CAZyme Information: SAPIO_CDS6627-t41_1-p1

Basic Information

• Species: Scedosporium apiospermum
• Lineage: Ascomycota; Sordariomycetes; ; Microascaceae; Scedosporium; Scedosporium apiospermum
• CAZyme ID: SAPIO_CDS6627-t41_1-p1
• CAZy Family: GH47
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1127	JOWA01000105|CGC2	125805.93	4.6759

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=JOWA01000105:207920-213053(-)

Full Sequence      

MAAPVDSKMLTAEANVLPTVMLNPNAANTRTRPARNVHSMCAVVHGVFAVIQSPSGQHGS
DVRDLVIGYWESWNLLSRGCAQRDLSHIRVDSLTHINVAFGFITPETYEIHPIRGASIAG
FQSVTNLKQHAPGLKVWLALGGWTFSDNGTDTQPVFGDLSSTPEKRQIFIDRLMTFMLEW
GFDGVDLDWEYPGAPDRGGQDRDVQNFVYLMKDIHDRFALDGRGWGVSFTAPTSFWYMRW
FDIGNLHPYVDWINLMTYDIYQKDQWVSYDDEHTIQKKVEFANDLGLRGLFIWAIDQDTY
ENSLLDAVLQPDGLGKFRDVNGAVGDGQDWRTVDLDGSCFWSNCDGSCPPGTNIITTVRC
PWFPKSSVNKPYQHLCCPMNNSPDPESCRWSAPTLFGGLECEQTNSCRVGEFRIATSQYY
KNSEGKDRACSFVGEADYCCEIEEGGTKLCEWDEGNCIDIDMSTRKPAGSDPCGPGKKFA
TFRKGRKCRSGYEALCCEGDVDMSSCVWRANPFDGCNPDCYGNEVSFGRHEMGGGIECRQ
KAPAGLSPPNLQADLIFWPQLCCDADDLRVKIRDLLVPLENLFPDHDEILESDKQTFAIQ
VDESMGGKRRPSGSDDPDANSFGWHIMSGPEEDISSLDKRDGSHWEVFDCDEEAHEGRQT
AKIVCTDESDESNCGVIFKGGVPDTVVEMPDHCGPGKYAMAVSLDLISEDTPVTIPKSLK
RRLSKRGVIQPRVYNLTFDYGFHRLQGRRDKRIKLRIDYSDNPGYWSEIVAAAPGSKKSK
REIEHEVKTMHSASWERYLDHTWRVERRSTPEHEMDELHKRWFSVAVADWVNRQKQVDLD
YDLVRHGVHENVRLILFEQEKECPGVDVYAKIWADLNINVETAAVVTLIGDLTDLASFEQ
SHATFRNKGDIEVSLNFQADAELRFSTGTKELFGVAALGASFKIPGIVTIGPQFRLLSQL
NGRATLNANARVSFDVAKWDFMQQYPAPSTWTRPFNPDVDDEPVIEDAGSGLAVSGKPQF
TYNVHAEGLVEAVVTPVITFGIVFDAALGVPNSAIDVGVDIKGRIYASGGSSTELAWEYC
YGAEAEYAVFGQVSAPTLFGVSISRRWDLKSQEFDLVPRTCAAADDE

Enzyme Prediction     

No EC number prediction in SAPIO_CDS6627-t41_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH18	66	261	1.1e-34	0.5135135135135135

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
395573	Glyco_hydro_18	1.12e-51	66	298	2	307	Glycosyl hydrolases family 18.
214753	Glyco_18	2.44e-50	66	298	2	334	Glyco_18 domain.
119349	GH18_chitinase-like	1.83e-49	66	298	1	210	The GH18 (glycosyl hydrolase, family 18) type II chitinases hydrolyze chitin, an abundant polymer of beta-1,4-linked N-acetylglucosamine (GlcNAc) which is a major component of the cell wall of fungi and the exoskeleton of arthropods. Chitinases have been identified in viruses, bacteria, fungi, protozoan parasites, insects, and plants. The structure of the GH18 domain is an eight-stranded beta/alpha barrel with a pronounced active-site cleft at the C-terminal end of the beta-barrel. The GH18 family includes chitotriosidase, chitobiase, hevamine, zymocin-alpha, narbonin, SI-CLP (stabilin-1 interacting chitinase-like protein), IDGF (imaginal disc growth factor), CFLE (cortical fragment-lytic enzyme) spore hydrolase, the type III and type V plant chitinases, the endo-beta-N-acetylglucosaminidases, and the chitolectins. The GH85 (glycosyl hydrolase, family 85) ENGases (endo-beta-N-acetylglucosaminidases) are closely related to the GH18 chitinases and are included in this alignment model.
119365	GH18_chitinase	3.75e-49	66	298	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.
119351	GH18_chitolectin_chitotriosidase	9.89e-40	66	298	1	341	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
QYT04777.1|GH18	1.33e-246	127	1121	3	1114
UQC78235.1|CBM24|GH18|GH71	5.05e-231	64	1124	646	1822
APA11915.1|CBM18|GH18	6.67e-157	52	1118	182	1295
CBX95390.1|CBM18|GH18	2.78e-153	52	1109	174	1310
ATY59023.1|CBM18|GH18	2.12e-138	45	1102	176	1323

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3WL1_A	3.40e-31	60	274	3	213	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	8.35e-31	60	274	3	213	Crystal Structure of the Ostrinia furnacalis Group I Chitinase catalytic domain E148Q mutant [Ostrinia furnacalis]
3W4R_A	1.68e-30	40	274	1	231	Crystal structure of an insect chitinase from the Asian corn borer, Ostrinia furnacalis [Ostrinia furnacalis]
3WL0_A	2.05e-30	60	274	3	213	Crystal structure of Ostrinia furnacalis Group I chitinase catalytic domain E148A mutant in complex with a(GlcNAc)2 [Ostrinia furnacalis]
6JM7_A	8.54e-22	65	261	5	196	Crystal structure of Ostrinia furnacalis Group IV chitinase [Ostrinia furnacalis],6JMB_A Chain A, ofchtiv-allosamidin [Ostrinia furnacalis]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|P36362|CHIT_MANSE	6.55e-27	60	274	19	229	Endochitinase OS=Manduca sexta OX=7130 PE=2 SV=1
sp|P20533|CHIA1_NIACI	1.54e-19	66	259	46	280	Chitinase A1 OS=Niallia circulans OX=1397 GN=chiA1 PE=1 SV=1
sp|Q91XA9|CHIA_MOUSE	1.80e-19	66	274	24	226	Acidic mammalian chitinase OS=Mus musculus OX=10090 GN=Chia PE=1 SV=2
sp|Q6RY07|CHIA_RAT	4.25e-19	66	274	24	226	Acidic mammalian chitinase OS=Rattus norvegicus OX=10116 GN=Chia PE=2 SV=1
sp|Q95M17|CHIA_BOVIN	9.94e-19	66	274	24	226	Acidic mammalian chitinase OS=Bos taurus OX=9913 GN=CHIA PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
0.999996	0.000036

TMHMM  Annotations     

There is no transmembrane helices in SAPIO_CDS6627-t41_1-p1.