CAZyme Information: EEP81862.1

Basic Information

• Species: Uncinocarpus reesii
• Lineage: Ascomycota; Eurotiomycetes; ; Onygenaceae; Uncinocarpus; Uncinocarpus reesii
• CAZyme ID: EEP81862.1
• CAZy Family: GT32
• CAZyme Description: conserved hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1247		136793.96	4.7448

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_Ureesii1704	7856	336963	96	7760

• Gene Location: location=CH476618:1775151-1779025(+)

Full Sequence      

MWLPPLLSLVLYFPISFVSAKSTPSFSPSEFERRVAGWQSQFQDSPPGIPKKCPVFCEEV
GLDPVGWSGYSSPDALKGCNETMLLDFPVHRSLDDPNLGIGVRACVAEYSSTSLKTSPSN
DNSCISAFASSKVERKDEVHITQSGKPSKNAASDTVAAASQLRNYLASDASSCTSNSTIT
FAFSGDAVVGLYAGAMLKQQGVMASLLNQFIDEAEHGKLITADTVVVELCGSKDRGSDFA
FGIAVSTSANIGLVQDAVKEWSSGRCAKTPGDNTSRRWKNVTFKTPPAADAPDSLSKFQA
GIAGRSHILVPRGDCRTISVDSGDSCASLASKCGVSGSDFTKYNPGSKFCSTLAVGQRVC
CSAGDLPDIRPKPKPDGHCADYTTQAGDFCAKIAASNGLTVDDLEEFNKDTWAWNGCKKL
QSQFRMCLSKGKPPMPAPMANAICGPQVPGTEPPIDGVELKDLNPCPIKACCNVWGQCGV
TEDFCNEEKEDNPNYCVASCGMDIVKSDPPAEYIKIGYFEAFNWNRPCLNAHIDWIDWKG
DGYTHIHYGFASITRNFEIDVSEYQLEFDRFKALKGVKRIVSFGGWGFSTEPATYDILRS
ALAEDNRLKFKENVVKFINEHDLDGVDFDWEYPGAPDIPGIPPGKPEDAVNYLLFLFVLW
GDLPSEKSLSIAAPASYWYLKQFPIDLMSQVVDYIVYMTYDLHGQWDYKIPFVNPGCPNS
MGNCLRSHVNLTETTNALAMVTKAGAPSNKIIVGVSSYGRSFKMTQAGCHGETCTFVGPE
SGAKKGECTDTAGYVSNAEIEKIIKENDNILRLDDHEKDLHNILVYNDTEWVAYMDSKNK
AARRKMYQGLNMGGTVDWAVDLEKSLDDEDHLGEDLDVIYPPCNDDLDTVDEIVKAADKL
PGRCVEQYLARALSIELKSALEKYDQILKDGYDRKFGYYSKAVKKSWEAAMDTIYQHHIP
EYFNCLQQVPTGDDKYKNETGVCPPEFEGHAYSVFLIPKDEDKFFKWVAEKFQVLEDWIF
FDKFFFAICLGDPEVECKDYGWIHGIPKIRSNAEVPNPKKSIADALKELRDTQSYLADVM
EELRFEVFDGFAADVVDGAAVPVYMVKEAIANMEEVAEIGEEIEEEERKRFILLFLTAFL
FVLPGLGQGLAAVTGLAVIARITALVAEIGGAALSLHEIAENPTDPANVFLNIFGAVLGA
AALRNAGKLSDAAKIKRGLSGAKLGELGDNVKKAVEKISPLVKACRR

Enzyme Prediction     

EC	3.2.1.14:3	3.2.1.14:3

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH18	515	865	2.2e-49	0.9358108108108109

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
119357	GH18_zymocin_alpha	0.0	515	863	2	345	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	1.54e-54	515	862	2	333	Glyco_18 domain.
395573	Glyco_hydro_18	1.10e-49	516	861	3	305	Glycosyl hydrolases family 18.
119351	GH18_chitolectin_chitotriosidase	2.03e-40	544	868	29	342	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.
119365	GH18_chitinase	5.08e-39	516	763	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CAP66963.1|CBM18|CBM50|GH18	3.89e-286	19	1241	24	1356
CDP28705.1|CBM18|CBM50|GH18	3.89e-286	19	1241	24	1356
VBB80335.1|CBM18|CBM50|GH18	4.32e-285	19	1241	24	1356
QLI73538.1|CBM18|CBM50|GH18	3.10e-283	29	1228	44	1349
EGX48217.1|CBM18|CBM50|GH18	2.68e-275	53	1228	35	1215

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5Y29_A	1.81e-26	511	863	5	351	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]
1HKK_A	1.95e-26	544	863	31	342	High resoultion crystal structure of human chitinase in complex with allosamidin [Homo sapiens]
1HKI_A	1.99e-26	544	863	31	342	Crystal structure of human chitinase in complex with glucoallosamidin B [Homo sapiens],1HKJ_A Crystal structure of human chitinase in complex with methylallosamidin [Homo sapiens],1HKM_A High resolution crystal structure of human chitinase in complex with demethylallosamidin [Homo sapiens]
1LG1_A	1.99e-26	544	863	31	342	Crystal Structure Of Human Chitotriosidase In Complex With Chitobiose [Homo sapiens],1LG2_A Crystal Structure Of Human Chitotriosidase In Complex With Ethylene Glycol [Homo sapiens],1LQ0_A Crystal Structure Of Human Chitotriosidase At 2.2 Angstrom Resolution [Homo sapiens],6ZE8_A Crystal structure of human chitotriosidase-1 (hCHIT) catalytic domain in complex with compound OATD-01 [Homo sapiens],6ZE8_B Crystal structure of human chitotriosidase-1 (hCHIT) catalytic domain in complex with compound OATD-01 [Homo sapiens],6ZE8_C Crystal structure of human chitotriosidase-1 (hCHIT) catalytic domain in complex with compound OATD-01 [Homo sapiens],6ZE8_D Crystal structure of human chitotriosidase-1 (hCHIT) catalytic domain in complex with compound OATD-01 [Homo sapiens],6ZE8_E Crystal structure of human chitotriosidase-1 (hCHIT) catalytic domain in complex with compound OATD-01 [Homo sapiens],6ZE8_F Crystal structure of human chitotriosidase-1 (hCHIT) catalytic domain in complex with compound OATD-01 [Homo sapiens]
1GUV_A	2.02e-26	544	863	31	342	Structure of human chitotriosidase [Homo sapiens]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|P09805|KTXA_KLULA	1.14e-100	191	952	89	806	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|Q95M17|CHIA_BOVIN	3.47e-25	513	863	22	365	Acidic mammalian chitinase OS=Bos taurus OX=9913 GN=CHIA PE=1 SV=1
sp|Q13231|CHIT1_HUMAN	4.34e-25	544	863	52	363	Chitotriosidase-1 OS=Homo sapiens OX=9606 GN=CHIT1 PE=1 SV=1
sp|P36362|CHIT_MANSE	3.03e-23	544	863	53	375	Endochitinase OS=Manduca sexta OX=7130 PE=2 SV=1
sp|Q6RY07|CHIA_RAT	1.16e-22	544	863	52	365	Acidic mammalian chitinase OS=Rattus norvegicus OX=10116 GN=Chia PE=2 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000224	0.999754	CS pos: 20-21. Pr: 0.9784

TMHMM  Annotations     

Start	End
1138	1160