CAZyme Information: AN9390-T-p1

Basic Information

• Species: Aspergillus nidulans
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus nidulans
• CAZyme ID: AN9390-T-p1
• CAZy Family: GT66
• CAZyme Description: Putative endochitinase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1150	ChrVIII_A_nidulans_FGSC_A4|CGC14	126794.52	4.4837

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AnidulansFGSCA4	10988	227321	276	10712

• Gene Location: location=ChrVIII_A_nidulans_FGSC_A4:494853-498525(+)

Full Sequence      

MSKDLQRFNMLLLYCSRFHLCVLAALICLAIVSAQQDYSCSPVRPCKLGCCGKNNVCGMG
PSYCASENCTSTCDAKSECDPGWGSQWSQRQSCPLNVCCSKYGFCGTTEEFCGDEKVTKP
SCPGGTSASKKVIGYYEGWSTSKKCNGLNPEDLLMGAYTHLNYAFAFIDPESYKIANMQD
SDEEYMPRLTALKNYNPSLEVWIAIGGWSMNDPDQPTRRTFSELAASKSHQDVFFESLLS
FMDKYGFDGVDIDWEYPVAEERSGAPEDFENYVSFLKNLRAVLGNRGLTITLPASFWYLQ
HFDIKNMEPILDWFNIMSYDLHGTWDGTNPYLGPYINSHTNLTEIDLAMELLWRNDIDPK
KVVMGMGFYGRSFTLSDPACNTPGCGFSAGGNPGKCSASAGSLMFSEIQEIIDAGGAKVT
NDEKAGVQMVTWDTNQWVSYDDDETLKAKMEYANELCLGGVMVWAASTDDHKGTAIRALA
KAAGRTDLTVPVLAAKANNDPSQCVWGECGADCPSGLIPVEESSSNKNPLGIELGCNQGT
RYFCCPSKSPPTCKWKGSPKFCGLLSKNRCTDDEIEVSASTEGCWTGHKSLCCTKTESTD
VLDACKWFGAAPICAASAFFPSLLGPLGGAFSFHSYGCDDDDNRPNELTKAKQGQGGQQS
CTYNGGFKSFCCENPTPWKDCKWRAGNTAWVQWENLLFGPIGALFFDFSTDCKTGCEPGE
TTVATDGWGCRSGTYSYFCCADPNQPASPDLPDINLCYGPNHLDSLTSDLEGESNLPNVY
EEETVFDYGCGTDDLTALLKGKRGTEDVAFASNLSQLAVLETSPFLLEEHDLVPRGARER
IAMALCGPNGQRSSIWVQQYPGASSILLATGRAWTVAKQGLCAAAGITSLSTLASNTDWV
TEHVLEKQEFRNALEYMAAGQTPSGTMLRSGAVPFAQVFGNNGIFQQSWPTVTYPTLTFT
HNLVGNINDFFTGLLGRTSDPGLSNRFIENLQVCDRDFNVYKEYMVKGADFISRTMWSNY
NPQERVGILLDVVDMHNYRSRTEVVAAFSSTYKNIATMFKDLTRYAATQGITYDFEDAWK
QIMPDYLNWQVERVRDTFETYVDEEILYWASSLAQNTYAPLVIKEMSDLLQDLKTNMNTL
LALPVTQMTS

Enzyme Prediction     

EC	3.2.1.14:2

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH18	129	478	1e-72	0.9695945945945946

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
214753	Glyco_18	3.66e-94	131	469	1	334	Glyco_18 domain.
119351	GH18_chitolectin_chitotriosidase	8.47e-83	132	474	1	346	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.
395573	Glyco_hydro_18	6.19e-79	131	469	1	307	Glycosyl hydrolases family 18.
119357	GH18_zymocin_alpha	9.19e-75	131	466	1	342	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.
119365	GH18_chitinase	6.09e-70	132	469	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
EAA66457.1|CBM18|GH18|3.2.1.14	0.0	1	1150	1	1132
AAG34171.1|CBM18|GH18|3.2.1.14	0.0	1	1024	1	1024
UQC79648.1|CBM18|GH18	0.0	34	1150	22	1125
QPG96533.1|CBM18|GH18	0.0	59	1150	1	1091
QUC19097.1|CBM18|GH18	0.0	59	1148	1	1087

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6JM7_A	4.87e-53	130	473	4	354	Crystal structure of Ostrinia furnacalis Group IV chitinase [Ostrinia furnacalis],6JMB_A Chain A, ofchtiv-allosamidin [Ostrinia furnacalis]
6JM8_A	5.62e-52	130	473	4	354	Crystal structure of Ostrinia furnacalis Group IV chitinase [Ostrinia furnacalis]
5Y2A_A	3.07e-48	131	473	4	352	Crystal structure of Ostrinia furnacalis Group II chitinase catalytic domain 2 [Ostrinia furnacalis],5Y2A_B Crystal structure of Ostrinia furnacalis Group II chitinase catalytic domain 2 [Ostrinia furnacalis]
5Y29_A	8.98e-48	131	472	8	354	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]
6JAV_A	1.20e-47	131	472	8	354	Crystal structure of Ostrinia furnacalis Group II chitinase catalytic domain 1 in complex with a piperidine-thienopyridine derivative [Ostrinia furnacalis],6JAW_A Crystal structure of Ostrinia furnacalis Group II chitinase catalytic domain 1 in complex with a napthalimide derivative [Ostrinia furnacalis],6JAX_A Crystal structure of Ostrinia furnacalis Group II chitinase catalytic domain 1 in complex with chitooctaose [(GlcN)8] [Ostrinia furnacalis],6JAY_A Crystal structure of Ostrinia furnacalis Group II chitinase catalytic domain 1 in complex with a dipyrido-pyrimidine derivative [Ostrinia furnacalis]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q9WTV1|CH3L1_RAT	2.91e-42	131	474	21	360	Chitinase-3-like protein 1 OS=Rattus norvegicus OX=10116 GN=Chi3l1 PE=2 SV=3
sp|Q13231|CHIT1_HUMAN	5.25e-42	123	473	17	367	Chitotriosidase-1 OS=Homo sapiens OX=9606 GN=CHIT1 PE=1 SV=1
sp|Q5RBP6|CH3L1_PONAB	7.54e-42	131	474	50	389	Chitinase-3-like protein 1 OS=Pongo abelii OX=9601 GN=CHI3L1 PE=2 SV=1
sp|P36222|CH3L1_HUMAN	4.69e-41	131	474	23	362	Chitinase-3-like protein 1 OS=Homo sapiens OX=9606 GN=CHI3L1 PE=1 SV=2
sp|Q9W5U2|CHI10_DROME	1.29e-39	129	473	1907	2257	Probable chitinase 10 OS=Drosophila melanogaster OX=7227 GN=Cht10 PE=2 SV=2

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000463	0.999485	CS pos: 34-35. Pr: 0.9721

TMHMM  Annotations     

Start	End
13	35