPIEAISAVVDYIVYMTYDLHGQWDYDNRW
ASPGCPEGNCLRSHINITETKLALAMITKAGVPNNKIMVGVSSYARTFKMVDGNCAGPNC
HFVGPESAAEKGSCTDTAGYISNAEIYSIAANDRVTWSESHLMNVDTSMTDIIVYDGDQW
VAFMLPINKWFRVGIYSDLNFGGVADWAIDLRVFDEGRIGDPDPDGEANIQIGCDETFNS
LEDIDKAKDKLTTACRSVYVLRLLSKMQRSALDSYNDLMAHGYDHKYDLYRDQVKKLAPA
ALAAFIKKRGNDFFDCYVEEQMLCCDWCEPRYGKAKCRYCDRTCSGYRDTTRFMHELCPP
NVSQRGVLVLYLEQATARYNVRWTLKPGKQDAFLAAALSEANIPNDWIGMVKDQQAPVPC
AGIWDCECGPSANPETCEHTGYWYNAPYIARTDDDGVSNPKDFVQEAVSKQGDIGTTKEE
LADQIEAYFYMGEASISDIIEAAALPILMLDEAVSTMKEVAKIGEEIDEKNQKNFIILLL
TSLLMLVPFVGQTVGTIARLGTLARTLALIGEAGQAALDIYSIVDNPDNAPLAIFGLVLG
AGALRDITKVAPAAKAARGTKADDLAKLGGRVESRMNAVKSIAGHSCAR

Enzyme Prediction     

EC	3.2.1.14:3	3.2.1.14:3	3.2.1.14:3

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH18	460	810	1.3e-43	0.9256756756756757

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
119357	GH18_zymocin_alpha	0.0	460	811	1	344	Zymocin, alpha subunit. Zymocin is a heterotrimeric enzyme that inhibits yeast cell cycle progression. The zymocin alpha subunit has a chitinase activity that is essential for holoenzyme action from the cell exterior while the gamma subunit contains the intracellular toxin responsible for G1 phase cell cycle arrest. The zymocin alpha and beta subunits are thought to act from the cell's exterior by docking to the cell wall-associated chitin, thus mediating gamma-toxin translocation. The alpha subunit has an eight-stranded TIM barrel fold similar to that of family 18 glycosyl hydrolases such as hevamine, chitolectin, and chitobiase.
214753	Glyco_18	9.34e-50	460	811	1	333	Glyco_18 domain.
395573	Glyco_hydro_18	1.17e-46	460	810	1	305	Glycosyl hydrolases family 18.
119365	GH18_chitinase	4.60e-38	462	709	2	267	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	2.00e-34	523	811	69	340	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
UKZ79373.1|CBM18|CBM50|GH18	9.44e-275	20	1249	24	1283
QGA18426.1|CBM18|CBM50|GH18	1.02e-258	26	1249	25	1313
UPK95779.1|CBM18|CBM50|GH18	2.88e-241	19	1205	21	1209
UKZ82482.1|CBM18|CBM50|GH18	3.34e-239	133	1247	65	1279
QGA13088.1|CBM18|CBM50|GH18	1.04e-233	31	1249	60	1294

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3WL1_A	2.79e-28	457	814	5	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]
3WKZ_A	6.82e-28	457	814	5	361	Crystal Structure of the Ostrinia furnacalis Group I Chitinase catalytic domain E148Q mutant [Ostrinia furnacalis]
5Y29_A	1.66e-27	457	811	5	350	Crystal structure of Ostrinia furnacalis Group II chitinase catalytic domain 1 [Ostrinia furnacalis],5Y2B_A Crystal structure of Ostrinia furnacalis Group II chitinase catalytic domain 1 in complex with HEPTA-N-ACETYLCHITOOCTAOSE (NAG)7 [Ostrinia furnacalis]
3WL0_A	1.67e-27	457	814	5	361	Crystal structure of Ostrinia furnacalis Group I chitinase catalytic domain E148A mutant in complex with a(GlcNAc)2 [Ostrinia furnacalis]
3W4R_A	1.99e-27	457	814	23	379	Crystal structure of an insect chitinase from the Asian corn borer, Ostrinia furnacalis [Ostrinia furnacalis]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|P09805|KTXA_KLULA	1.57e-80	299	816	205	716	Killer toxin subunits alpha/beta OS=Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) OX=284590 PE=1 SV=1
sp|P36362|CHIT_MANSE	4.28e-26	457	824	21	386	Endochitinase OS=Manduca sexta OX=7130 PE=2 SV=1
sp|Q95M17|CHIA_BOVIN	8.52e-24	446	814	9	367	Acidic mammalian chitinase OS=Bos taurus OX=9913 GN=CHIA PE=1 SV=1
sp|Q9W5U2|CHI10_DROME	2.20e-23	453	814	1899	2255	Probable chitinase 10 OS=Drosophila melanogaster OX=7227 GN=Cht10 PE=2 SV=2
sp|Q6RY07|CHIA_RAT	6.61e-22	446	814	9	367	Acidic mammalian chitinase OS=Rattus norvegicus OX=10116 GN=Chia PE=2 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
0.667538	0.332471

TMHMM  Annotations     

There is no transmembrane helices in SAPIO_CDS1773-t41_1-p1.